{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q79PF4","secondaryAccessions":["Q31NX3","Q9Z3H2"],"uniProtkbId":"KAIC_SYNE7","entryAudit":{"firstPublicDate":"2004-10-11","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2004-07-05","entryVersion":161,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)","commonName":"Anacystis nidulans R2","taxonId":1140,"lineage":["Bacteria","Bacillati","Cyanobacteriota","Cyanophyceae","Synechococcales","Synechococcaceae","Synechococcus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01836"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9727980"}],"value":"Circadian clock oscillator protein KaiC"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01836"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10618446"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12727878"}],"value":"2.7.11.1"},{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01836"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17901204"}],"value":"3.6.4.-"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01836"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9727980"}],"value":"kaiC"},"orderedLocusNames":[{"value":"Synpcc7942_1216"}],"orfNames":[{"value":"see0011"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14709675"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15831759"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16707582"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17717528"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17916691"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26113637"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34618577"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9727980"}],"value":"The KaiABC oscillator complex constitutes the main circadian regulator in cyanobacteria (PubMed:15831759, PubMed:17717528, PubMed:26113637, PubMed:28302852, PubMed:9727980). Complex composition changes during the circadian cycle to control KaiC phosphorylation; KaiA stimulates KaiC autophosphorylation, while KaiB sequesters KaiA, leading to KaiC autodephosphorylation (PubMed:26113637, PubMed:28302852). The Kai complex controls chromosome condensation, leading to a transcription accessible chromosome during the first half of the circadian cycle and a compact, less transcription-accessible chromosome during the latter half (PubMed:16707582). Clock output pathways impact the RpaA transcriptional regulator (PubMed:20133618, PubMed:26113637, PubMed:28302852). Circadian oscillations can be generated in vitro by incubating KaiA, KaiB and KaiC with 1 mM ATP. The cycle is self-sustainable for at least 3 cycles and resistant to temperature changes. Mutations in KaiC alone prolong or reduce the circadian rhythm (PubMed:15831759). A very robust clock is reconstituted with KaiA, KaiB, KaiC, SasA, CikA and RpaA; output is measured by transcription from an appropriate reporter (PubMed:34618577)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17916691"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26113637"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28302852"}],"value":"The level of KaiC phosphorylation and KaiC ATPase activity represent the key features of the biochemical oscillator. KaiA homodimer binding to the KaiC CII domain stimulates KaiC's ATPase activity and forms KaiA(2-4):KaiC(6) complexes, which stimulate KaiC autophosphorylation first on Thr-432 then Ser-431. Phospho-Ser-431-KaiC accumulation triggers binding of KaiB to CI to form the KaiB(6):KaiC(6) complex, leading to changes in the output regulators CikA and SasA. KaiB(6):KaiC(6) formation exposes a site for KaiA binding that sequesters KaiA from the CII domain, making the KaiC(6):KaiB(6):KaiA(12) complex that results in KaiC autodephosphorylation. Complete dephosphorylation of KaiC leads to dissociation of KaiA(2):KaiB(1), completing 1 cycle of the Kai oscillator"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17901204"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26113637"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29892030"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31767776"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34618577"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35427168"}],"value":"Has a weak, temperature-independent ATPase activity (about 15 molecules of ATP per day); the addition of KaiA and KaiB increases activity slightly and makes the activity oscillate with a circadian period in vitro for over 60 hours. ATPase activity defines the circadian period. The phosphorylation state of KaiC modulates its ATPase activity and effects KaiB binding"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16707582"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16882723"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20133618"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23541768"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26113641"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34618577"}],"value":"There are several clock output pathways; SasA/RpaA, CikA/RpaA and LabA (PubMed:20133618). KaiC enhances the autophosphorylation activity of SasA, which then transfers its phosphate group to RpaA to activate it. Phosphotransfer is maximal when KaiC phosphorylation is active during the circadian cycle (PubMed:16707582, PubMed:16882723, PubMed:23541768, PubMed:26113641, PubMed:34618577). KaiB and KaiC together enhance the phosphatase activity of CikA on phospho-RpaA (PubMed:23541768, PubMed:34618577)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25825710"}],"value":"KaiC is important for metabolic partitioning during the dark to light shift, modulating the balance between the Calvin cycle and oxidative pentose phosphate pathway under natural growth conditions"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17989"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:11604"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:83421"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01836"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15347809"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15347812"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:17990"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10618446"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12727878"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15347812"}]},{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:17991"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12727878"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22304631"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46608"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:11605"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:61977"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01836"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15347809"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15347812"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:46609"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10618446"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12727878"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15347812"}]},{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:46610"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12727878"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22304631"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01836"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17901204"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26113637"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34618577"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35427168"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:13066"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31767776"}]},{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:13067"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31767776"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01836"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15304218"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22304631"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35427168"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01836"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22304631"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35427168"}],"value":"Binds 2 Mg(2+) ions per subunit, one in each domain. Mg(2+) is required for hexamerization and phosphatase activity."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12391300"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12727878"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12727879"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15347812"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18728181"}],"value":"Interaction with KaiA stimulates autophosphorylation, KaiC interaction with KaiB sequesters KaiA, preventing it stimulating the KaiC kinase, leading to autodephosphorylation. A KaiA dimer is sufficient to enhance KaiC phosphorylation (PubMed:12391300, PubMed:12727878, PubMed:12727879, PubMed:15347812). Interaction of KaiA with the A-loop stimulates autokinase activity (PubMed:18728181)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17901204"}],"value":"ATPase activity is stable from 25 to 35 degrees Celsius."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10064581"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10786837"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11356188"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12727878"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12727879"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15304218"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15347809"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17088557"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17717528"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22304631"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23796516"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24474762"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26113641"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26200123"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28302852"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29892030"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34618577"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35427168"}],"value":"Homohexamer resembling 2 stacked donuts with a central pore nearly blocked on one side; hexamerization is dependent on ATP-binding. Binds 12 ATP; 6 between each subunit in both layers (PubMed:15304218, PubMed:15347809, PubMed:22304631, PubMed:24474762, PubMed:35427168). KaiB only binds to phospho-Ser-431 KaiC (not doubly phosphorylated KaiC) (PubMed:17717528, PubMed:29892030). Complex formation between KaiB and KaiC is regulated by the phosphorylation state of KaiC and by an ATP hydrolysis-driven conformation change in the CI ring of KaiC; complex formation is slow. Slow complex formation is crucial for the timing of the circadian period (PubMed:29892030). KaiB switches to a thioredoxin-like form called KaiB(fs) when bound to KaiC (PubMed:26113641). The KaiABC complex composition changes during the circadian cycle to control KaiC phosphorylation. Complexes KaiC(6), KaiA(2-4):KaiC(6), KaiB(6):KaiC(6) and KaiC(6):KaiB(6):KaiA(12) are among the most important forms, many form cooperatively (PubMed:28302852, PubMed:34618577). Interacts directly with KaiB and SasA (PubMed:10786837). The CI domain binds to KaiB and SasA; as they have a similar fold they compete for the same site on CI (PubMed:29892030, PubMed:34618577). CikA interacts with this protein in the clock complex (PubMed:17088557). Binds to the C-terminus of KaiA via a coiled-coil structure (PubMed:26200123). Forms KaiC(6):KaiB(1) and KaiC(6):KaiB(6) complexes (PubMed:23796516, PubMed:24474762)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q79PF4","intActId":"EBI-592287"},"interactantTwo":{"uniProtKBAccession":"Q79PF6","geneName":"kaiA","intActId":"EBI-592281"},"numberOfExperiments":22,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q79PF4","intActId":"EBI-592287"},"interactantTwo":{"uniProtKBAccession":"Q79PF5","geneName":"kaiB","intActId":"EBI-619150"},"numberOfExperiments":12,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q79PF4","intActId":"EBI-592287"},"interactantTwo":{"uniProtKBAccession":"Q79PF4","geneName":"kaiC","intActId":"EBI-592287"},"numberOfExperiments":12,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q79PF4","intActId":"EBI-592287"},"interactantTwo":{"uniProtKBAccession":"Q06904","geneName":"sasA","intActId":"EBI-626872"},"numberOfExperiments":6,"organismDiffer":false}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15229218"}],"value":"Accumulates in a circadian fashion, peaking at circadian time (CT) 15-18"}],"commentType":"DEVELOPMENTAL STAGE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14709675"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15347809"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17210789"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9727980"}],"value":"Transcribed in a circadian rhythm with maximal expression at 12 hours and minimal expression 12 hours later; expressed as a kaiB-kaiC opperon, this gene does not have its own promoter (PubMed:9727980). Autorepresses expression (PubMed:14709675, PubMed:15347809, PubMed:9727980). Negatively regulated by labA (PubMed:17210789). Non-phosphorylatable kaiC mutants still down-regulate the kaiBC operon (PubMed:15347809)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15304218"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15347809"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16628225"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17901204"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18728181"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22304631"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26113637"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26200123"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28302852"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29892030"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35427168"},{"evidenceCode":"ECO:0000312","source":"PDB","id":"4TLA"}],"value":"In the homohexamer the 2 domains (called CI and CII, joined by a linker) self-associate to each form a 'donut' layer; the compactness and local conformation of the domains varies over the cell cycle and impacts function (PubMed:15304218, PubMed:15347809, PubMed:16628225, PubMed:29892030, PubMed:35427168). CII has the autokinase and autophosphatase activities, both CI and CII have (weak) ATPase activity; CI has the clock pacemaker role (PubMed:17901204, PubMed:22304631, PubMed:26113637). The CI ring undergoes structural changes driven by ATP hydrolysis that together with the KaiC phosphorylation state regulate KaiB binding (PubMed:29892030). The C-terminus of CII (residues 488-519) is disordered, extending from the top of the structure near the central pore (PubMed:15304218, PubMed:15347809, PubMed:16628225). The A-loop (residues 488-497) switches between a buried and exposed state, determining the levels of autokinase and autophosphatase activities. When the A-loop is exposed it interacts with KaiA, activating the autokinase activity (PubMed:18728181). Binding to KaiA occurs via the extreme C-terminus which assumes a coiled-coil structure upon binding (PubMed:26200123). KaiB interacts with the CI domain which has bound ADP (PubMed:28302852). Communication between CI and CII occurs via the Glu-214-Arg-217-Gln-394 triad (PubMed:35427168)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01836"}],"value":"In the homohexamer the 2 domains (called CI and CII) self-associate to each form a 'donut' layer; the compactness and local conformation of the domains varies over the cell cycle and impacts function. CII has the autokinase and autophosphatase activities, both CI and CII have (weak) ATPase activity; CI has the clock pacemaker role"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12391300"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12727878"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12727879"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15347812"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17717528"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17916691"}],"value":"Has a 4 step phosphorylation cycle; the autokinase acts first on Thr-432, then Ser-431. When Ser-431 is modified KaiC switches to an autophosphatase mode, acting first on phospho-Thr-432 then phospho-Ser-431 (PubMed:17717528, PubMed:17916691). Phosphorylated and dephosphorylated on serine/threonine residues by autocatalysis. Unphosphorylated, mono- and di-phosphorylated forms exist. The phosphorylated form correlates with clock speed (PubMed:12391300, PubMed:15347812). The presence of KaiA increases phosphorylation and stabilizes these forms (PubMed:12391300, PubMed:15347812)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01836"}],"value":"Phosphorylated on serine and threonine residues by autocatalysis. Has a 4 step phosphorylation cycle; the autokinase acts first on Thr-432, then Ser-431. When Ser-431 is modified KaiC switches to an autophosphatase mode, acting first on phospho-Thr-432 then phospho-Ser-431"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16707582"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25825710"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9727980"}],"value":"Not essential for growth on low light, loss of circadian cycle and rhythmicity (PubMed:9727980). Loss of rhythmic chromosome compaction (PubMed:16707582). No visible phenotype during growth in a light/dark regime for 5-7 days (at 150 umol photons/m(2)/s). Accumulates much larger amounts of primary metabolites (especially those in and connected to the oxidative pentose phosphate pathway) in 4 hours after dark-light transition. Glycogen accumulates 4-5 hours earlier than normal, overall levels are higher, no change in glycogen degradation kinetics (PubMed:25825710)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9727980"}],"value":"'Kai' means 'cycle' in Japanese"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01836"},{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the KaiC family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":519,"modifier":"EXACT"}},"description":"Circadian clock oscillator protein KaiC","featureId":"PRO_0000217782"},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"KaiC 1","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01836"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15304218"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15347809"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15347812"}]},{"type":"Domain","location":{"start":{"value":261,"modifier":"EXACT"},"end":{"value":519,"modifier":"EXACT"}},"description":"KaiC 2","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01836"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15304218"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15347809"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15347812"}]},{"type":"Region","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"B-loop, required to bind KaiB and SasA","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q79V60"}]},{"type":"Region","location":{"start":{"value":248,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15304218"}]},{"type":"Region","location":{"start":{"value":488,"modifier":"EXACT"},"end":{"value":497,"modifier":"EXACT"}},"description":"A-loop, interacts with KaiA","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18728181"}]},{"type":"Active site","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"Proton acceptor in CI (KaiC 1)","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"22304631"}]},{"type":"Active site","location":{"start":{"value":318,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"Proton acceptor in CII (KaiC 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