{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P9WGR1","secondaryAccessions":["F2GEM2","P0A5Y6","P46533","Q540M9"],"uniProtkbId":"INHA_MYCTU","entryAudit":{"firstPublicDate":"2014-04-16","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2014-04-16","entryVersion":69,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","taxonId":83332,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7599116"}],"value":"Enoyl-[acyl-carrier-protein] reductase [NADH]"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12606558"}],"value":"ENR"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7599116"}],"value":"Enoyl-ACP reductase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7599116"}],"value":"1.3.1.9"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"FAS-II enoyl-ACP reductase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7599116"}],"value":"NADH-dependent 2-trans-enoyl-ACP reductase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8284673"}],"value":"inhA"},"orderedLocusNames":[{"value":"Rv1484"}],"orfNames":[{"value":"MTCY277.05"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7599116"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"25227413"}],"value":"Enoyl-ACP reductase of the type II fatty acid syntase (FAS-II) system, which is involved in the biosynthesis of mycolic acids, a major component of mycobacterial cell walls (PubMed:25227413). Catalyzes the NADH-dependent reduction of the double bond of 2-trans-enoyl-[acyl-carrier protein], an essential step in the fatty acid elongation cycle of the FAS-II pathway (PubMed:7599116). Shows preference for long-chain fatty acyl thioester substrates (>C16), and can also use 2-trans-enoyl-CoAs as alternative substrates (PubMed:7599116). The mycobacterial FAS-II system utilizes the products of the FAS-I system as primers to extend fatty acyl chain lengths up to C56, forming the meromycolate chain that serves as the precursor for final mycolic acids (PubMed:25227413)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12406221"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16906155"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17227913"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9417034"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8284673"}],"value":"Is the primary target of the first-line antitubercular drug isoniazid (INH) and of the second-line drug ethionamide (ETH) (PubMed:12406221, PubMed:16906155, PubMed:17227913, PubMed:8284673). Overexpressed inhA confers INH and ETH resistance to M.tuberculosis (PubMed:12406221). The mechanism of isoniazid action against InhA is covalent attachment of the activated form of the drug to the nicotinamide ring of NAD and binding of the INH-NAD adduct to the active site of InhA (PubMed:16906155, PubMed:9417034). Similarly, the ETH-NAD adduct binds InhA (PubMed:17227913)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10240"},{"database":"Rhea","id":"RHEA-COMP:9925"},{"database":"Rhea","id":"RHEA-COMP:9926"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:78784"},{"database":"ChEBI","id":"CHEBI:78785"}],"ecNumber":"1.3.1.9","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7599116"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:10242"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7599116"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 2,3-saturated acyl-CoA + NAD(+) = a (2E)-enoyl-CoA + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18177"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:58856"},{"database":"ChEBI","id":"CHEBI:65111"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10521269"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20864541"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21143326"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22987724"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7599116"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:18179"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7599116"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2E)-octenoyl-[ACP] + NADH + H(+) = octanoyl-[ACP] + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:41528"},{"database":"Rhea","id":"RHEA-COMP:9635"},{"database":"Rhea","id":"RHEA-COMP:9636"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:78462"},{"database":"ChEBI","id":"CHEBI:78463"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7599116"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:41529"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7599116"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2E)-octenoyl-CoA + NADH + H(+) = octanoyl-CoA + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:63232"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57386"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:62242"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20864541"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22987724"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7599116"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:63233"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7599116"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2E)-dodecenoyl-CoA + NADH + H(+) = dodecanoyl-CoA + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45408"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57330"},{"database":"ChEBI","id":"CHEBI:57375"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10521269"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21143326"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7599116"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:45409"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7599116"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2E)-hexadecenoyl-CoA + NADH + H(+) = hexadecanoyl-CoA + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46072"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57379"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:61526"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7599116"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:46073"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7599116"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2E)-eicosenoyl-CoA + NADH + H(+) = eicosanoyl-CoA + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46076"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57380"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:74691"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7599116"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:46077"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7599116"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2E)-tetracosenoyl-CoA + NADH + H(+) = tetracosanoyl-CoA + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46080"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:65052"},{"database":"ChEBI","id":"CHEBI:74693"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7599116"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:46081"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7599116"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12606558"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14623976"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17034137"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17163639"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17227913"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17723305"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19130456"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20200152"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20864541"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22987724"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24107081"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24292073"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24616444"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25568071"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26934341"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27428438"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9417034"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.5"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21143326"}],"value":"InhA activity is controlled via phosphorylation: phosphorylation on Thr-266 decreases InhA activity (5-fold reduction) and likely negatively regulates biosynthesis of mycolic acids and growth of the bacterium (PubMed:20864541, PubMed:21143326). The antitubercular pro-drug isoniazid (INH) is oxidatively activated by the catalase-peroxidase KatG and then covalently binds NAD to form an adduct that inhibits the activity of InhA (PubMed:14623976, PubMed:9417034, Ref.5). The inhibitory adduct is the isonicotinic-acyl-NADH where the isonicotinic-acyl group replaces the 4S (and not the 4R) hydrogen of NADH (PubMed:9417034). Similarly, the antitubercular pro-drugs ethionamide (ETH) and prothionamide (PTH) are activated by the flavoprotein monooxygenase EthA, and forms an adduct with NAD (ETH-NAD and PTH-NAD, respectively) that is a tight-binding inhibitor of InhA (PubMed:17227913). Is inhibited by triclosan and derivatives, pyrazole derivative Genz-8575, indole-5-amide Genz-10850, alkyl diphenyl ethers, pyrrolidine carboxamides, arylamides, pyridomycin, methyl-thiazoles, 4-hydroxy-2-pyridones, and N-benzyl-4-((heteroaryl)methyl)benzamides (PubMed:12606558, PubMed:17034137, PubMed:17163639, PubMed:17723305, PubMed:19130456, PubMed:20200152, PubMed:22987724, PubMed:24107081, PubMed:24616444, PubMed:25568071). Pyridomycin shows a unique mode of InhA inhibition by simultaneously blocking parts of the NADH and the lipid substrate-binding pocket of InhA (PubMed:24292073). Is also inhibited by thiadiazole compounds, that have very attractive antitubercular properties (PubMed:27428438)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":2.2,"unit":"umol/min/mg","enzyme":"enzyme for the reduction of 2-trans-octenoyl-ACP (at pH 6.8 and 25 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7599116"}]},{"velocity":3.6,"unit":"umol/min/mg","enzyme":"enzyme for the reduction of 2-trans-octenoyl-CoA (at pH 6.8 and 25 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7599116"}]},{"velocity":0.52,"unit":"umol/min/mg","enzyme":"enzyme for the reduction of 2-trans-octenoyl-CoA (at pH 6.8 and 25 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22987724"}]},{"velocity":15.3,"unit":"umol/min/mg","enzyme":"enzyme for the reduction of 2-trans-octenoyl-CoA (at pH 6.8)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20864541"}]},{"velocity":5.8,"unit":"umol/min/mg","enzyme":"enzyme for the reduction of 2-trans-dodecenoyl-CoA (at pH 6.8 and 25 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7599116"}]},{"velocity":11.4,"unit":"umol/min/mg","enzyme":"enzyme for the reduction of 2-trans-dodecenoyl-CoA (at pH 7.5 and 25 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21143326"}]},{"velocity":4.5,"unit":"umol/min/mg","enzyme":"enzyme for the reduction of 2-trans-hexadecenoyl-CoA (at pH 6.8 and 25 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7599116"}]}],"michaelisConstants":[{"constant":2.0,"unit":"uM","substrate":"2-trans-octenoyl-ACP (at pH 6.8 and 25 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7599116"}]},{"constant":8.1,"unit":"uM","substrate":"NADH (at pH 6.8 and 25 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7599116"}]},{"constant":66.0,"unit":"uM","substrate":"NADH (at pH 6.8 and 25 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10521269"}]},{"constant":19.1,"unit":"uM","substrate":"NADH (at pH 6.8)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20864541"}]},{"constant":13.5,"unit":"uM","substrate":"NADH (at pH 6.8 and 25 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22987724"}]},{"constant":467.0,"unit":"uM","substrate":"2-trans-octenoyl-CoA (at pH 6.8 and 25 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7599116"}]},{"constant":528.0,"unit":"uM","substrate":"2-trans-octenoyl-CoA (at pH 6.8)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20864541"}]},{"constant":48.0,"unit":"uM","substrate":"2-trans-dodecenoyl-CoA (at pH 6.8 and 25 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7599116"}]},{"constant":27.0,"unit":"uM","substrate":"2-trans-dodecenoyl-CoA (at pH 6.8 and 25 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10521269"}]},{"constant":40.9,"unit":"uM","substrate":"2-trans-dodecenoyl-CoA (at pH 7.5 and 25 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21143326"}]},{"constant":1.5,"unit":"uM","substrate":"2-trans-hexadecenoyl-CoA (at pH 6.8 and 25 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7599116"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10521269"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21143326"}],"value":"kcat is 320.4 min(-1) for the reduction of 2-trans-dodecenoyl-CoA (at pH 7.5 and 25 degrees Celsius) (PubMed:21143326). kcat is 278 min(-1) for the reduction of 2-trans-dodecenoyl-CoA (at pH 6.8 and 25 degrees Celsius) (PubMed:10521269)."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"25227413"}],"value":"Lipid metabolism; mycolic acid biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10336454"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16647717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7599116"}],"value":"Homodimer (PubMed:7599116). Homotetramer (PubMed:10336454, PubMed:16647717)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20864541"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21143326"}],"value":"Is phosphorylated on Thr-266 in vivo. In vitro, can be phosphorylated by multiple Ser/Thr protein kinases (STPK) such as PknA, PknB, PknE, PknH and PknL. Phosphorylation decreases enzymatic activity"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19099550"}],"value":"Was identified as a high-confidence drug target"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16906155"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7886450"}],"value":"Many isoniazid- and ethionamide-resistant clinical isolates contain mutations within the inhA locus. Resistance to isoniazid and ethionamide can be conferred by the single substitution of alanine for serine 94; this drug resistance seems to be directly related to a perturbation in the hydrogen-bonding network that decreases the binding of NADH and the INH-NAD adduct"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the short-chain dehydrogenases/reductases (SDR) family. 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