ID M9TGV3_MYCTX Unreviewed; 269 AA. AC M9TGV3; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 29-MAY-2024, entry version 89. DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000256|ARBA:ARBA00017755, ECO:0000256|PIRNR:PIRNR000094}; DE EC=1.3.1.9 {ECO:0000256|PIRNR:PIRNR000094}; GN Name=inhA {ECO:0000313|EMBL:AGJ50654.1}; GN Synonyms=inhA_2 {ECO:0000313|EMBL:OMH59404.1}; GN ORFNames=A4S10_01572 {ECO:0000313|EMBL:OMH59404.1}, ERS007679_02961 GN {ECO:0000313|EMBL:COW03350.1}, ERS007681_02786 GN {ECO:0000313|EMBL:CFE41166.1}, ERS007688_00531 GN {ECO:0000313|EMBL:CFE46976.1}, ERS007718_00529 GN {ECO:0000313|EMBL:COV75687.1}, ERS007741_01725 GN {ECO:0000313|EMBL:COW17773.1}, ERS027659_00857 GN {ECO:0000313|EMBL:CKR17592.1}, ERS027661_03047 GN {ECO:0000313|EMBL:CKS41591.1}, ERS035788_02466 GN {ECO:0000313|EMBL:CKY09036.1}, ERS053720_00426 GN {ECO:0000313|EMBL:CFH70051.1}, SAMEA2683035_01034 GN {ECO:0000313|EMBL:SGH39969.1}; OS Mycobacterium tuberculosis. OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=1773 {ECO:0000313|EMBL:AGJ50654.1}; RN [1] {ECO:0000313|EMBL:AGJ50654.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TB11-111 {ECO:0000313|EMBL:AGJ50654.1}, and TB11-153 RC {ECO:0000313|EMBL:AGJ50655.1}; RA Daum L.T., Rodriguez J.D., Bhattacharyya S.; RT "Ion Torrent full-gene sequencing and phenotypic drug susceptibility RT testing (DST) confirm multi-drug resistance (MDR) Mycobacterium RT tuberculosis in the United States."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AHA90961.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MtbPL.K131 {ECO:0000313|EMBL:AHA90961.1}; RX PubMed=24855126; DOI=10.1093/jac/dku161; RA Jagielski T., Bakula Z., Roeske K., Kaminski M., Napiorkowska A., RA Augustynowicz-Kopec E., Zwolska Z., Bielecki J.; RT "Detection of mutations associated with isoniazid resistance in multidrug- RT resistant Mycobacterium tuberculosis clinical isolates."; RL J. Antimicrob. Chemother. 69:2369-2375(2014). RN [3] {ECO:0000313|Proteomes:UP000041611, ECO:0000313|Proteomes:UP000046674} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=0351H {ECO:0000313|EMBL:CFH70051.1, RC ECO:0000313|Proteomes:UP000046674}, Bir 382 RC {ECO:0000313|EMBL:CKY09036.1, ECO:0000313|Proteomes:UP000048478}, and RC M09400937 {ECO:0000313|EMBL:COV75687.1, RC ECO:0000313|Proteomes:UP000041611}; RG Pathogen Informatics; RA Murphy D.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|Proteomes:UP000045842, ECO:0000313|Proteomes:UP000046947} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2926STDY5723788 {ECO:0000313|EMBL:SGH39969.1, RC ECO:0000313|Proteomes:UP000182946}, Bir 185 RC {ECO:0000313|EMBL:CKR17592.1, ECO:0000313|Proteomes:UP000050164}, Bir RC 187 {ECO:0000313|EMBL:CKS41591.1, ECO:0000313|Proteomes:UP000049023}, RC G09801536 {ECO:0000313|EMBL:COW03350.1, RC ECO:0000313|Proteomes:UP000045842}, G09901357 RC {ECO:0000313|EMBL:CFE41166.1, ECO:0000313|Proteomes:UP000048289}, RC H09601792 {ECO:0000313|EMBL:CFE46976.1, RC ECO:0000313|Proteomes:UP000046947}, and P00601463 RC {ECO:0000313|EMBL:COW17773.1, ECO:0000313|Proteomes:UP000048600}; RG Pathogen Informatics; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:OMH59404.1, ECO:0000313|Proteomes:UP000189452} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=6548 {ECO:0000313|EMBL:OMH59404.1, RC ECO:0000313|Proteomes:UP000189452}; RA Bigi M., Bigi F., Soria M.A.; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:OMH59404.1, ECO:0000313|Proteomes:UP000189452} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=6548 {ECO:0000313|EMBL:OMH59404.1, RC ECO:0000313|Proteomes:UP000189452}; RA Bigi M.M., Lopez B., Blanco F.C., Sasiain M.C., De La Barrera S., RA Ritacco V., Bigi F., Soria M.A.; RT "Protein polymorphisms may explain contrasting epidemiological fitness of RT two variants of a multidrug-resistant Mycobacterium tuberculosis strain."; RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2,3-saturated acyl-CoA + NAD(+) = a (2E)-enoyl-CoA + H(+) + CC NADH; Xref=Rhea:RHEA:18177, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; CC Evidence={ECO:0000256|ARBA:ARBA00001288}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18179; CC Evidence={ECO:0000256|ARBA:ARBA00001288}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + CC H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA- CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9; CC Evidence={ECO:0000256|ARBA:ARBA00000196}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10242; CC Evidence={ECO:0000256|ARBA:ARBA00000196}; CC -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis. CC {ECO:0000256|ARBA:ARBA00004796}. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) CC family. FabI subfamily. {ECO:0000256|ARBA:ARBA00009233, CC ECO:0000256|PIRNR:PIRNR000094}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KC692360; AGJ50654.1; -; Genomic_DNA. DR EMBL; KC692361; AGJ50655.1; -; Genomic_DNA. DR EMBL; KF563064; AHA90961.1; -; Genomic_DNA. DR EMBL; CFOE01000404; CFE41166.1; -; Genomic_DNA. DR EMBL; CFOH01000050; CFE46976.1; -; Genomic_DNA. DR EMBL; CFSW01000002; CFH70051.1; -; Genomic_DNA. DR EMBL; CNFT01000132; CKR17592.1; -; Genomic_DNA. DR EMBL; CNFU01000735; CKS41591.1; -; Genomic_DNA. DR EMBL; CHBD01000028; CKY09036.1; -; Genomic_DNA. DR EMBL; CSAT01000007; COV75687.1; -; Genomic_DNA. DR EMBL; CSAD01000466; COW03350.1; -; Genomic_DNA. DR EMBL; CHKL01000161; COW17773.1; -; Genomic_DNA. DR EMBL; LWDQ01000001; OMH59404.1; -; Genomic_DNA. DR EMBL; FPTZ01000005; SGH39969.1; -; Genomic_DNA. DR RefSeq; WP_003407553.1; NZ_WUCS01000015.1. DR GeneID; 45425463; -. DR PATRIC; fig|1773.206.peg.1259; -. DR OMA; GILDMIH; -. DR UniPathway; UPA00915; -. DR Proteomes; UP000041611; Unassembled WGS sequence. DR Proteomes; UP000045842; Unassembled WGS sequence. DR Proteomes; UP000046674; Unassembled WGS sequence. DR Proteomes; UP000046947; Unassembled WGS sequence. DR Proteomes; UP000048289; Unassembled WGS sequence. DR Proteomes; UP000048478; Unassembled WGS sequence. DR Proteomes; UP000048600; Unassembled WGS sequence. DR Proteomes; UP000049023; Unassembled WGS sequence. DR Proteomes; UP000050164; Unassembled WGS sequence. DR Proteomes; UP000182946; Unassembled WGS sequence. DR Proteomes; UP000189452; Chromosome. DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR CDD; cd05372; ENR_SDR; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; NF040631; InhA; 1. DR PANTHER; PTHR43159; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE; 1. DR PANTHER; PTHR43159:SF2; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH] FABI; 1. DR Pfam; PF13561; adh_short_C2; 1. DR PIRSF; PIRSF000094; Enoyl-ACP_rdct; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 3: Inferred from homology; KW Fatty acid biosynthesis {ECO:0000256|PIRNR:PIRNR000094}; KW Fatty acid metabolism {ECO:0000256|PIRNR:PIRNR000094}; KW Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR000094}; KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR000094}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000094}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR000094}. FT BINDING 14 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3" FT BINDING 20..21 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3" FT BINDING 64..65 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3" FT BINDING 95 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3" FT BINDING 165 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3" FT BINDING 194..198 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3" SQ SEQUENCE 269 AA; 28528 MW; F161D6D6A631CA08 CRC64; MTGLLDGKRI LVSGIITDSS IAFHIARVAQ EQGAQLVLTG FDRLRLIQRI TDRLPAKAPL LELDVQNEEH LASLAGRVTE AIGAGNKLDG VVHSIGFMPQ TGMGINPFFD APYADVSKGI HISAYSYASM AKALLPIMNP GGSIVGMDFD PSRAMPAYNW MTVAKSALES VNRFVAREAG KYGVRSNLVA AGPIRTLAMS AIVGGALGEE AGAQIQLLEE GWDQRAPIGW NMKDATPVAK TVCALLSDWL PATTGDIIYA DGGAHTQLL //