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}.
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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
//