INHA_MYCAV
ID INHA_MYCAV Reviewed; 268 AA.
AC O07400;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000250|UniProtKB:P9WGR1};
DE Short=ENR {ECO:0000250|UniProtKB:P9WGR1};
DE Short=Enoyl-ACP reductase {ECO:0000250|UniProtKB:P9WGR1};
DE EC=1.3.1.9 {ECO:0000250|UniProtKB:P9WGR1};
DE AltName: Full=FAS-II enoyl-ACP reductase {ECO:0000250|UniProtKB:P9WGR1};
DE AltName: Full=NADH-dependent 2-trans-enoyl-ACP reductase {ECO:0000250|UniProtKB:P9WGR1};
GN Name=inhA {ECO:0000312|EMBL:AAC46204.1};
OS Mycobacterium avium.
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=1764;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GIR10;
RX PubMed=9534249; DOI=10.1099/00221287-144-3-807;
RA Labo M., Gusberti L., de Rossi E., Speziale P., Riccardi G.;
RT "Determination of a 15437 bp nucleotide sequence around the inhA gene of
RT Mycobacterium avium and similarity analysis of the products of putative
RT ORFs.";
RL Microbiology 144:807-814(1998).
CC -!- FUNCTION: Enoyl-ACP reductase of the type II fatty acid syntase (FAS-
CC II) system, which is involved in the biosynthesis of mycolic acids, a
CC major component of mycobacterial cell walls. Catalyzes the NADH-
CC dependent reduction of the double bond of 2-trans-enoyl-[acyl-carrier
CC protein], an essential step in the fatty acid elongation cycle of the
CC FAS-II pathway. Shows preference for long-chain fatty acyl thioester
CC substrates, and can also use 2-trans-enoyl-CoAs as alternative
CC substrates. The mycobacterial FAS-II system utilizes the products of
CC the FAS-I system as primers to extend fatty acyl chain lengths up to
CC C56, forming the meromycolate chain that serves as the precursor for
CC final mycolic acids. {ECO:0000250|UniProtKB:P9WGR1}.
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:0000250|UniProtKB:P9WGR1};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10242;
CC Evidence={ECO:0000250|UniProtKB:P9WGR1};
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:0000250|UniProtKB:P9WGR1};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18179;
CC Evidence={ECO:0000250|UniProtKB:P9WGR1};
CC -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC {ECO:0000250|UniProtKB:P9WGR1}.
CC -!- SUBUNIT: Homodimer. Homotetramer. {ECO:0000250|UniProtKB:P9WGR1}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. FabI subfamily. {ECO:0000305}.
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DR EMBL; AF002133; AAC46204.1; -; Genomic_DNA.
DR AlphaFoldDB; O07400; -.
DR SMR; O07400; -.
DR UniPathway; UPA00915; -.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050343; F:trans-2-enoyl-CoA reductase (NAD+) activity; IEA:RHEA.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd05372; ENR_SDR; 1.
DR InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43159; PTHR43159; 1.
DR PIRSF; PIRSF000094; Enoyl-ACP_rdct; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; NAD; Oxidoreductase.
FT CHAIN 1..268
FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH]"
FT /id="PRO_0000054914"
FT BINDING 20..21
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGR1"
FT BINDING 64..65
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGR1"
FT BINDING 95..96
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGR1"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WGR1"
FT BINDING 164
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGR1"
FT BINDING 193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGR1"
FT SITE 148
FT /note="May act as an intermediate that passes the hydride
FT ion from NADH to the substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WGR1"
FT SITE 157
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P9WGR1"
SQ SEQUENCE 268 AA; 28530 MW; F73501BD2B0F9990 CRC64;
MAGLLDGKRI LVTGIITDSS IAFHIAKVAQ EAGAQLVLTG FDRLRLIQRI VDRLPEKAPL
IELDVQNEEH LNTLAQRVTG EIGEGNKLDG VVHSIASSET GMADQPFFDA PYEDVSKGIH
ISADSDASLA KALLPIMNPG GSIVGMDFDP SRAMPAYNWM TVAKSALESV NRFVAREAGP
HGVRSNLVAA GPIRTLAMAG IVGGVLGDQA AEQIRLLEEG WDQRAPIGWN MKDPTPVAKT
VCALLSDWLP ATTGTIIYAD RGASTQLL
