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 27-MAR-2024, entry version 103. 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; Actinomycetota; Actinomycetes; Mycobacteriales; 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}. 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; 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: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 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; 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 //