ID FABI_AQUAE Reviewed; 270 AA. AC O67505; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 27-MAR-2024, entry version 149. DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] FabI; DE Short=ENR; DE EC=1.3.1.9; DE AltName: Full=NADH-dependent enoyl-ACP reductase; GN Name=fabI; OrderedLocusNames=aq_1552; OS Aquifex aeolicus (strain VF5). OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Aquifex. OX NCBI_TaxID=224324; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VF5; RX PubMed=9537320; DOI=10.1038/32831; RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.; RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."; RL Nature 392:353-358(1998). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT. RG Southeast collaboratory for structural genomics (SECSG); RT "Crystal structure of enoyl-[acyl-carrier-protein] reductase (NADH) from RT Aquifex aeolicus VF5."; RL Submitted (APR-2007) to the PDB data bank. CC -!- FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an CC enoyl moiety that is covalently linked to an acyl carrier protein CC (ACP). Involved in the elongation cycle of fatty acid which are used in CC the lipid metabolism (By similarity). {ECO:0000250}. 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 -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|Ref.2}. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) CC family. FabI subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC07465.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AE000657; AAC07465.1; ALT_INIT; Genomic_DNA. DR PIR; G70434; G70434. DR RefSeq; NP_214070.1; NC_000918.1. DR PDB; 2P91; X-ray; 2.00 A; A/B/C/D=1-270. DR PDBsum; 2P91; -. DR AlphaFoldDB; O67505; -. DR SMR; O67505; -. DR STRING; 224324.aq_1552; -. DR EnsemblBacteria; AAC07465; AAC07465; aq_1552. DR KEGG; aae:aq_1552; -. DR PATRIC; fig|224324.8.peg.1204; -. DR eggNOG; COG0623; Bacteria. DR HOGENOM; CLU_010194_10_1_0; -. DR InParanoid; O67505; -. DR OrthoDB; 9803628at2; -. DR UniPathway; UPA00094; -. DR EvolutionaryTrace; O67505; -. DR Proteomes; UP000000798; Chromosome. DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; ISS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB. DR GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB. 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 InterPro; IPR002347; SDR_fam. 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 PRINTS; PR00081; GDHRDH. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 1: Evidence at protein level; KW 3D-structure; Fatty acid biosynthesis; Fatty acid metabolism; KW Lipid biosynthesis; Lipid metabolism; NAD; Oxidoreductase; KW Reference proteome. FT CHAIN 1..270 FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH] FabI" FT /id="PRO_0000054894" FT ACT_SITE 146 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 156 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 13 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 19..20 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 64..65 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 92 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 95 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 163 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 192..196 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT TURN 3..6 FT /evidence="ECO:0007829|PDB:2P91" FT STRAND 8..11 FT /evidence="ECO:0007829|PDB:2P91" FT HELIX 20..30 FT /evidence="ECO:0007829|PDB:2P91" FT STRAND 34..41 FT /evidence="ECO:0007829|PDB:2P91" FT HELIX 42..44 FT /evidence="ECO:0007829|PDB:2P91" FT HELIX 45..54 FT /evidence="ECO:0007829|PDB:2P91" FT STRAND 60..62 FT /evidence="ECO:0007829|PDB:2P91" FT HELIX 68..81 FT /evidence="ECO:0007829|PDB:2P91" FT STRAND 87..90 FT /evidence="ECO:0007829|PDB:2P91" FT HELIX 97..100 FT /evidence="ECO:0007829|PDB:2P91" FT HELIX 104..106 FT /evidence="ECO:0007829|PDB:2P91" FT HELIX 109..119 FT /evidence="ECO:0007829|PDB:2P91" FT HELIX 121..130 FT /evidence="ECO:0007829|PDB:2P91" FT HELIX 131..134 FT /evidence="ECO:0007829|PDB:2P91" FT STRAND 140..145 FT /evidence="ECO:0007829|PDB:2P91" FT HELIX 147..149 FT /evidence="ECO:0007829|PDB:2P91" FT TURN 154..157 FT /evidence="ECO:0007829|PDB:2P91" FT HELIX 158..178 FT /evidence="ECO:0007829|PDB:2P91" FT TURN 179..181 FT /evidence="ECO:0007829|PDB:2P91" FT STRAND 183..189 FT /evidence="ECO:0007829|PDB:2P91" FT HELIX 203..213 FT /evidence="ECO:0007829|PDB:2P91" FT HELIX 222..232 FT /evidence="ECO:0007829|PDB:2P91" FT HELIX 235..237 FT /evidence="ECO:0007829|PDB:2P91" FT STRAND 244..248 FT /evidence="ECO:0007829|PDB:2P91" FT HELIX 251..253 FT /evidence="ECO:0007829|PDB:2P91" SQ SEQUENCE 270 AA; 29725 MW; 2ACD6C85EE16DC68 CRC64; MGLLEGKRAL ITGVANERSI AYGIAKSFHR EGAQLAFTYA TPKLEKRVRE IAKGFGSDLV VKCDVSLDED IKNLKKFLEE NWGSLDIIVH SIAYAPKEEF KGGVIDTSRE GFKIAMDISV YSLIALTREL LPLMEGRNGA IVTLSYYGAE KVVPHYNVMG IAKAALESTV RYLAYDIAKH GHRINAISAG PVKTLAAYSI TGFHLLMEHT TKVNPFGKPI TIEDVGDTAV FLCSDWARAI TGEVVHVDNG YHIMGVFGRE EEIKKEVYGD //