FABI_AQUAE
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 03-AUG-2022, entry version 144.
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; 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};
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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 OMA; GILDMIH; -.
DR OrthoDB; 762291at2; -.
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:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
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 InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43159; PTHR43159; 1.
DR PIRSF; PIRSF000094; Enoyl-ACP_rdct; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 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
