FABV_ALIF1
ID FABV_ALIF1 Reviewed; 400 AA.
AC Q5E6G3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000255|HAMAP-Rule:MF_01838};
DE Short=ENR {ECO:0000255|HAMAP-Rule:MF_01838};
DE EC=1.3.1.9 {ECO:0000255|HAMAP-Rule:MF_01838};
GN Name=fabV {ECO:0000255|HAMAP-Rule:MF_01838}; OrderedLocusNames=VF_0888;
OS Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=312309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700601 / ES114;
RX PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT pathogenic congeners.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
CC -!- FUNCTION: Involved in the final reduction of the elongation cycle of
CC fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon-
CC carbon double bond in an enoyl moiety that is covalently linked to an
CC acyl carrier protein (ACP). {ECO:0000255|HAMAP-Rule:MF_01838}.
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:0000255|HAMAP-Rule:MF_01838};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_01838}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01838}.
CC -!- SIMILARITY: Belongs to the TER reductase family. {ECO:0000255|HAMAP-
CC Rule:MF_01838}.
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DR EMBL; CP000020; AAW85383.1; -; Genomic_DNA.
DR RefSeq; WP_011261553.1; NC_006840.2.
DR RefSeq; YP_204271.1; NC_006840.2.
DR PDB; 5XI0; X-ray; 2.09 A; A/B=1-400.
DR PDBsum; 5XI0; -.
DR AlphaFoldDB; Q5E6G3; -.
DR SMR; Q5E6G3; -.
DR STRING; 312309.VF_0888; -.
DR PRIDE; Q5E6G3; -.
DR EnsemblBacteria; AAW85383; AAW85383; VF_0888.
DR KEGG; vfi:VF_0888; -.
DR PATRIC; fig|312309.11.peg.884; -.
DR eggNOG; COG3007; Bacteria.
DR HOGENOM; CLU_057698_1_0_6; -.
DR OMA; EGCIEQI; -.
DR OrthoDB; 678530at2; -.
DR BRENDA; 1.3.1.9; 71.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000537; Chromosome I.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01838; FabV_reductase; 1.
DR InterPro; IPR024906; Eno_Rdtase_FAD-bd_dom.
DR InterPro; IPR024910; Enoyl-CoA_Rdtase_cat_dom.
DR InterPro; IPR010758; Trans-2-enoyl-CoA_reductase.
DR PANTHER; PTHR37480; PTHR37480; 1.
DR Pfam; PF07055; Eno-Rase_FAD_bd; 1.
DR Pfam; PF12242; Eno-Rase_NADH_b; 1.
DR Pfam; PF12241; Enoyl_reductase; 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..400
FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH]"
FT /id="PRO_1000070503"
FT ACT_SITE 235
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 48..53
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 74..75
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 111..112
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 139..140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 244
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 273..275
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT SITE 75
FT /note="Plays an important role in discriminating NADH
FT against NADPH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT HELIX 17..34
FT /evidence="ECO:0007829|PDB:5XI0"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:5XI0"
FT HELIX 52..63
FT /evidence="ECO:0007829|PDB:5XI0"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:5XI0"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:5XI0"
FT HELIX 86..100
FT /evidence="ECO:0007829|PDB:5XI0"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:5XI0"
FT HELIX 115..126
FT /evidence="ECO:0007829|PDB:5XI0"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:5XI0"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:5XI0"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:5XI0"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:5XI0"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:5XI0"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:5XI0"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:5XI0"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:5XI0"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:5XI0"
FT HELIX 186..196
FT /evidence="ECO:0007829|PDB:5XI0"
FT HELIX 199..209
FT /evidence="ECO:0007829|PDB:5XI0"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:5XI0"
FT STRAND 214..224
FT /evidence="ECO:0007829|PDB:5XI0"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:5XI0"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:5XI0"
FT HELIX 239..259
FT /evidence="ECO:0007829|PDB:5XI0"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:5XI0"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:5XI0"
FT TURN 276..279
FT /evidence="ECO:0007829|PDB:5XI0"
FT HELIX 283..297
FT /evidence="ECO:0007829|PDB:5XI0"
FT HELIX 304..314
FT /evidence="ECO:0007829|PDB:5XI0"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:5XI0"
FT TURN 336..339
FT /evidence="ECO:0007829|PDB:5XI0"
FT HELIX 341..350
FT /evidence="ECO:0007829|PDB:5XI0"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:5XI0"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:5XI0"
FT HELIX 359..362
FT /evidence="ECO:0007829|PDB:5XI0"
FT HELIX 365..375
FT /evidence="ECO:0007829|PDB:5XI0"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:5XI0"
SQ SEQUENCE 400 AA; 43774 MW; CA4E0787B029DD66 CRC64;
MIIKPRIRGF ICTTTHPVGC EQNVKEQIAL TKAQGPIANA PKRVLVVGSS SGYGLSSRIT
AAFGGGASTI GVFFEKAGTE KKPGTAGWYN SAAFDKFAKE EGLYSKSLNG DAFSNEAKQK
TIDLIKEDLG QIDMVVYSLA SPVRKMPETG EVIRSSLKPI GETYTATAVD TNKDAIIEAS
VEPATEQEIK DTVTVMGGED WELWINALSE AGVLADGCKT VAYSYIGTEL TWPIYWDGAL
GQAKMDLDRA ATALNEKLSA TGGTANVAVL KSVVTQASSA IPVMPLYIAM VFKKMREEGV
HEGCQEQILR MFSQRLYKAD GSAAEVDEKN RLRLDDWELR EDIQQHCRDL WPQVTTENLK
DLTDYVEYKE EFLKLFGFGV DGVDYDADVN PEVNFDVADI
