FABV1_VIBCH
ID FABV1_VIBCH Reviewed; 401 AA.
AC Q9KRA3; Q9KRA4;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] 1 {ECO:0000303|PubMed:18032386};
DE Short=ENR 1 {ECO:0000303|PubMed:18032386};
DE EC=1.3.1.9 {ECO:0000269|PubMed:18032386};
DE AltName: Full=Trans-2-enoyl-CoA reductase [NADH] {ECO:0000303|PubMed:18032386};
DE Short=TER {ECO:0000303|PubMed:18032386};
DE EC=1.3.1.44 {ECO:0000269|PubMed:18032386};
GN Name=fabV {ECO:0000303|PubMed:18032386}; OrderedLocusNames=VC_1738/VC_1739;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=18032386; DOI=10.1074/jbc.m708171200;
RA Massengo-Tiasse R.P., Cronan J.E.;
RT "Vibrio cholerae FabV defines a new class of enoyl-acyl carrier protein
RT reductase.";
RL J. Biol. Chem. 283:1308-1316(2008).
CC -!- FUNCTION: Involved in the final reduction of the elongation cycle of
CC fatty acid synthesis (FAS II). Catalyzes the NADH-dependent reduction
CC of a carbon-carbon double bond in an enoyl moiety that is covalently
CC linked to an acyl carrier protein (ACP). It can use both crotonyl-CoA
CC and crotonyl-ACP. {ECO:0000269|PubMed:18032386}.
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:0000269|PubMed:18032386};
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; EC=1.3.1.44;
CC Evidence={ECO:0000269|PubMed:18032386};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-butenoyl-[ACP] + H(+) + NADH = butanoyl-[ACP] + NAD(+);
CC Xref=Rhea:RHEA:54868, Rhea:RHEA-COMP:9627, Rhea:RHEA-COMP:9628,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:78453, ChEBI:CHEBI:78454;
CC Evidence={ECO:0000269|PubMed:18032386};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54869;
CC Evidence={ECO:0000269|PubMed:18032386};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + NAD(+) = (2E)-butenoyl-CoA + H(+) + NADH;
CC Xref=Rhea:RHEA:52572, ChEBI:CHEBI:15378, ChEBI:CHEBI:57332,
CC ChEBI:CHEBI:57371, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:18032386};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:52574;
CC Evidence={ECO:0000269|PubMed:18032386};
CC -!- ACTIVITY REGULATION: Weakly inhibited by triclosan.
CC {ECO:0000269|PubMed:18032386}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=195 uM for crotonyl-ACP {ECO:0000269|PubMed:18032386};
CC KM=1178 uM for crotonyl-CoA {ECO:0000269|PubMed:18032386};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18032386}.
CC -!- SIMILARITY: Belongs to the TER reductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF94889.1; Type=Frameshift; 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; AE003852; AAF94888.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE003852; AAF94889.1; ALT_FRAME; Genomic_DNA.
DR PIR; B82164; B82164.
DR PIR; C82164; C82164.
DR RefSeq; WP_000584512.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KRA3; -.
DR SMR; Q9KRA3; -.
DR STRING; 243277.VC_1738; -.
DR SwissLipids; SLP:000001777; -.
DR PRIDE; Q9KRA3; -.
DR DNASU; 2613743; -.
DR EnsemblBacteria; AAF94888; AAF94888; VC_1738.
DR EnsemblBacteria; AAF94889; AAF94889; VC_1739.
DR GeneID; 57740386; -.
DR GeneID; 66939580; -.
DR KEGG; vch:VC_1738; -.
DR KEGG; vch:VC_1739; -.
DR eggNOG; COG3007; Bacteria.
DR HOGENOM; CLU_057698_0_0_6; -.
DR SABIO-RK; Q9KRA3; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IDA:UniProtKB.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0050343; F:trans-2-enoyl-CoA reductase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:UniProtKB.
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 Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..401
FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH] 1"
FT /id="PRO_0000220052"
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"
SQ SEQUENCE 401 AA; 44057 MW; B1809B5BA4771082 CRC64;
MIIKPKIRGF ICTTTHPVGC EANVKEQIAY TKAQGPIKNA PKRVLVVGSS SGYGLSSRIA
AAFGGGAATI GVFFEKPGTD KKPGTAGFYN AAAFDKLAHE AGLYAKSLNG DAFSNEAKQK
AIELIKQDLG QIDLVVYSLA SPVRKMPDTG ELVRSALKPI GETYTSTAVD TNKDVIIEAS
VEPATEQEIA DTVTVMGGQD WELWIQALEE AGVLAEGCKT VAYSYIGTEL TWPIYWDGAL
GRAKMDLDRA ATALNEKLAA KGGTANVAVL KSVVTQASSA IPVMPLYIAM VFKKMREQGV
HEGCMEQIYR MFSQRLYKED GSAPEVDDHN RLRLDDWELR DDIQQHCRDL WPQITTENLR
ELTDYDMYKE EFIKLFGFGI EGIDYDADVN PEVEFDVIDI E
