FABV1_PHOPR
ID FABV1_PHOPR Reviewed; 400 AA.
AC Q6LPG9;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] 1 {ECO:0000255|HAMAP-Rule:MF_01838};
DE Short=ENR 1 {ECO:0000255|HAMAP-Rule:MF_01838};
DE EC=1.3.1.9 {ECO:0000255|HAMAP-Rule:MF_01838};
GN Name=fabV1 {ECO:0000255|HAMAP-Rule:MF_01838}; OrderedLocusNames=PBPRA2423;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG20807.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR378671; CAG20807.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011219091.1; NC_006370.1.
DR AlphaFoldDB; Q6LPG9; -.
DR SMR; Q6LPG9; -.
DR STRING; 298386.PBPRA2423; -.
DR EnsemblBacteria; CAG20807; CAG20807; PBPRA2423.
DR KEGG; ppr:PBPRA2423; -.
DR eggNOG; COG3007; Bacteria.
DR HOGENOM; CLU_057698_1_0_6; -.
DR OrthoDB; 678530at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000593; Chromosome 1.
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 3: Inferred from homology;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..400
FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH] 1"
FT /id="PRO_0000220045"
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 400 AA; 44011 MW; 7CEBC27E68E3621D CRC64;
MIIKPKIRGF ICTTAHPVGC EENVKEQIAY TKAQGPIANA PKRVLVVGSS SGYGLSSRIA
AAFGGDAATI GVFFEKPSTE KKPGTAGWYN SAAFDKLAKE EGLYSKSLNG DAFSHEAKQK
TIDLIKADLG QIDMVVYSLA SPVRKMPETG EVVRSSLKPM GETYTATAVD TNKDVLIEAS
IEPATEQEIA DTVTVMGGQD WELWINALSE AGVLADGCKT VAYSYIGTEI TWPIYWHGAL
GKAKMDLDRA ASELNNKLSA TGGSANVAVL KSVVTQASSA IPVMPLYIAM VFKKMREEGV
HEGCMQQIYR MFTQRLYKAD GTAPEVDEEN RLRLDDWELR EDIQKHCRDL WSSVTNENLF
EVADYQEYKD EFIKLFGFGI DSIDYDIDVN TLIEFDVESI
