FABV2_PHOPR
ID FABV2_PHOPR Reviewed; 400 AA.
AC Q6LP67;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] 2 {ECO:0000255|HAMAP-Rule:MF_01838};
DE Short=ENR 2 {ECO:0000255|HAMAP-Rule:MF_01838};
DE EC=1.3.1.9 {ECO:0000255|HAMAP-Rule:MF_01838};
GN Name=fabV2 {ECO:0000255|HAMAP-Rule:MF_01838}; OrderedLocusNames=PBPRA2527;
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=CAG20909.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR378671; CAG20909.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041394789.1; NC_006370.1.
DR AlphaFoldDB; Q6LP67; -.
DR SMR; Q6LP67; -.
DR STRING; 298386.PBPRA2527; -.
DR EnsemblBacteria; CAG20909; CAG20909; PBPRA2527.
DR KEGG; ppr:PBPRA2527; -.
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; IPR036291; NAD(P)-bd_dom_sf.
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.
DR SUPFAM; SSF51735; SSF51735; 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] 2"
FT /id="PRO_0000220044"
FT ACT_SITE 237
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 75..76
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 112..113
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 141..142
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 246
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 275..277
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT SITE 76
FT /note="Plays an important role in discriminating NADH
FT against NADPH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
SQ SEQUENCE 400 AA; 43771 MW; 7795E533A263014E CRC64;
MIIEPVVKGV VARSAHPFGC QQAVRNQINY VRTADPVTDG PKKVLVLGAS SGFGLASRIS
LAFGGSKADT IGISFERGPS EKGVGTAGWY NNIFFREEAE NAGLIGKNFI GDAFTPQMRQ
QVIDYIKTEF GGQLDLVVYS LATGVRPNPE TGELWRSSIK TMGEPVTGPT INIETDTMEQ
MTIGTATPAE IEDTEKVMGG EDWASWIDTL SEAGVLATGC KTVAYSYVGP KATYSIYHQG
TLGRAKAHLH ATADQLNDKM SEMGGEAYVS VCKALVTKAS VFIPAFSPYI LALFKVMKDK
GVHEGCIEQM QRLYSQRLYG KNKIVPVDDS RLIRVDDWEL EEDIQQQVSE LMVKITPENF
TTMGDYQGYK ADFMQLNGFG LEGVDYQADI DFETLTQLVA
