FABV_XANCP
ID FABV_XANCP Reviewed; 402 AA.
AC Q8PE66;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=XCC0115;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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; AE008922; AAM39434.1; -; Genomic_DNA.
DR RefSeq; NP_635510.1; NC_003902.1.
DR RefSeq; WP_011035373.1; NC_003902.1.
DR AlphaFoldDB; Q8PE66; -.
DR SMR; Q8PE66; -.
DR STRING; 340.xcc-b100_0124; -.
DR EnsemblBacteria; AAM39434; AAM39434; XCC0115.
DR KEGG; xcc:XCC0115; -.
DR PATRIC; fig|190485.4.peg.128; -.
DR eggNOG; COG3007; Bacteria.
DR HOGENOM; CLU_057698_1_0_6; -.
DR OMA; EGCIEQI; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IBA:GO_Central.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IBA:GO_Central.
DR GO; GO:0050343; F:trans-2-enoyl-CoA reductase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
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..402
FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH]"
FT /id="PRO_0000220060"
FT ACT_SITE 236
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 140..141
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 245
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 274..276
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 402 AA; 43959 MW; D977921F6A8133AF CRC64;
MIIHPKVRGF ICTTTHPLGC ERNVLDQIAA TRARGVRNDG PKKVLVIGAS SGYGLASRIT
AAFGFGADTL GVFFEKPGSD KKAGTAGWYN SAAFDTHAKA AGLYSKSING DAFSDEARAK
VIELIKTDMG GQVDLVVYSL ASPVRKLPST GEVKRSALKP IGNTYTATAI DTNKDTIIQA
SIEPATEQEI EDTITVMGGQ DWELWIDALD SAGVLAKGAR SVAFSYIGTE ITWPIYWHGA
LGKAKVDLDH TAQRLDARLQ ASGGGANVAV LKSVVTQASA AIPVMPLYIS MVYKIMKEKG
LHEGTIEQLD RLFRERLYRE DGQPAEVDEQ NRLRLDDWEL RDDVQDACKA LWPQVTTENL
FALTDYAGYK HEFLKLFGFE RKDVDYDADV DPDVKFDCIE LG
