ID D5VQ05_CAUST Unreviewed; 271 AA.
AC D5VQ05;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000256|PIRNR:PIRNR000094};
DE EC=1.3.1.9 {ECO:0000256|PIRNR:PIRNR000094};
GN OrderedLocusNames=Cseg_4168 {ECO:0000313|EMBL:ADG12578.1};
OS Caulobacter segnis (strain ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 /
OS LMG 17158 / TK0059) (Mycoplana segnis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=509190 {ECO:0000313|EMBL:ADG12578.1, ECO:0000313|Proteomes:UP000002629};
RN [1] {ECO:0000313|Proteomes:UP000002629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 / LMG 17158 /
RC TK0059 {ECO:0000313|Proteomes:UP000002629};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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:0000256|ARBA:ARBA00000175,
CC ECO:0000256|PIRNR:PIRNR000094};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. FabI subfamily. {ECO:0000256|ARBA:ARBA00009233,
CC ECO:0000256|PIRNR:PIRNR000094}.
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DR EMBL; CP002008; ADG12578.1; -; Genomic_DNA.
DR AlphaFoldDB; D5VQ05; -.
DR STRING; 509190.Cseg_4168; -.
DR KEGG; cse:Cseg_4168; -.
DR eggNOG; COG0623; Bacteria.
DR HOGENOM; CLU_010194_10_1_5; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000002629; Chromosome.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05372; ENR_SDR; 1.
DR Gene3D; 1.10.8.400; Enoyl acyl carrier protein reductase; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43159; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE; 1.
DR PANTHER; PTHR43159:SF2; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH] FABI; 1.
DR Pfam; PF13561; adh_short_C2; 1.
DR PIRSF; PIRSF000094; Enoyl-ACP_rdct; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|PIRNR:PIRNR000094};
KW Fatty acid metabolism {ECO:0000256|PIRNR:PIRNR000094};
KW Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR000094};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR000094};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000094};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000094}.
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-1"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-1"
FT BINDING 22
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT BINDING 28..29
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT BINDING 49
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT BINDING 73..74
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT BINDING 101
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-2"
FT BINDING 172
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
SQ SEQUENCE 271 AA; 28757 MW; D46A384E0883549D CRC64;
MADDYAFPKG ELMRGKKGLV MGVANHNSIA WGIASQLAAQ GAEMAFTYQG EELERRVRPL
AESIGVKTMI PADVTDDASM DAAFATIEKE FGTLDFVVHS VAFANKNELK GSFVDNTTRE
GFLMAMNISA FSFVDVAKRA SKLMPNGGSL ITMTYLGSER TIPNYNTMGV AKAALEASTR
YIARDLGPKG IRANAISAGA MRTLALAGIS GGRSMIAQGR AFSAMKEDTS MEGVAGCALW
LASDLGKSTT GEVVHVDAGF HMMGMPDQEE A
//
