GenomeNet

Database: UniProt
Entry: D8JPN7_HYPDA
LinkDB: D8JPN7_HYPDA
Original site: D8JPN7_HYPDA 
ID   D8JPN7_HYPDA            Unreviewed;       283 AA.
AC   D8JPN7;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 76.
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=Hden_1970 {ECO:0000313|EMBL:ADJ23771.1};
OS   Hyphomicrobium denitrificans (strain ATCC 51888 / DSM 1869 / NCIMB 11706 /
OS   TK 0415).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Hyphomicrobiaceae; Hyphomicrobium.
OX   NCBI_TaxID=582899 {ECO:0000313|EMBL:ADJ23771.1, ECO:0000313|Proteomes:UP000002033};
RN   [1] {ECO:0000313|Proteomes:UP000002033}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51888 / DSM 1869 / NCIB 11706 / TK 0415
RC   {ECO:0000313|Proteomes:UP000002033};
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}.
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; CP002083; ADJ23771.1; -; Genomic_DNA.
DR   RefSeq; WP_013215930.1; NC_014313.1.
DR   AlphaFoldDB; D8JPN7; -.
DR   STRING; 582899.Hden_1970; -.
DR   KEGG; hdn:Hden_1970; -.
DR   eggNOG; COG0623; Bacteria.
DR   HOGENOM; CLU_010194_10_1_5; -.
DR   OrthoDB; 9803628at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000002033; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002033}.
FT   ACT_SITE        157
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000094-1"
FT   ACT_SITE        167
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000094-1"
FT   BINDING         25
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT   BINDING         31..32
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT   BINDING         52
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT   BINDING         76..77
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT   BINDING         104
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT   BINDING         174
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
FT   BINDING         203..207
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000094-3"
SQ   SEQUENCE   283 AA;  30315 MW;  47BF6727A7F9E3BB CRC64;
     MAGSQANTSA AAGQLMAGKR GLVMGVANNR SIAWGIAKAC ASQGAEIALT YQGDALKKRV
     EPLAADLGTK LVLPCDVTDA SSIDAVFETL KKEWGELDFL VHAIAFSDKN ELDGRYVDTT
     EKNFTQSMLI SCFSFTALAQ RAEKLMPNGG SLLTLTYYGA EKVMPHYNVM GVAKAALEAS
     VRYLAADLGR NNIRVNAISA GPIKTLAAAG IADFRYILRW NEYNSALRRN VSIEDVGGAG
     LYLLSDMSRG VTGEVHHVDS GYHIQGMKNE DAPDISVVKS DET
//
DBGET integrated database retrieval system