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Database: UniProt
Entry: A0A0U4WTT7_9PSED
LinkDB: A0A0U4WTT7_9PSED
Original site: A0A0U4WTT7_9PSED 
ID   A0A0U4WTT7_9PSED        Unreviewed;       247 AA.
AC   A0A0U4WTT7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase {ECO:0000256|RuleBase:RU366074};
DE            EC=1.1.1.100 {ECO:0000256|RuleBase:RU366074};
GN   Name=fabG {ECO:0000313|EMBL:ALZ85597.1};
GN   ORFNames=APT59_15840 {ECO:0000313|EMBL:ALZ85597.1};
OS   Pseudomonas oryzihabitans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=47885 {ECO:0000313|EMBL:ALZ85597.1, ECO:0000313|Proteomes:UP000064137};
RN   [1] {ECO:0000313|EMBL:ALZ85597.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USDA-ARS-USMARC-56511 {ECO:0000313|EMBL:ALZ85597.1};
RA   Harhay G.P., Harhay D.M., Smith T.P.L., Bono J.L., Heaton M.P.,
RA   Clawson M.L., Chitko-Mckown C.G., Capik S.F., DeDonder K.D., Apley M.D.,
RA   Lubbers B.V., White B.J., Larson R.L.;
RT   "Annotation of Pseudomonas oryzihabitans USDA-ARS-USMARC-56511.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP
CC       substrates to beta-hydroxyacyl-ACP products, the first reductive step
CC       in the elongation cycle of fatty acid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00002607, ECO:0000256|RuleBase:RU366074}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC         + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC         COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC         Evidence={ECO:0000256|RuleBase:RU366074};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|RuleBase:RU366074}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU366074}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|RuleBase:RU366074}.
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DR   EMBL; CP013987; ALZ85597.1; -; Genomic_DNA.
DR   RefSeq; WP_059315736.1; NZ_CP013987.1.
DR   AlphaFoldDB; A0A0U4WTT7; -.
DR   KEGG; por:APT59_15840; -.
DR   OrthoDB; 9804774at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000064137; Chromosome.
DR   GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05333; BKR_SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR011284; 3oxo_ACP_reduc.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   NCBIfam; TIGR01830; 3oxo_ACP_reduc; 1.
DR   PANTHER; PTHR42879; 3-OXOACYL-(ACYL-CARRIER-PROTEIN) REDUCTASE; 1.
DR   PANTHER; PTHR42879:SF2; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] REDUCTASE FABG; 1.
DR   Pfam; PF13561; adh_short_C2; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Fatty acid biosynthesis {ECO:0000256|RuleBase:RU366074};
KW   Fatty acid metabolism {ECO:0000256|RuleBase:RU366074};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU366074};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU366074};
KW   NADP {ECO:0000256|PIRSR:PIRSR611284-2, ECO:0000256|RuleBase:RU366074};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU366074};
KW   Reference proteome {ECO:0000313|Proteomes:UP000064137}.
FT   ACT_SITE        154
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611284-1"
FT   BINDING         12..15
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT   BINDING         37
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT   BINDING         62..63
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT   BINDING         89
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT   BINDING         154..158
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT   BINDING         187
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
SQ   SEQUENCE   247 AA;  25479 MW;  4FB9E165835224EF CRC64;
     MSLQGKVALV TGATRGIGQA IALELGRLGA TVIGTATSEA GAQRIAESLK ANGIEGTGLV
     LNVSDNASVA TALEQVQAQF GAPSILVNNA GITRDNLMLR MKDDEWYDVI DTNLNSLFRL
     SKAVLKGMTK GRWGRIVSIG SVVGAMGNAG QANYAAAKAG LEGFTRALAR EVGSRNITVN
     AVAPGFIDTD MTRELPEAQR TALLTQIPAG RLGQADEIAK VVGFLAGEGA AYVTGATIPV
     NGGMYMS
//
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