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Database: UniProt
Entry: A0A1Y5E1L0_9PROT
LinkDB: A0A1Y5E1L0_9PROT
Original site: A0A1Y5E1L0_9PROT 
ID   A0A1Y5E1L0_9PROT        Unreviewed;       246 AA.
AC   A0A1Y5E1L0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase {ECO:0000256|RuleBase:RU366074};
DE            EC=1.1.1.100 {ECO:0000256|RuleBase:RU366074};
GN   ORFNames=A9Q83_13930 {ECO:0000313|EMBL:OUR76663.1};
OS   Alphaproteobacteria bacterium 46_93_T64.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=1856292 {ECO:0000313|EMBL:OUR76663.1, ECO:0000313|Proteomes:UP000196525};
RN   [1] {ECO:0000313|Proteomes:UP000196525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hu P., Dubinsky E.A., Probst A.J., Wang J., Sieber C.M.K., Tom L.M.,
RA   Gardinali P., Banfield J.F., Atlas R.M., Andersen G.L.;
RT   "Simulation of Deepwater Horizon oil plume reveals substrate specialization
RT   within a complex community of hydrocarbon-degraders.";
RL   Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2017).
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|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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OUR76663.1}.
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DR   EMBL; MAAN01000031; OUR76663.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y5E1L0; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000196525; Unassembled WGS sequence.
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}.
FT   ACT_SITE        153
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611284-1"
FT   BINDING         38
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT   BINDING         88
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT   BINDING         153..157
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT   BINDING         186
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
SQ   SEQUENCE   246 AA;  25423 MW;  2EFFBC3B5E6ACE60 CRC64;
     MFDLSGKCAL VTGASGGLGA AIAKDLHAAG ATVAISGTRE DALKALADEI GGDRVHVVPC
     NLSDMEAVDN LIKDADAAMG QVDILVNNAG LTRDGLAMRM KDADWDVVMD VNLKAAFKLS
     RNSLRGMMKR RNGRIIGITS IVGVTGNPGQ MNYAASKAGM IGMSKSLGQE VAGRGITVNC
     VAPGFIATAM TDELTDDQKS KLLTNVPAGR LGDPKDISAA VLYLASDEAA YITGQTLHVN
     GGMAMI
//
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