ID A0A3N4ULG0_9BURK Unreviewed; 247 AA.
AC A0A3N4ULG0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=EDC62_1318 {ECO:0000313|EMBL:RPE70828.1};
OS Tibeticola sediminis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Tibeticola.
OX NCBI_TaxID=1917811 {ECO:0000313|EMBL:RPE70828.1, ECO:0000313|Proteomes:UP000272193};
RN [1] {ECO:0000313|EMBL:RPE70828.1, ECO:0000313|Proteomes:UP000272193}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101684 {ECO:0000313|EMBL:RPE70828.1,
RC ECO:0000313|Proteomes:UP000272193};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (NOV-2018) 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|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:RPE70828.1}.
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DR EMBL; RKQL01000002; RPE70828.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4ULG0; -.
DR OrthoDB; 9803333at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000272193; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000272193}.
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-1"
FT BINDING 90
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT BINDING 155..159
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
SQ SEQUENCE 247 AA; 26226 MW; 409E7978FCEDF50B CRC64;
MKRLENKVSI ITGAAQGIGL ATALKFAQEG ARVVVCDVRQ DAVDAAVAQC QATGAEALGF
VMDVTQRAMV DAVVTQVLER MGRIDVLVNN AGITQDARLQ KMTIEQFDRV IDVNLRGVFH
CAQAVADTMV NQGSGAILNA SSVVGIYGNF GQTNYAASKF GVIGFTKTWS RELGPKGVRV
NAVAPGFVQT PILGTIPDKV IAEMEHRVPL RRLGQPEEIA NVYAFLASDE ASYINGAVIE
VSGGMTV
//
