ID H5T9X0_9ALTE Unreviewed; 245 AA.
AC H5T9X0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
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:GAB55097.1};
GN ORFNames=GPUN_0966 {ECO:0000313|EMBL:GAB55097.1};
OS Glaciecola punicea ACAM 611.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Glaciecola.
OX NCBI_TaxID=1121923 {ECO:0000313|EMBL:GAB55097.1, ECO:0000313|Proteomes:UP000053586};
RN [1] {ECO:0000313|EMBL:GAB55097.1, ECO:0000313|Proteomes:UP000053586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB55097.1,
RC ECO:0000313|Proteomes:UP000053586};
RX PubMed=22628500; DOI=10.1128/JB.00463-12;
RA Qin Q.-L., Xie B.-B., Shu Y.-L., Rong J.-C., Zhao D.-L., Zhang X.-Y.,
RA Chen X.-L., Zhou B.-C., Zhanga Y.-Z.;
RT "Genome sequence of proteorhodopsin-containing sea ice bacterium Glaciecola
RT punicea ACAM 611T.";
RL J. Bacteriol. 194:3267-3267(2012).
RN [2] {ECO:0000313|EMBL:GAB55097.1, ECO:0000313|Proteomes:UP000053586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB55097.1,
RC ECO:0000313|Proteomes:UP000053586};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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}.
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:GAB55097.1}.
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DR EMBL; BAET01000007; GAB55097.1; -; Genomic_DNA.
DR RefSeq; WP_006003859.1; NZ_BAET01000007.1.
DR AlphaFoldDB; H5T9X0; -.
DR STRING; 56804.BAE46_01400; -.
DR eggNOG; COG1028; Bacteria.
DR OrthoDB; 9804774at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000053586; 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 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 ECO:0000313|EMBL:GAB55097.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053586}.
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-1"
FT BINDING 13..16
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT BINDING 38
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT BINDING 60..61
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT BINDING 87
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT BINDING 152..156
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
FT BINDING 185
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR611284-2"
SQ SEQUENCE 245 AA; 25497 MW; 8706F5EDBAE8033B CRC64;
MFDLTGKVAL VTGASRGIGK ATAEQLASLG AIVIGTATSD CGADAISAYL GDSGTGMRLN
VTVDEEVSLV IADITAKYGG IDLLINNAGI TRDNLIMRMK EDEWNDILQT NLTSVFKLSK
AVMRGMMKKK NGRIVSIGSV VGSTGNAGQA NYAAAKAAVI GFSKSMAREI ASRGITVNVV
APGFIDTDMT RGLSDEQKTA IFKDIPANRL GDPKEIAATV AFLCSDAAAY ITGETIHVNG
GMHMS
//
