ID J6J753_9RHOB Unreviewed; 410 AA.
AC J6J753;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 2 {ECO:0000256|ARBA:ARBA00014657, ECO:0000256|PIRNR:PIRNR000447};
DE EC=2.3.1.179 {ECO:0000256|ARBA:ARBA00012356, ECO:0000256|PIRNR:PIRNR000447};
GN ORFNames=A33M_2666 {ECO:0000313|EMBL:EJW11885.1};
OS Rhodovulum sp. PH10.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=1187851 {ECO:0000313|EMBL:EJW11885.1, ECO:0000313|Proteomes:UP000002930};
RN [1] {ECO:0000313|EMBL:EJW11885.1, ECO:0000313|Proteomes:UP000002930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PH10 {ECO:0000313|EMBL:EJW11885.1,
RC ECO:0000313|Proteomes:UP000002930};
RX PubMed=23105089; DOI=10.1128/JB.01695-12;
RA Khatri I., Nupur, Korpole S., Subramanian S., Pinnaka A.K.;
RT "Draft Genome Sequence of Rhodovulum sp. Strain PH10, a Phototrophic
RT Alphaproteobacterium Isolated from a Soil Sample of Mangrove of Namkhana,
RT India.";
RL J. Bacteriol. 194:6363-6363(2012).
CC -!- FUNCTION: Involved in the type II fatty acid elongation cycle.
CC Catalyzes the elongation of a wide range of acyl-ACP by the addition of
CC two carbons from malonyl-ACP to an acyl acceptor. Can efficiently
CC catalyze the conversion of palmitoleoyl-ACP (cis-hexadec-9-enoyl-ACP)
CC to cis-vaccenoyl-ACP (cis-octadec-11-enoyl-ACP), an essential step in
CC the thermal regulation of fatty acid composition.
CC {ECO:0000256|PIRNR:PIRNR000447}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(11Z)-
CC octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:55040,
CC Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:10800,
CC Rhea:RHEA-COMP:14074, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:83989,
CC ChEBI:CHEBI:138538; EC=2.3.1.179;
CC Evidence={ECO:0000256|PIRNR:PIRNR000447};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC Evidence={ECO:0000256|PIRNR:PIRNR000447};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194, ECO:0000256|PIRNR:PIRNR000447}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|ARBA:ARBA00008467,
CC ECO:0000256|PIRNR:PIRNR000447, ECO:0000256|RuleBase:RU003694}.
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:EJW11885.1}.
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DR EMBL; AKZI01000045; EJW11885.1; -; Genomic_DNA.
DR AlphaFoldDB; J6J753; -.
DR STRING; 1187851.A33M_2666; -.
DR PATRIC; fig|1187851.3.peg.1862; -.
DR eggNOG; COG0304; Bacteria.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000002930; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00834; KAS_I_II; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR017568; 3-oxoacyl-ACP_synth-2.
DR InterPro; IPR000794; Beta-ketoacyl_synthase.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR03150; fabF; 1.
DR PANTHER; PTHR11712:SF321; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE 2; 1.
DR PANTHER; PTHR11712; POLYKETIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR PIRSF; PIRSF000447; KAS_II; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|PIRNR:PIRNR000447};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW ECO:0000256|PIRNR:PIRNR000447};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|PIRNR:PIRNR000447};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000002930};
KW Transferase {ECO:0000256|PIRNR:PIRNR000447, ECO:0000256|RuleBase:RU003694}.
FT DOMAIN 1..407
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT ACT_SITE 159
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000447-1"
SQ SEQUENCE 410 AA; 42912 MW; 91F5145E5A97486B CRC64;
MTPLGCGVDT SWQRLLAGES GARKVEKFDV SDLPAKIACM VPRGDGSDGT FNADQWMEPK
EQRKVDDFIV YAMSAAGQAL ADSGWKPATY DEQIRTGVMI GSGIGGLEGI AETAIVLKER
GARRVSPFFI PGRLINLASG YVSIAHGLKG PNHAVVTACS TGAHAIGDAA RLVMLGDADV
MVAGGAESPI CRIALAGFSA CRALSTGFND EPTKASRPYD RDRDGFVMGE GAGVVVLEEL
EHARARGAKI YAELIGYGLT GDAYHITAPT EDGDGAYRCM TMAIKRAGIS AADIDYVNAH
GTSTPLGDEI ELSAVQRVIG NDAAHVSMSS TKSSTGHLLG AAGAVEAIFS ILAMRDGIAP
PTINLDNPSV DTPIDLVPHQ AKKRDIDIAL SNSFGFGGTN ASLVFRRTVQ
//