ID A0A0M6XN56_9RHOB Unreviewed; 410 AA.
AC A0A0M6XN56;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 1 {ECO:0000256|ARBA:ARBA00039450};
DE EC=2.3.1.41 {ECO:0000256|ARBA:ARBA00013191};
DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase I {ECO:0000256|ARBA:ARBA00041620};
DE AltName: Full=Beta-ketoacyl-ACP synthase I {ECO:0000256|ARBA:ARBA00042143};
GN Name=fabB {ECO:0000313|EMBL:CTQ31613.1};
GN ORFNames=JAN5088_00371 {ECO:0000313|EMBL:CTQ31613.1};
OS Jannaschia rubra.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=282197 {ECO:0000313|EMBL:CTQ31613.1, ECO:0000313|Proteomes:UP000048908};
RN [1] {ECO:0000313|EMBL:CTQ31613.1, ECO:0000313|Proteomes:UP000048908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5088 {ECO:0000313|EMBL:CTQ31613.1,
RC ECO:0000313|Proteomes:UP000048908};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3Z)-decenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(5Z)-
CC dodecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:54940, Rhea:RHEA-
CC COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9927, Rhea:RHEA-
CC COMP:14042, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78798, ChEBI:CHEBI:138410;
CC Evidence={ECO:0000256|ARBA:ARBA00035917};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54941;
CC Evidence={ECO:0000256|ARBA:ARBA00035917};
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 EC=2.3.1.41; Evidence={ECO:0000256|ARBA:ARBA00023389};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837;
CC Evidence={ECO:0000256|ARBA:ARBA00023389};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|ARBA:ARBA00008467,
CC ECO:0000256|RuleBase:RU003694}.
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DR EMBL; CXPG01000009; CTQ31613.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M6XN56; -.
DR STRING; 282197.SAMN04488517_10148; -.
DR Proteomes; UP000048908; 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:InterPro.
DR CDD; cd00834; KAS_I_II; 1.
DR Gene3D; 3.40.47.10; -; 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 PANTHER; PTHR11712:SF306; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE 1; 1.
DR PANTHER; PTHR11712; POLYKETIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 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:0000313|EMBL:CTQ31613.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000048908};
KW Transferase {ECO:0000256|RuleBase:RU003694, ECO:0000313|EMBL:CTQ31613.1}.
FT DOMAIN 2..407
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 410 AA; 43435 MW; E6A0A69D226C50D1 CRC64;
MLRRVVVTGI GIVSPIGNTP DEVEASLRAG KSGITFAPIY AEHGFRSQVH GVPDIVVEDH
IDKRDLRFMG PGAAYNFIAM ERAIADSGLE QNEVSNERTG LVMGSGGPST SNFFTAFDTV
INKGSPKRMG PFMVTRCMSS TNSACLATPF GIKGVNYSIT SACTTSLHCM GNGVEQIQFG
KQDIVFAGGG EEVDWTLSCL FDAMGAMSSK YNDTPEKASR PYDATRDGFV IAGGAGVVVL
EERERAIARG AKIYGEVTGY GATSDGADMV APSGEGGERA MRLALSQLPE DRRIDYVNSH
GTSTPVGDIK EIVALRNIFG EGKTPPVSST KSMTGHSLGA TGVQEAIYSM LMMNKGFIAP
SINVTELDPK LSPSEINTEL KDGVEIDSIL SNSFGFGGTN GTVIISKHRT
//
