ID A0A1X6ZJ78_9RHOB Unreviewed; 409 AA.
AC A0A1X6ZJ78;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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:SLN51050.1};
GN ORFNames=ROA7450_02549 {ECO:0000313|EMBL:SLN51050.1};
OS Roseovarius albus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1247867 {ECO:0000313|EMBL:SLN51050.1, ECO:0000313|Proteomes:UP000193061};
RN [1] {ECO:0000313|EMBL:SLN51050.1, ECO:0000313|Proteomes:UP000193061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7450 {ECO:0000313|EMBL:SLN51050.1,
RC ECO:0000313|Proteomes:UP000193061};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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; FWFX01000007; SLN51050.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6ZJ78; -.
DR OrthoDB; 9808669at2; -.
DR Proteomes; UP000193061; 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; -; 1.
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:SLN51050.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193061};
KW Transferase {ECO:0000256|RuleBase:RU003694, ECO:0000313|EMBL:SLN51050.1}.
FT DOMAIN 1..406
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 409 AA; 42212 MW; F2EFA4C8305AF0C8 CRC64;
MRRVVVTGLG IVSSIGNNAE EVVASLKAGR SGITANESMA EHGFRSQIAG ALDIDVSEHI
DKRALRFMGP GAAYAHIAMG QAIADSGLSE DVISNPRTGL VAGSGGPSTS AMLTAHETVK
KTGATKRIGP FAVPKCMCST ISANLATAYK IKGINYSITS ACSTSLHCIG NAAEQIMMGK
QDVMFAGGGE ELDWTLSCLF DAMGAMSSKY NDTPAKASRA FDADRDGFVI SGGGGILILE
ELGHAKARGA KIYAEVTGYA ATSDGHDMVA PSGEGGERAM RLALSQLPEG RKVGYINAHG
TSTPVGDAGE VAAVRRIFGE GNVPPISSTK SMTGHAQGAA GALEAVFCLL ALRDDFIIPS
INVETLDPEL NAEEIATVRV DDAGLDTVMT NSFGFGGTNG SMLLSKYHG
//
