ID V9TUF4_9PROT Unreviewed; 407 AA.
AC V9TUF4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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:AHC73318.1};
GN ORFNames=P856_71 {ECO:0000313|EMBL:AHC73318.1};
OS Candidatus Endolissoclinum faulkneri L5.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Endolissoclinum.
OX NCBI_TaxID=1401328 {ECO:0000313|EMBL:AHC73318.1, ECO:0000313|Proteomes:UP000018700};
RN [1] {ECO:0000313|EMBL:AHC73318.1, ECO:0000313|Proteomes:UP000018700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=faulkneri L5 {ECO:0000313|Proteomes:UP000018700};
RX PubMed=24324632;
RA Kwan J.C., Schmidt E.W.;
RT "Bacterial endosymbiosis in a chordate host: long-term co-evolution and
RT conservation of secondary metabolism.";
RL PLoS ONE 8:E80822-E80822(2013).
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; CP006745; AHC73318.1; -; Genomic_DNA.
DR RefSeq; WP_025300204.1; NZ_CP006745.1.
DR AlphaFoldDB; V9TUF4; -.
DR STRING; 1401328.P856_71; -.
DR KEGG; efk:P856_71; -.
DR PATRIC; fig|1401328.3.peg.71; -.
DR eggNOG; COG0304; Bacteria.
DR HOGENOM; CLU_000022_69_2_5; -.
DR OrthoDB; 9808669at2; -.
DR Proteomes; UP000018700; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000018700};
KW Transferase {ECO:0000256|RuleBase:RU003694}.
FT DOMAIN 1..404
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 407 AA; 43313 MW; DAAE06B9C227F1B7 CRC64;
MRRVVVTGIG VISPIGNDKA EVVKSLKTGR SGITFAPEYK EIGFRSHVHG SLKINLDDRI
DRKLLRFMGD GVGYNYLAME EAIADSGLEN ADISNPRTGL VMGSGGPSTR NMMRAFDIAR
EKSPKRVGPY MVPRVMSSTN SANLSTIYKI NGLSYSISSA CSTSSHCIGN GVELIQYGKQ
DIILAGGGEE LHWTLSVLFD AMGALSSKYN DSPEKASRPY DTSRDGFVIA GGGGVVVLEE
FTHAKARGAN IYGEIIGYGA TSDGSDMVAP SGEGGLRAMQ LAMANVHDPV DYINTHGTST
PVGDMVELIS ISEAFRNQNK IPLISSTKSM TGHSQGAAGV HEAIYTLLMM NGNFIAPSIN
IEAIEPEAEA MPIVREPILG QHVNIALSNS FGFGGTNAVL AFRRGDV
//
