ID F8N774_9BACT Unreviewed; 409 AA.
AC F8N774;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 41.
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 ORFNames=Premu_1992 {ECO:0000313|EMBL:EGN57390.1};
OS Hallella multisaccharivorax DSM 17128.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hallella.
OX NCBI_TaxID=688246 {ECO:0000313|EMBL:EGN57390.1, ECO:0000313|Proteomes:UP000002772};
RN [1] {ECO:0000313|Proteomes:UP000002772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17128 {ECO:0000313|Proteomes:UP000002772};
RX PubMed=22180809; DOI=10.4056/sigs.2164949;
RA Pati A., Gronow S., Lu M., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pagani I., Mavromatis K., Mikhailova N., Huntemann M., Chen A.,
RA Palaniappan K., Land M., Hauser L., Detter J.C., Brambilla E.M., Rohde M.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Ivanova N.;
RT "Non-contiguous finished genome sequence of the opportunistic oral pathogen
RT Prevotella multisaccharivorax type strain (PPPA20).";
RL Stand. Genomic Sci. 5:41-49(2011).
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; GL945017; EGN57390.1; -; Genomic_DNA.
DR RefSeq; WP_007574918.1; NZ_GL945017.1.
DR AlphaFoldDB; F8N774; -.
DR STRING; 688246.Premu_1992; -.
DR eggNOG; COG0304; Bacteria.
DR HOGENOM; CLU_000022_69_2_10; -.
DR OrthoDB; 9808669at2; -.
DR Proteomes; UP000002772; 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:EGN57390.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002772};
KW Transferase {ECO:0000256|RuleBase:RU003694, ECO:0000313|EMBL:EGN57390.1}.
FT DOMAIN 2..406
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 409 AA; 44361 MW; 76CD1CDCC51161FE CRC64;
MNRRVVLTGM GIWSCLGTSL DEVRDALYEG RSGVVFSQER KDAGFRSGLC TRVPQPDLKP
FVKRNQRHFM PEEAQYAYMA TKAALEYAGI DQEFIDDNEI GIIYGNDSTI EATMRAMDKF
REFNDTAACG SGALFQSMNS NITMNLACLF HLKGINLTTS AACASSSQAI GLGALLIGQG
LQDCVVCGGA EENNLWGMVS FDGIQAFSLR EDAPMKASRP FDRDRDGLVP GGGAATVVLE
DYEYAMRRGA HIIAEIAGWG FSGNGDHIST PNIIGPTRSL QRCLKCSGID DLRAIGYVNA
HATSTQAGDG PEALTIANVF GDYRVPVTST KSQTGHEMWM AGASELIYST LMMKNGFIAG
NINFENPDEN TAKINVIPET IERKFDMFVE NSFGFGGTNS TLLVKDFKG
//