ID A9IDA3_BORPD Unreviewed; 398 AA.
AC A9IDA3;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=3-oxoacyl-[acyl-carrier-protein] synthase II {ECO:0000313|EMBL:CAP44787.1};
DE EC=2.3.1.41 {ECO:0000313|EMBL:CAP44787.1};
GN OrderedLocusNames=Bpet4436 {ECO:0000313|EMBL:CAP44787.1};
OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP44787.1, ECO:0000313|Proteomes:UP000001225};
RN [1] {ECO:0000313|EMBL:CAP44787.1, ECO:0000313|Proteomes:UP000001225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC {ECO:0000313|Proteomes:UP000001225};
RX PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA Martinez-Arias R.;
RT "The missing link: Bordetella petrii is endowed with both the metabolic
RT versatility of environmental bacteria and virulence traits of pathogenic
RT Bordetellae.";
RL BMC Genomics 9:449-449(2008).
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; AM902716; CAP44787.1; -; Genomic_DNA.
DR AlphaFoldDB; A9IDA3; -.
DR STRING; 94624.Bpet4436; -.
DR KEGG; bpt:Bpet4436; -.
DR eggNOG; COG0304; Bacteria.
DR Proteomes; UP000001225; Chromosome.
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:SF320; BETA-KETOACYL SYNTHASE; 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; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:CAP44787.1};
KW Transferase {ECO:0000256|RuleBase:RU003694, ECO:0000313|EMBL:CAP44787.1}.
FT DOMAIN 1..397
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 398 AA; 40904 MW; 0718A024179A569E CRC64;
MKETFWLDAP GVICTLGADT ATVRARLAAG DMTGLRRHDG WLAGRDVTLA SVESALPEIP
ASLPAHLDSR NNRLLLAAAL QIEANLRATV ARHGGARVGI VLGTSTSGVN DNAPAFTHLA
HAGGWPNGHD YRRQALNAPA EFLAAWLGTS GPAYTISTAC TSSARALLSA RRLLQMDICD
AVICGGADSL CRLTINGFSA LEAISDAHCL PFSANRAGIN IGEAAVLFVM HRGGSGEVAL
LGGAGSSDAW HMSAPEPTGA GARQAMQAAL ADAKVLANEI GWVNLHGTGT ALNDAMESHA
MHSVFPTGVP CASTKGLTGH TLGTAGALEA ALAWLTLDGT SLGAPLPRHA WDGVPDPELP
PLDFCDGTQA YAAGRRRIAM SNSFAFGGNN TSLILAAS
//
