ID Q2YNI5_BRUA2 Unreviewed; 425 AA.
AC Q2YNI5;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Beta-ketoacyl synthase:ATP/GTP-binding site motif A (P-loop) {ECO:0000313|EMBL:CAJ10828.1};
DE EC=2.3.1.41 {ECO:0000313|EMBL:CAJ10828.1};
GN OrderedLocusNames=BAB1_0872 {ECO:0000313|EMBL:CAJ10828.1};
OS Brucella abortus (strain 2308).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391 {ECO:0000313|EMBL:CAJ10828.1, ECO:0000313|Proteomes:UP000002719};
RN [1] {ECO:0000313|EMBL:CAJ10828.1, ECO:0000313|Proteomes:UP000002719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308 {ECO:0000313|EMBL:CAJ10828.1,
RC ECO:0000313|Proteomes:UP000002719};
RX PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005;
RG Microbial Genomics Group;
RG Lawrence Livermore National Laboratory;
RG and the Genome Analysis Group;
RG Oak Ridge National Laboratory;
RA Chain P., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
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; AM040264; CAJ10828.1; -; Genomic_DNA.
DR RefSeq; WP_002963983.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YNI5; -.
DR SMR; Q2YNI5; -.
DR STRING; 359391.BAB1_0872; -.
DR GeneID; 3787554; -.
DR KEGG; bmf:BAB1_0872; -.
DR PATRIC; fig|359391.11.peg.3180; -.
DR HOGENOM; CLU_000022_69_2_5; -.
DR PhylomeDB; Q2YNI5; -.
DR Proteomes; UP000002719; Chromosome I.
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:SF336; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE, MITOCHONDRIAL; 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:CAJ10828.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002719};
KW Transferase {ECO:0000256|RuleBase:RU003694, ECO:0000313|EMBL:CAJ10828.1}.
FT DOMAIN 10..422
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 425 AA; 44271 MW; 7E4C45C0D97E1F5F CRC64;
MTKYTDHLGR PIVAISGAGV VSSLGQGKDD NWAALTGGKS GIHTITRFPT ENLNTRFSGT
VDFLPESESG ASALSEALAR LAGEEALAQS GLSVTAFGGP LFLAAPPVEL DWKSRFALDA
SVKDEGPASY QLLLEACRRA RHDALFNTTQ FGYIAERLSQ AFGTRGLPIT LSTACASGAT
AIQLGVEAIR RGESDRVLSI GTDGSVSAEA LIRFSLLSAL STQNDKPEKA SKPFSKDRDG
FAMAEGSGAL VMESLESAVA RGAKVLGILA GCGEKADDFH RTRSKPDASP AIGTVRAALA
DAGLTEDQIS YINAHGTSTP ENDKMEYLAL STVFGDKLGS IPVSSNKSMI GHTLTAAGAI
EAVFSLLTIQ TGTLPPTINY DNPDPAIPLD VVPNVKREAK VAAVLSNSFG FGGQNTSLVL
TPNPN
//
