ID C7LR78_DESBD Unreviewed; 387 AA.
AC C7LR78;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:ACU89224.1};
GN OrderedLocusNames=Dbac_1120 {ECO:0000313|EMBL:ACU89224.1};
OS Desulfomicrobium baculatum (strain DSM 4028 / VKM B-1378 / X)
OS (Desulfovibrio baculatus).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfomicrobiaceae; Desulfomicrobium.
OX NCBI_TaxID=525897 {ECO:0000313|EMBL:ACU89224.1, ECO:0000313|Proteomes:UP000002216};
RN [1] {ECO:0000313|EMBL:ACU89224.1, ECO:0000313|Proteomes:UP000002216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4028 / VKM B-1378 / X {ECO:0000313|Proteomes:UP000002216};
RX PubMed=21304634; DOI=10.4056/sigs.13134;
RA Copeland A., Spring S., Goker M., Schneider S., Lapidus A., Del Rio T.G.,
RA Tice H., Cheng J.F., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavrommatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.C., Meincke L.,
RA Sims D., Brettin T., Detter J.C., Han C., Chain P., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lucas S.;
RT "Complete genome sequence of Desulfomicrobium baculatum type strain (X).";
RL Stand. Genomic Sci. 1:29-37(2009).
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; CP001629; ACU89224.1; -; Genomic_DNA.
DR RefSeq; WP_015773322.1; NC_013173.1.
DR AlphaFoldDB; C7LR78; -.
DR STRING; 525897.Dbac_1120; -.
DR KEGG; dba:Dbac_1120; -.
DR eggNOG; COG0304; Bacteria.
DR HOGENOM; CLU_000022_69_2_7; -.
DR Proteomes; UP000002216; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000002216};
KW Transferase {ECO:0000256|RuleBase:RU003694}.
FT DOMAIN 1..385
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 387 AA; 40283 MW; DBA36AF59D664F39 CRC64;
MDNRRVVVTG SGFVLPLGSS REDVFSALQE PHGPFLRSST DSQVAICPVS DFDLKSHVGR
CKNARYLTRG QQLCLAAAVR AVDDAGLGPD DLAEAGLFLG LGPNLQARPR EDKALWLLDY
LPNTVTAVMA EMLGVHGENL TILTACAAST QALGQAFRAV KAGLADVALA GGGDSRLSPE
AVRAYKQAGV LATDFKRPEL ACRPFDQGRS GFAIGEGGAV FTLECLEHAQ ARGAGILAEI
VSASSSLDGG SLTGPDTTGQ AACTAVRRCL KDLGDENLCV VAHGTGTVLN DEVEGEILAR
TVPQAMGIAA FKSRIGHLAA ACGCAELALG LVCAGQGSFP PIAGLENPCR DDLPLLRAPL
RLRPRNLLVQ SFGFGGQNAC LGVRPWI
//
