ID   B8J0G1_DESDA            Unreviewed;      1465 AA.
AC   B8J0G1;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:ACL49238.1};
GN   OrderedLocusNames=Ddes_1336 {ECO:0000313|EMBL:ACL49238.1};
OS   Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=525146 {ECO:0000313|EMBL:ACL49238.1};
RN   [1] {ECO:0000313|EMBL:ACL49238.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27774 {ECO:0000313|EMBL:ACL49238.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Hazen T.C.;
RT   "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT   ATCC 27774.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001358; ACL49238.1; -; Genomic_DNA.
DR   STRING; 525146.Ddes_1336; -.
DR   KEGG; dds:Ddes_1336; -.
DR   eggNOG; COG3321; Bacteria.
DR   HOGENOM; CLU_000022_35_4_7; -.
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; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          5..420
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1357..1433
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1465 AA;  156146 MW;  EEA7FB7FAB26885A CRC64;
     MSDDSLKIAV IGMAGRFPGA DDIGTFWHNL KLGISGGKVL SQSDDGRVHY GFPLADADRF
     DADFFDVPAR EAKMLDPQHR LFLECAYSAF EHAGIAPRSP RQVTGVFGGC NFNGYALRFA
     NRILQANPLD LVDMLAANDK DYLAARVAYK LNLKGPALTV QCACSSSLAA VVTACQALLS
     GQCDVALAGG VGLKTSEGEG YSYEPEGPLS VDGHVRAYSD DASGVNEGEG VGAVVLKRLD
     DALRDGNVVY AVISGYAIGN DGADKTGFYA PSVTGQAAVI AEALAMSGVD PLEIGYVEGH
     GTGTPIGDPI EVAALVQAWQ LPDTAPRQYC RLGSVKTGLG HLNAAAGVAS LIKTVLALHH
     KIIPASLDFH APNPRLSLET TPFSIAGHTA DWEVAAGKTR KAAVNSLGIG GNNVHLILEE
     GPEPAVTTYS GAALITLSAK TKTALEKRAV ELGAWLRKHP TPLADVAHTL LRGRDMQAFR
     LSLVCEDAAA LSAMLESPGL LRKSARLDDP DKATPVAFLF PGFGSQHQGM AVNLRDTLPA
     FKQPFDRICA TFDKETGIDV LAAISSAEAL ADTETGTFAL FAVEYALARL LMDLGIMPSI
     VMGHSAGEYV AATIAGVFSE DDAVRLIVER SRLIGNSPEG GMLFVQMGHE DLRERLPGGV
     SIGAVIIPDG CVASGSIQGI EALHAALSAE NVPASKIAAD RAGHSSLLEG AKPHLRKVLE
     SVVLHRPRIR ILSNVTGALL SDSEATDPDY WVRQMCEPVL LSNEIFTLCD TEQAVMLEVG
     PSRKLSAMLR RHPAFRDRPP LIPIMPSEQG KTSETAALLE ALGLLWQGGG LADWERVDAL
     CGNGRTVALP GYPFERKRFW LEGQDKDTAG KSAPGKGQIS SLCWQQMLLP RQTAFNGLVG
     FIGNEGVGWA EALKKRGWST AVFQTLDALK RGVTIPDVLV DCRFGGEGAD CLDAAATVCR
     QAVELCSWLA ESAGGRDLSV YWPTAGAAAF GTEIPHIDKS ALLAPARVLP FEAKNTLGCV
     LDVEKGLSHE EMACILATAI THRLASTALT SLVAARSGAF WQETPMNIPL TGKAVSAMRL
     RQGAAYIVLG GSGGIGRTFM HELAAQADAQ QCRITLVPVQ RQPCPADFWE QVENDWAAVQ
     PCSVDLNDHE AFMKAVDIVL KQYKKIGGIV HASGVAGGGL MQAQSSRVQD TENWNTKVFP
     LLGIEKILQH RNVDFVVLNS SIGALCGSVG QLDNTVANTL LDAWSSRQQA QTGTRVLSLR
     WDVWRQVGMI NRMASLHERL SGEELKGGIT PDEAMRAFRA CFAAGVATPV VSGRNLFSML
     DESRARRGLA TDALESADLK VEGAASQRPA LAVQWKGARH VLDRVLIDLF ESRLGLTGIG
     IDDDYVELGG DSLMAMPLAK EIRELLNLSS FSVAQIFRRR NVASIADALT ESPEEKERLF
     ALAELLENIK GMTPGEVSKS LEALS
//