GenomeNet

Database: UniProt
Entry: B5X0I3_STIAD
LinkDB: B5X0I3_STIAD
Original site: B5X0I3_STIAD 
ID   B5X0I3_STIAD            Unreviewed;      1837 AA.
AC   B5X0I3;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=CrpB-like protein {ECO:0000313|EMBL:ADO72614.1};
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:CAQ34920.1};
GN   Name=dkxI {ECO:0000313|EMBL:CAQ34920.1};
GN   OrderedLocusNames=STAUR_4836 {ECO:0000313|EMBL:ADO72614.1};
OS   Stigmatella aurantiaca (strain DW4/3-1).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Archangiaceae; Stigmatella.
OX   NCBI_TaxID=378806 {ECO:0000313|EMBL:CAQ34920.1};
RN   [1] {ECO:0000313|EMBL:CAQ34920.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Meiser P., Weissman K.J., Bode H.B., Krug D., Dickschat J.S., Sandmann A.,
RA   Bode H.B., Mueller R.;
RT   "DKxanthene Biosynthesis - Understanding the Basis for Diversity-Oriented
RT   Synthesis in Myxobacterial Secondary Metabolism.";
RL   Chem. Biol. 15:771-781(2008).
RN   [2] {ECO:0000313|EMBL:ADO72614.1, ECO:0000313|Proteomes:UP000001351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO72614.1,
RC   ECO:0000313|Proteomes:UP000001351};
RX   PubMed=21037205; DOI=10.1093/molbev/msq292;
RA   Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA   Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA   Sogaard-Andersen L.;
RT   "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL   Mol. Biol. Evol. 28:1083-1097(2011).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002271; ADO72614.1; -; Genomic_DNA.
DR   EMBL; BN001209; CAQ34920.1; -; Genomic_DNA.
DR   RefSeq; WP_013376467.1; NZ_AAMD01000058.1.
DR   STRING; 378806.STAUR_4836; -.
DR   KEGG; sur:STAUR_4836; -.
DR   eggNOG; COG1028; Bacteria.
DR   eggNOG; COG3321; Bacteria.
DR   HOGENOM; CLU_000022_31_5_7; -.
DR   OrthoDB; 5478077at2; -.
DR   Proteomes; UP000001351; Chromosome.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd08955; KR_2_FAS_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 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   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
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; IPR049490; C883_1060-like_KR_N.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
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; PF21394; Beta-ketacyl_N; 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; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 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; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
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   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          32..455
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1740..1816
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1837 AA;  199231 MW;  FEE43A08266002B9 CRC64;
     MAKLSTRLSE MPPVKLAYLA SQLRAKKEIL AAEPIAVIGM SCRFPGGGER PETFWEFLKG
     AGDATREVPR ERWDIDEIYD PTPGVRGKVY TRRGAFIEDV DLFDPGFFGI PPRDAKDMDP
     QQRLLHEECW RALERAGIPP AGLVGSRTGV FVGLMHNDYN VLGITSGVEM FAASLNYPSM
     AAGRIAHTLG FQGPALTVDT ACSSSAVCIH LACQSLRNDE SDLALAGGVS LSLSPITMMF
     GCENRMLSVD GRCKTFDASA DGFARGEGCG VVVLKRLSDA LAKGDPILGI IRGSAVNHDG
     RSSGLMVPNG RAQERVIRMA LDGCGVEPHQ ISYVEAHGTG TALGDPIEME AIRSVFGRKT
     TRSEPLLVGS VKTNIGHLEA AAGVSGLIKV ILSLQNEIIP AHLNFERPNP NIRWDDLPVI
     IPTSMRPWPR GEKRRIAGVS SFGFSGTNAH LIVEEAPLTA RPPLEKERPI HVLTMSAKTD
     ASLDALVEAH ERALPNDDAS LGDWCYTANV GRSHFEHRLA VSGATSASLR AGLARLRAEK
     LRPDREPRQG TESPKPVFLF TGQGALQPGV GRELYETQPA FRAALQRCSS VLESKLGLRL
     ENLLFGEEAP ALLEDTRNAQ PVLVALEYAL SELWASWGVI PGALVGHSLG EYAAAAVAGV
     MSIEDALGLS VERARLMSAA PGEGAMLAIS ASQEVTAQAI EPYPGVVSFA AINGPEDMVV
     SGGKSALEAL KGDLERRGIH CKFLRVPHAF HSPLMDPVLG PFAEVLKGVK LSVPHIPFVS
     TLEGRPVTDP LTQPEYWCRH LREPVHFAKG LGFLREQGHR TYLELGPAPI LAGIGRRLFP
     EAEELCWLPS LRPSEGETAQ MLSSLSALYV RGFEVDWAAF DAPFERRTRD LPTYPFQRDR
     YWIEAQNTGS LQYMTDRGTS KDAAHPLAGV ALSLAGSKET RFAARLSIRE PAFIAEHRIL
     GMTVLPAACY VEMALGAVYH ADSRERPIEL KAIELERPLV FTEAEGCDVQ TVLTPEEANS
     RFEIYAQGAG SERRWARLAQ GRVEEGSGWA GRIDLKAELF ERFPQQGSVV ALYELMDRSG
     LEYGPSFRAI HELRFGENGC LAHVRLPDSL IVGLDSYRLH PLILDACFQA VAAVFMEDDA
     QFKGERRQRM PVAIERLRWF KKAGSSVWVH VQRNSRSSTS AEVLSASLRI LGEDGEVIAE
     VDGLLLKQVD RNAFKASFAD STRELLFELA WREQRASQER DRVVSPPGHW LLFADSGSVA
     ERLKELVLQH SRTCVTVSPG AGYEKLGRDH YRLDPADPAG FDRLFQDLSA GGVAPATVAY
     LWGLDERGAA ELSAEELAGV TARSSAGALH LVQAMARVAW AQRPALWMVT RGAVAAVPSD
     GVGGLSQTPI WGLGRAAAIE HPELGCRLAD LDGDEGAPAR LFQLMAEPPE ENMMALRGSQ
     LLGARLVRPD KAVSRSSPVR IRSDGTYLLT GGMGALGLAT AEWLVEEGAR QLVLVGRGEP
     GEAVKARINA LTARGCHVTV TRADVSRREE VQRLVEGISA RESQLLGIFH IAGVLDDGVF
     MLQSRERIAQ VFVPKVLGAW NLHLATAQLP LDLFVMYSSA ASLVGVAGQA NYVAANSFLD
     ALAYHRSRQG LPALSVNWGR WSGEGMAAKT SAKGSTQGVD AGNLSPRRAL QILGDLLMLD
     VVQMGVVSFA VAAVDSALSP GHGPLFSELM MREQARSSSV ARMHELLGEL KSADSVRRRG
     LLTHYVQGRM APLLGFAPDH EVFQKKVSLN EMGLDSLRAV ELKNRIGREL GVDLPMARFI
     DGTNLEGIVE ALHSQLELNE LLARPPSAAV EIEELTL
//
DBGET integrated database retrieval system