UniProt: B0XZV6

Database: UniProt
Entry: B0XZV6_ASPFC

LinkDB:  B0XZV6_ASPFC 
Original site:  B0XZV6_ASPFC

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Ontology (6)   
   GO (6)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (41)   
   InterPro (22)   
   Pfam (10)   
   PROSITE (3)   
   SMART (6)   
Literature (1)   
   PubMed (1)   
All databases (49)   

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ID   B0XZV6_ASPFC            Unreviewed;      2514 AA.
AC   B0XZV6;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   SubName: Full=Polyketide synthase, putative {ECO:0000313|EMBL:EDP52288.1};
GN   ORFNames=AFUB_034520 {ECO:0000313|EMBL:EDP52288.1};
OS   Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS   fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804 {ECO:0000313|EMBL:EDP52288.1, ECO:0000313|Proteomes:UP000001699};
RN   [1] {ECO:0000313|EMBL:EDP52288.1, ECO:0000313|Proteomes:UP000001699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163
RC   {ECO:0000313|Proteomes:UP000001699};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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DR   EMBL; DS499596; EDP52288.1; -; Genomic_DNA.
DR   EnsemblFungi; EDP52288; EDP52288; AFUB_034520.
DR   VEuPathDB; FungiDB:AFUB_034520; -.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   PhylomeDB; B0XZV6; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 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   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR011032; GroES-like_sf.
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; IPR020843; PKS_ER.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF28; SYNTHASE, PUTATIVE-RELATED; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 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; PF13489; Methyltransf_23; 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; SM00829; PKS_ER; 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; SSF50129; GroES-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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          66..486
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2427..2504
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2514 AA;  274729 MW;  BB252C01838A9B93 CRC64;
     MIRQVTDCEA STFYVEFTSM TMDESTGTNG HGVTMGSDTT NGATPNGVYA NGTNGTLAHG
     VLRGAQVPIA ICGMACRLPG GLTTPDELWD FLLAKKDARC RVPHSRYDID SYYSDTKKPG
     TVSTEYGYFL DESVDVGALD TSFFSMTRTE VERADPQQRL MLEVAREAFE DAGVTHWRGK
     TIGTYIGNFG EDWLEMFGKE TQPWGIHRIS GSGDFVVANR LSYEFDLQGP SMTIRTACSS
     ALVALNEACA AISRGDCGSA LVGGVNLILA PGMSMAMQEQ GVLSSDGSCK TFSADANGYA
     RGEAVTAIFI KPLADALRDG NPIRAVVRAT SHNADGKTPT LSQPSTDAQE ALMRRAYELG
     GITDYAETAM VECHGTGTPT GDPIEAAAVA RVFGDKGVYI GSVKPNLGHT EAASGLVSLL
     KMVKALEHRV IPPNIKFTSP NPNIPFAEGK LTVPTDPLPW PKDRLERVSV NSFGIGGANA
     HVILESAATY NVPVAVHETP ETPQLLLFTA NSSKSITRMI DGYKAWVEQN PDKVSDLAYT
     LARRREHLPH RAFAIFRNGV LESVSQPANS KAAKPPSVVM VFTGQGAQWP QMGRDLLRSN
     DVFRSSIRLL DQHLQTIAGE KPQYSIEEEL KKPAKKSRLS LAEFSQPLCT AVQIALVDTL
     ASAGIHPDAV VGHSSGEIAA AYAAGALSAG EAITAAHHRG AVTSRQKRVG TMAAIGMSWA
     ETEKYLVPNV TIACDNSPRS ITISGDVDAV KSVVAAIKEA QPQMLARLLQ VDKAYHSYHM
     KEIGEDYQSL INEEVVGREP SALFFSSVTG QVLGPDHSTW SKYWQENLES PVRFREAVTA
     ILKHDVGKNA VFLEVGPHGA LAGPLRQIFT QATSSAPYVS VMARNQDCNA SFLAAIGALH
     SLNVDVNLEA LFPTGCCLPD LPRYPWNHEG SYWYESRLSK EWRNRRFPYH DLLGARVAES
     SDGEPAWRNM FHVTNTPWMR DHEVGEHIVF PFCGYIALAG EAIRQLTNVE EGFSVRNIIV
     STALVLSEGK PTEMMATFRP HRLTNFLNSA WWEFTVSAYN GRNWTKHCTG EVCAQSSAPE
     QTQDPAGLPR TLNVRKWYEK MGKGGLNLGG SFQTLETMTT STSEQRAVGK VVNGRQGDEA
     NYHIHPTVLD ATLQILGAAA VKGYARKTKT WLPTSIDKFT VHRCASDMVT SVSAQLSSNF
     SVVGDGRCTS GGTTVVDAVG IRMSLADGAG AADISDTHAA SRCEWRPDID FLDVHELFRS
     PANRTDHLRL LEELGDICLL LSQWHFSEAS NPIPPHLQQY MAWVGSQSGA IAFRLPSTWT
     GLDHEAISDR IDSILSQLAD TPAAPVANAI HQVCVNMESL LSGESLDSIL PGETLTHVHE
     FLGQVDRREF IQLLSHSKPN LRILEIGTGN GVSLHRDILA ELTRPDGEIL CAKYTLTAPG
     YVVATTQEKI FPNMQFASLD ISQDPFEQGF EDVGYDLIIA VNALRECKNT EESLANLRKL
     LSSDGRLLLQ ELCPSSRWIR YVLGVLPTWW AGPADEPIET PYLSQEEWQT TIAAAGFGDI
     EAVALDSEEP HQVTTTMVVR QAREAPMKKV TVLVEEEGPA VTHIVSELEK EGYEVTRCRL
     EDDPPAGQDV MSLLDIEQPF FHGIDEARFL LFKSFLLGLQ DRNAGMLWTT HLIDIGCRDP
     RYGQVLGLAR TIRTEQLADL GTCQIDSFDS SASIRGLLRL FAKFQTRQGD EELNPDFEWA
     IVNGQVQVAR FHPFILADEL LVSEDSKNEM ATLNVRTPGR VNSLHYARHE RKDLEKDEVE
     VEVYCAGLNF RDILVALGIV ELPVRLFGIE AAGTVTRVGA DVSPDDLQVG DRVVCFCRKD
     AFSTYTTTLA AVCVRIPDSL TFDQAGTMLI PYFTAIHSMV NVGRVTKGQS VLIHSACGGV
     GLAAIQVAQM LEADVYVTVG SEEKVKYLME NYHIPRHKIF HSRDRSFVDG VMRETNGRGM
     DFILNSLSGE LLHATWSCVA EFGTLLEIGK RDLIGDGKLD MRPFLANRNY CCVDIDGLWK
     RIHVARALIF SILDFYDKGY ITPLPMTIFP ATQTQDAFRF MEKGQHIGRV GVSFKPADGG
     PQLGLETTKR ALTIAFNGSA SYLMVGGLGG IGRAVSTWMV DHGARELVYL SRSAGRTPKD
     DDFVTELQSM GCAVRLVSGD TTKLADVQRA IAAATYPLKG IVQMSMVVAN ENFTRMSFAE
     WTASTAPKVQ GTWNLHDASV AAGINLDFFV MFSSVSGIVG QAGQANYASG NSFLDAFAQY
     RNGLGLPASV VDMGAVEDVG WISEHQGMMG KMSRSGFKPV LEQEVIDAMA ISMLVHNQAR
     QAIADEALAA DSKATSYFVH KNTFLVGLAL LIPLHDPSNY VIWKKDRRMA SYHNNSTVAA
     ATAASTDVLK TYLSSAKADP SILKSPEAAK LFAVEIGKRL FDLLLKPHEE PNTSWPLLDL
     GLDSLVALEL RAWIKQVFSF DLPMLEMMSI GSLDILGQYA ANEVYRITTD NNEG
//

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