ID A0A2C5WV75_9PEZI Unreviewed; 2309 AA.
AC A0A2C5WV75;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Highly reducing polyketide synthase azaB {ECO:0000313|EMBL:PHH49683.1};
GN Name=azaB {ECO:0000313|EMBL:PHH49683.1};
GN ORFNames=CFIMG_006861RA {ECO:0000313|EMBL:PHH49683.1};
OS Ceratocystis fimbriata CBS 114723.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX NCBI_TaxID=1035309 {ECO:0000313|EMBL:PHH49683.1, ECO:0000313|Proteomes:UP000222788};
RN [1] {ECO:0000313|EMBL:PHH49683.1, ECO:0000313|Proteomes:UP000222788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH49683.1,
RC ECO:0000313|Proteomes:UP000222788};
RX PubMed=23931120; DOI=10.1016/j.funbio.2013.06.004;
RA Simpson M.C., Wilken P.M., Coetzee M.P., Wingfield M.J., Wingfield B.D.;
RT "Analysis of microsatellite markers in the genome of the plant pathogen
RT Ceratocystis fimbriata.";
RL Fungal Biol. 117:545-555(2013).
RN [2] {ECO:0000313|EMBL:PHH49683.1, ECO:0000313|Proteomes:UP000222788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH49683.1,
RC ECO:0000313|Proteomes:UP000222788};
RX PubMed=24563841; DOI=10.5598/imafungus.2013.04.02.14;
RA Wilken P.M., Steenkamp E.T., Wingfield M.J., de Beer Z.W., Wingfield B.D.;
RT "IMA Genome-F 1: Ceratocystis fimbriata: Draft nuclear genome sequence for
RT the plant pathogen, Ceratocystis fimbriata.";
RL IMA Fungus 4:357-358(2013).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PHH49683.1}.
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DR EMBL; APWK03000177; PHH49683.1; -; Genomic_DNA.
DR STRING; 1035309.A0A2C5WV75; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000222788; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05274; KR_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; 3.90.180.10; 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 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; 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; 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 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; 1.
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; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000222788};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 22..474
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2224..2301
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2309 AA; 251170 MW; 5247A70820F5C2F9 CRC64;
MTHIPLSSPS LSESATAVAT HPENAVVVGM GCRFPGSATS PSRLWDMLCR RESGWSPIER
FNARGFYHPD PKRQGSIPVK GAHFLASDPA SFDASFFSVP AADARSMDPQ QRILLEVTYE
ALESAGITLD ELKGSRTSVF IASFVKDYEA ISLRDIDGQP DLAATGNGTA ILANRISYFF
DLKGPSVTID TACSGSLVAI DLAIQSLKSG SSDMAIVGGV NMMLIPDTMV PMSSMGFLSP
EGKCYTFDSR ANGYGRGEGA GIVILKRLSD AVSHNDPIRA EVVGHGVNQD GRTSGMFASS
CFSNPLSRPI FLFVWILTIS TGITMPNAAS QEMNIRDVYT RNDLCFSDTA YVECHGTGTI
VGDAMEMSAI SSGIRLRQPP GQSPLVIGSI KTNIGHLEGA AGVAGFIKSV LAVEHGKIPP
IINFENPRQD VNAGELGLQI PLETMDWPRS YRRRQASINS FGFGGTNAHA VVADVEYLSQ
KAQNPVFSRS TLTTKESPQP FVFSAHGASS LKKILSQFLA HLEEMPSAGQ EYLNDLAYTL
GCRRSRLETR IAISASSLEH LQSQLRAADE VDFTKVNSLP PKVCFVFAGQ GGVWAQMGQS
LRSFQAYRES IAAANTFIQK TYHCSFNIED LLAASAEEGS RVSNVDIAQI ITTTVQVACI
DLLASLGVEA TYVIGHSSGE IAAAYAAKKI TRQFAWSCAF LRGLWVRLLL TRDPDVEGGM
ISAGLSVEDA EAFLNELQLN RNRVVIACIN SPRSVTISGR ALEMSTVARE LSARKIFHRV
LQIPCGYHSP DMGKIEVDYV QSLYVHPQSE PFFSAAEIAS APAMYSTLLG QALDKAPLVH
RYWGMNLVHQ VQFQAGLEAM ATSFTNSTSS NQPLIFIEVG TAGVMRTPVL DSISAHFSGK
KTQPRYFSLL NMKQTSESAV IQRLGEMWSC GIDINMSKVI SRSSTLFAGQ LHCLVDLPSY
PWNHENKYWF ESHLTKSHLS RVWPRRDLVG ARSIDSTPFE MKWRGFHRLA ENPWMKDHKI
QGTVLYPAAG MIAMVIEAAS ELATESTSDI VSFEITNFSI HQAMVVPDDA HGLESTLSLK
LNNSLTEIKY TFDIFSQVSF GPVQRNASGI LTLVSASPEH GLFLNKQNAR LLESFSLCNQ
DGSTVELYET LESIGLQYGP TFRNITDIRR KGNCSYATLR VPDTKAVMPY AFEFEHVIHP
ATLDSMLHAL FSPDSQPMVP VGIEKIVISA SLRGGKAGSH FYGFGDLTSH GIRESTGDVV
MALGLADQPQ VVLNGIRLAA LQLPEGWLAP HRNLASEIVW KEDIATLNPR DSLPCAIEDV
LEALIFKSPC LSVLQIGWSV TQSPDLLLHL STRCRHLKLT AQGHISQPLD DEFLKRSNIQ
HKIVDTFDKQ TQLAKSYDLV IVCNQDGIDI ASLQARLSSH GVMLLTGSLA KVKACLQLNQ
PLVDFSRAFA VSCFGDDLTL IRSPQRTGAI SSPVAILVPQ DRSHDVISMA ANIRSLLLQS
GITTKVVVMP LENSFSIAGH QCISLCHLSR DTTVWEKKED IEEIRRLKKS ASAVLFVTQP
VLGNSMFGAQ ITGLVRTLIS EGSRVPLAVL KLSEEAELAS TCISSLVRDA ATQVFGELGV
CDVEFEERES RLLVPRLQLL SEVNSLIDPS LVQAVEADFF SADLQKQTVL KSRKMMSEAD
NLHWVQTSLP LPGPGEIVFR RFATLLSSAD VMQLKSRTSS SSFPFLGCDF FGADPSPPST
YVSRFEQGSS VVGLMLPQPF SSHVVTNPLL VRPLPKPLSY FSLSAYVAAV AALAGSHPVM
EALESFEPSS FVNGHNPGVG KSRYLFQVAD RDSASVALSR PRGTIHYEWD IKQLLEEDVL
FLSQMIDIVQ ALSYAGRLTL SYAGPIHEAS SIIEAVRQRE ASPNHGMVVA AFEPNHRVSL
TPRVEMPSLS SRITSDSFYV IAGAPRGLAG SIGRMLVNCG ARRLAFLSRS AGTSVEDKKL
VMELEALGAV VRVLAVDLTN CGHVAAIAST LMQLGGVKGV IQCAGVLQDC VFDSMTQDQW
DEVMKPKVQG TQNLVAAFTP ANTPLPALPW FLFLSSAAGV IGNRGQANYA AANTWQDAFA
LALRTHGICA TALAFGPVMG PGMIARNPEV MRALKANGFF GIRHDDFLRC VRIAVAAGDA
LPAHMAFGLG SGGLQRQMKT ADPYWLNTAI YRHLALVDVD IDNDMATEND ATQGTSKKAQ
LNLESVESVQ QAIVEALAER LEIAPSSIDV ERSMLAYGLD SFSGFWLRKW VEDNMGVEIL
VFEIIGDVTL AALAQNVVRR WQSLQETKG
//
