ID A0A135V9I4_9PEZI Unreviewed; 1224 AA.
AC A0A135V9I4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Zn(2)-C6 fungal-type domain-containing protein {ECO:0000259|PROSITE:PS00463};
GN ORFNames=CSAL01_09506 {ECO:0000313|EMBL:KXH69272.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH69272.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH69272.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH69272.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-
CC methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate
CC + thiamine phosphate; Xref=Rhea:RHEA:47848, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, ChEBI:CHEBI:37575,
CC ChEBI:CHEBI:57841, ChEBI:CHEBI:62890; EC=2.5.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000876};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl
CC phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2
CC H(+) = CO2 + diphosphate + thiamine phosphate; Xref=Rhea:RHEA:47844,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, ChEBI:CHEBI:62899; EC=2.5.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00001829};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 4-methyl-
CC 5-(2-phosphooxyethyl)-thiazole + H(+) = diphosphate + thiamine
CC phosphate; Xref=Rhea:RHEA:22328, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, ChEBI:CHEBI:57841,
CC ChEBI:CHEBI:58296; EC=2.5.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00001159};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-
CC phosphooxyethyl)-thiazole + ADP + H(+); Xref=Rhea:RHEA:24212,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17957, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58296, ChEBI:CHEBI:456216; EC=2.7.1.50;
CC Evidence={ECO:0000256|ARBA:ARBA00001771};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-
CC methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-
CC methylthiazole: step 1/1. {ECO:0000256|ARBA:ARBA00004868}.
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine
CC and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005165}.
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:KXH69272.1}.
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DR EMBL; JFFI01000138; KXH69272.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135V9I4; -.
DR STRING; 1209931.A0A135V9I4; -.
DR OrthoDB; 2784451at2759; -.
DR UniPathway; UPA00060; UER00139.
DR Proteomes; UP000070121; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd12148; fungal_TF_MHR; 1.
DR CDD; cd01170; THZ_kinase; 1.
DR CDD; cd00564; TMP_TenI; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 1.
DR HAMAP; MF_00228; Thz_kinase; 1.
DR HAMAP; MF_00097; TMP_synthase; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000417; Hyethyz_kinase.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR036206; ThiamineP_synth_sf.
DR InterPro; IPR022998; ThiamineP_synth_TenI.
DR InterPro; IPR034291; TMP_synthase.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR InterPro; IPR001138; Zn2Cys6_DnaBD.
DR NCBIfam; TIGR00693; thiE; 1.
DR NCBIfam; TIGR00694; thiM; 1.
DR PANTHER; PTHR20857:SF15; THIAMINE BIOSYNTHETIC BIFUNCTIONAL ENZYME; 1.
DR PANTHER; PTHR20857; THIAMINE-PHOSPHATE PYROPHOSPHORYLASE; 1.
DR Pfam; PF02110; HK; 1.
DR Pfam; PF02581; TMP-TENI; 1.
DR PRINTS; PR01099; HYETHTZKNASE.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
DR SUPFAM; SSF51391; Thiamin phosphate synthase; 1.
DR SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000070121};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 12..43
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000259|PROSITE:PS00463"
FT REGION 40..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1224 AA; 130123 MW; 58682873D0D3DF8A CRC64;
MDIDHRNKGP RACTTCAKAK ARCISGPDGS NKCERCHRLR KPCGSQTPAP PRAKKEPKPT
KVSELEKRLD ELTTQLSAGA TTQQQGSGSG GGVVDGVGGR NSNSSTAEVA TTVANGTVVG
SANSPLPPSG SIAPASAKIP INCDHLFPPE DVVVVGGEGG WSDTSPAPSA STADDHHTVG
SSQADTNGGA GAGTGTGPTT TDSPWPLNNE QSKVLKLFMD EMQELYPFVI VPPHMGPTQL
AAERPFLWKG IMMTACHLDA TKQVLLGEEL LQDIVQAAFM KPKKSLDVLQ GLQLLIAWYH
YNINSYQLTN LLFLARSMCV SLGFKDSPMQ LGERGGKGSG ICISFQKPES EARKVQTQEE
ISAQLELMRA FAGCYYLNTL VFTTNKRPDA FMNTTYLESC CRQIEEAAEY PSDALLVHLF
KIQQLAQTIS LTLGTESTSF QSLQLPLTMV VQSFQQQLDI FKTSLPAHLK DNVGLLAHIS
IAQVLLYEIG IPEARSPASF ISLTERLELL WGCCSAAKTF LEIRFPRNHL SVQPRFTCLS
SSDFLYVFIV CLKLMTLDQV PGWDLPLVQK HLDLGGVVES QVAHLEVFVA HRSGKFRRAA
ADAAAARGEE GMAAATDVPG PKVVDPFLRL TEMLRYFKDI VKGELCGLKS QPAIQEPIQL
PANLSDGTQA MIRDLDASFW TGVLGEDAGT WDVGNYSLYL VTDSTPAILG DRDLSSVVAA
AVRGGVTIVQ YRDKTSDTGE LVVNARKLHA VCRAAGVPLL INDRVDVALA VGCEGVHIGQ
DDMELTAARK ILGPDAIIGV TASTIEEALK ACEDGADYLG IGTVFATSTK ENTKHIIGTA
GLRTILTKLA AAGHLPRVKT VCIGGLNPSN IQRVLYQSAT PDSPSPAAID GVALVSAIVA
ARDPESASRS LLELVKTSPS YRSITSLSSS SSGSGASADV AQLLAQIPSV ITRVATTSPL
SHNMTNLVVQ NFAANVALAV GASPIMANYG EEAPDLARLG GSLVINMGTV TPDGIANYLK
ALAAYNAARR PVVFDPVGAG ATSIRRNAVK TILAGGYLDL IKGNEGEIAT VWGEGAMEQQ
KGVDSSSTLT PAQKARLVRD LARRERNVVL MTGKTDYLSD GNRTLAVDNG HELLGQITGT
GCVLGTTVSA MLAAWADEDK LLAVLAGLLH FEIAAEWAAV RADVQGPGTF VPAFIDELAR
VRRVTVEGDL TWLQGAKVEV VDVE
//
