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Database: UniProt
Entry: A0A150UXZ2_9PEZI
LinkDB: A0A150UXZ2_9PEZI
Original site: A0A150UXZ2_9PEZI 
ID   A0A150UXZ2_9PEZI        Unreviewed;       804 AA.
AC   A0A150UXZ2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Carbohydrate kinase PfkB domain-containing protein {ECO:0000259|Pfam:PF00294};
GN   ORFNames=M433DRAFT_112694 {ECO:0000313|EMBL:KYG43161.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG43161.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG43161.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG43161.1,
RC   ECO:0000313|Proteomes:UP000075602};
RX   PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA   Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA   Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA   Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT   "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT   Carbon Cycling in Acid Mine Drainage.";
RL   Front. Microbiol. 7:238-238(2016).
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:KYG43161.1}.
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DR   EMBL; JPDO01000351; KYG43161.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150UXZ2; -.
DR   STRING; 766039.A0A150UXZ2; -.
DR   Proteomes; UP000075602; Unassembled WGS sequence.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004730; F:pseudouridylate synthase activity; IEA:InterPro.
DR   CDD; cd01941; YeiC_kinase_like; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   Gene3D; 3.40.1790.10; Indigoidine synthase domain; 1.
DR   HAMAP; MF_01876; PsiMP_glycosidase; 1.
DR   InterPro; IPR022830; Indigdn_synthA-like.
DR   InterPro; IPR011611; PfkB_dom.
DR   InterPro; IPR007342; PsuG.
DR   InterPro; IPR029056; Ribokinase-like.
DR   PANTHER; PTHR42909:SF1; PFKB DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR42909; ZGC:136858; 1.
DR   Pfam; PF04227; Indigoidine_A; 1.
DR   Pfam; PF00294; PfkB; 1.
DR   SUPFAM; SSF110581; Indigoidine synthase A-like; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075602}.
FT   DOMAIN          431..625
FT                   /note="Carbohydrate kinase PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
SQ   SEQUENCE   804 AA;  87136 MW;  DABDD28BB447E930 CRC64;
     MSRFRWLWDC CQTKSIGTSP AYRSYINARS LSNNSRFFKI SEEVQQATAE NRPIVALEST
     IYTHGFPYPD NLSLATHLES LVRINGGVPA TIGILEGVAR VGLEAEELIR LLIRLVSFDE
     HSEKLKISRR DLGFACGLVG IDGKSFNGGT TVAATMILAS MAGIRVFATG GLGGVHRGVE
     ETMDISADLT ELGRTPVAVI SSGCKSFLDI PKTLEYLETQ GVPVATFADG RGGKIDFPAF
     YSRESCVRSP AVVRDEMDAA RVAHAHFSLG LQSGLHFANP IPVHHEIPFQ EMEKAIDCAL
     REARASGVTG AANTPYILAR LKEITGSKSI QSNRALIESN VVRGTRVAVA LKMLEMSHAT
     QTDRYREVST RKHDCIVKAT AGLRTQKASV STPNRPFAAS WPEIIIAGSL NVDVACDFRP
     KSMTEPQSPE LHTSNPATIT QSLGGVGHNV ASAAHFIGAN TRLFSAIGDD ITGRAAREMI
     EASGMDTSGI FVFPSSSGSR TSQYVAINDK NKDLMLAMAD VSILEQTGQD SILVQAFDEF
     WLPQLRRTKP RFMVIDANWA PSYLSRWLGE AKKIQAHVTF EPVSNTKSTR LFKLPKQQPL
     SVFPAPHVSL ATPNAHEITA MHNAAREAGY FERQDWWEVI DALGIPDSGA RTQLVMATNN
     ELVDRGIPQQ SIQLLPFIPS ICTKLGSQGV LLTQLLSAND PRLTNANYAP YILSRCANGT
     EETLGVGGIY MRLFPALENI KAEDVVSVNG VGDTFAGTLV AGLAKRGSSA RIEDLVDVAQ
     QAAILTLKDS RSVSPSLDTL QNLL
//
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