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Database: UniProt
Entry: A0A166XYY5_9HYPO
LinkDB: A0A166XYY5_9HYPO
Original site: A0A166XYY5_9HYPO 
ID   A0A166XYY5_9HYPO        Unreviewed;       521 AA.
AC   A0A166XYY5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Phosphomethylpyrimidine kinase type-1 {ECO:0000313|EMBL:OAA36348.1};
GN   ORFNames=BBO_08225 {ECO:0000313|EMBL:OAA36348.1};
OS   Beauveria brongniartii RCEF 3172.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC   Beauveria brongniartii.
OX   NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA36348.1, ECO:0000313|Proteomes:UP000076863};
RN   [1] {ECO:0000313|EMBL:OAA36348.1, ECO:0000313|Proteomes:UP000076863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA36348.1,
RC   ECO:0000313|Proteomes:UP000076863};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(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:OAA36348.1}.
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DR   EMBL; AZHA01000036; OAA36348.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166XYY5; -.
DR   OrthoDB; 5477821at2759; -.
DR   Proteomes; UP000076863; Unassembled WGS sequence.
DR   GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR   GO; GO:0050334; F:thiaminase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
DR   CDD; cd01169; HMPP_kinase; 1.
DR   CDD; cd19367; TenA_C_ScTHI20-like; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   Gene3D; 1.20.910.10; Heme oxygenase-like; 1.
DR   InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR   InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR   InterPro; IPR013749; PM/HMP-P_kinase-1.
DR   InterPro; IPR029056; Ribokinase-like.
DR   InterPro; IPR004305; Thiaminase-2/PQQC.
DR   InterPro; IPR027574; Thiaminase_II.
DR   NCBIfam; TIGR00097; HMP-P_kinase; 1.
DR   NCBIfam; TIGR04306; salvage_TenA; 1.
DR   PANTHER; PTHR20858:SF17; HYDROXYMETHYLPYRIMIDINE_PHOSPHOMETHYLPYRIMIDINE KINASE THI20-RELATED; 1.
DR   PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 1.
DR   Pfam; PF08543; Phos_pyr_kin; 1.
DR   Pfam; PF03070; TENA_THI-4; 1.
DR   SUPFAM; SSF48613; Heme oxygenase-like; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:OAA36348.1};
KW   Transferase {ECO:0000313|EMBL:OAA36348.1}.
FT   DOMAIN          13..288
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
FT   DOMAIN          311..517
FT                   /note="Thiaminase-2/PQQC"
FT                   /evidence="ECO:0000259|Pfam:PF03070"
SQ   SEQUENCE   521 AA;  56548 MW;  207D288127C60AA3 CRC64;
     MVQGRVLVVA GSDPSGGAGL EADQKVLAAH QCYAMTATTA LTVQNTKGVM GVHVVPAEFV
     GRQIDAVVED IGVDVVKTGM LGSVETIDVL SDMIEKHNLT TVVVDPVMIS TSGARLLPHE
     AIKHLSDRLL ARTTLLTPNV PEAKLLLAEN CIAEQRPNNN NNVGGVEELE ALAQTIRDRL
     GPRWVLVKGG HVPLRAADMT AAAGDEDKDA DKVVVDVLVG PEGEVVKVQS PFQPSTSTHG
     TGCSLASAIS AHLAKGQDVP TAVRAACRYV AAGIRTAPQL GGGNGPLNHF HSSYALPFSP
     GYFVEYLLER PDVRRMWKEF VQHPFVMALG NGTLPLDSFK GYIIQDYLFL VQFARANSLA
     AYKAKNIIDI QRSNEIVSHI VREMDLHINY CKGFGISEQE IQATPELQAC TAYTRYVLDI
     GQSEDLLALQ MALAPCLLGY GAVAQMLAAH PATVRDQQAN TYWPWIETYG AADYVEAVRL
     GSDLIEKKIR DCSPARIEEL VKIFIHGTRM EIGFWEMFPS K
//
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