ID A0A166CM73_9AGAM Unreviewed; 555 AA.
AC A0A166CM73;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Phosphomethylpyrimidine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FIBSPDRAFT_921540 {ECO:0000313|EMBL:KZP13804.1};
OS Fibularhizoctonia sp. CBS 109695.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP13804.1, ECO:0000313|Proteomes:UP000076532};
RN [1] {ECO:0000313|EMBL:KZP13804.1, ECO:0000313|Proteomes:UP000076532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP13804.1,
RC ECO:0000313|Proteomes:UP000076532};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV417627; KZP13804.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166CM73; -.
DR STRING; 436010.A0A166CM73; -.
DR OrthoDB; 5477821at2759; -.
DR Proteomes; UP000076532; Unassembled WGS sequence.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
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 NCBIfam; TIGR00097; HMP-P_kinase; 1.
DR PANTHER; PTHR20858:SF17; HYDROXYMETHYLPYRIMIDINE_PHOSPHOMETHYLPYRIMIDINE KINASE THI20-RELATED; 1.
DR PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 1.
DR Pfam; PF08543; Phos_pyr_kin; 2.
DR Pfam; PF03070; TENA_THI-4; 1.
DR SUPFAM; SSF48613; Heme oxygenase-like; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000076532}.
FT DOMAIN 17..199
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT DOMAIN 234..312
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT DOMAIN 341..553
FT /note="Thiaminase-2/PQQC"
FT /evidence="ECO:0000259|Pfam:PF03070"
SQ SEQUENCE 555 AA; 59918 MW; 6017713C6584039C CRC64;
MSPKTGPPAI LTIAGSDSGG GAGIQADLKT FTALECYGTT VITALTAQNT TGVQGIHPVP
PEFVKQQIES VLNDLDIRAI KTGMLFDADN TRAVASALRA RYPDLESAPP LVCDPVCVST
SGHTLLQPEA VEVLINEIFP LTSLVTPNKS EAELLLSHRD FPCKIENVED MLTAAGNLST
FVPKSILLKG GHLKTSMSEI QLVSLRHPNL SIVGDGMFGE NMEILKAAEG PISEKELVVD
LLYESADKIT MIIQPRIQST STHGTGCTLS AAIACGLGAG MTVVQAVQRA AKYTHLGIET
AVPIGGGCGP LNHLHGISPR IVPSRTSSNP NPLTRSLIQA TSKTWKEYVQ HDFVVQLGRG
TLAKQSFVHF IKQDYHYLKY YARAHGLLAA KSPSYASNES AAQIILDIAK ESRTHTSFCA
DWDVSRDELE ATPESLATMA YGSYLIDVGL QGDTAKLVMA VSACLFGYGE VGLWLKKEAA
KPNSWVVIEG NPYQKWIEDY SGPLYQAAVT KGIATIEAMA EADPPSETRL AEWQAVWEKC
TWLEKNFWDM AMNLS
//
