ID A0A165MV72_9AGAM Unreviewed; 562 AA.
AC A0A165MV72;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Phosphomethylpyrimidine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=NEOLEDRAFT_1079281 {ECO:0000313|EMBL:KZT18824.1};
OS Neolentinus lepideus HHB14362 ss-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Neolentinus.
OX NCBI_TaxID=1314782 {ECO:0000313|EMBL:KZT18824.1, ECO:0000313|Proteomes:UP000076761};
RN [1] {ECO:0000313|EMBL:KZT18824.1, ECO:0000313|Proteomes:UP000076761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB14362 ss-1 {ECO:0000313|EMBL:KZT18824.1,
RC ECO:0000313|Proteomes:UP000076761};
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; KV425660; KZT18824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165MV72; -.
DR STRING; 1314782.A0A165MV72; -.
DR InParanoid; A0A165MV72; -.
DR OrthoDB; 5477821at2759; -.
DR Proteomes; UP000076761; 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 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:UP000076761}.
FT DOMAIN 22..205
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT DOMAIN 244..319
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT DOMAIN 348..559
FT /note="Thiaminase-2/PQQC"
FT /evidence="ECO:0000259|Pfam:PF03070"
SQ SEQUENCE 562 AA; 60948 MW; 5E764CFFFE82F984 CRC64;
MFSAAHLYDG TPPAVMTIAG TDSSGGAGVQ ADLKAFTTLG CYGTSIITAM TAQNTTGVQN
VHPSPPEFVR QQLNSVLSDI KIQAIKTGML FDAGNTLAVA TGLKAHFGGP SLPTMPPLVC
DPVCVSTSGH TLLQSDAVKV MITDLFPITT LVTPNSQEAE LILSQDGQQI NINSLEDMVS
AAKKLRDLGP AAVLLKGGHI SITMKDVERA CSLNADIELV QDGLLEDNME ILQVAETDPS
TWQLAVDVLH QKNGVTTIFV RPRIDSTSTH GTGCTLSAAI ACALAKGHNI KDATRLGTTY
THTGIEMAFP VGSGYGPLNH MHSIILRSIP LPTPSIPHPF TRLLIQATSG IWKAYVEHDF
VRQLGEGTLP RECFIHFIKQ DYHYLKYYGR AYALLGAKSP SFPAIHASAQ TMLNVVTEVK
THASFCAQWG VSRKELEITP ESPATTAYGA FIMDTGLQGD RSKLVMALAA CLLGYGEVGL
WLRKEASKPN SWVKWEGNPY LKWMEDYSGE HYQNAVRTGL EAIEMEAVAD PPSRARFNEW
VRIWGRCTTL EKGFWDMAMG LL
//
