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Database: UniProt
Entry: A0A3D9VD94_THECX
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ID   A0A3D9VD94_THECX        Unreviewed;       268 AA.
AC   A0A3D9VD94;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   08-OCT-2025, entry version 26.
DE   SubName: Full=Hydroxymethylpyrimidine kinase /phosphomethylpyrimidine kinase {ECO:0000313|EMBL:REF35271.1};
GN   ORFNames=DFJ64_0645 {ECO:0000313|EMBL:REF35271.1};
OS   Thermasporomyces composti.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Thermasporomyces.
OX   NCBI_TaxID=696763 {ECO:0000313|EMBL:REF35271.1, ECO:0000313|Proteomes:UP000256485};
RN   [1] {ECO:0000313|EMBL:REF35271.1, ECO:0000313|Proteomes:UP000256485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22891 {ECO:0000313|EMBL:REF35271.1,
RC   ECO:0000313|Proteomes:UP000256485};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine
CC       phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
CC       {ECO:0000256|ARBA:ARBA00003848}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ATP = 4-
CC         amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + ADP;
CC         Xref=Rhea:RHEA:19893, ChEBI:CHEBI:30616, ChEBI:CHEBI:57841,
CC         ChEBI:CHEBI:58354, ChEBI:CHEBI:456216; EC=2.7.4.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00000565};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-
CC         methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+);
CC         Xref=Rhea:RHEA:23096, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58354, ChEBI:CHEBI:456216;
CC         EC=2.7.1.49; Evidence={ECO:0000256|ARBA:ARBA00000151};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-
CC       amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-
CC       ribosyl)imidazole: step 3/3. {ECO:0000256|ARBA:ARBA00004769}.
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:REF35271.1}.
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DR   EMBL; QTUC01000001; REF35271.1; -; Genomic_DNA.
DR   RefSeq; WP_115849086.1; NZ_QTUC01000001.1.
DR   AlphaFoldDB; A0A3D9VD94; -.
DR   OrthoDB; 34166at2; -.
DR   UniPathway; UPA00060; UER00138.
DR   Proteomes; UP000256485; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC.
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; cd01169; HMPP_kinase; 1.
DR   FunFam; 3.40.1190.20:FF:000003; Phosphomethylpyrimidine kinase ThiD; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR   InterPro; IPR013749; PM/HMP-P_kinase-1.
DR   InterPro; IPR029056; Ribokinase-like.
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; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:REF35271.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000256485};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          13..261
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   268 AA;  28644 MW;  1117F8880ED62A03 CRC64;
     MNPPIALTIA TSDPSGGAGI QADLKTFSAL GAYGTAVLVA LTAQNTHGVT GVHVVPTAFI
     TQQLETLVAD VSVDAVKIGM LANAEVVNTV ADFLERHRPP SVVLDPVMVA TSGDRLLDAS
     AVRDLRDRLL PLADLVTPNL PEAAALLETE PAREDEEIIR QADALRELGV ARVLLKGGHR
     VESAESADYY VDGDVSRWLR APRVDTTHTH GTGCTLSSAI AALRPRRPDW LSAIEDAKRY
     VTQSLRAADA VKVGSGHGPV HHFHAWWR
//
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