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Database: UniProt
Entry: A0A140LDK1_9CLOT
LinkDB: A0A140LDK1_9CLOT
Original site: A0A140LDK1_9CLOT 
ID   A0A140LDK1_9CLOT        Unreviewed;       265 AA.
AC   A0A140LDK1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase {ECO:0000256|ARBA:ARBA00019161};
DE            EC=2.7.1.49 {ECO:0000256|ARBA:ARBA00012135};
DE            EC=2.7.4.7 {ECO:0000256|ARBA:ARBA00012963};
DE   AltName: Full=Hydroxymethylpyrimidine kinase {ECO:0000256|ARBA:ARBA00042102};
DE   AltName: Full=Hydroxymethylpyrimidine phosphate kinase {ECO:0000256|ARBA:ARBA00043176};
GN   Name=thiD {ECO:0000313|EMBL:KXG78626.1};
GN   ORFNames=AN619_01520 {ECO:0000313|EMBL:KXG78626.1};
OS   Thermotalea metallivorans.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Thermotalea.
OX   NCBI_TaxID=520762 {ECO:0000313|EMBL:KXG78626.1, ECO:0000313|Proteomes:UP000070456};
RN   [1] {ECO:0000313|EMBL:KXG78626.1, ECO:0000313|Proteomes:UP000070456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B2-1 {ECO:0000313|EMBL:KXG78626.1,
RC   ECO:0000313|Proteomes:UP000070456};
RA   Patel B.K.;
RT   "Draft genome sequence of the thermoanaerobe Thermotalea metallivorans, an
RT   isolate from the runoff channel of the Great Artesian Basin, Australia.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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 2/3. {ECO:0000256|ARBA:ARBA00037917}.
CC   -!- SIMILARITY: Belongs to the ThiD family.
CC       {ECO:0000256|ARBA:ARBA00009879}.
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:KXG78626.1}.
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DR   EMBL; LOEE01000004; KXG78626.1; -; Genomic_DNA.
DR   RefSeq; WP_068554109.1; NZ_LOEE01000004.1.
DR   AlphaFoldDB; A0A140LDK1; -.
DR   STRING; 520762.AN619_01520; -.
DR   PATRIC; fig|520762.4.peg.178; -.
DR   OrthoDB; 9810880at2; -.
DR   Proteomes; UP000070456; Unassembled WGS sequence.
DR   GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008972; F:phosphomethylpyrimidine kinase 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   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   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KXG78626.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070456};
KW   Transferase {ECO:0000313|EMBL:KXG78626.1}.
FT   DOMAIN          11..254
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   265 AA;  28633 MW;  8F01155734E0E6A1 CRC64;
     MKKALTIAGS DSCGGAGIQA DLKTFSALGV YGMSVITAIT AQNTQGVMGV EEISPQMVGM
     QIDAVFQDIE VDAVKIGMVS NREIIKIIGD KLKAYNVQKA VVDTVMVSKS GCHLLRLEAK
     ETLIKQLIPR AFLVTPNLYE AEVLTGKKIK TIGDMEEAAR IIHAMGPLHV LVKGGHLEGK
     ATDVLYDGKT FTYCEEERIH TPNTHGTGCT FASAIAAHLA LGYDLREAVQ KSKTYITMAI
     AHALNIGKGV GPTHHFYQFY PERSI
//
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