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Database: UniProt
Entry: A0A1H2SWJ0_9FIRM
LinkDB: A0A1H2SWJ0_9FIRM
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ID   A0A1H2SWJ0_9FIRM        Unreviewed;       283 AA.
AC   A0A1H2SWJ0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
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   ORFNames=SAMN05216391_10632 {ECO:0000313|EMBL:SDW35972.1};
OS   Lachnospiraceae bacterium KHCPX20.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1855375 {ECO:0000313|EMBL:SDW35972.1, ECO:0000313|Proteomes:UP000199590};
RN   [1] {ECO:0000313|EMBL:SDW35972.1, ECO:0000313|Proteomes:UP000199590}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KHCPX20 {ECO:0000313|EMBL:SDW35972.1,
RC   ECO:0000313|Proteomes:UP000199590};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNOC01000006; SDW35972.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2SWJ0; -.
DR   STRING; 1855375.SAMN05216391_10632; -.
DR   Proteomes; UP000199590; Unassembled WGS sequence.
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:0000313|EMBL:SDW35972.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199590};
KW   Transferase {ECO:0000313|EMBL:SDW35972.1}.
FT   DOMAIN          16..270
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   283 AA;  29916 MW;  9671240E5F213D9A CRC64;
     MTRTTKKVAL TIAGSDPSGG AGIAADLKTF MANGVYGCSV ITALTAQNTK EYWATQPVAG
     HMVTDQLLSV LTDIRPDAVK IGMLPNAGIM GEVAEVLGQE ELSPVVVDPV MVSTSGKALM
     ADNARKAFVQ KILPLCDLVT PNIPETVELL KLSGQEDMAE PFADEKEWMQ QAAKVLSEAF
     GINVLVKGGH GQTGASDYLY LCDEKKGKWF HGLYIDNPNN HGTGCTLSSA IAAGLAKGYD
     MVRAVAIGKE YVTTCLSAGL DLGEGCGPMD HSCALRGDYL EEE
//
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