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Database: UniProt
Entry: H1D1G1_9FIRM
LinkDB: H1D1G1_9FIRM
Original site: H1D1G1_9FIRM 
ID   H1D1G1_9FIRM            Unreviewed;       269 AA.
AC   H1D1G1;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
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=HMPREF9453_01449 {ECO:0000313|EMBL:EHO62584.1};
OS   Dialister succinatiphilus YIT 11850.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Dialister.
OX   NCBI_TaxID=742743 {ECO:0000313|EMBL:EHO62584.1, ECO:0000313|Proteomes:UP000003277};
RN   [1] {ECO:0000313|EMBL:EHO62584.1, ECO:0000313|Proteomes:UP000003277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIT 11850 {ECO:0000313|EMBL:EHO62584.1,
RC   ECO:0000313|Proteomes:UP000003277};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Dunbar C., Gearin G.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Lui A.,
RA   MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Dialister succinatiphilus YIT 11850.";
RL   Submitted (NOV-2011) 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:EHO62584.1}.
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DR   EMBL; ADLT01000049; EHO62584.1; -; Genomic_DNA.
DR   RefSeq; WP_008859943.1; NZ_JH591188.1.
DR   AlphaFoldDB; H1D1G1; -.
DR   STRING; 742743.HMPREF9453_01449; -.
DR   PATRIC; fig|742743.3.peg.1474; -.
DR   eggNOG; COG0351; Bacteria.
DR   HOGENOM; CLU_020520_0_1_9; -.
DR   OrthoDB; 9810880at2; -.
DR   Proteomes; UP000003277; 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:EHO62584.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003277};
KW   Transferase {ECO:0000313|EMBL:EHO62584.1}.
FT   DOMAIN          11..256
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   269 AA;  28336 MW;  A2D774CB89EF838B CRC64;
     MIPVLTVAGS DSSGGAGIQA DLKTFAALGT YGMSCICALT AQNTKGVTMV VNTPVDMVKA
     QLEAVFDDIP PRAVKTGMLS SAPIVETVAD FLSSHGKVPL VVDPVMVATS GAVLLEEEAI
     QSYKEKLIPL STLITPNIPE AEVLSGLSIQ NEEDMKKAAL ALMDLGPSAV LVKGGHSVED
     ARDILYDGRE FHVFSGRRIS TENTHGTGCT LSSAIAASMA RGLSLTEAVG EAKKYMEGAI
     RRAAVDSVGH GHGPVHHFWF YGENWGHME
//
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