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Database: UniProt
Entry: R9LX02_9FIRM
LinkDB: R9LX02_9FIRM
Original site: R9LX02_9FIRM 
ID   R9LX02_9FIRM            Unreviewed;       269 AA.
AC   R9LX02;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
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=C816_03910 {ECO:0000313|EMBL:EOS62851.1};
OS   Oscillibacter sp. 1-3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Oscillibacter.
OX   NCBI_TaxID=1235797 {ECO:0000313|EMBL:EOS62851.1, ECO:0000313|Proteomes:UP000014108};
RN   [1] {ECO:0000313|EMBL:EOS62851.1, ECO:0000313|Proteomes:UP000014108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1-3 {ECO:0000313|EMBL:EOS62851.1,
RC   ECO:0000313|Proteomes:UP000014108};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Oscillibacter bacterium 1-3.";
RL   Submitted (APR-2013) 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:EOS62851.1}.
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DR   EMBL; ASTC01000030; EOS62851.1; -; Genomic_DNA.
DR   RefSeq; WP_016324152.1; NZ_KE159711.1.
DR   AlphaFoldDB; R9LX02; -.
DR   STRING; 1235797.C816_03910; -.
DR   PATRIC; fig|1235797.3.peg.4315; -.
DR   eggNOG; COG0351; Bacteria.
DR   HOGENOM; CLU_020520_0_1_9; -.
DR   OrthoDB; 9810880at2; -.
DR   Proteomes; UP000014108; 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:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EOS62851.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014108};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EOS62851.1}.
FT   DOMAIN          11..253
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   269 AA;  28315 MW;  B3A14E4CCF7341ED CRC64;
     MKTALSIAGT DPSGGAGIQA DLKTMTMNGV FAMSAITALV AQNTTGVREI VEMTPEFLGQ
     QIDAVFEDIP PDAVKTGMVA SCGLIEKIAE RLRFYRAKNI VVDPVMVATS GDRLISEAAL
     DTLKTCLLPL AAVATPNIPE AEILAGVTIH SQSDIEAAAK WIGDTYGCAV LLKGGHNISD
     ANDFLYADHA GTWFYGAHID NPNTHGTGCT LSSAIAANLA KGFDLPTSIR RSKDYLSGAL
     GAMLDLGKGR GPMQHNFNLT GEYAKEAEQ
//
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