ID A0A0A0BZ78_9CELL Unreviewed; 281 AA.
AC A0A0A0BZ78;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Hydroxymethylpyrimidine kinase {ECO:0000313|EMBL:KGM13017.1};
GN ORFNames=N869_16770 {ECO:0000313|EMBL:KGM13017.1};
OS Cellulomonas bogoriensis 69B4 = DSM 16987.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1386082 {ECO:0000313|EMBL:KGM13017.1, ECO:0000313|Proteomes:UP000054314};
RN [1] {ECO:0000313|EMBL:KGM13017.1, ECO:0000313|Proteomes:UP000054314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=69B4 {ECO:0000313|EMBL:KGM13017.1,
RC ECO:0000313|Proteomes:UP000054314};
RA Chen F., Li Y., Wang G.;
RT "Genome sequencing of Cellulomonas bogoriensis 69B4.";
RL Submitted (AUG-2013) 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:KGM13017.1}.
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DR EMBL; AXCZ01000074; KGM13017.1; -; Genomic_DNA.
DR RefSeq; WP_052105262.1; NZ_AXCZ01000074.1.
DR AlphaFoldDB; A0A0A0BZ78; -.
DR OrthoDB; 34166at2; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000054314; Unassembled WGS sequence.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 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 Kinase {ECO:0000313|EMBL:KGM13017.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054314};
KW Transferase {ECO:0000313|EMBL:KGM13017.1}.
FT DOMAIN 24..270
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 281 AA; 28752 MW; 7C378D8671693657 CRC64;
MTGDTRGGGP QPSRVRALSV AGTDPTGGAG IHADLKSFAA HGAYGMAVVT ALVAQNTCGV
RQVHVPDVGF LRAQLDAVGD DVDVDAVKVG MVGTRDVAEE ITSWLVRTRP PVVVVDPVMV
ATSGDRLLDA GAEEAVRGML TCADLVTPNL PELAVLLGTA PARSWSRALE QARELAARHG
LTVLVKGGHL DGARSPDAVV DGATVVELDA PRVATSATHG TGCSLSAALA ALRPVSQDWP
EAARRAKAWL TGALRAGEAL QVGRGNGPVD HLHGLHPGRG A
//
