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Database: UniProt
Entry: C5AJL0_BURGB
LinkDB: C5AJL0_BURGB
Original site: C5AJL0_BURGB 
ID   C5AJL0_BURGB            Unreviewed;       265 AA.
AC   C5AJL0;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:ACR32090.1};
GN   OrderedLocusNames=bglu_2g17500 {ECO:0000313|EMBL:ACR32090.1};
OS   Burkholderia glumae (strain BGR1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=626418 {ECO:0000313|EMBL:ACR32090.1, ECO:0000313|Proteomes:UP000002187};
RN   [1] {ECO:0000313|EMBL:ACR32090.1, ECO:0000313|Proteomes:UP000002187}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGR1 {ECO:0000313|EMBL:ACR32090.1,
RC   ECO:0000313|Proteomes:UP000002187};
RX   PubMed=19329631; DOI=10.1128/JB.00349-09;
RA   Lim J., Lee T.H., Nahm B.H., Choi Y.D., Kim M., Hwang I.;
RT   "Complete genome sequence of Burkholderia glumae BGR1.";
RL   J. Bacteriol. 191:3758-3759(2009).
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.
CC       {ECO:0000256|ARBA:ARBA00004948}.
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DR   EMBL; CP001504; ACR32090.1; -; Genomic_DNA.
DR   RefSeq; WP_015877773.1; NC_012721.2.
DR   AlphaFoldDB; C5AJL0; -.
DR   STRING; 626418.bglu_2g17500; -.
DR   KEGG; bgl:bglu_2g17500; -.
DR   PATRIC; fig|626418.3.peg.2062; -.
DR   eggNOG; COG0351; Bacteria.
DR   HOGENOM; CLU_020520_0_1_4; -.
DR   UniPathway; UPA00060; UER00138.
DR   Proteomes; UP000002187; Chromosome 2.
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   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:ACR32090.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002187};
KW   Transferase {ECO:0000313|EMBL:ACR32090.1}.
FT   DOMAIN          12..258
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   265 AA;  27820 MW;  51054AC693853662 CRC64;
     MIANVLSIAG TDPTGGAGIQ ADLKTFSALG AYGMSAITAV VAQNTRGVRG FHTLEPAFIV
     EQIDAVFDDV TVHAVKLGML ATAAIAEAVA EALVRHRATT VVLDPVMVAK SGDRLLAPDA
     VAAIRERLVP LATLITPNLP EAGVLLDRPA PASLAEMHDA LQALHGLGPR WVLLKGGHLR
     GADSTDLLFG ASGTTELAAP RIATRNDHGT GCTLSAAVAA LLPHHPMEES VRRAKAYLNR
     ALAESWRLEV GHGRGPTHHF HALWR
//
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