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Database: UniProt
Entry: B4ECQ2_BURCJ
LinkDB: B4ECQ2_BURCJ
Original site: B4ECQ2_BURCJ 
ID   B4ECQ2_BURCJ            Unreviewed;       269 AA.
AC   B4ECQ2;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:CAR52412.1};
DE            EC=2.7.4.7 {ECO:0000313|EMBL:CAR52412.1};
GN   Name=thiD {ECO:0000313|EMBL:CAR52412.1};
GN   ORFNames=BCAL2112 {ECO:0000313|EMBL:CAR52412.1};
OS   Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS   NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=216591 {ECO:0000313|EMBL:CAR52412.1, ECO:0000313|Proteomes:UP000001035};
RN   [1] {ECO:0000313|EMBL:CAR52412.1, ECO:0000313|Proteomes:UP000001035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 /
RC   CF5610 {ECO:0000313|Proteomes:UP000001035};
RX   PubMed=18931103; DOI=10.1128/JB.01230-08;
RA   Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA   Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA   Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA   Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA   Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA   Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT   "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT   cystic fibrosis patients.";
RL   J. Bacteriol. 191:261-277(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; AM747720; CAR52412.1; -; Genomic_DNA.
DR   RefSeq; WP_006488249.1; NC_011000.1.
DR   AlphaFoldDB; B4ECQ2; -.
DR   GeneID; 56558601; -.
DR   KEGG; bcj:BCAL2112; -.
DR   eggNOG; COG0351; Bacteria.
DR   HOGENOM; CLU_020520_0_1_4; -.
DR   BioCyc; BCEN216591:G1G1V-2312-MONOMER; -.
DR   UniPathway; UPA00060; UER00138.
DR   Proteomes; UP000001035; Chromosome 1.
DR   GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:RHEA.
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: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:CAR52412.1};
KW   Transferase {ECO:0000313|EMBL:CAR52412.1}.
FT   DOMAIN          15..263
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   269 AA;  27801 MW;  FCC5027FD3438D7D CRC64;
     MTHPIPNILT IAGSDSGGGA GIQADLKTFS ALGAYGASVI TALTAQNTRG VTGVHAPDAA
     FVTAQLDAVF GDIRIDAVKI GMLANAAIVQ AVADALRRYA PRFVVLDTVM ISKSAHALLA
     PDAVDALRDT LLPLATVVTP NLPEAAALLN DAPATTEDEM VRQGRALLQT GARAVLMKGG
     HLPDASASPD WLVEATRTVR LDGARVPVSN THGTGCTLSS AIAALLPQQP DLESAVREAK
     TYLTGAIAAS GHLDVGHGVG PVHHFHRWW
//
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