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Database: UniProt
Entry: A0A1F4JDP4_9BURK
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Original site: A0A1F4JDP4_9BURK 
ID   A0A1F4JDP4_9BURK        Unreviewed;       268 AA.
AC   A0A1F4JDP4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase {ECO:0000313|EMBL:OGB20432.1};
GN   ORFNames=A3I66_18400 {ECO:0000313|EMBL:OGB20432.1};
OS   Burkholderiales bacterium RIFCSPLOWO2_02_FULL_57_36.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=1797562 {ECO:0000313|EMBL:OGB20432.1, ECO:0000313|Proteomes:UP000176765};
RN   [1] {ECO:0000313|EMBL:OGB20432.1, ECO:0000313|Proteomes:UP000176765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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}.
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:OGB20432.1}.
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DR   EMBL; MESE01000148; OGB20432.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F4JDP4; -.
DR   STRING; 1797562.A3I66_18400; -.
DR   UniPathway; UPA00060; UER00138.
DR   Proteomes; UP000176765; 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   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   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:OGB20432.1};
KW   Transferase {ECO:0000313|EMBL:OGB20432.1}.
FT   DOMAIN          13..252
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   268 AA;  28551 MW;  4859CF1646D36C38 CRC64;
     MIRPSVLVFS GVDPSAGAGM HADIQAIAAL GAHPLSAITA LTVQDNDRVF AVHPIPALLL
     RQQAQALINK IDIAAIKIGI VANHANAEVI AAIITELRKK QPNLPVVFDP VLASGHGDAL
     AVDNAIQIIA PLIEIATLVT PNLPEAAALC GGDRRSETQA ESLLRRGCRH VLIKGGHGKD
     NGKVVNQWFT QGHSRSWSWP RLKGAFHGSG CTLASAIAAL LASGKTMEQA LDIGQAYCQQ
     ALEQSYAIAE GQRIPDRFIL NFRDQERL
//
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