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Database: UniProt
Entry: V4NDA3_9CAUL
LinkDB: V4NDA3_9CAUL
Original site: V4NDA3_9CAUL 
ID   V4NDA3_9CAUL            Unreviewed;       260 AA.
AC   V4NDA3;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:ESQ79902.1};
GN   ORFNames=AEYBE204_08630 {ECO:0000313|EMBL:ESQ79902.1};
OS   Asticcacaulis sp. YBE204.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=1282363 {ECO:0000313|EMBL:ESQ79902.1, ECO:0000313|Proteomes:UP000017808};
RN   [1] {ECO:0000313|EMBL:ESQ79902.1, ECO:0000313|Proteomes:UP000017808}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YBE204 {ECO:0000313|EMBL:ESQ79902.1,
RC   ECO:0000313|Proteomes:UP000017808};
RX   PubMed=24463524; DOI=10.1038/nature12900;
RA   Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT   "Sequential evolution of bacterial morphology by co-option of a
RT   developmental regulator.";
RL   Nature 506:489-493(2014).
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:ESQ79902.1}.
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DR   EMBL; AWGF01000004; ESQ79902.1; -; Genomic_DNA.
DR   RefSeq; WP_023462020.1; NZ_AWGF01000004.1.
DR   AlphaFoldDB; V4NDA3; -.
DR   STRING; 1282363.AEYBE204_08630; -.
DR   PATRIC; fig|1282363.3.peg.1708; -.
DR   OrthoDB; 9810880at2; -.
DR   UniPathway; UPA00060; UER00138.
DR   Proteomes; UP000017808; 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   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:ESQ79902.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017808};
KW   Transferase {ECO:0000313|EMBL:ESQ79902.1}.
FT   DOMAIN          11..254
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   260 AA;  26804 MW;  9726EF8C04B61EB2 CRC64;
     MRRVLIIAGS DPSGGAGIQA DLKAVTCLGG YGMTAITALT VQNTLGVTDV MPVPEAIITA
     QGRACLSDIG ADAIKTGMLG TIPVVETVAA LIDEAPDAFI VVDPVMVAKG GHPLLPSEAI
     SAIRSVLIPR AGLLTPNAPE AAVLTGIEVV DENSQRKAGE ALLKLGAKAV LMKGGHIDGD
     EVVDWLMTPD GGERYSAKRV ETRHTHGTGC TLASACATLI TSERPLSESV GMARDYVLGA
     ILMAPNLGHG HGPLRHNWVL
//
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