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Database: UniProt
Entry: Q87JW2_VIBPA
LinkDB: Q87JW2_VIBPA
Original site: Q87JW2_VIBPA 
ID   Q87JW2_VIBPA            Unreviewed;       285 AA.
AC   Q87JW2;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 85.
DE   SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:BAC61479.1};
GN   OrderedLocusNames=VPA0136 {ECO:0000313|EMBL:BAC61479.1};
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC61479.1, ECO:0000313|Proteomes:UP000002493};
RN   [1] {ECO:0000313|EMBL:BAC61479.1, ECO:0000313|Proteomes:UP000002493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
RX   PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; BA000032; BAC61479.1; -; Genomic_DNA.
DR   RefSeq; NP_799646.1; NC_004605.1.
DR   RefSeq; WP_005459962.1; NC_004605.1.
DR   AlphaFoldDB; Q87JW2; -.
DR   GeneID; 1190815; -.
DR   KEGG; vpa:VPA0136; -.
DR   PATRIC; fig|223926.6.peg.3096; -.
DR   eggNOG; COG0351; Bacteria.
DR   HOGENOM; CLU_020520_0_1_6; -.
DR   OMA; DNRHTHG; -.
DR   UniPathway; UPA00060; UER00138.
DR   Proteomes; UP000002493; 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:BAC61479.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002493};
KW   Transferase {ECO:0000313|EMBL:BAC61479.1}.
FT   DOMAIN          27..275
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   285 AA;  30133 MW;  E4CB1E7DF03F820B CRC64;
     MTQQSQPYSH QTPALPTPIV LTIAGSDSGG GAGIQADIKA MSATGSFACS VITAITSQNT
     QGVSAIFPIP LDHVESQLDA VFTDLNIVAV KVGMLADSNI IKVVASKIRQ YQPKHLVIDP
     VMVATSGDLL LEQSAISTLR EELIPLADII TPNLPEGAAL TGKPVPHSES EMNDMIDDLR
     ALGAKAILLK GGHLEEDENS NDLLIMQNSA ELISAKRFPT KNTHGTGCTL SSAIASYLGQ
     GNNLHKAVHL GKQYISQAIA HADELEVGKG HGPVHHFFAG HTYVR
//
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