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
//