ID B5EXY5_SALA4 Unreviewed; 266 AA.
AC B5EXY5;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:ACH51393.1};
DE EC=2.7.4.7 {ECO:0000313|EMBL:ACH51393.1};
GN Name=thiD {ECO:0000313|EMBL:ACH51393.1};
GN OrderedLocusNames=SeAg_B2289 {ECO:0000313|EMBL:ACH51393.1};
OS Salmonella agona (strain SL483).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454166 {ECO:0000313|EMBL:ACH51393.1, ECO:0000313|Proteomes:UP000008819};
RN [1] {ECO:0000313|EMBL:ACH51393.1, ECO:0000313|Proteomes:UP000008819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL483 {ECO:0000313|EMBL:ACH51393.1,
RC ECO:0000313|Proteomes:UP000008819};
RX PubMed=21602358; DOI=10.1128/JB.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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; CP001138; ACH51393.1; -; Genomic_DNA.
DR RefSeq; WP_001188955.1; NC_011149.1.
DR AlphaFoldDB; B5EXY5; -.
DR KEGG; sea:SeAg_B2289; -.
DR HOGENOM; CLU_020520_0_1_6; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000008819; Chromosome.
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:ACH51393.1};
KW Transferase {ECO:0000313|EMBL:ACH51393.1}.
FT DOMAIN 13..260
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 266 AA; 28560 MW; 19E94332E16179D9 CRC64;
MQRINALTIA GTDPSGGAGI QADLKTFSAL GAYGCSVITA LVAQNTCGVQ SVYRIEPDFV
AAQLDSVFSD VRIDTTKIGM LAETDIVEAV AERLQRHHVR NVVLDTVMLA KSGDPLLSPS
AIETLRVRLL PQVSLITPNL PEAAALLDAP HARTEQEMLA QGRALLAMGC EAVLMKGGHL
EDAQSPDWLF TREGEQRFSA PRVNTKNTHG TGCTLSAALA ALRPRHRCWG ETVNEAKAWL
SAALAQADTL EVGKGIGPVH HFHAWW
//
