ID   Q8X7G5_ECO57            Unreviewed;       266 AA.
AC   Q8X7G5; A0A0H3JGP0; A0A6M0JP24; Q7ACK6;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 142.
DE   SubName: Full=Hydroxy-methylpyrimidine kinase and hydroxy-phosphomethylpyrimidine kinase {ECO:0000313|EMBL:BAB36329.1};
GN   Name=thiD {ECO:0000313|EMBL:BAB36329.1};
GN   ORFNames=ECs_2906 {ECO:0000313|EMBL:BAB36329.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB36329.1, ECO:0000313|Proteomes:UP000000558};
RN   [1] {ECO:0000313|EMBL:BAB36329.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 /
RC   EHEC {ECO:0000313|Proteomes:UP000000558};
RX   PubMed=11258796; DOI=.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; BA000007; BAB36329.1; -; Genomic_DNA.
DR   RefSeq; NP_310933.1; NC_002695.1.
DR   RefSeq; WP_000822268.1; NZ_VOAI01000013.1.
DR   AlphaFoldDB; Q8X7G5; -.
DR   STRING; 155864.Z3267; -.
DR   GeneID; 916609; -.
DR   KEGG; ecs:ECs_2906; -.
DR   PATRIC; fig|386585.9.peg.3038; -.
DR   eggNOG; COG0351; Bacteria.
DR   HOGENOM; CLU_020520_0_1_6; -.
DR   OMA; DNRHTHG; -.
DR   UniPathway; UPA00060; UER00138.
DR   Proteomes; UP000000558; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000313|EMBL:BAB36329.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000558};
KW   Transferase {ECO:0000313|EMBL:BAB36329.1}.
FT   DOMAIN          13..260
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   266 AA;  28618 MW;  A8E31593E52196F4 CRC64;
     MKRINALTIA GTDPSGGAGI QADLKTFSAL GAYGCSVITA LVAQNTRGVQ SVYRIEPDFV
     AAQLDSVFSD VRIDTTKIGM LAETDIVEAV AERLQRYQIQ NVVLDTVMLA KSGDPLLSPS
     AVATLRSRLL PQVSLITPNL PEAAALLDAP HARTEQEMLE QGRALLAMGC GAVLMKGGHL
     DDEQSPDWLF TREGEQRFTA PRIMTKNTHG TGCTLSAALA ALRPRHTNWA DTVQEAKSWL
     SSALAQADTL EVGHGIGPVH HFHAWW
//