ID E6NS24_HELPQ Unreviewed; 269 AA.
AC E6NS24;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Thiamine biosynthesis protein {ECO:0000313|EMBL:BAJ59940.1};
GN Name=thiD {ECO:0000313|EMBL:BAJ59940.1};
GN OrderedLocusNames=HPF57_0866 {ECO:0000313|EMBL:BAJ59940.1};
OS Helicobacter pylori (strain F57).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=866346 {ECO:0000313|EMBL:BAJ59940.1, ECO:0000313|Proteomes:UP000008082};
RN [1] {ECO:0000313|EMBL:BAJ59940.1, ECO:0000313|Proteomes:UP000008082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F57 {ECO:0000313|EMBL:BAJ59940.1,
RC ECO:0000313|Proteomes:UP000008082};
RX PubMed=21575176; DOI=10.1186/1471-2180-11-104;
RA Kawai M., Furuta Y., Yahara K., Tsuru T., Oshima K., Handa N.,
RA Takahashi N., Yoshida M., Azuma T., Hattori M., Uchiyama I., Kobayashi I.;
RT "Evolution in an oncogenic bacterial species with extreme genome
RT plasticity: Helicobacter pylori East Asian genomes.";
RL BMC Microbiol. 11:104-104(2011).
RN [2] {ECO:0000313|EMBL:BAJ59940.1, ECO:0000313|Proteomes:UP000008082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F57 {ECO:0000313|EMBL:BAJ59940.1,
RC ECO:0000313|Proteomes:UP000008082};
RX PubMed=21212362; DOI=10.1073/pnas.1012579108;
RA Furuta Y., Kawai M., Yahara K., Takahashi N., Handa N., Tsuru T.,
RA Oshima K., Yoshida M., Azuma T., Hattori M., Uchiyama I., Kobayashi I.;
RT "Birth and death of genes linked to chromosomal inversion.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:1501-1506(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; AP011945; BAJ59940.1; -; Genomic_DNA.
DR RefSeq; WP_000708617.1; NC_017367.1.
DR AlphaFoldDB; E6NS24; -.
DR KEGG; hex:HPF57_0866; -.
DR PATRIC; fig|866346.4.peg.927; -.
DR HOGENOM; CLU_020520_0_1_7; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000008082; Chromosome.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
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;
FT DOMAIN 14..261
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 269 AA; 28876 MW; 5F6705A53BADA696 CRC64;
MKIYPQVLSI AGSDSGGGAG IQADLKAFQT LGVFGTSVIT CITAQNTQGV HGVYPLSVES
VRAQILAIRD DFSIKAFKMG ALCNAQIIEC VADTLKTCDF GWCVLDPVMV AKNGALLLEE
EAILSLKKRL LPTTHLLTPN LPEVFALTGV QVRDNKSASK AMGILRDLGV KNAVIKGGHT
EHFQGEFSND WVFLEDAEFI LNAKRFNTKN THGTGCTLSS LIVGLLAQGL DLKNAISKAK
ELLTIIIQNP LNIGHGHGPL NLWSVKKLV
//
