THID_SALTY
ID THID_SALTY Reviewed; 266 AA.
AC P55882;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase;
DE EC=2.7.1.49 {ECO:0000250|UniProtKB:P76422};
DE EC=2.7.4.7 {ECO:0000250|UniProtKB:P76422};
DE AltName: Full=Hydroxymethylpyrimidine kinase;
DE Short=HMP kinase;
DE AltName: Full=Hydroxymethylpyrimidine phosphate kinase;
DE Short=HMP-P kinase;
DE Short=HMP-phosphate kinase;
DE Short=HMPP kinase;
GN Name=thiD; OrderedLocusNames=STM2146;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=9244280; DOI=10.1128/jb.179.15.4894-4900.1997;
RA Petersen L.A., Downs D.M.;
RT "Identification and characterization of an operon in Salmonella typhimurium
RT involved in thiamine biosynthesis.";
RL J. Bacteriol. 179:4894-4900(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP 4-AMINO-5-HYDROXYMETHYL-2-METHYLPYRIMIDINE, AND SUBUNIT.
RX PubMed=11839308; DOI=10.1016/s0969-2126(02)00708-6;
RA Cheng G., Bennett E.M., Begley T.P., Ealick S.E.;
RT "Crystal structure of 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate
RT kinase from Salmonella typhimurium at 2.3 A resolution.";
RL Structure 10:225-235(2002).
CC -!- FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine
CC phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
CC {ECO:0000250|UniProtKB:P76422}.
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:0000250|UniProtKB:P76422};
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:0000250|UniProtKB:P76422};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-
CC amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-
CC ribosyl)imidazole: step 2/3.
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-
CC amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-
CC ribosyl)imidazole: step 3/3.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11839308}.
CC -!- SIMILARITY: Belongs to the ThiD family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U87940; AAB66492.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21049.1; -; Genomic_DNA.
DR RefSeq; NP_461090.1; NC_003197.2.
DR RefSeq; WP_001188957.1; NC_003197.2.
DR PDB; 1JXH; X-ray; 2.30 A; A/B=1-266.
DR PDB; 1JXI; X-ray; 2.64 A; A/B=1-266.
DR PDBsum; 1JXH; -.
DR PDBsum; 1JXI; -.
DR AlphaFoldDB; P55882; -.
DR SMR; P55882; -.
DR STRING; 99287.STM2146; -.
DR DrugBank; DB02022; 4-Amino-5-Hydroxymethyl-2-Methylpyrimidine.
DR PaxDb; P55882; -.
DR PRIDE; P55882; -.
DR EnsemblBacteria; AAL21049; AAL21049; STM2146.
DR GeneID; 1253667; -.
DR KEGG; stm:STM2146; -.
DR PATRIC; fig|99287.12.peg.2271; -.
DR HOGENOM; CLU_020520_0_1_6; -.
DR OMA; DNRHTHG; -.
DR PhylomeDB; P55882; -.
DR BioCyc; SENT99287:STM2146-MON; -.
DR BRENDA; 2.7.1.49; 5542.
DR BRENDA; 2.7.4.7; 5542.
DR UniPathway; UPA00060; UER00137.
DR UniPathway; UPA00060; UER00138.
DR EvolutionaryTrace; P55882; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IBA:GO_Central.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IBA:GO_Central.
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; IPR045029; HMP/HMP-P_kinase.
DR InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR029056; Ribokinase-like.
DR PANTHER; PTHR20858; PTHR20858; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Thiamine biosynthesis; Transferase.
FT CHAIN 1..266
FT /note="Hydroxymethylpyrimidine/phosphomethylpyrimidine
FT kinase"
FT /id="PRO_0000192026"
FT BINDING 44
FT /ligand="4-amino-5-hydroxymethyl-2-methylpyrimidine"
FT /ligand_id="ChEBI:CHEBI:16892"
FT /evidence="ECO:0000269|PubMed:11839308"
FT CONFLICT 44
FT /note="Q -> E (in Ref. 1; AAB66492)"
FT /evidence="ECO:0000305"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:1JXH"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1JXH"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:1JXH"
FT STRAND 33..45
FT /evidence="ECO:0007829|PDB:1JXH"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:1JXH"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:1JXH"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:1JXH"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:1JXH"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:1JXH"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:1JXH"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1JXH"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:1JXH"
FT HELIX 140..147
FT /evidence="ECO:0007829|PDB:1JXH"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:1JXH"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:1JXH"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1JXH"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:1JXH"
FT HELIX 211..222
FT /evidence="ECO:0007829|PDB:1JXH"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:1JXH"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:1JXH"
FT HELIX 229..244
FT /evidence="ECO:0007829|PDB:1JXH"
FT HELIX 245..249
FT /evidence="ECO:0007829|PDB:1JXH"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:1JXH"
FT TURN 261..265
FT /evidence="ECO:0007829|PDB:1JXH"
SQ SEQUENCE 266 AA; 28544 MW; F8B94332E1616368 CRC64;
MQRINALTIA GTDPSGGAGI QADLKTFSAL GAYGCSVITA LVAQNTCGVQ SVYRIEPDFV
AAQLDSVFSD VRIDTTKIGM LAETDIVEAV AERLQRHHVR NVVLDTVMLA KSGDPLLSPS
AIETLRVRLL PQVSLITPNL PEAAALLDAP HARTEQEMLA QGRALLAMGC EAVLMKGGHL
EDAQSPDWLF TREGEQRFSA PRVNTKNTHG TGCTLSAALA ALRPRHRSWG ETVNEAKAWL
SAALAQADTL EVGKGIGPVH HFHAWW
