THID_SYNE7
ID THID_SYNE7 Reviewed; 263 AA.
AC O85786; Q31KL0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 104.
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=Synpcc7942_2379;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Mori T., Golden S.S., Johnson C.H.;
RT "Cloning and sequence of ftsZ and flanking regions from the cyanobacterium
RT Synechococcus sp. PCC7942.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the ThiD family. {ECO:0000305}.
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DR EMBL; AF076530; AAC26228.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB58409.1; -; Genomic_DNA.
DR PIR; T51093; T51093.
DR RefSeq; WP_011378435.1; NC_007604.1.
DR AlphaFoldDB; O85786; -.
DR SMR; O85786; -.
DR STRING; 1140.Synpcc7942_2379; -.
DR PRIDE; O85786; -.
DR EnsemblBacteria; ABB58409; ABB58409; Synpcc7942_2379.
DR KEGG; syf:Synpcc7942_2379; -.
DR eggNOG; COG0351; Bacteria.
DR HOGENOM; CLU_020520_0_0_3; -.
DR OMA; DNRHTHG; -.
DR OrthoDB; 461201at2; -.
DR BioCyc; SYNEL:SYNPCC7942_2379-MON; -.
DR UniPathway; UPA00060; UER00137.
DR UniPathway; UPA00060; UER00138.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC.
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:UniProtKB-KW.
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 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Thiamine biosynthesis;
KW Transferase.
FT CHAIN 1..263
FT /note="Hydroxymethylpyrimidine/phosphomethylpyrimidine
FT kinase"
FT /id="PRO_0000192036"
FT BINDING 44
FT /ligand="4-amino-5-hydroxymethyl-2-methylpyrimidine"
FT /ligand_id="ChEBI:CHEBI:16892"
FT /evidence="ECO:0000250"
FT CONFLICT 243
FT /note="L -> F (in Ref. 1; AAC26228)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="L -> F (in Ref. 1; AAC26228)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 27251 MW; A530A3F53A2DC46A CRC64;
MAVPIALTIA GSDSGGGAGI QADLRTFAFH QVHGTCAITC VTAQNTLGVT RVDAIAPAGV
AAQLDAVLSD LPPQALKTGM LLNAEIMEVV AGTIAPLFIP RIIDPVMVSR TGAVLIDQAA
IAVLRDHLLP LATVLTPNRY EAQLLAGMDI QDAADLDRAA RIIRDLGPQA VLIKGGAATG
DWHGVDWWWD GQQSHILKTE AIATPHTHGS GCTLAAAIAA NAALGLEILA AAQAAKHYVT
KALRHSLAIG QGQGPLGHFY PLF
