THID_RHIME
ID THID_RHIME Reviewed; 266 AA.
AC P56904; Q52914;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 113.
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=RB1087; ORFNames=SMb20962;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymB (megaplasmid 2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=042B;
RA Yang S., Chen X.;
RT "Cloning of a DNA fragment related to salt tolerance in Sinorhizobium
RT meliloti.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481431; DOI=10.1073/pnas.161294698;
RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT endosymbiont Sinorhizobium meliloti.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 103-266.
RC STRAIN=RCR2011 / SU47;
RX PubMed=8246891; DOI=10.1007/bf00284690;
RA Becker A., Kleickmann A., Keller M., Arnold W., Puehler A.;
RT "Identification and analysis of the Rhizobium meliloti exoAMONP genes
RT involved in exopolysaccharide biosynthesis and mapping of promoters located
RT on the exoHKLAMONP fragment.";
RL Mol. Gen. Genet. 241:367-379(1993).
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; AF070520; AAD46983.1; -; Genomic_DNA.
DR EMBL; AL591985; CAC49487.1; -; Genomic_DNA.
DR EMBL; Z22636; CAA80350.1; ALT_SEQ; Genomic_DNA.
DR PIR; G95977; G95977.
DR PIR; S78110; S78110.
DR RefSeq; NP_437627.1; NC_003078.1.
DR RefSeq; WP_010975923.1; NC_003078.1.
DR AlphaFoldDB; P56904; -.
DR SMR; P56904; -.
DR STRING; 266834.SM_b20962; -.
DR EnsemblBacteria; CAC49487; CAC49487; SM_b20962.
DR GeneID; 61601043; -.
DR KEGG; sme:SM_b20962; -.
DR PATRIC; fig|266834.11.peg.6017; -.
DR eggNOG; COG0351; Bacteria.
DR HOGENOM; CLU_020520_0_1_5; -.
DR OMA; KDEVGYA; -.
DR UniPathway; UPA00060; UER00137.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000001976; Plasmid pSymB.
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; Plasmid; Reference proteome;
KW Thiamine biosynthesis; Transferase.
FT CHAIN 1..266
FT /note="Hydroxymethylpyrimidine/phosphomethylpyrimidine
FT kinase"
FT /id="PRO_0000192025"
FT BINDING 43
FT /ligand="4-amino-5-hydroxymethyl-2-methylpyrimidine"
FT /ligand_id="ChEBI:CHEBI:16892"
FT /evidence="ECO:0000250"
FT CONFLICT 98..99
FT /note="KR -> RL (in Ref. 1; AAD46983)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="L -> F (in Ref. 1; AAD46983)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="V -> A (in Ref. 1; AAD46983)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 266 AA; 27423 MW; 803D0C58EB9A1830 CRC64;
MTAIALSIAG SDSGGGAGIQ ADLKTFSALG VYGASVITAI TAQNTRGVTA VEDVSAEIVS
AQMDAVFSDL DVKAVKIGMV SRRETIAAIA DGLRRFGKRA VVDPVMVATS GDALLRPDAV
AALIEELLPL ALVVTPNLAE AALMTGRAIA GDEAEMARQA EAIMRTGAHA VLVKGGHLKG
QEATDLFFDG DTLVRLPAGR IETRNDHGTG CTLSAAIAAG LAKGVPLIEA VSAAKAYLHA
AISAADRLEI GQGRGPVHHF HRWWKD
