THIDN_THEMA
ID THIDN_THEMA Reviewed; 398 AA.
AC Q9WZP7;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Bifunctional thiamine biosynthesis protein ThiDN;
DE Includes:
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;
DE Includes:
DE RecName: Full=Thiamine-phosphate synthase ThiN;
DE Short=TP synthase;
DE Short=TPS;
DE EC=2.5.1.3 {ECO:0000269|PubMed:12794638};
DE AltName: Full=Thiamine-phosphate pyrophosphorylase;
DE Short=TMP pyrophosphorylase;
DE Short=TMP-PPase;
GN Name=thiDN; OrderedLocusNames=TM_0790;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP FUNCTION AS A THIAMINE-PHOSPHATE SYNTHASE VIA ITS C-TERMINAL DOMAIN, AND
RP CATALYTIC ACTIVITY.
RX PubMed=12794638; DOI=10.1038/nbt834;
RA Morett E., Korbel J.O., Rajan E., Saab-Rincon G., Olvera L., Olvera M.,
RA Schmidt S., Snel B., Bork P.;
RT "Systematic discovery of analogous enzymes in thiamin biosynthesis.";
RL Nat. Biotechnol. 21:790-795(2003).
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 -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole
CC monophosphate (THZ-P) and 4-amino-5-hydroxymethyl pyrimidine
CC pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
CC {ECO:0000269|PubMed:12794638}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl
CC phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2
CC H(+) = CO2 + diphosphate + thiamine phosphate; Xref=Rhea:RHEA:47844,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, ChEBI:CHEBI:62899; EC=2.5.1.3;
CC Evidence={ECO:0000269|PubMed:12794638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-
CC methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate
CC + thiamine phosphate; Xref=Rhea:RHEA:47848, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, ChEBI:CHEBI:37575,
CC ChEBI:CHEBI:57841, ChEBI:CHEBI:62890; EC=2.5.1.3;
CC Evidence={ECO:0000269|PubMed:12794638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 4-methyl-
CC 5-(2-phosphooxyethyl)-thiazole + H(+) = diphosphate + thiamine
CC phosphate; Xref=Rhea:RHEA:22328, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, ChEBI:CHEBI:57841,
CC ChEBI:CHEBI:58296; EC=2.5.1.3;
CC Evidence={ECO:0000269|PubMed:12794638};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-
CC amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-
CC ribosyl)imidazole.
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine
CC and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ThiD family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ThiN family.
CC {ECO:0000305}.
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DR EMBL; AE000512; AAD35872.1; -; Genomic_DNA.
DR PIR; G72333; G72333.
DR RefSeq; NP_228599.1; NC_000853.1.
DR RefSeq; WP_004080887.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9WZP7; -.
DR SMR; Q9WZP7; -.
DR STRING; 243274.THEMA_00700; -.
DR DNASU; 898458; -.
DR EnsemblBacteria; AAD35872; AAD35872; TM_0790.
DR KEGG; tma:TM0790; -.
DR eggNOG; COG0351; Bacteria.
DR eggNOG; COG1992; Bacteria.
DR InParanoid; Q9WZP7; -.
DR OMA; AWIEIPA; -.
DR OrthoDB; 461201at2; -.
DR UniPathway; UPA00060; UER00141.
DR Proteomes; UP000008183; 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:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC.
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; -; 2.
DR Gene3D; 3.40.225.10; -; 1.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
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 InterPro; IPR019293; ThiN.
DR PANTHER; PTHR20858; PTHR20858; 1.
DR Pfam; PF08543; Phos_pyr_kin; 2.
DR Pfam; PF10120; ThiP_synth; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Multifunctional enzyme; Nucleotide-binding;
KW Reference proteome; Thiamine biosynthesis; Transferase.
FT CHAIN 1..398
FT /note="Bifunctional thiamine biosynthesis protein ThiDN"
FT /id="PRO_0000415381"
FT REGION 1..216
FT /note="Hydroxymethylpyrimidine/phosphomethylpyrimidine
FT kinase"
FT REGION 217..398
FT /note="Thiamine-phosphate synthase"
FT BINDING 40
FT /ligand="4-amino-5-hydroxymethyl-2-methylpyrimidine"
FT /ligand_id="ChEBI:CHEBI:16892"
FT /evidence="ECO:0000250"
SQ SEQUENCE 398 AA; 45392 MW; DCE6977F471BF649 CRC64;
MVLVVAGFDP SGGAGIIQDV KVLSALGVKT HAVISALTVQ NENRVFSVNF RDWEEMRKEI
EVLTPPRVIK VGLSAPETVK RLREMFPDSA IVWNVVLESS SGFGFQDPEE VKKFVEYADY
VILNSEEAKK LGEYNNFIVT GGHEKGNTVK VKYRDFVFEI PRVPGEFHGT GCAFSSAVSG
FLAMSYPVEE AIRSAMELLK KILERSSGVV ETEKLLRDWY RYDTLNTLDE ILPEFLEIGH
LTVPEVGQNV SYALPWAKNE FEVGKFPGRI RLKEGKAVAV SCASFKDRSH TARMAVTMMR
YHPHMRCVVN VRYEREYVER AKKRGLKVFH YDRSKEPKEV QEKEGQSMVW MIEQAIAELK
SPPDVIYDEG WWGKEAMIRV FGRNPKEVLE KIKLMVRE
