(data stored in ACNUC7421 zone)

SWISSPROT: Q5LWJ0_RUEPO

ID   Q5LWJ0_RUEPO            Unreviewed;       198 AA.
AC   Q5LWJ0;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 104.
DE   RecName: Full=Thiamine-phosphate synthase {ECO:0000256|RuleBase:RU003826};
DE            EC=2.5.1.3 {ECO:0000256|RuleBase:RU003826};
DE   AltName: Full=Thiamine-phosphate pyrophosphorylase {ECO:0000256|RuleBase:RU003826};
GN   Name=thiE {ECO:0000313|EMBL:AAV93379.1};
GN   OrderedLocusNames=SPO0048 {ECO:0000313|EMBL:AAV93379.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93379.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93379.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93379.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole
CC       monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl
CC       pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate
CC       (TMP). {ECO:0000256|SAAS:SAAS00709677}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-
CC         amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 +
CC         diphosphate + thiamine phosphate; Xref=Rhea:RHEA:47848,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, ChEBI:CHEBI:62890;
CC         EC=2.5.1.3; Evidence={ECO:0000256|RuleBase:RU003826,
CC         ECO:0000256|SAAS:SAAS01116526};
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 +
CC         2 H(+) = CO2 + diphosphate + thiamine phosphate;
CC         Xref=Rhea:RHEA:47844, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, ChEBI:CHEBI:57841,
CC         ChEBI:CHEBI:62899; EC=2.5.1.3;
CC         Evidence={ECO:0000256|RuleBase:RU003826,
CC         ECO:0000256|SAAS:SAAS01116528};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 4-
CC         methyl-5-(2-phosphooxyethyl)-thiazole + H(+) = diphosphate +
CC         thiamine 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:0000256|RuleBase:RU003826,
CC         ECO:0000256|SAAS:SAAS01116520};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC       thiamine phosphate from 4-amino-2-methyl-5-
CC       diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-
CC       thiazole: step 1/1. {ECO:0000256|RuleBase:RU004253,
CC       ECO:0000256|SAAS:SAAS00709682}.
CC   -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family.
CC       {ECO:0000256|RuleBase:RU003826}.
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DR   EMBL; CP000031; AAV93379.1; -; Genomic_DNA.
DR   RefSeq; WP_011045821.1; NC_003911.12.
DR   STRING; 246200.SPO0048; -.
DR   EnsemblBacteria; AAV93379; AAV93379; SPO0048.
DR   KEGG; sil:SPO0048; -.
DR   eggNOG; ENOG4108UV6; Bacteria.
DR   eggNOG; COG0352; LUCA.
DR   HOGENOM; HOG000155781; -.
DR   KO; K00788; -.
DR   OMA; ITAFQFR; -.
DR   OrthoDB; 461201at2; -.
DR   BioCyc; RPOM246200:G1G48-49-MONOMER; -.
DR   UniPathway; UPA00060; UER00141.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC.
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; cd00564; TMP_TenI; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR036206; ThiamineP_synth_sf.
DR   InterPro; IPR022998; ThiamineP_synth_TenI.
DR   InterPro; IPR034291; TMP_synthase.
DR   Pfam; PF02581; TMP-TENI; 1.
DR   SUPFAM; SSF51391; SSF51391; 1.
DR   TIGRFAMs; TIGR00693; thiE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5LWJ0.
DR   SWISS-2DPAGE; Q5LWJ0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   Magnesium {ECO:0000256|SAAS:SAAS00709725};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00709674};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023};
KW   Thiamine biosynthesis {ECO:0000256|RuleBase:RU003826,
KW   ECO:0000256|SAAS:SAAS00709833};
KW   Transferase {ECO:0000256|RuleBase:RU003826,
KW   ECO:0000256|SAAS:SAAS00709679, ECO:0000313|EMBL:AAV93379.1}.
FT   DOMAIN       12    180       TMP-TENI. {ECO:0000259|Pfam:PF02581}.
SQ   SEQUENCE   198 AA;  22089 MW;  7EB8780A172D928F CRC64;
     MTLDRFYPIF DHTDWLRRML PLGVKLVQLR IKDQSDPVIR AEIDTARDLC RAHGAVLVIN
     DYWQAAIDAG CDWLHLGQED LDQADLPAIR KAGLRLGVST HDDDELERVL GMDPDYVALG
     PVYPTILKQM KWHQQGLPRV TEWKARVGSI PLVGIGGMSV ERAPGVLGAG ADIVSVVTDI
     TLNADPEARV HQWIEVTR
//

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