(data stored in ACNUC7421 zone)

SWISSPROT: A0KFE7_AERHH

ID   A0KFE7_AERHH            Unreviewed;       538 AA.
AC   A0KFE7;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 97.
DE   RecName: Full=Thiamine-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00097};
DE            Short=TP synthase {ECO:0000256|HAMAP-Rule:MF_00097};
DE            Short=TPS {ECO:0000256|HAMAP-Rule:MF_00097};
DE            EC=2.5.1.3 {ECO:0000256|HAMAP-Rule:MF_00097};
DE   AltName: Full=Thiamine-phosphate pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00097};
DE            Short=TMP pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00097};
DE            Short=TMP-PPase {ECO:0000256|HAMAP-Rule:MF_00097};
GN   Name=thiE {ECO:0000256|HAMAP-Rule:MF_00097};
GN   OrderedLocusNames=AHA_0440 {ECO:0000313|EMBL:ABK38267.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK38267.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK38267.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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|HAMAP-Rule:MF_00097}.
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|HAMAP-Rule:MF_00097,
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00097, 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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00097, ECO:0000256|SAAS:SAAS01116520};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00097};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00097};
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|HAMAP-Rule:MF_00097,
CC       ECO:0000256|SAAS:SAAS00709682}.
CC   -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00097}.
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DR   EMBL; CP000462; ABK38267.1; -; Genomic_DNA.
DR   RefSeq; WP_011704414.1; NC_008570.1.
DR   RefSeq; YP_854969.1; NC_008570.1.
DR   STRING; 380703.AHA_0440; -.
DR   EnsemblBacteria; ABK38267; ABK38267; AHA_0440.
DR   GeneID; 4490403; -.
DR   KEGG; aha:AHA_0440; -.
DR   PATRIC; fig|380703.7.peg.430; -.
DR   eggNOG; ENOG4108F0B; Bacteria.
DR   eggNOG; COG0351; LUCA.
DR   eggNOG; COG0352; LUCA.
DR   HOGENOM; HOG000155781; -.
DR   KO; K14153; -.
DR   OMA; PIVWTIA; -.
DR   BioCyc; AHYD380703:G1G7B-441-MONOMER; -.
DR   UniPathway; UPA00060; UER00141.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR   GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01169; HMPP_kinase; 1.
DR   CDD; cd00564; TMP_TenI; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   HAMAP; MF_00097; TMP_synthase; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR004399; HMP/HMP-P_kinase.
DR   InterPro; IPR013749; PM/HMP-P_kinase-1.
DR   InterPro; IPR029056; Ribokinase-like.
DR   InterPro; IPR036206; ThiamineP_synth_sf.
DR   InterPro; IPR022998; ThiamineP_synth_TenI.
DR   InterPro; IPR034291; TMP_synthase.
DR   Pfam; PF08543; Phos_pyr_kin; 1.
DR   Pfam; PF02581; TMP-TENI; 1.
DR   SUPFAM; SSF51391; SSF51391; 1.
DR   SUPFAM; SSF53613; SSF53613; 1.
DR   TIGRFAMs; TIGR00097; HMP-P_kinase; 1.
DR   TIGRFAMs; TIGR00693; thiE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KFE7.
DR   SWISS-2DPAGE; A0KFE7.
KW   ATP-binding {ECO:0000256|SAAS:SAAS00228462};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Kinase {ECO:0000256|SAAS:SAAS00228485};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00097,
KW   ECO:0000256|SAAS:SAAS00709725};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00097,
KW   ECO:0000256|SAAS:SAAS00709674};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00440335};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00097,
KW   ECO:0000256|SAAS:SAAS00709833};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00097,
KW   ECO:0000256|SAAS:SAAS00709679}.
FT   DOMAIN       30    275       Phos_pyr_kin. {ECO:0000259|Pfam:PF08543}.
FT   DOMAIN      330    499       TMP-TENI. {ECO:0000259|Pfam:PF02581}.
FT   REGION      347    351       HMP-PP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   REGION      444    446       THZ-P binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   REGION      496    497       THZ-P binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   METAL       380    380       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   METAL       399    399       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   BINDING     379    379       HMP-PP. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   BINDING     418    418       HMP-PP. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   BINDING     447    447       HMP-PP. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   BINDING     476    476       THZ-P; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00097}.
SQ   SEQUENCE   538 AA;  56979 MW;  723D773D14D5F54D CRC64;
     MSSASGAVSP ADLSPVTDSR PVVWTIAGSD SGGGAGIQAD LHTLHDLGVH GCSVISAITA
     QNSVAVKMVD PVLMQTFTAQ IDALGLDLPP AAIKVGLLPT RLHVEVLARR LPTVDAPFVV
     YDPVAIASTG TPMAEPNMLE AVREQLLPRL SLITPNGPEL EALTGLPATS PELVRLAARR
     LRELGARAVL VKGGHLAWSG DLCLDYYQDE TREFWLTAPR LDTRHGHGTG CCYASAIAAV
     VAQDYPVEDA ITLARAYLQQ GLAAAQGVGA GPGPIAHLGW PADLAHFPRA VLAGSALDRR
     FGLYETSSAR LPQGPFAPTE HNLGLYPVVD SVKWLKRLLG AGVKTIQLRI KDLPAAQVAP
     AIRDAVALGR RHGARLFIND YWQQAIEAGA WGVHLGQEDM ETADLAAIQA AGLRLGISTH
     GYFELMRARE LAPSYIALGH IFPTNTKAMP SRPQGLKRLH RYRALMCDWP TVAIGGISEE
     RVAAVKESGV GSIALVSAIT ASDDWQGATE RLLAAVGAGD EPRSALLMTD MQEAAHAL
//

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