(data stored in ACNUC7421 zone)

SWISSPROT: C6WGQ8_ACTMD

ID   C6WGQ8_ACTMD            Unreviewed;       252 AA.
AC   C6WGQ8;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 65.
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=Amir_0407 {ECO:0000313|EMBL:ACU34374.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34374.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34374.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
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       ECO:0000256|SAAS:SAAS00709677}.
CC   -!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine +
CC       2-((2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate
CC       = diphosphate + thiamine phosphate + CO(2). {ECO:0000256|HAMAP-
CC       Rule:MF_00097, ECO:0000256|RuleBase:RU003826,
CC       ECO:0000256|SAAS:SAAS00709728}.
CC   -!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine +
CC       2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate = diphosphate +
CC       thiamine phosphate + CO(2). {ECO:0000256|HAMAP-Rule:MF_00097,
CC       ECO:0000256|RuleBase:RU003826, ECO:0000256|SAAS:SAAS00709678}.
CC   -!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine +
CC       4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine
CC       phosphate. {ECO:0000256|HAMAP-Rule:MF_00097,
CC       ECO:0000256|RuleBase:RU003826, ECO:0000256|SAAS:SAAS00709726}.
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|RuleBase:RU004253, ECO:0000256|SAAS:SAAS00709682}.
CC   -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00097, ECO:0000256|RuleBase:RU003826}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00097}.
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DR   EMBL; CP001630; ACU34374.1; -; Genomic_DNA.
DR   RefSeq; WP_012783037.1; NC_013093.1.
DR   ProteinModelPortal; C6WGQ8; -.
DR   STRING; 446462.Amir_0407; -.
DR   EnsemblBacteria; ACU34374; ACU34374; Amir_0407.
DR   KEGG; ami:Amir_0407; -.
DR   eggNOG; ENOG4107Y5I; Bacteria.
DR   eggNOG; COG0352; LUCA.
DR   HOGENOM; HOG000155781; -.
DR   KO; K00788; -.
DR   OMA; ITAFQFR; -.
DR   OrthoDB; POG091H01SL; -.
DR   UniPathway; UPA00060; UER00141.
DR   Proteomes; UP000002213; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP.
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   HAMAP; MF_00097; TMP_synthase; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR022998; ThiamineP_synth_TenI.
DR   InterPro; IPR034291; TMP_synthase.
DR   Pfam; PF02581; TMP-TENI; 2.
DR   SUPFAM; SSF51391; SSF51391; 2.
DR   TIGRFAMs; TIGR00693; thiE; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6WGQ8.
DR   SWISS-2DPAGE; C6WGQ8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
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   Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00097,
KW   ECO:0000256|RuleBase:RU003826, ECO:0000256|SAAS:SAAS00709833};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00097,
KW   ECO:0000256|RuleBase:RU003826, ECO:0000256|SAAS:SAAS00709679,
KW   ECO:0000313|EMBL:ACU34374.1}.
FT   DOMAIN       18    160       TMP-TENI. {ECO:0000259|Pfam:PF02581}.
FT   DOMAIN      198    228       TMP-TENI. {ECO:0000259|Pfam:PF02581}.
FT   REGION       44     48       HMP-PP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   REGION      142    144       THZ-P binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   METAL        77     77       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   METAL        96     96       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   BINDING      76     76       HMP-PP. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   BINDING     115    115       HMP-PP. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   BINDING     145    145       HMP-PP. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   BINDING     205    205       THZ-P; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00097}.
SQ   SEQUENCE   252 AA;  25682 MW;  323D82068CD37A64 CRC64;
     MPGLDATQIR RRLADARLYL CTPHRPDLAE FADAALAGGV DVVQLREKGM EARQELAALE
     VLAEACARHG ALLAVNDRAD VALAAGADVL HLGQDDLPVP LARRVVGEEV VIGRSTHDVA
     QASAAAVEPG VDYFCTGPCW PTPTKPGRPA PGLDLVRAVA GWDAARASAA GGPGGLGASG
     AGRPGAGAPG AGAAPPARPW FAIGGIDRHR LPEVISAGAR RVVVVRAITE SSDPRAAAAW
     LKIQLSGVPS SP
//

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