(data stored in ACNUC7421 zone)

SWISSPROT: Q3IFN5_PSEHT

ID   Q3IFN5_PSEHT            Unreviewed;       508 AA.
AC   Q3IFN5;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 91.
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=thiDE {ECO:0000313|EMBL:CAI85580.1};
GN   Synonyms=thiE {ECO:0000256|HAMAP-Rule:MF_00097};
GN   OrderedLocusNames=PSHAa0484 {ECO:0000313|EMBL:CAI85580.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85580.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85580.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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: 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|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|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|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|SAAS:SAAS00709682}.
CC   -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00097}.
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; CR954246; CAI85580.1; -; Genomic_DNA.
DR   RefSeq; WP_011327193.1; NC_007481.1.
DR   ProteinModelPortal; Q3IFN5; -.
DR   STRING; 326442.PSHAa0484; -.
DR   EnsemblBacteria; CAI85580; CAI85580; PSHAa0484.
DR   KEGG; pha:PSHAa0484; -.
DR   PATRIC; fig|326442.8.peg.460; -.
DR   eggNOG; ENOG4108F0B; Bacteria.
DR   eggNOG; COG0351; LUCA.
DR   eggNOG; COG0352; LUCA.
DR   HOGENOM; HOG000155781; -.
DR   KO; K14153; -.
DR   OMA; PIVWTIA; -.
DR   OrthoDB; POG091H01V0; -.
DR   UniPathway; UPA00060; UER00141.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
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; 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; 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; Q3IFN5.
DR   SWISS-2DPAGE; Q3IFN5.
KW   ATP-binding {ECO:0000256|SAAS:SAAS00440402};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Kinase {ECO:0000256|SAAS:SAAS00440394, ECO:0000313|EMBL:CAI85580.1};
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:SAAS00228482};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
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, ECO:0000313|EMBL:CAI85580.1}.
FT   DOMAIN       12    266       Phos_pyr_kin. {ECO:0000259|Pfam:PF08543}.
FT   DOMAIN      321    490       TMP-TENI. {ECO:0000259|Pfam:PF02581}.
FT   REGION      338    342       HMP-PP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   REGION      435    437       THZ-P binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   METAL       371    371       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   METAL       390    390       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   BINDING     370    370       HMP-PP. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   BINDING     409    409       HMP-PP. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   BINDING     438    438       HMP-PP. {ECO:0000256|HAMAP-Rule:
FT                                MF_00097}.
FT   BINDING     467    467       THZ-P; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00097}.
SQ   SEQUENCE   508 AA;  54755 MW;  D57957A6FB489019 CRC64;
     MNNVVWTIAG SDSGGGAGIQ ADIKAMQSFG VHGCTAITAL TAQNSLGVEA INAVSTDIIE
     SQLLALEKDM KAKVIKIGML ANVQQIQLIS EHISHYKAKW PVPPVIVYDP VAIASSGDLL
     TEEDTVSAIK ECLLPLVDVI TPNTHETQLL TGVYLIGPAA IKEAANKLLS WGAKAVVIKG
     GHWDYPSGYC IDYCINNFTQ KGEEYWLGNE KIQTPHNHGT GCSMASVIAA CLAKDYPLKD
     AFILAKAYIN QGLKVAVRYG EGIGPVAQTS FPTNLADYPQ VIEAGSWLGD ELDFDVPLDF
     NMAADFAPCE SKSLGLYAVV DSVDWLEKCL QQGVKTVQLR VKNKDDAQLD ELVAKAVALG
     EQYNAQVFIN DYWQLAIKHG AYGVHLGQQD LENTNLAAIK NAGLRLGLST HGFYEMLRAH
     NYRPSYLAFG AIYPTTTKDM TGQIQGLEKL FKFVPLMQSY PTVAIGGIDL KRASQVAKTG
     VGSVAVVRAI SEADDYVQAI SALQAAIN
//

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