(data stored in ACNUC7421 zone)

SWISSPROT: THIG_PSEHT

ID   THIG_PSEHT              Reviewed;         263 AA.
AC   Q3IFN6;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 76.
DE   RecName: Full=Thiazole synthase {ECO:0000255|HAMAP-Rule:MF_00443};
DE            EC=2.8.1.10 {ECO:0000255|HAMAP-Rule:MF_00443};
GN   Name=thiG {ECO:0000255|HAMAP-Rule:MF_00443};
GN   OrderedLocusNames=PSHAa0483;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   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: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-
CC       phosphate (DXP) to produce the thiazole phosphate moiety of
CC       thiamine. Sulfur is provided by the thiocarboxylate moiety of the
CC       carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
CC       {ECO:0000255|HAMAP-Rule:MF_00443}.
CC   -!- CATALYTIC ACTIVITY: 1-deoxy-D-xylulose 5-phosphate + 2-
CC       iminoacetate + thiocarboxy-[sulfur-carrier protein ThiS] = 2-
CC       ((2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate +
CC       [sulfur-carrier protein ThiS] + 2 H(2)O. {ECO:0000255|HAMAP-
CC       Rule:MF_00443}.
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00443}.
CC   -!- SUBUNIT: Homotetramer. Forms heterodimers with either ThiH or
CC       ThiS. {ECO:0000255|HAMAP-Rule:MF_00443}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00443}.
CC   -!- SIMILARITY: Belongs to the ThiG family. {ECO:0000255|HAMAP-
CC       Rule:MF_00443}.
DR   EMBL; CR954246; CAI85579.1; -; Genomic_DNA.
DR   RefSeq; WP_011327192.1; NC_007481.1.
DR   ProteinModelPortal; Q3IFN6; -.
DR   SMR; Q3IFN6; -.
DR   STRING; 326442.PSHAa0483; -.
DR   EnsemblBacteria; CAI85579; CAI85579; PSHAa0483.
DR   KEGG; pha:PSHAa0483; -.
DR   PATRIC; fig|326442.8.peg.459; -.
DR   eggNOG; ENOG4105CA8; Bacteria.
DR   eggNOG; COG2022; LUCA.
DR   HOGENOM; HOG000248049; -.
DR   KO; K03149; -.
DR   OMA; AQYPSPA; -.
DR   OrthoDB; POG091H01K9; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; cd04728; ThiG; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00443; ThiG; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR033983; Thiazole_synthase_ThiG.
DR   InterPro; IPR008867; ThiG.
DR   Pfam; PF05690; ThiG; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IFN6.
DR   SWISS-2DPAGE; Q3IFN6.
KW   Complete proteome; Cytoplasm; Reference proteome; Schiff base;
KW   Thiamine biosynthesis; Transferase.
FT   CHAIN         1    263       Thiazole synthase.
FT                                /FTId=PRO_0000236355.
FT   REGION      188    189       DXP binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00443}.
FT   REGION      210    211       DXP binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00443}.
FT   ACT_SITE    100    100       Schiff-base intermediate with DXP.
FT                                {ECO:0000255|HAMAP-Rule:MF_00443}.
FT   BINDING     161    161       DXP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00443}.
SQ   SEQUENCE   263 AA;  28403 MW;  676B156556FCBFDF CRC64;
     MPNNDYLTIY GEQIKSRLLI GSALYPSPAV MNESIVASGA EIVTVSLRRQ QSAAAGDDFW
     QLIKNTGLKI LPNTAGCHSV KEAITLAKMC REVFATDWIK LELIGDDYNL QPDPFALLEA
     TKILIDDGFK VLPYCTDDLV LCQRLNALGC EVLMPWGAPI GTGKGLLNSY NLKTIRERLP
     EATLIVDAGL GLPSHACQAL ELGYDAVLLN SAIAGAGCPI TMSRAFKAAV EAGRFAYNAK
     AMPEKDVAAP STPTMGMPFW HQE
//

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