(data stored in ACNUC7421 zone)

SWISSPROT: THIG_PSEAB

ID   THIG_PSEAB              Reviewed;         265 AA.
AC   Q02U32;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   07-JUN-2017, entry version 63.
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=PA14_04980;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ15347.1; -; Genomic_DNA.
DR   RefSeq; WP_003084517.1; NC_008463.1.
DR   ProteinModelPortal; Q02U32; -.
DR   SMR; Q02U32; -.
DR   EnsemblBacteria; ABJ15347; ABJ15347; PA14_04980.
DR   KEGG; pau:PA14_04980; -.
DR   HOGENOM; HOG000248049; -.
DR   KO; K03149; -.
DR   OMA; AQYPSPA; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000000653; Chromosome.
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; Q02U32.
DR   SWISS-2DPAGE; Q02U32.
KW   Complete proteome; Cytoplasm; Schiff base; Thiamine biosynthesis;
KW   Transferase.
FT   CHAIN         1    265       Thiazole synthase.
FT                                /FTId=PRO_1000026027.
FT   REGION      194    195       DXP binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00443}.
FT   REGION      216    217       DXP binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00443}.
FT   ACT_SITE    107    107       Schiff-base intermediate with DXP.
FT                                {ECO:0000255|HAMAP-Rule:MF_00443}.
FT   BINDING     168    168       DXP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00443}.
SQ   SEQUENCE   265 AA;  28235 MW;  EE3F74F94F0501E2 CRC64;
     MSQASSTDTP FVIAGRTYGS RLLVGTGKYK DLDETRRAIE ASGAEIVTVA VRRTNIGQNP
     DEPNLLDVIP PDRYTILPNT AGCYDAVEAV RTCRLARELL DGHNLVKLEV LADQKTLFPN
     VVETLKAAEQ LVKDGFDVMV YTSDDPIIAR QLAEIGCIAV MPLAGLIGSG LGICNPYNLR
     IILEEAKVPV LVDAGVGTAS DAAIAMELGC EAVLMNTAIA HAKDPVMMAE AMKHAIVAGR
     LAYLAGRMPR KLYASASSPL DGLID
//

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