(data stored in ACNUC29543 zone)

SWISSPROT: A5GQ00_SYNR3

ID   A5GQ00_SYNR3            Unreviewed;       280 AA.
AC   A5GQ00;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 70.
DE   RecName: Full=Thiazole synthase {ECO:0000256|HAMAP-Rule:MF_00443, ECO:0000256|SAAS:SAAS00958550};
DE            EC=2.8.1.10 {ECO:0000256|HAMAP-Rule:MF_00443, ECO:0000256|SAAS:SAAS00958549};
GN   Name=thiG {ECO:0000256|HAMAP-Rule:MF_00443,
GN   ECO:0000313|EMBL:CAK26959.1};
GN   OrderedLocusNames=SynRCC307_0056 {ECO:0000313|EMBL:CAK26959.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK26959.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00443, ECO:0000256|SAAS:SAAS00958548}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate +
CC         [sulfur-carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH = 2-
CC         [(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate
CC         + [sulfur-carrier protein ThiS]-C-terminal Gly-Gly + 2 H(+) + 2
CC         H2O; Xref=Rhea:RHEA:26297, Rhea:RHEA-COMP:12908, Rhea:RHEA-
CC         COMP:12909, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57792, ChEBI:CHEBI:62899, ChEBI:CHEBI:77846,
CC         ChEBI:CHEBI:90619, ChEBI:CHEBI:90778; EC=2.8.1.10;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00443,
CC         ECO:0000256|SAAS:SAAS01116553};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00443, ECO:0000256|SAAS:SAAS00958556}.
CC   -!- SUBUNIT: Homotetramer. Forms heterodimers with either ThiH or
CC       ThiS. {ECO:0000256|HAMAP-Rule:MF_00443,
CC       ECO:0000256|SAAS:SAAS00958543}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00443,
CC       ECO:0000256|SAAS:SAAS00963437}.
CC   -!- SIMILARITY: Belongs to the ThiG family. {ECO:0000256|HAMAP-
CC       Rule:MF_00443, ECO:0000256|SAAS:SAAS00958557}.
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DR   EMBL; CT978603; CAK26959.1; -; Genomic_DNA.
DR   STRING; 316278.SynRCC307_0056; -.
DR   EnsemblBacteria; CAK26959; CAK26959; SynRCC307_0056.
DR   KEGG; syr:SynRCC307_0056; -.
DR   eggNOG; ENOG4105CA8; Bacteria.
DR   eggNOG; COG2022; LUCA.
DR   HOGENOM; HOG000248049; -.
DR   KO; K03149; -.
DR   OMA; AQYPSPA; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000001115; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016783; F:sulfurtransferase 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; 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   PANTHER; PTHR34266; PTHR34266; 1.
DR   Pfam; PF05690; ThiG; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GQ00.
DR   SWISS-2DPAGE; A5GQ00.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00443,
KW   ECO:0000256|SAAS:SAAS00963440};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
KW   Schiff base {ECO:0000256|HAMAP-Rule:MF_00443,
KW   ECO:0000256|SAAS:SAAS00664421};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00443,
KW   ECO:0000256|SAAS:SAAS00958544};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00443,
KW   ECO:0000256|SAAS:SAAS00958551}.
FT   DOMAIN       24    274       ThiG. {ECO:0000259|Pfam:PF05690}.
FT   REGION      209    210       DXP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00443}.
FT   REGION      231    232       DXP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00443}.
FT   ACT_SITE    122    122       Schiff-base intermediate with DXP.
FT                                {ECO:0000256|HAMAP-Rule:MF_00443}.
FT   BINDING     183    183       DXP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00443}.
SQ   SEQUENCE   280 AA;  28873 MW;  969890E4FD3FBB47 CRC64;
     MRKAGATPHD QIMATTTQDT PLQIGSRCFN SRLMTGTGKY PDIPSLQQSI EASGCEIVTV
     AVRRVQSGAP GHGGLMEAID WTKIWMLPNT AGCTTAEDAV RVARLGRELA ALAGQSDNTF
     VKLEVIPEGS YLLPDPIGTL EAAEQLVAEG FTVLPYINAD PLLARRLEAV GCATVMPLAS
     PIGSGQGLAN LANIKLIIEA ASVPVVVDAG IGVPSDAALA MEIGADALLI NSAIALSGHP
     PTTARAMALA AEAGRLSHLS GAMPKRAHAS ASSPQQGRIT
//

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