(data stored in ACNUC1104 zone)

SWISSPROT: D3VIV6_XENNA

ID   D3VIV6_XENNA            Unreviewed;       255 AA.
AC   D3VIV6;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 54.
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:CBJ88656.1};
GN   OrderedLocusNames=XNC1_0582 {ECO:0000313|EMBL:CBJ88656.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88656.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88656.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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; FN667742; CBJ88656.1; -; Genomic_DNA.
DR   RefSeq; WP_010848938.1; NC_014228.1.
DR   STRING; 406817.XNC1_0582; -.
DR   EnsemblBacteria; CBJ88656; CBJ88656; XNC1_0582.
DR   KEGG; xne:XNC1_0582; -.
DR   eggNOG; ENOG4105CA8; Bacteria.
DR   eggNOG; COG2022; LUCA.
DR   HOGENOM; HOG000248049; -.
DR   KO; K03149; -.
DR   OMA; AQYPSPA; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000008075; 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; D3VIV6.
DR   SWISS-2DPAGE; D3VIV6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00443,
KW   ECO:0000256|SAAS:SAAS00963440};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
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        3    247       ThiG. {ECO:0000259|Pfam:PF05690}.
FT   REGION      182    183       DXP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00443}.
FT   REGION      204    205       DXP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00443}.
FT   ACT_SITE     95     95       Schiff-base intermediate with DXP.
FT                                {ECO:0000256|HAMAP-Rule:MF_00443}.
FT   BINDING     156    156       DXP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00443}.
SQ   SEQUENCE   255 AA;  26842 MW;  A391CD781677DE28 CRC64;
     MLKIADTTFH SRLFTGTGKF ANAGLMIDAI RASGSQLVTM AMKRIDLHGN DDGILVPLQQ
     LGVKLLPNTS GAKTAEEAVF AARLAKEALG THWVKLEIHP DVKYLLPDPI ETLKAAEQLL
     KEGFIVLPYC GADPVLCRRL EEAGCAAVMP LGAPIGSNKG LLTRDFLQII IEQANVPVVV
     DAGIGAPSHA LTAIEMGADA VLVNTAIAVA RHPVKMAQAF KTAIEAGELS HQAGVASQKS
     HAETSSPLTD FLGAL
//

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