(data stored in SCRATCH zone)

SWISSPROT: C6WGR1_ACTMD

ID   C6WGR1_ACTMD            Unreviewed;       262 AA.
AC   C6WGR1;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 56.
DE   RecName: Full=Thiazole synthase {ECO:0000256|HAMAP-Rule:MF_00443, ECO:0000256|SAAS:SAAS00664431};
DE            EC=2.8.1.10 {ECO:0000256|HAMAP-Rule:MF_00443, ECO:0000256|SAAS:SAAS00664422};
GN   Name=thiG {ECO:0000256|HAMAP-Rule:MF_00443};
GN   OrderedLocusNames=Amir_0410 {ECO:0000313|EMBL:ACU34377.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34377.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34377.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
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:SAAS00664436}.
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:0000256|HAMAP-
CC       Rule:MF_00443, ECO:0000256|SAAS:SAAS00664446}.
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00443, ECO:0000256|SAAS:SAAS00664440}.
CC   -!- SUBUNIT: Homotetramer. Forms heterodimers with either ThiH or
CC       ThiS. {ECO:0000256|HAMAP-Rule:MF_00443,
CC       ECO:0000256|SAAS:SAAS00664441}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00443,
CC       ECO:0000256|SAAS:SAAS00666772}.
CC   -!- SIMILARITY: Belongs to the ThiG family. {ECO:0000256|HAMAP-
CC       Rule:MF_00443, ECO:0000256|SAAS:SAAS00664444}.
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DR   EMBL; CP001630; ACU34377.1; -; Genomic_DNA.
DR   RefSeq; WP_012783040.1; NC_013093.1.
DR   ProteinModelPortal; C6WGR1; -.
DR   STRING; 446462.Amir_0410; -.
DR   EnsemblBacteria; ACU34377; ACU34377; Amir_0410.
DR   KEGG; ami:Amir_0410; -.
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; UP000002213; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016783; F:sulfurtransferase 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; 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; C6WGR1.
DR   SWISS-2DPAGE; C6WGR1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00443,
KW   ECO:0000256|SAAS:SAAS00666777};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213};
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:SAAS00664428};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00443,
KW   ECO:0000256|SAAS:SAAS00664434}.
FT   DOMAIN       16    258       ThiG. {ECO:0000259|Pfam:PF05690}.
FT   REGION      193    194       DXP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00443}.
FT   REGION      215    216       DXP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00443}.
FT   ACT_SITE    106    106       Schiff-base intermediate with DXP.
FT                                {ECO:0000256|HAMAP-Rule:MF_00443}.
FT   BINDING     167    167       DXP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00443}.
SQ   SEQUENCE   262 AA;  27315 MW;  496FE93D704DFB79 CRC64;
     MTEPDRIAPA PDPLRIADRE FTSRLITGTG GATNLTVLER ALRASGTELT TVALRRADGS
     GGTGVLQLLR RLGIDLLPNT AGCRTAAEAV LTARLAREAL GTSWVKLEVH ADDRTLLPDP
     VETLDAARRL VADGFTVLPY TNDDPVLALR LEDAGCAAVM PLGSPIGTGL GIRNPHNLEL
     IVARASVPVI LDAGVGTASD AAVAMELGCA AVLLATAVTR AQDPELMASA MRSAVRAGRW
     ARLAGRAPKR FWAHASSPAP DA
//

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