THIG_MYCTU
ID THIG_MYCTU Reviewed; 252 AA.
AC P9WG73; L0T6E5; P96263;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
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}; OrderedLocusNames=Rv0417;
GN ORFNames=MTCY22G10.14;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate
CC (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is
CC provided by the thiocarboxylate moiety of the carrier protein ThiS. In
CC vitro, sulfur can be provided by H(2)S. {ECO:0000255|HAMAP-
CC Rule:MF_00443}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + [sulfur-
CC carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH = 2-[(2R,5Z)-2-
CC carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-
CC carrier protein ThiS]-C-terminal Gly-Gly + 2 H(+) + 2 H2O;
CC Xref=Rhea:RHEA:26297, Rhea:RHEA-COMP:12908, Rhea:RHEA-COMP:12909,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57792,
CC ChEBI:CHEBI:62899, ChEBI:CHEBI:77846, ChEBI:CHEBI:90619,
CC ChEBI:CHEBI:90778; EC=2.8.1.10; Evidence={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 ThiS.
CC {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}.
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DR EMBL; AL123456; CCP43148.1; -; Genomic_DNA.
DR PIR; G70629; G70629.
DR RefSeq; NP_214931.1; NC_000962.3.
DR RefSeq; WP_003916659.1; NZ_NVQJ01000002.1.
DR PDB; 5Z9Y; X-ray; 1.48 A; A/B=2-252.
DR PDBsum; 5Z9Y; -.
DR AlphaFoldDB; P9WG73; -.
DR SMR; P9WG73; -.
DR STRING; 83332.Rv0417; -.
DR PaxDb; P9WG73; -.
DR DNASU; 886396; -.
DR GeneID; 886396; -.
DR KEGG; mtu:Rv0417; -.
DR TubercuList; Rv0417; -.
DR eggNOG; COG2022; Bacteria.
DR OMA; PHNFQLI; -.
DR PhylomeDB; P9WG73; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990107; F:thiazole synthase activity; IEA:RHEA.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Schiff base;
KW Thiamine biosynthesis; Transferase.
FT CHAIN 1..252
FT /note="Thiazole synthase"
FT /id="PRO_0000162832"
FT ACT_SITE 98
FT /note="Schiff-base intermediate with DXP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT BINDING 159
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT BINDING 185..186
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT BINDING 207..208
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:5Z9Y"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:5Z9Y"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:5Z9Y"
FT HELIX 27..37
FT /evidence="ECO:0007829|PDB:5Z9Y"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:5Z9Y"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:5Z9Y"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:5Z9Y"
FT HELIX 78..92
FT /evidence="ECO:0007829|PDB:5Z9Y"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:5Z9Y"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:5Z9Y"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:5Z9Y"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:5Z9Y"
FT HELIX 137..146
FT /evidence="ECO:0007829|PDB:5Z9Y"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:5Z9Y"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:5Z9Y"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:5Z9Y"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:5Z9Y"
FT HELIX 190..198
FT /evidence="ECO:0007829|PDB:5Z9Y"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:5Z9Y"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:5Z9Y"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:5Z9Y"
FT HELIX 216..236
FT /evidence="ECO:0007829|PDB:5Z9Y"
SQ SEQUENCE 252 AA; 25878 MW; C1B4DC1492B7920E CRC64;
MAESKLVIGD RSFASRLIMG TGGATNLAVL EQALIASGTE LTTVAIRRVD ADGGTGLLDL
LNRLGITPLP NTAGSRSAAE AVLTAQLARE ALNTNWVKLE VIADERTLWP DAVELVRAAE
QLVDDGFVVL PYTTDDPVLA RRLEDTGCAA VMPLGSPIGT GLGIANPHNI EMIVAGARVP
VVLDAGIGTA SDAALAMELG CDAVLLASAV TRAADPPAMA AAMAAAVTAG YLARCAGRIP
KRFWAQASSP AR
