THIG_PSEAE
ID THIG_PSEAE Reviewed; 265 AA.
AC Q9I6B4;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=PA0381;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RG New York structural genomics research consortium (NYSGRC);
RT "Crystal structure of thiamine biosynthesis protein from Pseudomonas
RT aeruginosa.";
RL Submitted (FEB-2009) to the PDB data bank.
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; AE004091; AAG03770.1; -; Genomic_DNA.
DR PIR; E83599; E83599.
DR RefSeq; NP_249072.1; NC_002516.2.
DR RefSeq; WP_003084517.1; NZ_QZGE01000016.1.
DR PDB; 1WV2; X-ray; 2.90 A; A/B=1-265.
DR PDBsum; 1WV2; -.
DR AlphaFoldDB; Q9I6B4; -.
DR SMR; Q9I6B4; -.
DR STRING; 287.DR97_3348; -.
DR PaxDb; Q9I6B4; -.
DR PRIDE; Q9I6B4; -.
DR DNASU; 879802; -.
DR EnsemblBacteria; AAG03770; AAG03770; PA0381.
DR GeneID; 879802; -.
DR KEGG; pae:PA0381; -.
DR PATRIC; fig|208964.12.peg.401; -.
DR PseudoCAP; PA0381; -.
DR HOGENOM; CLU_062233_1_1_6; -.
DR InParanoid; Q9I6B4; -.
DR OMA; PHNFQLI; -.
DR PhylomeDB; Q9I6B4; -.
DR BioCyc; PAER208964:G1FZ6-385-MON; -.
DR UniPathway; UPA00060; -.
DR EvolutionaryTrace; Q9I6B4; -.
DR Proteomes; UP000002438; 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..265
FT /note="Thiazole synthase"
FT /id="PRO_0000162845"
FT ACT_SITE 107
FT /note="Schiff-base intermediate with DXP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT BINDING 168
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT BINDING 194..195
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT BINDING 216..217
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1WV2"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:1WV2"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:1WV2"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1WV2"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:1WV2"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:1WV2"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:1WV2"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1WV2"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:1WV2"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:1WV2"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:1WV2"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:1WV2"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:1WV2"
FT HELIX 121..132
FT /evidence="ECO:0007829|PDB:1WV2"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:1WV2"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:1WV2"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:1WV2"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:1WV2"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1WV2"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:1WV2"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:1WV2"
FT HELIX 199..208
FT /evidence="ECO:0007829|PDB:1WV2"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:1WV2"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:1WV2"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:1WV2"
FT HELIX 225..245
FT /evidence="ECO:0007829|PDB:1WV2"
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
