TRPC_CAMJE
ID TRPC_CAMJE Reviewed; 258 AA.
AC Q9PI11; Q0PB15;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Indole-3-glycerol phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00134};
DE Short=IGPS {ECO:0000255|HAMAP-Rule:MF_00134};
DE EC=4.1.1.48 {ECO:0000255|HAMAP-Rule:MF_00134};
GN Name=trpC {ECO:0000255|HAMAP-Rule:MF_00134}; OrderedLocusNames=Cj0498;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+)
CC = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O;
CC Xref=Rhea:RHEA:23476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58613, ChEBI:CHEBI:58866; EC=4.1.1.48;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00134};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 4/5. {ECO:0000255|HAMAP-
CC Rule:MF_00134}.
CC -!- SIMILARITY: Belongs to the TrpC family. {ECO:0000255|HAMAP-
CC Rule:MF_00134}.
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DR EMBL; AL111168; CAL34646.1; -; Genomic_DNA.
DR PIR; E81395; E81395.
DR RefSeq; WP_002854779.1; NC_002163.1.
DR RefSeq; YP_002343932.1; NC_002163.1.
DR PDB; 6BMA; X-ray; 1.98 A; A/B=1-258.
DR PDBsum; 6BMA; -.
DR AlphaFoldDB; Q9PI11; -.
DR SMR; Q9PI11; -.
DR IntAct; Q9PI11; 4.
DR STRING; 192222.Cj0498; -.
DR PaxDb; Q9PI11; -.
DR PRIDE; Q9PI11; -.
DR EnsemblBacteria; CAL34646; CAL34646; Cj0498.
DR GeneID; 904828; -.
DR KEGG; cje:Cj0498; -.
DR PATRIC; fig|192222.6.peg.490; -.
DR eggNOG; COG0134; Bacteria.
DR HOGENOM; CLU_034247_2_0_7; -.
DR OMA; RGPHDLI; -.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00331; IGPS; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00134_A; IGPS_A; 1.
DR HAMAP; MF_00134_B; IGPS_B; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR045186; Indole-3-glycerol_P_synth.
DR InterPro; IPR013798; Indole-3-glycerol_P_synth_dom.
DR InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR22854; PTHR22854; 1.
DR Pfam; PF00218; IGPS; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR PROSITE; PS00614; IGPS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Decarboxylase; Lyase; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..258
FT /note="Indole-3-glycerol phosphate synthase"
FT /id="PRO_0000154218"
FT HELIX 2..20
FT /evidence="ECO:0007829|PDB:6BMA"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:6BMA"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:6BMA"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:6BMA"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:6BMA"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:6BMA"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:6BMA"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:6BMA"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:6BMA"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:6BMA"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:6BMA"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:6BMA"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:6BMA"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:6BMA"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:6BMA"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:6BMA"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:6BMA"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:6BMA"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:6BMA"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:6BMA"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:6BMA"
FT HELIX 201..205
FT /evidence="ECO:0007829|PDB:6BMA"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:6BMA"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:6BMA"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:6BMA"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:6BMA"
FT HELIX 242..246
FT /evidence="ECO:0007829|PDB:6BMA"
FT HELIX 250..257
FT /evidence="ECO:0007829|PDB:6BMA"
SQ SEQUENCE 258 AA; 29573 MW; E7CB15E30CBE41C9 CRC64;
MILDKIFEKT KEDLKERKLK LPYDMLGRSL ASNPFFPKDV IKALKRVEKE VKIIAEVKKA
SPSKGVIRED FDPLSIALNY EKNKAAAISV LTEPHFFKGS LEYLSLIRRY TQIPLLRKDF
IFDEYQILEA LVYGADFVLL IAKMLSMKEL KKLLEFARHL GLEALVEIHD KEDLSKAIFA
GADIIGINHR NLEDFTMDMS LCEKLIPQIP NSKIIIAESG LENKEFLEHL QNLGVDAFLI
GEYFMREKDE GKALKALL
