TRPC_BRUA2
ID TRPC_BRUA2 Reviewed; 268 AA.
AC Q2YRR4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=BAB1_1164;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM040264; CAJ11120.1; -; Genomic_DNA.
DR RefSeq; WP_002964269.1; NZ_KN046823.1.
DR PDB; 3TSM; X-ray; 2.15 A; A/B=1-268.
DR PDBsum; 3TSM; -.
DR AlphaFoldDB; Q2YRR4; -.
DR SMR; Q2YRR4; -.
DR STRING; 359391.BAB1_1164; -.
DR EnsemblBacteria; CAJ11120; CAJ11120; BAB1_1164.
DR GeneID; 45052184; -.
DR GeneID; 55590824; -.
DR KEGG; bmf:BAB1_1164; -.
DR PATRIC; fig|359391.11.peg.62; -.
DR HOGENOM; CLU_034247_2_0_5; -.
DR OMA; RGPHDLI; -.
DR PhylomeDB; Q2YRR4; -.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000002719; Chromosome I.
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_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..268
FT /note="Indole-3-glycerol phosphate synthase"
FT /id="PRO_1000018448"
FT HELIX 5..34
FT /evidence="ECO:0007829|PDB:3TSM"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:3TSM"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:3TSM"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3TSM"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:3TSM"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:3TSM"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:3TSM"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:3TSM"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:3TSM"
FT HELIX 105..113
FT /evidence="ECO:0007829|PDB:3TSM"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:3TSM"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:3TSM"
FT HELIX 129..136
FT /evidence="ECO:0007829|PDB:3TSM"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:3TSM"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:3TSM"
FT HELIX 151..163
FT /evidence="ECO:0007829|PDB:3TSM"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:3TSM"
FT HELIX 175..181
FT /evidence="ECO:0007829|PDB:3TSM"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:3TSM"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:3TSM"
FT HELIX 204..212
FT /evidence="ECO:0007829|PDB:3TSM"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:3TSM"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:3TSM"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:3TSM"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:3TSM"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:3TSM"
FT HELIX 254..263
FT /evidence="ECO:0007829|PDB:3TSM"
SQ SEQUENCE 268 AA; 29269 MW; 7BDF1668C6EAEC55 CRC64;
MSTDILRKIE AYKREEIAAA KARLALDELK ARTRDQSAPR GFLKALEAKR AAGQFALIAE
IKKASPSKGL IRPDFDPPAL AKAYEEGGAA CLSVLTDTPS FQGAPEFLTA ARQACSLPAL
RKDFLFDPYQ VYEARSWGAD CILIIMASVD DDLAKELEDT AFALGMDALI EVHDEAEMER
ALKLSSRLLG VNNRNLRSFE VNLAVSERLA KMAPSDRLLV GESGIFTHED CLRLEKSGIG
TFLIGESLMR QHDVAAATRA LLTGAEKL
