TRPC_STAAE
ID TRPC_STAAE Reviewed; 260 AA.
AC A6QGS2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=NWMN_1282;
OS Staphylococcus aureus (strain Newman).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=426430;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Newman;
RX PubMed=17951380; DOI=10.1128/jb.01000-07;
RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT analysis of staphylococcal genomes: polymorphism and evolution of two major
RT pathogenicity islands.";
RL J. Bacteriol. 190:300-310(2008).
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; AP009351; BAF67554.1; -; Genomic_DNA.
DR RefSeq; WP_000154118.1; NZ_CP023390.1.
DR AlphaFoldDB; A6QGS2; -.
DR SMR; A6QGS2; -.
DR EnsemblBacteria; BAF67554; BAF67554; NWMN_1282.
DR KEGG; sae:NWMN_1282; -.
DR HOGENOM; CLU_034247_2_1_9; -.
DR OMA; RGPHDLI; -.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000006386; 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_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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Decarboxylase;
KW Lyase; Tryptophan biosynthesis.
FT CHAIN 1..260
FT /note="Indole-3-glycerol phosphate synthase"
FT /id="PRO_1000095892"
SQ SEQUENCE 260 AA; 29557 MW; 6861BD29CFFB91D4 CRC64;
MTILSEIVKY KQSLLQNGYY QDKLNTLKSV KIQNKKSFIN AIEKEPKLAI IAEIKSKSPT
VNDLPERDLS QQISDYDQYG ANAVSILTDE KYFSGSFERL QALTTKTTLP VLCKDFIIDP
LQIDVAKQAG ASMILLIVNI LSDKQLKDLY NYAISQNLEV LVEVHDRHEL ERAYKVNAKL
IGVNNRDLKR FVTNVEHTNT ILENKKTNHY YISESGIHDA SDVRKILHSG IDGLLIGEAL
MRCDNLSEFL PQLKMQKVKS