TRPC_STAAR
ID TRPC_STAAR Reviewed; 260 AA.
AC Q6GH35;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=SAR1383;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG40381.1; -; Genomic_DNA.
DR RefSeq; WP_000153717.1; NC_002952.2.
DR AlphaFoldDB; Q6GH35; -.
DR SMR; Q6GH35; -.
DR KEGG; sar:SAR1383; -.
DR HOGENOM; CLU_034247_2_1_9; -.
DR OMA; RGPHDLI; -.
DR OrthoDB; 1789381at2; -.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000000596; 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_0000154252"
SQ SEQUENCE 260 AA; 29620 MW; DB0DE43B5F4B8793 CRC64;
MTILEEIVEY KQLLLQNGYY QDKLNTLKSV NIQNKKSFIN AIEKEPKLAI IAEIKSKSPT
VNDLPERDLS QQISDYEQYG ANAVSILTDE KYFGGSFERL QALTTKTTLP VLCKDFIIDP
LQIDVAKQAG ASMILLIVNI LSDKQLKDLY NYAISQNLEV LVEVHDRHEL ERAYKVNAKL
IGVNNRDLKR FVTNVEHTNT ILENKKPNHY YISESGIHDV SDVRKILHSG IDGLLIGEAL
MRCDNLSEFL PQLKMQKVKS