TRPC2_STRCO
ID TRPC2_STRCO Reviewed; 258 AA.
AC Q9Z4X0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Indole-3-glycerol phosphate synthase 2;
DE Short=IGPS 2;
DE EC=4.1.1.48;
GN Name=trpC2; OrderedLocusNames=SCO3211; ORFNames=SCE8.04c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- FUNCTION: The function of the second trp operon in S.coelicolor is to
CC produce tryptophane for the biosynthesis of calcium-dependent
CC antibiotic (CDA).
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 -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 4/5.
CC -!- SIMILARITY: Belongs to the TrpC family. {ECO:0000305}.
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DR EMBL; AL939115; CAB38582.1; -; Genomic_DNA.
DR PIR; T36303; T36303.
DR RefSeq; NP_627425.1; NC_003888.3.
DR RefSeq; WP_011028830.1; NZ_VNID01000013.1.
DR AlphaFoldDB; Q9Z4X0; -.
DR SMR; Q9Z4X0; -.
DR STRING; 100226.SCO3211; -.
DR GeneID; 1098645; -.
DR KEGG; sco:SCO3211; -.
DR PATRIC; fig|100226.15.peg.3271; -.
DR eggNOG; COG0134; Bacteria.
DR HOGENOM; CLU_034247_2_0_11; -.
DR InParanoid; Q9Z4X0; -.
DR OMA; REIVWQK; -.
DR PhylomeDB; Q9Z4X0; -.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IBA:GO_Central.
DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IBA:GO_Central.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
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; Antibiotic biosynthesis;
KW Aromatic amino acid biosynthesis; Decarboxylase; Lyase; Reference proteome;
KW Tryptophan biosynthesis.
FT CHAIN 1..258
FT /note="Indole-3-glycerol phosphate synthase 2"
FT /id="PRO_0000154260"
SQ SEQUENCE 258 AA; 26816 MW; B2A31BF4B5C6428A CRC64;
MSGILAGLVA EAESQTGRRR ALRTEAKLTE LAAAAPPARD FAAALREPGL AVIAEMKPRS
PSKGPLTDDY RPAELARAYQ GGGAHAVSVL THEAGFGGSP DHLAVARAAC ELPVLRKDFV
VDEYQILEAR ALGADALLLI VAALAPARLA ALLARTRACG MEALVEVHDE REVDVALEAG
ADVIGVNHRD LRDFSIDRTL SARLRGRVGT GRVMVGESGV RGAPDARALE AAGVDAVLVG
ELLMRAGDPG TTIKGLVG