TRPC_YERPE
ID TRPC_YERPE Reviewed; 475 AA.
AC Q8ZEG8; Q0WEW2;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Tryptophan biosynthesis protein TrpCF;
DE Includes:
DE RecName: Full=Indole-3-glycerol phosphate synthase;
DE Short=IGPS;
DE EC=4.1.1.48;
DE Includes:
DE RecName: Full=N-(5'-phospho-ribosyl)anthranilate isomerase;
DE Short=PRAI;
DE EC=5.3.1.24;
GN Name=trpC; OrderedLocusNames=YPO2205, y2049, YP_2003;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes two sequential steps of
CC tryptophan biosynthetic pathway. The first reaction is catalyzed by the
CC isomerase, coded by the TrpF domain; the second reaction is catalyzed
CC by the synthase, coded by the TrpC domain (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-
CC carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate;
CC Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613;
CC EC=5.3.1.24;
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 3/5.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 4/5.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the TrpC family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the TrpF family.
CC {ECO:0000305}.
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DR EMBL; AL590842; CAL20834.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM85614.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS62219.1; -; Genomic_DNA.
DR PIR; AG0268; AG0268.
DR RefSeq; WP_002210632.1; NZ_WUCM01000001.1.
DR RefSeq; YP_002347176.1; NC_003143.1.
DR AlphaFoldDB; Q8ZEG8; -.
DR SMR; Q8ZEG8; -.
DR IntAct; Q8ZEG8; 2.
DR STRING; 214092.YPO2205; -.
DR PaxDb; Q8ZEG8; -.
DR PRIDE; Q8ZEG8; -.
DR DNASU; 1146996; -.
DR EnsemblBacteria; AAM85614; AAM85614; y2049.
DR EnsemblBacteria; AAS62219; AAS62219; YP_2003.
DR GeneID; 57976462; -.
DR KEGG; ype:YPO2205; -.
DR KEGG; ypk:y2049; -.
DR KEGG; ypm:YP_2003; -.
DR PATRIC; fig|214092.21.peg.2602; -.
DR eggNOG; COG0134; Bacteria.
DR eggNOG; COG0135; Bacteria.
DR HOGENOM; CLU_007713_0_1_6; -.
DR OMA; YDIIGIN; -.
DR UniPathway; UPA00035; UER00042.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR CDD; cd00331; IGPS; 1.
DR CDD; cd00405; PRAI; 1.
DR Gene3D; 3.20.20.70; -; 2.
DR HAMAP; MF_00134_B; IGPS_B; 1.
DR HAMAP; MF_00135; PRAI; 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; IPR001240; PRAI_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR22854; PTHR22854; 1.
DR Pfam; PF00218; IGPS; 1.
DR Pfam; PF00697; PRAI; 1.
DR SUPFAM; SSF51366; SSF51366; 2.
DR PROSITE; PS00614; IGPS; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Decarboxylase;
KW Isomerase; Lyase; Multifunctional enzyme; Reference proteome;
KW Tryptophan biosynthesis.
FT CHAIN 1..475
FT /note="Tryptophan biosynthesis protein TrpCF"
FT /id="PRO_0000154287"
FT REGION 1..279
FT /note="Indole-3-glycerol phosphate synthase"
FT REGION 280..475
FT /note="N-(5'-phosphoribosyl)anthranilate isomerase"
SQ SEQUENCE 475 AA; 52117 MW; 181CF84E2F15F2FB CRC64;
MQETGGYKTE GYNVGSDKVD SDKTKTVLHQ IVHDKEIWVA ARKLQQPLTR FQNEITQSQR
DFYHALQGDK TVFILECKKA SPSKGVIRDN FNPAEIAGVY KHYASAISVL TDEKYFQGSF
DFLPQVSAAV TQPVLCKDFI IDAYQIQLAR FYHADAILLM LSVLDDEAYR QLAAVAHSLN
MGVLTEASNA EELERAITLG AKVVGINNRD LRDLSIDLNR TRELAPRLPE GVTIISESGI
SHYRQVRELS QFANGFLIGS ALMSEPDLNA AVRRVLLGEN KVCGLTRAQD AATAYHAGAV
YGGLIFVDSS PRYVDIASAR TVISGAPLKY VGVFRHAEIE TVRQTAEQLS LAAVQLHGHE
DQQYINQLRK VLPADCQIWK ALSVGDTMPE RNLQQVERYV LDHGTGGTGQ RFDWSLLADQ
ALDNVLLAGG LGPDNCDVAA QLGCAGLDVN SGVESAPGIK DPQRIAAVFQ ALRVY
