SCMU_YERPE
ID SCMU_YERPE Reviewed; 186 AA.
AC Q7CHH5; Q74VQ2;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Secreted chorismate mutase {ECO:0000303|PubMed:18727669};
DE Short=CM {ECO:0000303|PubMed:18727669};
DE EC=5.4.99.5 {ECO:0000269|PubMed:18727669};
DE AltName: Full=*YpCM {ECO:0000303|PubMed:18727669};
DE Flags: Precursor;
GN Name=pheA2; OrderedLocusNames=y2828, YP_1243, YPO1353;
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=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).
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=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 [4] {ECO:0007744|PDB:2GBB}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 16-105 IN COMPLEX WITH SUBSTRATE
RP ANALOGS, FUNCTION AS A CHORISMATE MUTASE, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, SUBUNIT, AND DISULFIDE
RP BOND.
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=18727669; DOI=10.1111/j.1742-4658.2008.06621.x;
RA Kim S.K., Reddy S.K., Nelson B.C., Robinson H., Reddy P.T., Ladner J.E.;
RT "A comparative biochemical and structural analysis of the intracellular
RT chorismate mutase (Rv0948c) from Mycobacterium tuberculosis H(37)R(v) and
RT the secreted chorismate mutase (y2828) from Yersinia pestis.";
RL FEBS J. 275:4824-4835(2008).
CC -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC prephenate. May play some role in the pathogenicity.
CC {ECO:0000269|PubMed:18727669}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897,
CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5;
CC Evidence={ECO:0000269|PubMed:18727669};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13898;
CC Evidence={ECO:0000269|PubMed:18727669};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=500 uM for chorismate (at 30 degrees Celsius and at pH 7.5)
CC {ECO:0000269|PubMed:18727669};
CC Note=kcat is 70 sec(-1). {ECO:0000269|PubMed:18727669};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC prephenate from chorismate: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18727669}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:18727669}.
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DR EMBL; AE009952; AAM86379.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS61486.1; -; Genomic_DNA.
DR EMBL; AL590842; CAL20005.1; -; Genomic_DNA.
DR PIR; AC0165; AC0165.
DR RefSeq; WP_002211366.1; NZ_WUCM01000027.1.
DR RefSeq; YP_002346376.1; NC_003143.1.
DR PDB; 2GBB; X-ray; 2.10 A; A/B/C/D=31-186.
DR PDBsum; 2GBB; -.
DR AlphaFoldDB; Q7CHH5; -.
DR SMR; Q7CHH5; -.
DR STRING; 214092.YPO1353; -.
DR PaxDb; Q7CHH5; -.
DR DNASU; 1147775; -.
DR EnsemblBacteria; AAM86379; AAM86379; y2828.
DR EnsemblBacteria; AAS61486; AAS61486; YP_1243.
DR GeneID; 66842186; -.
DR KEGG; ype:YPO1353; -.
DR KEGG; ypk:y2828; -.
DR KEGG; ypm:YP_1243; -.
DR PATRIC; fig|214092.21.peg.1671; -.
DR eggNOG; COG1605; Bacteria.
DR HOGENOM; CLU_118625_0_0_6; -.
DR OMA; MADWLAT; -.
DR BRENDA; 5.4.99.5; 4559.
DR SABIO-RK; Q7CHH5; -.
DR UniPathway; UPA00120; UER00203.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004106; F:chorismate mutase activity; IDA:UniProtKB.
DR GO; GO:0046417; P:chorismate metabolic process; IDA:UniProtKB.
DR GO; GO:0009697; P:salicylic acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.20.59.10; -; 1.
DR InterPro; IPR036263; Chorismate_II_sf.
DR InterPro; IPR008240; Chorismate_mutase_periplasmic.
DR InterPro; IPR036979; CM_dom_sf.
DR InterPro; IPR002701; CM_II_prokaryot.
DR Pfam; PF01817; CM_2; 1.
DR PIRSF; PIRSF026640; Peripl_chor_mut; 1.
DR SMART; SM00830; CM_2; 1.
DR SUPFAM; SSF48600; SSF48600; 1.
DR TIGRFAMs; TIGR01806; CM_mono2; 1.
DR PROSITE; PS51168; CHORISMATE_MUT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Isomerase; Periplasm; Reference proteome;
KW Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..186
FT /note="Secreted chorismate mutase"
FT /id="PRO_0000414907"
FT DOMAIN 31..107
FT /note="Chorismate mutase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00515"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WIB9"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WIB9"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WIB9"
FT BINDING 99..103
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WIB9"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WIB9"
FT DISULFID 33..148
FT /evidence="ECO:0000269|PubMed:18727669,
FT ECO:0007744|PDB:2GBB"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:2GBB"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:2GBB"
FT HELIX 64..80
FT /evidence="ECO:0007829|PDB:2GBB"
FT HELIX 85..112
FT /evidence="ECO:0007829|PDB:2GBB"
FT HELIX 123..147
FT /evidence="ECO:0007829|PDB:2GBB"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:2GBB"
FT HELIX 156..162
FT /evidence="ECO:0007829|PDB:2GBB"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:2GBB"
SQ SEQUENCE 186 AA; 20745 MW; DB0B2C8B6E21AF6B CRC64;
MQPTHTLTRL TVIGKLIIAS SFFLSLAVQA QQCGQTAPLI NERLSYMKDV AGYKAENHLP
IEDRIQEEKV INSAMAQAES LGLNGESIKP LMVAQINAAK AIQYRYRADW LSQPEPGWQP
KPLDDVRANI GELSTKILEQ IAEELKTCKP AEMGDKAHFI NTIRQHNLTS ADVEAIFSTF
NQVKLK
