CHMU_MYCTU
ID CHMU_MYCTU Reviewed; 105 AA.
AC P9WIC1; L0T5D6; P64767; P71562;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Intracellular chorismate mutase {ECO:0000303|PubMed:18727669};
DE Short=CM {ECO:0000303|PubMed:18727669};
DE EC=5.4.99.5 {ECO:0000269|PubMed:15737998, ECO:0000269|PubMed:18727669, ECO:0000269|PubMed:19556970};
GN OrderedLocusNames=Rv0948c; ORFNames=MTCY10D7.26;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15737998; DOI=10.1074/jbc.m413026200;
RA Prakash P., Aruna B., Sardesai A.A., Hasnain S.E.;
RT "Purified recombinant hypothetical protein coded by open reading frame
RT Rv1885c of Mycobacterium tuberculosis exhibits a monofunctional AroQ class
RT of periplasmic chorismate mutase activity.";
RL J. Biol. Chem. 280:19641-19648(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 16-105, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INTERACTION WITH AROG,
RP MASS SPECTROMETRY, AND PATHWAY.
RC STRAIN=ATCC 25618 / H37Rv;
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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 16-105 IN COMPLEX WITH SUBSTRATE
RP ANALOGS AND WITH AROG, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP SUBUNIT, INTERACTION WITH AROG, MUTAGENESIS OF ARG-61; GLY-101; ARG-102 AND
RP LEU-103, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND PATHWAY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19556970; DOI=10.1038/emboj.2009.165;
RA Sasso S., Okvist M., Roderer K., Gamper M., Codoni G., Krengel U., Kast P.;
RT "Structure and function of a complex between chorismate mutase and DAHP
RT synthase: efficiency boost for the junior partner.";
RL EMBO J. 28:2128-2142(2009).
CC -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC prephenate. Probably involved in the aromatic amino acid biosynthesis.
CC {ECO:0000269|PubMed:15737998, ECO:0000269|PubMed:18727669,
CC ECO:0000269|PubMed:19556970}.
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:15737998, ECO:0000269|PubMed:18727669,
CC ECO:0000269|PubMed:19556970};
CC -!- ACTIVITY REGULATION: The formation of the complex with AroG activates
CC the chorismate mutase activity by more than two orders of magnitude to
CC a catalytic efficiency (kcat/Km) typical for chorismate mutase. This
CC activation is primarily caused by a more than 30-fold-decreased Km
CC value, but also by a four-fold increase in kcat. The activity of the
CC complex is inhibited by phenylalanine and tyrosine by about 70 and 40%,
CC respectively. {ECO:0000269|PubMed:19556970}.
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:15737998};
CC KM=1140 uM for chorismate (at 30 degrees Celsius and at pH 7.5)
CC {ECO:0000269|PubMed:19556970};
CC KM=1500 uM for chorismate (at 30 degrees Celsius and at pH 7.5)
CC {ECO:0000269|PubMed:18727669};
CC Vmax=1.2 umol/min/mg enzyme (at 30 degrees Celsius and at pH 7.5)
CC {ECO:0000269|PubMed:15737998};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC prephenate from chorismate: step 1/1. {ECO:0000269|PubMed:15737998,
CC ECO:0000269|PubMed:18727669, ECO:0000269|PubMed:19556970}.
CC -!- SUBUNIT: Homodimer. Interacts with AroG. {ECO:0000269|PubMed:18727669,
CC ECO:0000269|PubMed:19556970}.
CC -!- INTERACTION:
CC P9WIC1; O53512: aroG; NbExp=2; IntAct=EBI-5241850, EBI-5241825;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=11771; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18727669};
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DR EMBL; AL123456; CCP43696.1; -; Genomic_DNA.
DR PIR; B70716; B70716.
DR RefSeq; NP_215463.1; NC_000962.3.
DR RefSeq; WP_003404838.1; NZ_NVQJ01000001.1.
DR PDB; 2QBV; X-ray; 2.00 A; A=16-105.
DR PDB; 2VKL; X-ray; 1.65 A; A=16-105.
DR PDB; 2W19; X-ray; 2.15 A; C/D=16-105.
DR PDB; 2W1A; X-ray; 2.35 A; C/D=16-105.
DR PDB; 5CKX; X-ray; 2.70 A; C/D=16-105.
DR PDB; 5MPV; X-ray; 1.49 A; D=16-93.
DR PDB; 6YGT; X-ray; 1.64 A; AAA=16-105.
DR PDBsum; 2QBV; -.
DR PDBsum; 2VKL; -.
DR PDBsum; 2W19; -.
DR PDBsum; 2W1A; -.
DR PDBsum; 5CKX; -.
DR PDBsum; 5MPV; -.
DR PDBsum; 6YGT; -.
DR AlphaFoldDB; P9WIC1; -.
DR SMR; P9WIC1; -.
DR IntAct; P9WIC1; 1.
DR MINT; P9WIC1; -.
DR STRING; 83332.Rv0948c; -.
DR BindingDB; P9WIC1; -.
DR ChEMBL; CHEMBL2069157; -.
DR PaxDb; P9WIC1; -.
DR DNASU; 885485; -.
DR GeneID; 45424917; -.
DR GeneID; 885485; -.
DR KEGG; mtu:Rv0948c; -.
DR PATRIC; fig|83332.111.peg.1051; -.
DR TubercuList; Rv0948c; -.
DR eggNOG; COG1605; Bacteria.
DR OMA; RFSELGQ; -.
DR PhylomeDB; P9WIC1; -.
DR BRENDA; 5.4.99.5; 3445.
DR SABIO-RK; P9WIC1; -.
DR UniPathway; UPA00120; UER00203.
DR PRO; PR:P9WIC1; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0004106; F:chorismate mutase activity; IDA:MTBBASE.
DR GO; GO:0009095; P:aromatic amino acid family biosynthetic process, prephenate pathway; IDA:MTBBASE.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0046417; P:chorismate metabolic process; IDA:MTBBASE.
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; IPR010958; Chorismate_mutase_highGC-bac.
DR InterPro; IPR036979; CM_dom_sf.
DR InterPro; IPR002701; CM_II_prokaryot.
DR Pfam; PF01817; CM_2; 1.
DR SMART; SM00830; CM_2; 1.
DR SUPFAM; SSF48600; SSF48600; 1.
DR TIGRFAMs; TIGR01808; CM_M_hiGC-arch; 1.
DR PROSITE; PS51168; CHORISMATE_MUT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Cytoplasm; Isomerase; Reference proteome.
FT CHAIN 1..105
FT /note="Intracellular chorismate mutase"
FT /id="PRO_0000119200"
FT DOMAIN 23..105
FT /note="Chorismate mutase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00515"
FT BINDING 61
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000305|PubMed:19556970,
FT ECO:0007744|PDB:2VKL"
FT BINDING 70
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000305|PubMed:19556970,
FT ECO:0007744|PDB:2VKL"
FT BINDING 74
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000305|PubMed:19556970,
FT ECO:0007744|PDB:2VKL"
FT SITE 61
FT /note="Important for catalysis"
FT /evidence="ECO:0000269|PubMed:19556970"
FT SITE 101
FT /note="Important for activation via AroG"
FT /evidence="ECO:0000269|PubMed:19556970"
FT SITE 102
FT /note="Important for activation via AroG"
FT /evidence="ECO:0000269|PubMed:19556970"
FT SITE 103
FT /note="Important for activation via AroG"
FT /evidence="ECO:0000269|PubMed:19556970"
FT MUTAGEN 61
FT /note="R->K: It is catalytically catastrophic, but strongly
FT activated by AroG."
FT /evidence="ECO:0000269|PubMed:19556970"
FT MUTAGEN 101
FT /note="G->A: The catalytic efficiency and the affinity are
FT 5 and 3-fold lower than the wild-type. The activation by
FT AroG is 10-fold lower than the wild-type."
FT /evidence="ECO:0000269|PubMed:19556970"
FT MUTAGEN 102
FT /note="R->A: The catalytic efficiency and the affinity are
FT slightly modified. The activation by AroG is 2-fold lower
FT than the wild-type."
FT /evidence="ECO:0000269|PubMed:19556970"
FT MUTAGEN 103..105
FT /note="Missing: The catalytic efficiency and the affinity
FT are higher than the wild-type. The activation by AroG is
FT 20-fold lower than the wild-type."
FT MUTAGEN 103
FT /note="L->A: The catalytic efficiency and the affinity are
FT identical to the wild-type. The activation by AroG is 10-
FT fold lower than the wild type."
FT /evidence="ECO:0000269|PubMed:19556970"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:5MPV"
FT HELIX 30..63
FT /evidence="ECO:0007829|PDB:5MPV"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:5MPV"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:5MPV"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:5MPV"
SQ SEQUENCE 105 AA; 11771 MW; 6A387E4A53CC9F6D CRC64;
MRPEPPHHEN AELAAMNLEM LESQPVPEID TLREEIDRLD AEILALVKRR AEVSKAIGKA
RMASGGTRLV HSREMKVIER YSELGPDGKD LAILLLRLGR GRLGH
