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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
 
 
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