CHMU_MYCS2
ID CHMU_MYCS2 Reviewed; 104 AA.
AC A0R3N5; I7GFF2;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Intracellular chorismate mutase {ECO:0000250|UniProtKB:P9WIC1};
DE Short=CM {ECO:0000250|UniProtKB:P9WIC1};
DE EC=5.4.99.5 {ECO:0000269|PubMed:17965159};
GN OrderedLocusNames=MSMEG_5536, MSMEI_5383;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH MSMEG_4244.
RX PubMed=17965159; DOI=10.1128/jb.01332-07;
RA Schneider C.Z., Parish T., Basso L.A., Santos D.S.;
RT "The two chorismate mutases from both Mycobacterium tuberculosis and
RT Mycobacterium smegmatis: biochemical analysis and limited regulation of
RT promoter activity by aromatic amino acids.";
RL J. Bacteriol. 190:122-134(2008).
CC -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC prephenate. Probably involved in the aromatic amino acid biosynthesis.
CC {ECO:0000269|PubMed:17965159}.
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:17965159};
CC -!- ACTIVITY REGULATION: The formation of the complex with AroG activates
CC the chorismate mutase activity. {ECO:0000250|UniProtKB:P9WIC1}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC prephenate from chorismate: step 1/1. {ECO:0000250|UniProtKB:P9WIC1}.
CC -!- SUBUNIT: Homodimer (By similarity). Probably interacts with AroG
CC (MSMEG_4244) (PubMed:17965159). {ECO:0000250|UniProtKB:P9WIC1,
CC ECO:0000269|PubMed:17965159}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK71866.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AFP41824.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK71866.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001663; AFP41824.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_889773.1; NC_008596.1.
DR AlphaFoldDB; A0R3N5; -.
DR SMR; A0R3N5; -.
DR STRING; 246196.MSMEI_5383; -.
DR EnsemblBacteria; ABK71866; ABK71866; MSMEG_5536.
DR EnsemblBacteria; AFP41824; AFP41824; MSMEI_5383.
DR KEGG; msg:MSMEI_5383; -.
DR KEGG; msm:MSMEG_5536; -.
DR PATRIC; fig|246196.19.peg.5395; -.
DR eggNOG; COG1605; Bacteria.
DR UniPathway; UPA00120; UER00203.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004106; F:chorismate mutase activity; IDA:UniProtKB.
DR GO; GO:0009095; P:aromatic amino acid family biosynthetic process, prephenate pathway; ISS:UniProtKB.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0046417; P:chorismate metabolic process; IDA:UniProtKB.
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 Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm;
KW Isomerase; Reference proteome.
FT CHAIN 1..104
FT /note="Intracellular chorismate mutase"
FT /id="PRO_0000414904"
FT DOMAIN 23..104
FT /note="Chorismate mutase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00515"
FT BINDING 59
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P9WIC1"
FT BINDING 68
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P9WIC1"
FT BINDING 72
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P9WIC1"
FT SITE 59
FT /note="Important for catalysis"
FT /evidence="ECO:0000250|UniProtKB:P9WIC1"
FT SITE 100
FT /note="Important for activation via AroG"
FT /evidence="ECO:0000250|UniProtKB:P9WIC1"
FT SITE 101
FT /note="Important for activation via AroG"
FT /evidence="ECO:0000250|UniProtKB:P9WIC1"
FT SITE 102
FT /note="Important for activation via AroG"
FT /evidence="ECO:0000250|UniProtKB:P9WIC1"
SQ SEQUENCE 104 AA; 11754 MW; FE8C0C16F012CF91 CRC64;
MRPDHRMGPP HDEEPHMPET IDAVPEIDDL RREIDELDAT IIAAIQRRTE VSKTIGKARM
ASGGTRLVHS REMKVIERYI DALGPEGKDL AMLLLRLGRG RLGY
