(data stored in SCRATCH zone)

SWISSPROT: Q2IMD0_ANADE

ID   Q2IMD0_ANADE            Unreviewed;       117 AA.
AC   Q2IMD0;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 77.
DE   RecName: Full=Chorismate mutase {ECO:0000256|PROSITE-ProRule:PRU00514};
DE            EC=5.4.99.5 {ECO:0000256|PROSITE-ProRule:PRU00514};
GN   OrderedLocusNames=Adeh_0182 {ECO:0000313|EMBL:ABC79959.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC79959.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|EMBL:ABC79959.1, ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|EMBL:ABC79959.1,
RC   ECO:0000313|Proteomes:UP000001935};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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:0000256|PROSITE-ProRule:PRU00514};
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DR   EMBL; CP000251; ABC79959.1; -; Genomic_DNA.
DR   RefSeq; WP_011419242.1; NC_007760.1.
DR   STRING; 290397.Adeh_0182; -.
DR   EnsemblBacteria; ABC79959; ABC79959; Adeh_0182.
DR   KEGG; ade:Adeh_0182; -.
DR   eggNOG; ENOG4105KHN; Bacteria.
DR   eggNOG; COG4401; LUCA.
DR   HOGENOM; HOG000043606; -.
DR   KO; K06208; -.
DR   OMA; CIRVMMT; -.
DR   BioCyc; ADEH290397:G1G5W-188-MONOMER; -.
DR   Proteomes; UP000001935; Chromosome.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02185; AroH; 1.
DR   Gene3D; 3.30.1330.40; -; 1.
DR   InterPro; IPR008243; Chorismate_mutase_AroH.
DR   InterPro; IPR035959; RutC-like_sf.
DR   PANTHER; PTHR21164; PTHR21164; 1.
DR   Pfam; PF07736; CM_1; 1.
DR   PIRSF; PIRSF005965; Chor_mut_AroH; 1.
DR   ProDom; PD031888; Chorismate_mutase_AroH; 1.
DR   SUPFAM; SSF55298; SSF55298; 1.
DR   TIGRFAMs; TIGR01796; CM_mono_aroH; 1.
DR   PROSITE; PS51167; CHORISMATE_MUT_1; 1.
PE   4: Predicted;
DR   PRODOM; Q2IMD0.
DR   SWISS-2DPAGE; Q2IMD0.
KW   Amino-acid biosynthesis {ECO:0000256|PROSITE-ProRule:PRU00514};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PROSITE-
KW   ProRule:PRU00514};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00514,
KW   ECO:0000313|EMBL:ABC79959.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935}.
FT   BINDING       5      5       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR005965-1}.
FT   BINDING      87     87       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR005965-1}.
FT   BINDING     102    102       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR005965-1}.
FT   BINDING     110    110       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR005965-1}.
SQ   SEQUENCE   117 AA;  12991 MW;  917FFF7A95B35EC4 CRC64;
     MRGLRGATQC SANTVEAIED AVTELCRELT SRNQLEPQQI VWAIFTVTHD LDADFPARAA
     RVQGWNGVPM ICSQEIPVPG SMPRVVRVLL HVDSDGPRNH VYLRGAQALR PDLHVRP
//

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