ID   A3DDB7_ACET2            Unreviewed;       118 AA.
AC   A3DDB7;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=chorismate mutase {ECO:0000256|PROSITE-ProRule:PRU00514};
DE            EC=5.4.99.5 {ECO:0000256|PROSITE-ProRule:PRU00514};
GN   OrderedLocusNames=Cthe_0711 {ECO:0000313|EMBL:ABN51946.1};
OS   Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS   103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetivibrio.
OX   NCBI_TaxID=203119 {ECO:0000313|EMBL:ABN51946.1, ECO:0000313|Proteomes:UP000002145};
RN   [1] {ECO:0007829|PDB:1XHO}
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).
RX   PubMed=15983419; DOI=10.1107/S0907444905010644;
RA   Xu H., Yang C., Chen L., Kataeva I.A., Tempel W., Lee D., Habel J.E.,
RA   Nguyen D., Pflugrath J.W., Ferrara J.D., Arendall W.B., Richardson J.S.,
RA   Richardson D.C., Liu Z.J., Newton M.G., Rose J.P., Wang B.C.;
RT   "Away from the edge II: in-house Se-SAS phasing with chromium radiation.";
RL   Acta Crystallogr. D 61:960-966(2005).
RN   [2] {ECO:0000313|Proteomes:UP000002145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 /
RC   NRRL B-4536 / VPI 7372 {ECO:0000313|Proteomes:UP000002145};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA   Newcomb M., Richardson P.;
RT   "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ABN51946.1, ECO:0000313|Proteomes:UP000002145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 /
RC   NRRL B-4536 / VPI 7372 {ECO:0000313|Proteomes:UP000002145};
RX   PubMed=24295562; DOI=10.1186/1754-6834-6-179;
RA   Wilson C.M., Rodriguez M.Jr., Johnson C.M., Martin S.L., Chu T.M.,
RA   Wolfinger R.D., Hauser L.J., Land M.L., Klingeman D.M., Syed M.H.,
RA   Ragauskas A.J., Tschaplinski T.J., Mielenz J.R., Brown S.D.;
RT   "Global transcriptome analysis of Clostridium thermocellum ATCC 27405
RT   during growth on dilute acid pretreated Populus and switchgrass.";
RL   Biotechnol. Biofuels 6:179-179(2013).
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; CP000568; ABN51946.1; -; Genomic_DNA.
DR   RefSeq; WP_003516211.1; NC_009012.1.
DR   PDB; 1XHO; X-ray; 2.20 A; A/B/C=1-118.
DR   PDBsum; 1XHO; -.
DR   AlphaFoldDB; A3DDB7; -.
DR   SMR; A3DDB7; -.
DR   STRING; 203119.Cthe_0711; -.
DR   GeneID; 57418959; -.
DR   KEGG; cth:Cthe_0711; -.
DR   eggNOG; COG4401; Bacteria.
DR   HOGENOM; CLU_133236_1_0_9; -.
DR   OrthoDB; 9802232at2; -.
DR   UniPathway; UPA00120; UER00203.
DR   EvolutionaryTrace; A3DDB7; -.
DR   Proteomes; UP000002145; Chromosome.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-UniRule.
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; RutC-like; 1.
DR   InterPro; IPR008243; Chorismate_mutase_AroH.
DR   InterPro; IPR035959; RutC-like_sf.
DR   NCBIfam; TIGR01796; CM_mono_aroH; 1.
DR   PANTHER; PTHR21164; CHORISMATE MUTASE; 1.
DR   PANTHER; PTHR21164:SF0; CHORISMATE MUTASE AROH; 1.
DR   Pfam; PF07736; CM_1; 1.
DR   PIRSF; PIRSF005965; Chor_mut_AroH; 1.
DR   SUPFAM; SSF55298; YjgF-like; 1.
DR   PROSITE; PS51167; CHORISMATE_MUT_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:1XHO};
KW   Amino-acid biosynthesis {ECO:0000256|PIRSR:PIRSR005965-1,
KW   ECO:0000256|PROSITE-ProRule:PRU00514};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PIRSR:PIRSR005965-1,
KW   ECO:0000256|PROSITE-ProRule:PRU00514};
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00514};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002145}.
FT   BINDING         6
FT                   /ligand="prephenate"
FT                   /ligand_id="ChEBI:CHEBI:29934"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005965-1"
FT   BINDING         88
FT                   /ligand="prephenate"
FT                   /ligand_id="ChEBI:CHEBI:29934"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005965-1"
FT   BINDING         106
FT                   /ligand="prephenate"
FT                   /ligand_id="ChEBI:CHEBI:29934"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005965-1"
SQ   SEQUENCE   118 AA;  13096 MW;  E015FF82080E3EB0 CRC64;
     MVWAIRGATT VSDNTADEIV AETQKLLKEM AEKNGLEEDD IISIIFTVTK DLDAAFPAIA
     ARNMGWTSTA LMCMNEIDVP GSLEKCIRVM MHVNTDKDKK DIKHVYLNGA KVLRPDLT
//