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Database: UniProt
Entry: I9DNE4_9ALTE
LinkDB: I9DNE4_9ALTE
Original site: I9DNE4_9ALTE 
ID   I9DNE4_9ALTE            Unreviewed;       383 AA.
AC   I9DNE4;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Bifunctional chorismate mutase/prephenate dehydratase {ECO:0000256|ARBA:ARBA00014401};
DE            EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147};
DE            EC=5.4.99.5 {ECO:0000256|ARBA:ARBA00012404};
DE   AltName: Full=Chorismate mutase-prephenate dehydratase {ECO:0000256|ARBA:ARBA00031520};
DE   AltName: Full=p-protein {ECO:0000256|ARBA:ARBA00031175};
GN   ORFNames=AGRI_15841 {ECO:0000313|EMBL:EIW87505.1};
OS   Alishewanella agri BL06.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alishewanella.
OX   NCBI_TaxID=1195246 {ECO:0000313|EMBL:EIW87505.1, ECO:0000313|Proteomes:UP000035062};
RN   [1] {ECO:0000313|EMBL:EIW87505.1, ECO:0000313|Proteomes:UP000035062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL06 {ECO:0000313|EMBL:EIW87505.1,
RC   ECO:0000313|Proteomes:UP000035062};
RX   PubMed=22933763; DOI=10.1128/JB.01129-12;
RA   Kim J., Jung J., Sung J.S., Chun J., Park W.;
RT   "Genome Sequence of Pectin-Degrading Alishewanella agri, Isolated from
RT   Landfill Soil.";
RL   J. Bacteriol. 194:5135-5136(2012).
CC   -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC       prephenate and the decarboxylation/dehydration of prephenate to
CC       phenylpyruvate. {ECO:0000256|ARBA:ARBA00002364}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O;
CC         Xref=Rhea:RHEA:21648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:18005, ChEBI:CHEBI:29934; EC=4.2.1.51;
CC         Evidence={ECO:0000256|ARBA:ARBA00000913};
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|ARBA:ARBA00000824};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004741}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC       prephenate from chorismate: step 1/1. {ECO:0000256|ARBA:ARBA00004817}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIW87505.1}.
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DR   EMBL; AKKU01000028; EIW87505.1; -; Genomic_DNA.
DR   RefSeq; WP_008985897.1; NZ_AKKU01000028.1.
DR   AlphaFoldDB; I9DNE4; -.
DR   STRING; 1195246.AGRI_15841; -.
DR   PATRIC; fig|1195246.3.peg.3143; -.
DR   eggNOG; COG0077; Bacteria.
DR   eggNOG; COG1605; Bacteria.
DR   UniPathway; UPA00120; UER00203.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000035062; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04905; ACT_CM-PDT; 1.
DR   CDD; cd13631; PBP2_Ct-PDT_like; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 1.20.59.10; Chorismate mutase; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR008242; Chor_mutase/pphenate_deHydtase.
DR   InterPro; IPR036263; Chorismate_II_sf.
DR   InterPro; IPR036979; CM_dom_sf.
DR   InterPro; IPR002701; CM_II_prokaryot.
DR   InterPro; IPR010952; CM_P_1.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   NCBIfam; TIGR01797; CM_P_1; 1.
DR   PANTHER; PTHR21022; PREPHENATE DEHYDRATASE P PROTEIN; 1.
DR   PANTHER; PTHR21022:SF19; PREPHENATE DEHYDRATASE-RELATED; 1.
DR   Pfam; PF01817; CM_2; 1.
DR   Pfam; PF00800; PDT; 1.
DR   PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR   SMART; SM00830; CM_2; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF48600; Chorismate mutase II; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51168; CHORISMATE_MUT_2; 1.
DR   PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035062}.
FT   DOMAIN          1..88
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000259|PROSITE:PS51168"
FT   DOMAIN          101..281
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          295..372
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   BINDING         7
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   BINDING         24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   BINDING         35
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   BINDING         44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   BINDING         48
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   BINDING         80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
SQ   SEQUENCE   383 AA;  42373 MW;  268F3B52ACE4CA9F CRC64;
     MELDQIRTAI SDTDQQLLGL LAKRRALALA VAEAKLSQNK PIRDQKREQE LLLSLIEQGK
     PLGLDAQYVT RIYHVIIEDS VLQQQAKVQD QLNGEHTPAV RVAFLGGQGS YSYWATQKYF
     TRRAERIIEL GCDSFNDIVK AVETGHADYA VLPIENTSSG SINEVYDLLQ HTRLSIVGEL
     THPIEHCLLG LPGTDLSKVR QVCSHPQVIA QCSQFLLGLT NVKIEYCESS SAAFAKVKAL
     QDPTIIAIGG EEGGKLYGLE VLTRELANQK QNVSRFIVVA RKPVQVAKAI PAKTTFIMYT
     GQQPGALVEA LLVLKQHGIS MSKLESRPIP GNPWEEMFYV DVSANLNDYA MTRALEELNN
     LTKFVKVLGC YPSDEVTPTE IQA
//
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