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
//