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Database: UniProt
Entry: A0A0F6TQK5_9GAMM
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ID   A0A0F6TQK5_9GAMM        Unreviewed;       405 AA.
AC   A0A0F6TQK5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=TQ33_1187 {ECO:0000313|EMBL:AKE52147.1};
OS   Kangiella geojedonensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Kangiellales; Kangiellaceae;
OC   Kangiella.
OX   NCBI_TaxID=914150 {ECO:0000313|EMBL:AKE52147.1, ECO:0000313|Proteomes:UP000034071};
RN   [1] {ECO:0000313|EMBL:AKE52147.1, ECO:0000313|Proteomes:UP000034071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCS-5 {ECO:0000313|EMBL:AKE52147.1,
RC   ECO:0000313|Proteomes:UP000034071};
RA   Kim K.M.;
RT   "Complete genome sequence of Kangiella geojedonensis strain YCS-5T.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP010975; AKE52147.1; -; Genomic_DNA.
DR   RefSeq; WP_046561249.1; NZ_CP010975.1.
DR   AlphaFoldDB; A0A0F6TQK5; -.
DR   STRING; 914150.TQ33_1187; -.
DR   KEGG; kge:TQ33_1187; -.
DR   HOGENOM; CLU_035008_1_0_6; -.
DR   OrthoDB; 9802281at2; -.
DR   UniPathway; UPA00120; UER00203.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000034071; Chromosome.
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; IPR001086; Preph_deHydtase.
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; 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:UP000034071}.
FT   DOMAIN          9..100
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000259|PROSITE:PS51168"
FT   DOMAIN          113..293
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          307..384
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   BINDING         19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   BINDING         36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   BINDING         47
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   BINDING         60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   BINDING         92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   SITE            286
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ   SEQUENCE   405 AA;  45021 MW;  D61A076F7D0B94FC CRC64;
     MSEESSAVSE GVNGLDNLRQ SIGRLDEELL KIFAERRKLS LAVAANKLTT NKKVRDQAQE
     KNLLSNLTKK GQKLGIDPSV TLSLFHNIIE DSVRSQYDFF LENSKAEELE PLKLAVLGEP
     DSYSHIAAQQ HFATKKRCFT PEHCPSFLSI FKAIESGQVE LGIVPIENTT AGNITEVYDL
     LLQYQLKIVG EEKLKVKHCL VATKGATING IKDVYSHPQA IAQCKSFFNQ HPFINSHFRS
     STSSALKLVA EYQNPTIAAI ASEQAAENSG LEVLSYGINN YQENYTRFLL IAKKDIAVPN
     AIPAKTTITL QTPQKPGALL DCLQVFKSHG INMMKLESRP IPTKPWQELF YIDFEGNASD
     IIIEKAITEL KHLASEVTVL GSYPMHDILA TKLDHHALSN QFNTL
//
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