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Database: UniProt
Entry: A0A1S8THW6_9CLOT
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Original site: A0A1S8THW6_9CLOT 
ID   A0A1S8THW6_9CLOT        Unreviewed;       376 AA.
AC   A0A1S8THW6;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Bifunctional chorismate mutase/prephenate dehydratase {ECO:0000256|ARBA:ARBA00014401};
DE            EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147};
DE   AltName: Full=Chorismate mutase-prephenate dehydratase {ECO:0000256|ARBA:ARBA00031520};
DE   AltName: Full=p-protein {ECO:0000256|ARBA:ARBA00031175};
GN   Name=pheA {ECO:0000313|EMBL:OOM77276.1};
GN   ORFNames=CLPUN_23930 {ECO:0000313|EMBL:OOM77276.1};
OS   Clostridium puniceum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=29367 {ECO:0000313|EMBL:OOM77276.1, ECO:0000313|Proteomes:UP000190890};
RN   [1] {ECO:0000313|EMBL:OOM77276.1, ECO:0000313|Proteomes:UP000190890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2619 {ECO:0000313|EMBL:OOM77276.1,
RC   ECO:0000313|Proteomes:UP000190890};
RA   Poehlein A., Montoya Solano J.D., Flitsch S., Krabben P., Duerre P.,
RA   Daniel R.;
RT   "Microbial solvent formation.";
RL   Submitted (MAY-2016) 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}.
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:OOM77276.1}.
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DR   EMBL; LZZM01000153; OOM77276.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S8THW6; -.
DR   STRING; 29367.CLPUN_23930; -.
DR   OrthoDB; 9802281at2; -.
DR   UniPathway; UPA00120; UER00203.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000190890; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
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; IPR011279; Chorismate_mutase_GmP.
DR   InterPro; IPR036979; CM_dom_sf.
DR   InterPro; IPR002701; CM_II_prokaryot.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   NCBIfam; TIGR01805; CM_mono_grmpos; 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; PS00857; PREPHENATE_DEHYDR_1; 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:UP000190890}.
FT   DOMAIN          1..88
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000259|PROSITE:PS51168"
FT   DOMAIN          106..283
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          295..376
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   BINDING         8
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   BINDING         25
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         45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   BINDING         49
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   SITE            276
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ   SEQUENCE   376 AA;  43396 MW;  0B2D6AD1AB593776 CRC64;
     MESLDYYRKN IDELDKKITE LFEKRMDIVL KVAKYKNKNG VPIFDRNREN EVIEKNLGYL
     KNKDYTKETR KFFIRLMEIA RELEYRKSKV TTSTSLLDQS SVSKDRIGFY GVRGSFTEEA
     MIKYFGENKE AKAYEEFENV FVAIKNGELD YGVLPIENSS TGAISDVYDL LYKYGFYILG
     EVCIRINQNL VGIKGTTLET ITEIYSHPQG FGQSTEFLKV HDKWKKIPFH STATSAKLVN
     DLNDNSKAAI ASKRVASIYN LEIIEENINN QSENFTRFIV IGKTLERSSK ANKVSVVFSL
     DDEAGTLYKL LSHFAENNIN MIKIESRPMK HGPWKYFLYI DFEGDLYSDK VTKALSLIQK
     SSPYFKLLGA YEKNID
//
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