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Database: UniProt
Entry: C0GJD2_9FIRM
LinkDB: C0GJD2_9FIRM
Original site: C0GJD2_9FIRM 
ID   C0GJD2_9FIRM            Unreviewed;       274 AA.
AC   C0GJD2;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   16-JAN-2019, entry version 33.
DE   RecName: Full=Prephenate dehydratase {ECO:0000256|RuleBase:RU361254};
DE            Short=PDT {ECO:0000256|RuleBase:RU361254};
DE            EC=4.2.1.51 {ECO:0000256|RuleBase:RU361254};
GN   Name=pheA {ECO:0000256|RuleBase:RU361254};
GN   ORFNames=DealDRAFT_2591 {ECO:0000313|EMBL:EEG76617.1};
OS   Dethiobacter alkaliphilus AHT 1.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Syntrophomonadaceae;
OC   Dethiobacter.
OX   NCBI_TaxID=555088 {ECO:0000313|EMBL:EEG76617.1, ECO:0000313|Proteomes:UP000006443};
RN   [1] {ECO:0000313|EMBL:EEG76617.1, ECO:0000313|Proteomes:UP000006443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AHT 1 {ECO:0000313|EMBL:EEG76617.1,
RC   ECO:0000313|Proteomes:UP000006443};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L.,
RA   Hauser L., Muyzer G.;
RT   "Sequencing of the draft genome and assembly of Dethiobacter
RT   alkaliphilus AHT 1.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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;
CC         EC=4.2.1.51; Evidence={ECO:0000256|RuleBase:RU361254};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1.
CC       {ECO:0000256|RuleBase:RU361254}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EEG76617.1}.
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DR   EMBL; ACJM01000015; EEG76617.1; -; Genomic_DNA.
DR   RefSeq; WP_008518141.1; NZ_ACJM01000015.1.
DR   STRING; 555088.DealDRAFT_2591; -.
DR   EnsemblBacteria; EEG76617; EEG76617; DealDRAFT_2591.
DR   eggNOG; ENOG4105CQC; Bacteria.
DR   eggNOG; COG0077; LUCA.
DR   OrthoDB; 1280729at2; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000006443; Unassembled WGS sequence.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF00800; PDT; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Aromatic amino acid biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006443};
KW   Lyase {ECO:0000256|RuleBase:RU361254, ECO:0000313|EMBL:EEG76617.1};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006443}.
FT   DOMAIN        4    182       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      194    271       ACT. {ECO:0000259|PROSITE:PS51671}.
SQ   SEQUENCE   274 AA;  29616 MW;  3FBD38F80019AE28 CRC64;
     MSIKIAYLGP AGTFSEEAAE CFANKASLEA ELEPCATVAD CAGRAEDDAV KYAVVPLENS
     LEGSVHATLD VLMTSLELSI QAELVLDIEH NLLCPHKEMG QISQVYSHPQ ALAQCRDFLR
     QRLPQARLVP ALSTAEAAAQ VAREQSGAAI ASKRAAKRYG LHILAENIQD SENRTRFIVL
     GKETPVPALP QKASLVFSVT NAAGSLFRVL QAFADHGVNL TRIESRPARK QLGDYIFFVD
     LDGTPDDINV KKALRQAAKE AVVLKLLGSY PVLP
//
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