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Database: UniProt
Entry: A0A1I2KIL4_9ACTN
LinkDB: A0A1I2KIL4_9ACTN
Original site: A0A1I2KIL4_9ACTN 
ID   A0A1I2KIL4_9ACTN        Unreviewed;       313 AA.
AC   A0A1I2KIL4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   11-DEC-2019, entry version 8.
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=SAMN05216574_1219 {ECO:0000313|EMBL:SFF64941.1};
OS   Blastococcus sp. DSM 46838.
OC   Bacteria; Actinobacteria; Geodermatophilales; Geodermatophilaceae;
OC   Blastococcus; unclassified Blastococcus.
OX   NCBI_TaxID=1798228 {ECO:0000313|EMBL:SFF64941.1, ECO:0000313|Proteomes:UP000198589};
RN   [1] {ECO:0000313|EMBL:SFF64941.1, ECO:0000313|Proteomes:UP000198589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 46838 {ECO:0000313|EMBL:SFF64941.1,
RC   ECO:0000313|Proteomes:UP000198589};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; EC=4.2.1.51;
CC         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}.
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DR   EMBL; FOND01000021; SFF64941.1; -; Genomic_DNA.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000198589; Unassembled WGS sequence.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
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; IPR008242; Chor_mutase/pphenate_deHydtase.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF00800; PDT; 1.
DR   PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00857; PREPHENATE_DEHYDR_1; 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   Lyase {ECO:0000256|RuleBase:RU361254};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198589}.
FT   DOMAIN          9..186
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          200..275
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   SITE            179
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ   SEQUENCE   313 AA;  31699 MW;  DA3A2222402A41DC CRC64;
     MPPSTSPTRF AYLGPEGTFA EAALSAVSSA GGSRYPQPSV PAALAAVRSG DADAALVPLE
     NSVEGSVPAT MDGLADGAPL VITREVFLDV AFVLAVRPGT EQAGVRSVAS HPHALAQTAG
     RLAELFPGVV PLPVSSTAGA AAAVAAGDFD AAVCAPIAAE RYGLVALVDD LADTPGAVTR
     FVLVEPAGAL PAPTGNDKTS LVAVVGDRTG ALLALLSEFA VRGISLTRIE SRPTRERLGV
     YSFSLDCEGH IADARVGEAL AALHRVCDDV RFLGSYARAD GRENVPVPDV AADAAFADAE
     GWLAGIRGGP SPR
//
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