(data stored in ACNUC7421 zone)

SWISSPROT: C7QHB3_CATAD

ID   C7QHB3_CATAD            Unreviewed;       314 AA.
AC   C7QHB3;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   13-FEB-2019, entry version 51.
DE   SubName: Full=Prephenate dehydratase {ECO:0000313|EMBL:ACU69052.1};
DE            EC=4.2.1.51 {ECO:0000313|EMBL:ACU69052.1};
GN   OrderedLocusNames=Caci_0097 {ECO:0000313|EMBL:ACU69052.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69052.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69052.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
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DR   EMBL; CP001700; ACU69052.1; -; Genomic_DNA.
DR   RefSeq; WP_012784347.1; NC_013131.1.
DR   STRING; 479433.Caci_0097; -.
DR   EnsemblBacteria; ACU69052; ACU69052; Caci_0097.
DR   KEGG; cai:Caci_0097; -.
DR   eggNOG; ENOG4105CQC; Bacteria.
DR   eggNOG; COG0077; LUCA.
DR   HOGENOM; HOG000018970; -.
DR   KO; K04518; -.
DR   OMA; REVMSAC; -.
DR   OrthoDB; 1280729at2; -.
DR   BioCyc; CACI479433:G1GFP-99-MONOMER; -.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:InterPro.
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; 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; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
DR   PRODOM; C7QHB3.
DR   SWISS-2DPAGE; C7QHB3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Lyase {ECO:0000313|EMBL:ACU69052.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851}.
FT   DOMAIN       12    191       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      206    283       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   SITE        184    184       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   314 AA;  33922 MW;  C3C9844C0F95DB92 CRC64;
     MTDTASPRVP TRYGFLGPAG TFTEAALLSV PGARDAERVP YESVPAALDA VRRDEVAGAV
     VAFENSVEGA VPATLDDLST EEPPLHIVRE ILLPVEFALM GRPDTALADI KTVSSHPHAY
     PQCRRWLAEN LPDARWVAAS SNADAARLVS EGVHDAALAG SFAAPFYRLT LLAENIHDVS
     GAVTRFVMVV PPGPPPARTG ADKTSLAVVL RDNHPGALLE ILEEFAVRGV DLMRIESRPT
     RSKLGTYWFS IDCEGHLEDA RVGEVLTGLR RVAAEVRYLG SYPRADGRAA EIRKGTSDED
     FHEAAEWLAG LRNR
//

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