GenomeNet

Database: UniProt
Entry: Q9ZHY3
LinkDB: Q9ZHY3
Original site: Q9ZHY3 
ID   PHEA_NEIG1              Reviewed;         362 AA.
AC   Q9ZHY3; Q5F6N9;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   01-OCT-2014, entry version 101.
DE   RecName: Full=P-protein;
DE   Includes:
DE     RecName: Full=Chorismate mutase;
DE              Short=CM;
DE              EC=5.4.99.5;
DE   Includes:
DE     RecName: Full=Prephenate dehydratase;
DE              Short=PDT;
DE              EC=4.2.1.51;
GN   Name=pheA; OrderedLocusNames=NGO1510;
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=242231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10094619; DOI=10.1046/j.1365-2958.1998.01089.x;
RA   Mehr I.J., Seifert H.S.;
RT   "Differential roles of homologous recombination pathways in Neisseria
RT   gonorrhoeae pilin antigenic variation, DNA transformation and DNA
RT   repair.";
RL   Mol. Microbiol. 30:697-710(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090;
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Chorismate = prephenate.
CC   -!- CATALYTIC ACTIVITY: Prephenate = phenylpyruvate + H(2)O + CO(2).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate
CC       biosynthesis; prephenate from chorismate: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Contains 1 ACT domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU01007}.
CC   -!- SIMILARITY: Contains 1 chorismate mutase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00515}.
CC   -!- SIMILARITY: Contains 1 prephenate dehydratase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00517}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD05425.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAW90148.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF047375; AAD05425.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE004969; AAW90148.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_208560.1; NC_002946.2.
DR   ProteinModelPortal; Q9ZHY3; -.
DR   STRING; 242231.NGO1510; -.
DR   PRIDE; Q9ZHY3; -.
DR   EnsemblBacteria; AAW90148; AAW90148; NGO1510.
DR   GeneID; 3281542; -.
DR   KEGG; ngo:NGO1510; -.
DR   PATRIC; 20336494; VBINeiGon24812_1795.
DR   eggNOG; COG0077; -.
DR   HOGENOM; HOG000018971; -.
DR   KO; K14170; -.
DR   OMA; SLAMATH; -.
DR   OrthoDB; EOG6WHNT1; -.
DR   BioCyc; NGON242231:GI2G-1414-MONOMER; -.
DR   UniPathway; UPA00120; UER00203.
DR   UniPathway; UPA00121; UER00345.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
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   Gene3D; 1.20.59.10; -; 1.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR008242; Chor_mutase/pphenate_deHydtase.
DR   InterPro; IPR002701; Chorismate_mutase.
DR   InterPro; IPR020822; Chorismate_mutase_type_II.
DR   InterPro; IPR010957; G/b/e-P-prot_chorismate_mutase.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   Pfam; PF01842; ACT; 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; SSF48600; SSF48600; 1.
DR   TIGRFAMs; TIGR01807; CM_P2; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51168; CHORISMATE_MUT_2; 1.
DR   PROSITE; PS00857; PREPHENATE_DEHYDR_1; 1.
DR   PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Cytoplasm; Isomerase; Lyase;
KW   Multifunctional enzyme; Phenylalanine biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    362       P-protein.
FT                                /FTId=PRO_0000119189.
FT   DOMAIN        3     91       Chorismate mutase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00515}.
FT   DOMAIN       92    269       Prephenate dehydratase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00517}.
FT   DOMAIN      281    356       ACT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01007}.
FT   REGION      270    362       Regulatory (Phe-binding).
FT   SITE        262    262       Essential for prephenate dehydratase
FT                                activity. {ECO:0000255}.
SQ   SEQUENCE   362 AA;  39354 MW;  BEC6582338E84DE2 CRC64;
     MSQTIDELLI PHRNAIDTID AEILRLLNER AQHAHAIGEL KGTGAVYRPE REVAVLRRIQ
     DLNKGPLPDE SVARLFREVM SECLAVERPL TIAYLGPQGT FTQQAAIKHF GHAAHTMACP
     TIDDCFKQVE TRQADYLVAP VENSTEGSVG RTLDLLAVTA LQACGEVVLR IHHNLLRKNN
     GSTEGIAKVF SHAQALAQCN DWLGRRLPNA ERIAVSSNAE AARLVAESDD GTVAAIAGRT
     AAEIYGLDMV AECIEDEPNN TTRFLVMGHH ETGASGSDKT SLAVSAPNRA GAVASLLQPL
     TESGISMTKF ESRPSKSVLW EYLFFIDIEG HRRDAQIQTA LERLGERASF VKAIGSYPTA
     VL
//
DBGET integrated database retrieval system