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-MAY-2013, entry version 94.
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.
CC -!- SIMILARITY: Contains 1 chorismate mutase domain.
CC -!- SIMILARITY: Contains 1 prephenate dehydratase domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD05425.1; Type=Erroneous initiation;
CC Sequence=AAW90148.1; Type=Erroneous initiation;
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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 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; WREVMSA; -.
DR ProtClustDB; CLSK877559; -.
DR BioCyc; NGON242231:GI2G-1376-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:EC.
DR GO; GO:0004664; F:prephenate dehydratase activity; IEA: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; Chorismate_mut; 1.
DR TIGRFAMs; TIGR01807; CM_P2; 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 4: Predicted;
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.
FT DOMAIN 92 269 Prephenate dehydratase.
FT DOMAIN 280 356 ACT.
FT REGION 270 362 Regulatory (Phe-binding).
FT SITE 262 262 Essential for prephenate dehydratase
FT activity (Potential).
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
//
