CMPDT_NEIG1
ID CMPDT_NEIG1 Reviewed; 362 AA.
AC Q9ZHY3; Q5F6N9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Bifunctional chorismate mutase/prephenate dehydratase {ECO:0000250|UniProtKB:P0A9J8};
DE AltName: Full=Chorismate mutase-prephenate dehydratase {ECO:0000250|UniProtKB:P0A9J8};
DE AltName: Full=P-protein {ECO:0000250|UniProtKB:P0A9J8};
DE Includes:
DE RecName: Full=Chorismate mutase {ECO:0000250|UniProtKB:P0A9J8};
DE Short=CM {ECO:0000250|UniProtKB:P0A9J8};
DE EC=5.4.99.5 {ECO:0000250|UniProtKB:P0A9J8};
DE Includes:
DE RecName: Full=Prephenate dehydratase {ECO:0000250|UniProtKB:P0A9J8};
DE Short=PDT {ECO:0000250|UniProtKB:P0A9J8};
DE EC=4.2.1.51 {ECO:0000250|UniProtKB:P0A9J8};
GN Name=pheA; OrderedLocusNames=NGO1510;
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC 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 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 -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC prephenate and the decarboxylation/dehydration of prephenate to
CC phenylpyruvate. {ECO:0000250|UniProtKB:P0A9J8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897,
CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5;
CC Evidence={ECO:0000250|UniProtKB:P0A9J8};
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:0000250|UniProtKB:P0A9J8};
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC phenylpyruvate from prephenate: step 1/1.
CC {ECO:0000250|UniProtKB:P0A9J8}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC prephenate from chorismate: step 1/1. {ECO:0000250|UniProtKB:P0A9J8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A9J8}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD05425.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAW90148.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF047375; AAD05425.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE004969; AAW90148.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_003689394.1; NC_002946.2.
DR RefSeq; WP_025455824.1; NC_002946.2.
DR AlphaFoldDB; Q9ZHY3; -.
DR SMR; Q9ZHY3; -.
DR STRING; 242231.NGO_1510; -.
DR EnsemblBacteria; AAW90148; AAW90148; NGO_1510.
DR GeneID; 66753710; -.
DR KEGG; ngo:NGO_1510; -.
DR HOGENOM; CLU_035008_0_1_4; -.
DR UniPathway; UPA00120; UER00203.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000000535; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR008242; Chor_mutase/pphenate_deHydtase.
DR InterPro; IPR036263; Chorismate_II_sf.
DR InterPro; IPR036979; CM_dom_sf.
DR InterPro; IPR002701; CM_II_prokaryot.
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 SUPFAM; SSF55021; SSF55021; 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; Cytoplasm;
KW Isomerase; Lyase; Multifunctional enzyme; Phenylalanine biosynthesis;
KW Reference proteome.
FT CHAIN 1..362
FT /note="Bifunctional chorismate mutase/prephenate
FT dehydratase"
FT /id="PRO_0000119189"
FT DOMAIN 3..91
FT /note="Chorismate mutase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00515"
FT DOMAIN 92..269
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT DOMAIN 281..356
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT BINDING 13
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT SITE 262
FT /note="Essential for prephenate dehydratase activity"
FT /evidence="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
