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Database: UniProt
Entry: A0A0G3GNM6_9CORY
LinkDB: A0A0G3GNM6_9CORY
Original site: A0A0G3GNM6_9CORY 
ID   A0A0G3GNM6_9CORY        Unreviewed;       384 AA.
AC   A0A0G3GNM6;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   08-MAY-2019, entry version 17.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|PIRNR:PIRNR001361};
DE            EC=2.5.1.54 {ECO:0000256|PIRNR:PIRNR001361};
GN   ORFNames=CEPID_04390 {ECO:0000313|EMBL:AKK02749.1};
OS   Corynebacterium epidermidicanis.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1050174 {ECO:0000313|EMBL:AKK02749.1, ECO:0000313|Proteomes:UP000035368};
RN   [1] {ECO:0000313|EMBL:AKK02749.1, ECO:0000313|Proteomes:UP000035368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45586 {ECO:0000313|EMBL:AKK02749.1,
RC   ECO:0000313|Proteomes:UP000035368};
RA   Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT   "Complete genome sequence of Corynebacterium epidermidicanis DSM
RT   45586, isolated from the skin of a dog suffering from pruritus.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Stereospecific condensation of phosphoenolpyruvate (PEP)
CC       and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-
CC       arabino-heptulosonate-7-phosphate (DAHP).
CC       {ECO:0000256|PIRNR:PIRNR001361}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-
CC         phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate;
CC         Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702;
CC         EC=2.5.1.54; Evidence={ECO:0000256|PIRNR:PIRNR001361};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 1/7. {ECO:0000256|PIRNR:PIRNR001361}.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC       {ECO:0000256|PIRNR:PIRNR001361}.
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DR   EMBL; CP011541; AKK02749.1; -; Genomic_DNA.
DR   RefSeq; WP_047239896.1; NZ_CP011541.1.
DR   EnsemblBacteria; AKK02749; AKK02749; CEPID_04390.
DR   KEGG; cei:CEPID_04390; -.
DR   PATRIC; fig|1050174.4.peg.889; -.
DR   KO; K01626; -.
DR   OrthoDB; 853329at2; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000035368; Chromosome.
DR   GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006219; DHAP_synth_1.
DR   PANTHER; PTHR21225; PTHR21225; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   PIRSF; PIRSF001361; DAHP_synthase; 1.
DR   TIGRFAMs; TIGR00034; aroFGH; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW   Complete proteome {ECO:0000313|Proteomes:UP000035368};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035368};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361,
KW   ECO:0000256|SAAS:SAAS00080156, ECO:0000313|EMBL:AKK02749.1}.
FT   DOMAIN       48    359       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
SQ   SEQUENCE   384 AA;  41334 MW;  FBCDFC94182D3ACB CRC64;
     MSAPVSLQDA ASTSNRRVIA FHDLPSPAEL LAQLPLSVQQ AAKVERDRQE IADIFAGEDD
     RLVVVVGPCS IHDPNAALEY AHRLAPLAQL LSDDLKIVMR VYFEKPRTTI GWKGLINDPH
     LDGTYDIAYG LRLARQVVVD VLNTGLPVGC EFLEPNSPQY YADAVAWGAI GARTTESQVH
     RQLASGMSMP IGFKNGTDGN VQVAVDAVQA ASHQHFFFGT SDEGHPAVVE TAGNDNCHII
     LRGGTSGPNY SPEHIAAAEE SMSAGQLRER RLMIDASHAN SNKDDERQLL VLREIAQHIA
     DPDAATAHSI AGVMIESFLV AGAQKLDPAK LRKNGGEGLA YGQSVTDRCI DIASTVDVLE
     ELAQAVRTRR AGKRDLAQPS GDDQ
//
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