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Database: UniProt
Entry: A0A0T2ZFG1_9BURK
LinkDB: A0A0T2ZFG1_9BURK
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ID   A0A0T2ZFG1_9BURK        Unreviewed;       377 AA.
AC   A0A0T2ZFG1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   31-JUL-2019, entry version 18.
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=ASE11_21895 {ECO:0000313|EMBL:KRC10013.1};
OS   Hydrogenophaga sp. Root209.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hydrogenophaga.
OX   NCBI_TaxID=1736490 {ECO:0000313|EMBL:KRC10013.1, ECO:0000313|Proteomes:UP000050889};
RN   [1] {ECO:0000313|EMBL:KRC10013.1, ECO:0000313|Proteomes:UP000050889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root209 {ECO:0000313|EMBL:KRC10013.1,
RC   ECO:0000313|Proteomes:UP000050889};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRC10013.1, ECO:0000313|Proteomes:UP000050889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root209 {ECO:0000313|EMBL:KRC10013.1,
RC   ECO:0000313|Proteomes:UP000050889};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KRC10013.1}.
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DR   EMBL; LMIE01000005; KRC10013.1; -; Genomic_DNA.
DR   RefSeq; WP_056267863.1; NZ_LMIE01000005.1.
DR   EnsemblBacteria; KRC10013; KRC10013; ASE11_21895.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000050889; Unassembled WGS sequence.
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:UP000050889};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050889};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361,
KW   ECO:0000256|SAAS:SAAS00080156, ECO:0000313|EMBL:KRC10013.1}.
FT   DOMAIN       61    359       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
FT   REGION        1     25       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   377 AA;  41022 MW;  897D315B5FD34050 CRC64;
     MTAKHAPASS DAWHTRSIDK TSQTDDERIK DITVLPPPEH LIRFFPIGGT PVERLISQTR
     QRIHNILHGK DDRLLVIIGP CSIHDPAAAV DYARRLQPLR EKYADTLEIV MRVYFEKPRT
     TVGWKGLIND PYLDESFRID EGLRIARQLL IEINRLGLPA GSEFLDVISP QYIGDLIAWG
     AIGARTTESQ VHRELASGLS APIGFKNGTD GNIKIATDAI QAASRGHHFL SVHKNGQVAI
     VQTNGNKDCH VILRGGKAPN YDAASVAASV KELEAAKLAP RLMVDCSHAN SSKQHEKQLD
     VARDIASQIA SGSRSVFGVM IESHIEAGAQ KFTPGKDEVG ALKYGQSITD ACLGWSDSLQ
     ALEVLSGAVQ SARKAKA
//
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