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Database: UniProt
Entry: A0A085DXD5_9GAMM
LinkDB: A0A085DXD5_9GAMM
Original site: A0A085DXD5_9GAMM 
ID   A0A085DXD5_9GAMM        Unreviewed;       357 AA.
AC   A0A085DXD5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   08-MAY-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=DK37_01265 {ECO:0000313|EMBL:KFC51630.1};
OS   Halomonas sp. SUBG004.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1485007 {ECO:0000313|EMBL:KFC51630.1};
RN   [1] {ECO:0000313|EMBL:KFC51630.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SUBG004 {ECO:0000313|EMBL:KFC51630.1};
RA   Patel J.H., Thaker V.S.;
RT   "Genomic sequences of Halomonas sp.";
RL   Submitted (JUN-2014) 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:KFC51630.1}.
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DR   EMBL; JPEU01000001; KFC51630.1; -; Genomic_DNA.
DR   EnsemblBacteria; KFC51630; KFC51630; DK37_01265.
DR   UniPathway; UPA00053; UER00084.
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   Transferase {ECO:0000256|PIRNR:PIRNR001361,
KW   ECO:0000256|SAAS:SAAS00080156, ECO:0000313|EMBL:KFC51630.1}.
FT   DOMAIN       51    349       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
SQ   SEQUENCE   357 AA;  38858 MW;  9BDA75E87F6E9DC7 CRC64;
     MNAPIHTANT ACPTTAPASS LMSATALPLP AELRQRVSVN STLRSQIDQQ RQAVQRILNG
     HDDRLLVVVG PCSIHDPDAA LEYADRLAAL SDEVSERILP VMRVYVEKPR TTVGWKGLAY
     DPELDGSGDM PRGMTLSREL MHAVASRGLP VATELLQPML APYLDDLLSW VAIGARTTES
     QLHRELASDL SAAVGFKNAT SGDVQVAIDA MQAAAHSHQR FAMDSQGRPI MQETAGNPHT
     HVVLRGGHGE PNYQAHHVRR AVNTLCEAGQ NPRLMVDCSH ANARKDHRRQ SEVMLDVLAQ
     RQAGDANLVA LMLESHLYEG KQALTPSALR YGVSVTDACV SWETTERLLK TAAERLT
//
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