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Database: UniProt
Entry: R5XN90_9FIRM
LinkDB: R5XN90_9FIRM
Original site: R5XN90_9FIRM 
ID   R5XN90_9FIRM            Unreviewed;       343 AA.
AC   R5XN90;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   11-DEC-2019, entry version 19.
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=BN537_01340 {ECO:0000313|EMBL:CDA14014.1};
OS   Firmicutes bacterium CAG:212.
OC   Bacteria; Firmicutes; environmental samples.
OX   NCBI_TaxID=1263009 {ECO:0000313|EMBL:CDA14014.1, ECO:0000313|Proteomes:UP000018345};
RN   [1] {ECO:0000313|EMBL:CDA14014.1, ECO:0000313|Proteomes:UP000018345}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:212 {ECO:0000313|Proteomes:UP000018345};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Stereospecific condensation of phosphoenolpyruvate (PEP) and
CC       D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-
CC       heptulosonate-7-phosphate (DAHP). {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; EC=2.5.1.54;
CC         Evidence={ECO:0000256|PIRNR:PIRNR001361};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       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 EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDA14014.1}.
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DR   EMBL; CBBF010000043; CDA14014.1; -; Genomic_DNA.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000018345; 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   Reference proteome {ECO:0000313|Proteomes:UP000018345};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361, ECO:0000256|SAAS:SAAS00080156}.
FT   DOMAIN          32..335
FT                   /note="DAHP_synth_1"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   343 AA;  38722 MW;  754ACD0D5C94C779 CRC64;
     MGMRINAELP LPADLKAEYP LSDKIIKIKE KRDAEIRDIF TGKSDKFIVI VGPCSADNED
     AVCEYVNRLA RVNEKVSDRL MIIPRIYTNK PRTTGEGYKG MLHQPDPDKA PDLLAGIIAI
     RKMHIRAIEE TGLTAADEML YPENRSYLDD ILSYEAIGAR SVENQQHRLT ASGMNIPIGM
     KNPTSGDFLV MLNSVIAAQH SHSFIYRGMD VTTDGNDLAH VILRGGVDKY GTCNPNYHYE
     DLVRLLSLYQ KMELKNPAAI IDANHSNSNK KFKEQIRITS EVLHSRSYNP ELKKLIKGVM
     IESYLEEGNQ KICPDMIYGK SITDPCLGWE DTERLIYEIA EKC
//
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