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Database: UniProt
Entry: J4KD91_9PAST
LinkDB: J4KD91_9PAST
Original site: J4KD91_9PAST 
ID   J4KD91_9PAST            Unreviewed;       353 AA.
AC   J4KD91;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   11-DEC-2019, entry version 32.
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=HMPREF1128_1758 {ECO:0000313|EMBL:EJP29361.1};
OS   Haemophilus sputorum HK 2154.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=1078483 {ECO:0000313|EMBL:EJP29361.1, ECO:0000313|Proteomes:UP000006974};
RN   [1] {ECO:0000313|EMBL:EJP29361.1, ECO:0000313|Proteomes:UP000006974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HK2154 {ECO:0000313|Proteomes:UP000006974};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (JUL-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:EJP29361.1}.
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DR   EMBL; ALJP01000009; EJP29361.1; -; Genomic_DNA.
DR   RefSeq; WP_007524581.1; NZ_ALJP01000009.1.
DR   EnsemblBacteria; EJP29361; EJP29361; HMPREF1128_1758.
DR   GeneID; 40397539; -.
DR   PATRIC; fig|1078483.3.peg.1127; -.
DR   BioCyc; GCF_000287615-HMP:HMPREF1128_RS05650-MONOMER; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000006974; 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:UP000006974};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361, ECO:0000256|SAAS:SAAS00080156,
KW   ECO:0000313|EMBL:EJP29361.1}.
FT   DOMAIN          44..339
FT                   /note="DAHP_synth_1"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   353 AA;  38696 MW;  22FA5ED397E1D51D CRC64;
     MKLAANNINI RDEALLLTPE QLKTELPLSA KLAEQIDGFR KEIADIIHGR DDRKLIVIGP
     CSIHDPKAAI EYARKLKALS DKVSDKLFLV MRVYFEKPRT TIGWKGLIND PNLDGSFDIE
     KGLRISRQLC LEIAKIGIPL AAEALDPMTP QYLMDLFSWA AIGARTTESQ PHRELASGLS
     MAVGFKNSTD GSLNVALHAI QAASQSHSFL GINQNGQVTV LKSKGNPNGH IILRGGKTPN
     FEKPYIEACE KALREAGLPE AIMVDCSHGN SNKDYRRQPL VARNVLDQIL SGNRSIIGLM
     IESHLHAGNQ SSEQPVDKMQ YGVSITDACI DWATSEEVLS EFASQLRALP LAA
//
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