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AROH_BUCBP
ID   AROH_BUCBP              Reviewed;         348 AA.
AC   Q89AW0;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase, Trp-sensitive;
DE            EC=2.5.1.54;
DE   AltName: Full=3-deoxy-D-arabino-heptulosonate 7-phosphate synthase;
DE   AltName: Full=DAHP synthase;
DE   AltName: Full=Phospho-2-keto-3-deoxyheptonate aldolase;
GN   Name=aroH; OrderedLocusNames=bbp_118;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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).
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   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       1/7.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family. {ECO:0000305}.
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DR   EMBL; AE016826; AAO26852.1; -; Genomic_DNA.
DR   RefSeq; WP_011091253.1; NC_004545.1.
DR   AlphaFoldDB; Q89AW0; -.
DR   SMR; Q89AW0; -.
DR   STRING; 224915.bbp_118; -.
DR   EnsemblBacteria; AAO26852; AAO26852; bbp_118.
DR   GeneID; 56470662; -.
DR   KEGG; bab:bbp_118; -.
DR   eggNOG; COG0722; Bacteria.
DR   HOGENOM; CLU_030903_0_1_6; -.
DR   OMA; PCLSWED; -.
DR   OrthoDB; 853329at2; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000000601; 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:0008652; P:cellular amino acid 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; Aromatic amino acid biosynthesis;
KW   Reference proteome; Transferase.
FT   CHAIN           1..348
FT                   /note="Phospho-2-dehydro-3-deoxyheptonate aldolase, Trp-
FT                   sensitive"
FT                   /id="PRO_0000140839"
SQ   SEQUENCE   348 AA;  38539 MW;  0FAA40909DE764FD CRC64;
     MKKTDELRTI RIDPLVTPAE LAQRHVITPS IMDTVISTRK NIANIMTGLD PRLLVIIGPC
     SVHDPVAAVE YAGRLQVLRK KYESRLEIVM RTYFEKPRTV IGWKGLISDP DLNGSFHVNN
     GLSIARKLLL DINKLGVPAA TEFLDMVIGQ FIADLISWGA IGARTTESQI HREMASALSC
     PVGFKNGTDG NIRIAVDAIR AASVEHLFLA PNKYGQMTIN YTSGNPFGHV IMRGGKSPNY
     HAKDIAIAIK YLHEFTLSEY LMIDFSHGNC LKQHRRQLDV GESIAKQIRD GSTAIFGVMI
     ESFLEEGSQK VIDNKSLVYG KSITDPCLGW NDSAFLLEKL ANAVDSRF
 
 
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