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ADHS_AQUAE
ID   ADHS_AQUAE              Reviewed;         264 AA.
AC   O67506;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase {ECO:0000255|HAMAP-Rule:MF_00960};
DE            Short=ADH synthase {ECO:0000255|HAMAP-Rule:MF_00960};
DE            Short=ADHS {ECO:0000255|HAMAP-Rule:MF_00960};
DE            Short=ADTH synthase {ECO:0000255|HAMAP-Rule:MF_00960};
DE            EC=2.2.1.10 {ECO:0000255|HAMAP-Rule:MF_00960};
GN   Name=aroA' {ECO:0000255|HAMAP-Rule:MF_00960}; OrderedLocusNames=aq_1554;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: Catalyzes a transaldol reaction between 6-deoxy-5-
CC       ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with
CC       an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7-
CC       dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an
CC       alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ),
CC       which is involved in the canonical pathway for the biosynthesis of
CC       aromatic amino acids. {ECO:0000255|HAMAP-Rule:MF_00960}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate + L-aspartate 4-
CC         semialdehyde = 2,3-dioxopropyl phosphate + 2-amino-2,3,7-trideoxy-D-
CC         lyxo-hept-6-ulosonate; Xref=Rhea:RHEA:25952, ChEBI:CHEBI:58859,
CC         ChEBI:CHEBI:58860, ChEBI:CHEBI:58861, ChEBI:CHEBI:537519;
CC         EC=2.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00960};
CC   -!- SUBUNIT: Homodecamer. {ECO:0000255|HAMAP-Rule:MF_00960}.
CC   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. ADHS subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00960}.
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DR   EMBL; AE000657; AAC07474.1; -; Genomic_DNA.
DR   PIR; H70434; H70434.
DR   RefSeq; NP_214071.1; NC_000918.1.
DR   RefSeq; WP_010881009.1; NC_000918.1.
DR   AlphaFoldDB; O67506; -.
DR   SMR; O67506; -.
DR   STRING; 224324.aq_1554; -.
DR   EnsemblBacteria; AAC07474; AAC07474; aq_1554.
DR   KEGG; aae:aq_1554; -.
DR   PATRIC; fig|224324.8.peg.1205; -.
DR   eggNOG; COG1830; Bacteria.
DR   HOGENOM; CLU_057069_2_0_0; -.
DR   InParanoid; O67506; -.
DR   OMA; CEYWGMP; -.
DR   OrthoDB; 1560751at2; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro.
DR   GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
DR   GO; GO:0016744; F:transketolase or transaldolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00958; DhnA; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00960; ADH_synthase; 1.
DR   InterPro; IPR010210; ADH_synthase.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR041720; FbaB-like.
DR   Pfam; PF01791; DeoC; 1.
DR   PIRSF; PIRSF038992; Aldolase_Ia; 1.
DR   SMART; SM01133; DeoC; 1.
DR   TIGRFAMs; TIGR01949; AroFGH_arch; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Reference proteome; Schiff base; Transferase.
FT   CHAIN           1..264
FT                   /note="2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate
FT                   synthase"
FT                   /id="PRO_0000138944"
FT   ACT_SITE        26
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00960"
FT   ACT_SITE        146
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00960"
FT   ACT_SITE        177
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00960"
FT   BINDING         26..30
FT                   /ligand="1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58861"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00960"
FT   BINDING         146..148
FT                   /ligand="1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58861"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00960"
FT   BINDING         202..203
FT                   /ligand="1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58861"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00960"
FT   BINDING         230..231
FT                   /ligand="1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58861"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00960"
SQ   SEQUENCE   264 AA;  28493 MW;  408DFD163E9CAB91 CRC64;
     MGIGKEIRLE RIMNRETRKT IIVPMDHGVS SGPIEGIVNI REAVEKVAEG GANAVVLHKG
     MVRAGHRGRG RDIGLIVHLS ASTDLSPRKN DKVLVCTVEE AIRLGADAVS IHVNIGAEGE
     REMLKDFGYV SKVCEEWQMP LLAMVYGRGP KIENQYDPKV VAHCARVGAE LGADIVKVPY
     TGDPETFKLA IEGSPIPVVI AGGPKMKSER EVLEMVQGAM QAGAAGLSIG RNIFQAKDPA
     KMVRAMSLIV HEGKSVEEAF EILK
 
 
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