(data stored in SCRATCH zone)

SWISSPROT: D3UY30_XENBS

ID   D3UY30_XENBS            Unreviewed;       365 AA.
AC   D3UY30;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=3-dehydroquinate synthase {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00336730};
DE            Short=DHQS {ECO:0000256|HAMAP-Rule:MF_00110};
DE            EC=4.2.3.4 {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00336723};
GN   Name=aroB {ECO:0000256|HAMAP-Rule:MF_00110,
GN   ECO:0000313|EMBL:CBJ79208.1};
GN   OrderedLocusNames=XBJ1_0057 {ECO:0000313|EMBL:CBJ79208.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79208.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79208.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79208.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-
CC       heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
CC       {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00858858}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-
CC         dehydroquinate + phosphate; Xref=Rhea:RHEA:21968,
CC         ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394;
CC         EC=4.2.3.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00110,
CC         ECO:0000256|SAAS:SAAS01116881};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00110};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00110};
CC       Note=Binds 1 divalent metal cation per subunit. Can use either
CC       Co(2+) or Zn(2+). {ECO:0000256|HAMAP-Rule:MF_00110};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00110, ECO:0000256|SAAS:SAAS00336779};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|SAAS:SAAS00607009};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 2/7. {ECO:0000256|HAMAP-Rule:MF_00110,
CC       ECO:0000256|SAAS:SAAS00210851}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00110,
CC       ECO:0000256|SAAS:SAAS00336740}.
CC   -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily.
CC       Dehydroquinate synthase family. {ECO:0000256|HAMAP-Rule:MF_00110,
CC       ECO:0000256|SAAS:SAAS00858850}.
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DR   EMBL; FN667741; CBJ79208.1; -; Genomic_DNA.
DR   RefSeq; WP_012986681.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0057; -.
DR   EnsemblBacteria; CBJ79208; CBJ79208; XBJ1_0057.
DR   GeneID; 8829685; -.
DR   KEGG; xbo:XBJ1_0057; -.
DR   PATRIC; fig|406818.4.peg.50; -.
DR   eggNOG; ENOG4105D49; Bacteria.
DR   eggNOG; COG0337; LUCA.
DR   HOGENOM; HOG000007970; -.
DR   KO; K01735; -.
DR   OMA; CGFIADP; -.
DR   BioCyc; XBOV406818:XBJ1_RS00265-MONOMER; -.
DR   UniPathway; UPA00053; UER00085.
DR   Proteomes; UP000002045; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd08195; DHQS; 1.
DR   HAMAP; MF_00110; DHQ_synthase; 1.
DR   InterPro; IPR016037; DHQ_synth_AroB.
DR   InterPro; IPR030963; DHQ_synth_fam.
DR   InterPro; IPR030960; DHQS/DOIS.
DR   Pfam; PF01761; DHQ_synthase; 1.
DR   PIRSF; PIRSF001455; DHQ_synth; 1.
DR   TIGRFAMs; TIGR01357; aroB; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3UY30.
DR   SWISS-2DPAGE; D3UY30.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00110,
KW   ECO:0000256|SAAS:SAAS00415276};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00110,
KW   ECO:0000256|SAAS:SAAS00415253};
KW   Cobalt {ECO:0000256|HAMAP-Rule:MF_00110,
KW   ECO:0000256|SAAS:SAAS00415284};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00110,
KW   ECO:0000256|SAAS:SAAS00415252};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00958949,
KW   ECO:0000313|EMBL:CBJ79208.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00110,
KW   ECO:0000256|SAAS:SAAS01080055};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00415338};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00110,
KW   ECO:0000256|SAAS:SAAS00858852};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00210932}.
FT   DOMAIN       67    326       DHQ_synthase. {ECO:0000259|Pfam:PF01761}.
FT   NP_BIND      71     76       NAD. {ECO:0000256|HAMAP-Rule:MF_00110}.
FT   NP_BIND     105    109       NAD. {ECO:0000256|HAMAP-Rule:MF_00110}.
FT   NP_BIND     129    130       NAD. {ECO:0000256|HAMAP-Rule:MF_00110}.
FT   NP_BIND     169    172       NAD. {ECO:0000256|HAMAP-Rule:MF_00110}.
FT   METAL       184    184       Cobalt or zinc. {ECO:0000256|HAMAP-Rule:
FT                                MF_00110}.
FT   METAL       248    248       Cobalt or zinc; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00110}.
FT   METAL       265    265       Cobalt or zinc; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00110}.
FT   BINDING     142    142       NAD; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00110}.
FT   BINDING     151    151       NAD. {ECO:0000256|HAMAP-Rule:MF_00110}.
SQ   SEQUENCE   365 AA;  39684 MW;  1ABEE672535069F5 CRC64;
     MEQVTVTLGE RSYPIAIAQG LFSSDEAFKS LQAGQQVMIV TNETLAPLYL EQVKSTLQGM
     GLRVDEVILP DGEQYKSLFV VNDIFSALLE NNHGRDTTLI ALGGGVIGDM TGFAAACYQR
     GIRFIQIPTT LLSQVDSSVG GKTGVNHPLG KNMIGAFYQP ASVIIDINCL KTLPAQELHA
     GLAEVIKYGI ILDGEFFNWL ESNIEQLLAL DNQVIAYCIR RCCELKAWVV AADEQERNGM
     RALLNLGHTF GHAIEAEMGY GVWLHGQAVA AGMVMAARTS ELMGTFSKQD TQRIISLLER
     AKLPVNGPVE MSPEIYLPHM MRDKKVSAGK LHLVLPTAIG KAELRSDIGS DVILDAIHLC
     LPSTS
//

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