(data stored in ACNUC27125 zone)

SWISSPROT: 3DHQ1_ASPFU

ID   3DHQ1_ASPFU             Reviewed;         150 AA.
AC   Q6MYX3; Q4WSU3;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 100.
DE   RecName: Full=Catabolic 3-dehydroquinase 1 {ECO:0000255|HAMAP-Rule:MF_03136};
DE            Short=cDHQase 1 {ECO:0000255|HAMAP-Rule:MF_03136};
DE            EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_03136};
DE   AltName: Full=3-dehydroquinate dehydratase 1 {ECO:0000255|HAMAP-Rule:MF_03136};
GN   Name=qutE1 {ECO:0000255|HAMAP-Rule:MF_03136};
GN   ORFNames=AfA5A2.045, AFUA_1G11610;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=14998527; DOI=10.1016/j.fgb.2003.12.003;
RA   Pain A., Woodward J.R., Quail M.A., Anderson M.J., Clark R., Collins M.,
RA   Fosker N., Fraser A., Harris D.E., Larke N., Murphy L.D., Humphray S.,
RA   O'Neil S., Pertea M., Price C., Rabbinowitsch E., Rajandream M.A.,
RA   Salzberg S.L., Saunders D., Seeger K., Sharp S., Warren T., Denning D.W.,
RA   Barrell B.G., Hall N.;
RT   "Insight into the genome of Aspergillus fumigatus: analysis of a 922 kb
RT   region encompassing the nitrate assimilation gene cluster.";
RL   Fungal Genet. Biol. 41:443-453(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- FUNCTION: Is involved in the catabolism of quinate. Allows the
CC       utilization of quinate as carbon source via the beta-ketoadipate
CC       pathway. {ECO:0000255|HAMAP-Rule:MF_03136}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
CC         Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC         ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03136};
CC   -!- PATHWAY: Aromatic compound metabolism; 3,4-dihydroxybenzoate
CC       biosynthesis; 3,4-dihydroxybenzoate from 3-dehydroquinate: step 1/2.
CC       {ECO:0000255|HAMAP-Rule:MF_03136}.
CC   -!- SUBUNIT: Homododecamer. Adopts a ring-like structure, composed of an
CC       arrangement of two hexameric rings stacked on top of one another.
CC       {ECO:0000255|HAMAP-Rule:MF_03136}.
CC   -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_03136}.
DR   EMBL; BX649605; CAE47886.1; -; Genomic_DNA.
DR   EMBL; AAHF01000004; EAL90489.1; -; Genomic_DNA.
DR   RefSeq; XP_752527.1; XM_747434.1.
DR   SMR; Q6MYX3; -.
DR   STRING; 746128.CADAFUBP00001085; -.
DR   EnsemblFungi; EAL90489; EAL90489; AFUA_1G11610.
DR   GeneID; 3510176; -.
DR   KEGG; afm:AFUA_1G11610; -.
DR   EuPathDB; FungiDB:Afu1g11610; -.
DR   HOGENOM; HOG000217278; -.
DR   InParanoid; Q6MYX3; -.
DR   KO; K03786; -.
DR   OMA; LVDWIHE; -.
DR   OrthoDB; 1284624at2759; -.
DR   UniPathway; UPA00088; UER00178.
DR   Proteomes; UP000002530; Chromosome 1.
DR   Proteomes; UP000002530; Unassembled WGS sequence.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046279; P:3,4-dihydroxybenzoate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019630; P:quinate metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00466; DHQase_II; 1.
DR   Gene3D; 3.40.50.9100; -; 1.
DR   HAMAP; MF_00169; AroQ; 1.
DR   InterPro; IPR001874; DHquinase_II.
DR   InterPro; IPR018509; DHquinase_II_CS.
DR   InterPro; IPR036441; DHquinase_II_sf.
DR   PANTHER; PTHR21272; PTHR21272; 1.
DR   Pfam; PF01220; DHquinase_II; 1.
DR   PIRSF; PIRSF001399; DHquinase_II; 1.
DR   SUPFAM; SSF52304; SSF52304; 1.
DR   TIGRFAMs; TIGR01088; aroQ; 1.
DR   PROSITE; PS01029; DEHYDROQUINASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6MYX3.
DR   SWISS-2DPAGE; Q6MYX3.
KW   Lyase; Quinate metabolism; Reference proteome.
FT   CHAIN           1..150
FT                   /note="Catabolic 3-dehydroquinase 1"
FT                   /id="PRO_0000402354"
FT   REGION          102..103
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT   ACT_SITE        24
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT   ACT_SITE        101
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT   BINDING         75
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT   BINDING         81
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT   BINDING         88
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT   BINDING         112
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT   SITE            19
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
SQ   SEQUENCE   150 AA;  16042 MW;  9C0A9DC3A17A5D8B CRC64;
     MGKSILLING PNLNLLGTRE PHIYGNTTLA DVEASCKAHA ESLGATLATF QSNHEGAIID
     RIQAARGNVD GIIINPGAFT HTSVAIRDAL LGVGIPFIEL HVSNVHAREP WRHHSYFSDK
     AAGIIVGLGV YGYKVAVEHV ALNFKERAAL
//

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