3DHQ_CANAL
ID 3DHQ_CANAL Reviewed; 146 AA.
AC Q59Z17; A0A1D8PHW2; Q59Z79;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 3.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Catabolic 3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_03136};
DE Short=cDHQase {ECO:0000255|HAMAP-Rule:MF_03136};
DE EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_03136};
DE AltName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_03136};
GN Name=DQD1 {ECO:0000255|HAMAP-Rule:MF_03136}; Synonyms=DHQ99;
GN OrderedLocusNames=CAALFM_C207260CA; ORFNames=CaO19.2283, CaO19.9823;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 2-146, AND SUBUNIT.
RX PubMed=20445226; DOI=10.1107/s0907444910002763;
RA Trapani S., Schoehn G., Navaza J., Abergel C.;
RT "Macromolecular crystal data phased by negative-stained electron-microscopy
RT reconstructions.";
RL Acta Crystallogr. D 66:514-521(2010).
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, ECO:0000269|PubMed:20445226}.
CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC {ECO:0000255|HAMAP-Rule:MF_03136}.
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DR EMBL; CP017624; AOW27724.1; -; Genomic_DNA.
DR RefSeq; XP_714872.2; XM_709779.2.
DR PDB; 3KIP; X-ray; 2.95 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=2-146.
DR PDBsum; 3KIP; -.
DR AlphaFoldDB; Q59Z17; -.
DR SMR; Q59Z17; -.
DR STRING; 237561.Q59Z17; -.
DR PRIDE; Q59Z17; -.
DR GeneID; 3643488; -.
DR KEGG; cal:CAALFM_C207260CA; -.
DR CGD; CAL0000191356; DQD1.
DR VEuPathDB; FungiDB:C2_07260C_A; -.
DR eggNOG; ENOG502S1A9; Eukaryota.
DR HOGENOM; CLU_090968_1_0_1; -.
DR InParanoid; Q59Z17; -.
DR OrthoDB; 1284624at2759; -.
DR UniPathway; UPA00088; UER00178.
DR PRO; PR:Q59Z17; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IBA:GO_Central.
DR GO; GO:0046279; P:3,4-dihydroxybenzoate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019631; P:quinate catabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Lyase; Quinate metabolism; Reference proteome.
FT CHAIN 1..146
FT /note="Catabolic 3-dehydroquinase"
FT /id="PRO_0000402361"
FT ACT_SITE 24
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT ACT_SITE 104
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT BINDING 105..106
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT BINDING 115
FT /ligand="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"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:3KIP"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:3KIP"
FT HELIX 29..42
FT /evidence="ECO:0007829|PDB:3KIP"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:3KIP"
FT HELIX 57..69
FT /evidence="ECO:0007829|PDB:3KIP"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:3KIP"
FT HELIX 80..84
FT /evidence="ECO:0007829|PDB:3KIP"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:3KIP"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:3KIP"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:3KIP"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:3KIP"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:3KIP"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:3KIP"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:3KIP"
SQ SEQUENCE 146 AA; 16060 MW; 1917C92FA9D2C908 CRC64;
MVKKVLLING PNLNLLGTRE PEKYGTTSLS DIEQAAIEQA KLKNNDSEVL VFQSNTEGFI
IDRIHEAKRQ GVGFVVINAG AYTHTSVGIR DALLGTAIPF IEVHITNVHQ REPFRHQSYL
SDKAVAVICG LGVYGYTAAI EYALNY
