AROD_ARCFU
ID AROD_ARCFU Reviewed; 196 AA.
AC O30011;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_00214};
DE Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00214};
DE EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_00214};
DE AltName: Full=Type I DHQase {ECO:0000255|HAMAP-Rule:MF_00214};
DE AltName: Full=Type I dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00214};
DE Short=DHQ1 {ECO:0000255|HAMAP-Rule:MF_00214};
GN Name=aroD {ECO:0000255|HAMAP-Rule:MF_00214}; OrderedLocusNames=AF_0228;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS), AND SUBUNIT.
RX PubMed=18931429; DOI=10.1107/s1744309108028546;
RA Smith N.N., Gallagher D.T.;
RT "Structure and lability of archaeal dehydroquinase.";
RL Acta Crystallogr. F 64:886-892(2008).
CC -!- FUNCTION: Involved in the third step of the chorismate pathway, which
CC leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-
CC dehydration of 3-dehydroquinate (DHQ) and introduces the first double
CC bond of the aromatic ring to yield 3-dehydroshikimate.
CC {ECO:0000255|HAMAP-Rule:MF_00214}.
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_00214};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 3/7. {ECO:0000255|HAMAP-Rule:MF_00214}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00214,
CC ECO:0000269|PubMed:18931429}.
CC -!- SIMILARITY: Belongs to the type-I 3-dehydroquinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00214}.
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DR EMBL; AE000782; AAB91004.1; -; Genomic_DNA.
DR PIR; D69278; D69278.
DR RefSeq; WP_010877739.1; NC_000917.1.
DR PDB; 2OX1; X-ray; 2.33 A; A/B/C/D=1-196.
DR PDBsum; 2OX1; -.
DR AlphaFoldDB; O30011; -.
DR SMR; O30011; -.
DR STRING; 224325.AF_0228; -.
DR EnsemblBacteria; AAB91004; AAB91004; AF_0228.
DR GeneID; 24793762; -.
DR KEGG; afu:AF_0228; -.
DR eggNOG; arCOG02097; Archaea.
DR HOGENOM; CLU_064444_2_0_2; -.
DR OMA; EFRYARA; -.
DR OrthoDB; 75928at2157; -.
DR PhylomeDB; O30011; -.
DR BRENDA; 4.2.1.10; 414.
DR UniPathway; UPA00053; UER00086.
DR EvolutionaryTrace; O30011; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase 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 GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00502; DHQase_I; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00214; AroD; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001381; DHquinase_I.
DR Pfam; PF01487; DHquinase_I; 1.
DR TIGRFAMs; TIGR01093; aroD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Lyase; Reference proteome; Schiff base.
FT CHAIN 1..196
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_0000138826"
FT ACT_SITE 98
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT ACT_SITE 122
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 23..25
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 45
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 159
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 182
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2OX1"
FT HELIX 10..15
FT /evidence="ECO:0007829|PDB:2OX1"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:2OX1"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:2OX1"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:2OX1"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:2OX1"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:2OX1"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2OX1"
FT HELIX 57..71
FT /evidence="ECO:0007829|PDB:2OX1"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:2OX1"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:2OX1"
FT STRAND 90..101
FT /evidence="ECO:0007829|PDB:2OX1"
FT HELIX 106..114
FT /evidence="ECO:0007829|PDB:2OX1"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:2OX1"
FT HELIX 130..142
FT /evidence="ECO:0007829|PDB:2OX1"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:2OX1"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:2OX1"
FT HELIX 157..164
FT /evidence="ECO:0007829|PDB:2OX1"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:2OX1"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:2OX1"
SQ SEQUENCE 196 AA; 22207 MW; 9BF77DEB9B984B8B CRC64;
MKLVATLSSP EELELAEKAD VVELRIDLFD FSGARVDKEK ILTCRRVSDG GKFEGDERER
IEKMKRAFDS LNPDYVDLES DLPDSAFDFN CRIIESYHNF IRTPDYSELK GIVEGRRGDL
VKIATMGKSK RDVETIVRIL TNYDDVVAFL MGERFSFTRV LAAYLGSPFI YCYVGSPKAP
GQISLDDARE IISRLG
