AROQ_YERPE
ID AROQ_YERPE Reviewed; 150 AA.
AC Q8ZAX1; Q0WAZ2;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_00169};
DE Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00169};
DE EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_00169};
DE AltName: Full=Type II DHQase {ECO:0000255|HAMAP-Rule:MF_00169};
GN Name=aroQ {ECO:0000255|HAMAP-Rule:MF_00169};
GN OrderedLocusNames=YPO3660, y0207, YP_3886;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
CC -!- FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate.
CC {ECO:0000255|HAMAP-Rule:MF_00169}.
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_00169};
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_00169}.
CC -!- SUBUNIT: Homododecamer. {ECO:0000255|HAMAP-Rule:MF_00169}.
CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00169}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL590842; CAL22249.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM83801.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS64031.1; -; Genomic_DNA.
DR PIR; AF0445; AF0445.
DR RefSeq; WP_002210071.1; NZ_WUCM01000059.1.
DR RefSeq; YP_002348546.1; NC_003143.1.
DR PDB; 3LWZ; X-ray; 1.65 A; A/B/C/D=1-150.
DR PDBsum; 3LWZ; -.
DR AlphaFoldDB; Q8ZAX1; -.
DR SMR; Q8ZAX1; -.
DR STRING; 214092.YPO3660; -.
DR PaxDb; Q8ZAX1; -.
DR DNASU; 1145154; -.
DR EnsemblBacteria; AAM83801; AAM83801; y0207.
DR EnsemblBacteria; AAS64031; AAS64031; YP_3886.
DR GeneID; 66844012; -.
DR KEGG; ype:YPO3660; -.
DR KEGG; ypk:y0207; -.
DR KEGG; ypm:YP_3886; -.
DR PATRIC; fig|214092.21.peg.4165; -.
DR eggNOG; COG0757; Bacteria.
DR HOGENOM; CLU_090968_1_0_6; -.
DR OMA; AYTHYSY; -.
DR UniPathway; UPA00053; UER00086.
DR EvolutionaryTrace; Q8ZAX1; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IBA:GO_Central.
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 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; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Lyase; Reference proteome.
FT CHAIN 1..150
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_0000159946"
FT ACT_SITE 26
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT ACT_SITE 103
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 104..105
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT SITE 21
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:3LWZ"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:3LWZ"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:3LWZ"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:3LWZ"
FT HELIX 31..44
FT /evidence="ECO:0007829|PDB:3LWZ"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:3LWZ"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:3LWZ"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:3LWZ"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:3LWZ"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:3LWZ"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:3LWZ"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:3LWZ"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:3LWZ"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:3LWZ"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:3LWZ"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:3LWZ"
FT HELIX 133..148
FT /evidence="ECO:0007829|PDB:3LWZ"
SQ SEQUENCE 150 AA; 16395 MW; 76D8085848BD78E3 CRC64;
MSDKFHILLL NGPNLNLLGT REPEKYGYTT LAEIVSQLEI QAQGMDVALS HLQSNAEHAL
IDSIHQARGN TDFILINPAA FTHTSVALRD ALLGVQIPFI EIHLSNVHAR EPFRHHSYLS
DIAVGVICGL GADGYNFALQ AAVNRLSKSN
