AROQ_PSYIN
ID AROQ_PSYIN Reviewed; 149 AA.
AC A1SZA3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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}; OrderedLocusNames=Ping_3121;
OS Psychromonas ingrahamii (strain 37).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Psychromonadaceae; Psychromonas.
OX NCBI_TaxID=357804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=37;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA Richardson P.;
RT "Complete sequence of Psychromonas ingrahamii 37.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000510; ABM04818.1; -; Genomic_DNA.
DR RefSeq; WP_011771372.1; NC_008709.1.
DR PDB; 6HSQ; X-ray; 1.46 A; A/B/C/D=1-149.
DR PDB; 6HSR; X-ray; 2.00 A; A/B/C/D=1-149.
DR PDB; 6HSU; X-ray; 1.60 A; A/B/C/D/E/F/G/H/I/J/K/L=1-149.
DR PDBsum; 6HSQ; -.
DR PDBsum; 6HSR; -.
DR PDBsum; 6HSU; -.
DR AlphaFoldDB; A1SZA3; -.
DR SMR; A1SZA3; -.
DR STRING; 357804.Ping_3121; -.
DR EnsemblBacteria; ABM04818; ABM04818; Ping_3121.
DR KEGG; pin:Ping_3121; -.
DR eggNOG; COG0757; Bacteria.
DR HOGENOM; CLU_090968_1_0_6; -.
DR OMA; AYTHYSY; -.
DR OrthoDB; 1872106at2; -.
DR BRENDA; 4.2.1.10; 11857.
DR UniPathway; UPA00053; UER00086.
DR Proteomes; UP000000639; 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; 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..149
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_1000023501"
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:6HSQ"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:6HSQ"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:6HSQ"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:6HSQ"
FT HELIX 31..43
FT /evidence="ECO:0007829|PDB:6HSQ"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:6HSQ"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:6HSQ"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:6HSQ"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:6HSQ"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:6HSQ"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:6HSQ"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:6HSQ"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:6HSQ"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:6HSQ"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:6HSQ"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:6HSQ"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:6HSQ"
FT HELIX 133..147
FT /evidence="ECO:0007829|PDB:6HSQ"
SQ SEQUENCE 149 AA; 16501 MW; F6EE464E3ECC7F06 CRC64;
MTQQIKLLVL NGPNLNLLGQ REPEVYGSKT LDDIIKALTD EAALQNVALS HLQSNREYEL
IEKIHDAFEK IDFIIINPAA FTHTSVALRD ALLGVNIPFI EVHLSNVHAR ESFRHHSYLS
DIAQGVICGL GAKGYSFALQ SAIGKLRNI
