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3-dehydroquinate synthase (DHQS) (EC 4.2.3.4)

 A0A0L6JC07_9RHIZ        Unreviewed;       381 AA.
A0A0L6JC07;
11-NOV-2015, integrated into UniProtKB/TrEMBL.
11-NOV-2015, sequence version 1.
25-OCT-2017, entry version 15.
RecName: Full=3-dehydroquinate synthase {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00210916};
Short=DHQS {ECO:0000256|HAMAP-Rule:MF_00110};
EC=4.2.3.4 {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00210941};
Name=aroB {ECO:0000256|HAMAP-Rule:MF_00110};
ORFNames=AKJ13_06160 {ECO:0000313|EMBL:KNY23376.1};
Methylobacterium sp. ARG-1.
Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
Methylobacteriaceae; Methylobacterium.
NCBI_TaxID=1692501 {ECO:0000313|EMBL:KNY23376.1, ECO:0000313|Proteomes:UP000036734};
[1] {ECO:0000313|Proteomes:UP000036734}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ARG-1 {ECO:0000313|Proteomes:UP000036734};
Hirst R., James-Pederson M., Tai A.;
"Draft Genome Sequence of Methylobacterium sp. Strain ARG-1 Isolated
from the White-Rot Fungus, Armillaria gallica.";
Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-
heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
{ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00858858}.
-!- CATALYTIC ACTIVITY: 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
= 3-dehydroquinate + phosphate. {ECO:0000256|HAMAP-Rule:MF_00110,
ECO:0000256|SAAS:SAAS00336744}.
-!- COFACTOR:
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000256|HAMAP-Rule:MF_00110};
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|HAMAP-Rule:MF_00110};
Note=Binds 1 divalent metal cation per subunit. Can use either
Co(2+) or Zn(2+). {ECO:0000256|HAMAP-Rule:MF_00110};
-!- COFACTOR:
Name=NAD(+); Xref=ChEBI:CHEBI:57540;
Evidence={ECO:0000256|HAMAP-Rule:MF_00110,
ECO:0000256|SAAS:SAAS00336779};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|SAAS:SAAS00607009};
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 2/7. {ECO:0000256|HAMAP-Rule:MF_00110,
ECO:0000256|SAAS:SAAS00210851}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00110,
ECO:0000256|SAAS:SAAS00210934}.
-!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily.
Dehydroquinate synthase family. {ECO:0000256|HAMAP-Rule:MF_00110,
ECO:0000256|SAAS:SAAS00858850}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00110}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KNY23376.1}.
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EMBL; LHCD01000004; KNY23376.1; -; Genomic_DNA.
RefSeq; WP_050732563.1; NZ_LHCD01000004.1.
EnsemblBacteria; KNY23376; KNY23376; AKJ13_06160.
PATRIC; fig|1692501.3.peg.4414; -.
UniPathway; UPA00053; UER00085.
Proteomes; UP000036734; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
HAMAP; MF_00110; DHQ_synthase; 1.
InterPro; IPR016037; DHQ_synth_AroB.
InterPro; IPR030963; DHQ_synth_fam.
InterPro; IPR030960; DHQS/DOIS.
Pfam; PF01761; DHQ_synthase; 1.
PIRSF; PIRSF001455; DHQ_synth; 1.
TIGRFAMs; TIGR01357; aroB; 1.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00110,
ECO:0000256|SAAS:SAAS00210867};
Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00110,
ECO:0000256|SAAS:SAAS00210867};
Cobalt {ECO:0000256|HAMAP-Rule:MF_00110,
ECO:0000256|SAAS:SAAS00210864};
Complete proteome {ECO:0000313|Proteomes:UP000036734};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00110,
ECO:0000256|SAAS:SAAS00210856};
Lyase {ECO:0000256|HAMAP-Rule:MF_00110,
ECO:0000256|SAAS:SAAS00210861};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00110,
ECO:0000256|SAAS:SAAS00858959};
NAD {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00210880};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00110,
ECO:0000256|SAAS:SAAS00858852};
Zinc {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00210870}.
DOMAIN 77 340 DHQ_synthase. {ECO:0000259|Pfam:PF01761}.
NP_BIND 115 119 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}.
NP_BIND 139 140 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}.
NP_BIND 179 182 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}.
METAL 194 194 Cobalt or zinc. {ECO:0000256|HAMAP-
Rule:MF_00110}.
METAL 256 256 Cobalt or zinc; via tele nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00110}.
METAL 275 275 Cobalt or zinc; via tele nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00110}.
BINDING 152 152 NAD; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_00110}.
BINDING 161 161 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}.
SEQUENCE 381 AA; 39661 MW; 2E261F5D2B1164FD CRC64;
MSELSTHPVP LTVHVPLDAG RDYDILIGRG LIETAGARVA ALGGRRAAIV TDANVAALYG
DRLRTSLERA GLGSGIVTVA PGEGSKSYAG YAQVCDGLLA LKVERGDLVV ALGGGVVGDL
AGFAAATLRR GVRFVQVPTS LLAQVDSSVG GKTGINAPLG KNLIGAFHQP RLVLADTATL
DTLSEREMRA GYAEVAKYGL IADAGFFDWC EANWRGIFSG GPEREEAVAA CCRAKAAVVT
RDEREDGERA LLNLGHTFGH ALERITGYDS ARLVHGEGVA IGTALAFRFS ARLGLCPGQD
AGRVANHLAL AGLPTRLQAV PGGCGDADAL VEAMAQDKKV RDGALTFILA RGIGQSFIAP
GIDRSEVRAF LQDELAADLR P


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