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3-dehydroquinate synthase (DHQS) (EC 4.2.3.4)

 F4ANH3_GLAS4            Unreviewed;       355 AA.
F4ANH3;
28-JUN-2011, integrated into UniProtKB/TrEMBL.
28-JUN-2011, sequence version 1.
25-OCT-2017, entry version 43.
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};
OrderedLocusNames=Glaag_0731 {ECO:0000313|EMBL:AEE21694.1};
Glaciecola sp. (strain 4H-3-7+YE-5).
Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
Alteromonadaceae; Glaciecola.
NCBI_TaxID=983545 {ECO:0000313|EMBL:AEE21694.1, ECO:0000313|Proteomes:UP000006544};
[1] {ECO:0000313|EMBL:AEE21694.1, ECO:0000313|Proteomes:UP000006544}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=4H-3-7+YE-5 {ECO:0000313|EMBL:AEE21694.1,
ECO:0000313|Proteomes:UP000006544};
PubMed=21705587; DOI=10.1128/JB.05468-11;
US DOE Joint Genome Institute;
Klippel B., Lochner A., Bruce D.C., Davenport K.W., Detter C.,
Goodwin L.A., Han J., Han S., Land M.L., Mikhailova N., Nolan M.,
Pennacchio L., Pitluck S., Tapia R., Woyke T., Wiebusch S., Basner A.,
Abe F., Horikoshi K., Keller M., Antranikian G.;
"Complete genome sequence of the marine, cellulose and xylan degrading
bacterium Glaciecola sp. 4H-3-7+YE-5.";
J. Bacteriol. 193:4547-4548(2011).
[2]
NUCLEOTIDE SEQUENCE.
STRAIN=4H-3-7+YE-5;
US DOE Joint Genome Institute;
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I.,
Piela B., Lochner A., Antranikian F.I., Woyke T.;
"Complete sequence of chromosome of Glaciecola sp. 4H-3-7+YE-5.";
Submitted (FEB-2011) 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}.
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EMBL; CP002526; AEE21694.1; -; Genomic_DNA.
RefSeq; WP_013752896.1; NC_015497.1.
STRING; 983545.Glaag_0731; -.
EnsemblBacteria; AEE21694; AEE21694; Glaag_0731.
KEGG; gag:Glaag_0731; -.
eggNOG; ENOG4105D49; Bacteria.
eggNOG; COG0337; LUCA.
KO; K01735; -.
OrthoDB; POG091H0125; -.
UniPathway; UPA00053; UER00085.
Proteomes; UP000006544; Chromosome.
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:UP000006544};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00110,
ECO:0000256|SAAS:SAAS00210856};
Lyase {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00210861,
ECO:0000313|EMBL:AEE21694.1};
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 65 323 DHQ_synthase. {ECO:0000259|Pfam:PF01761}.
NP_BIND 69 74 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}.
NP_BIND 103 107 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}.
NP_BIND 127 128 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}.
NP_BIND 167 170 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}.
METAL 182 182 Cobalt or zinc. {ECO:0000256|HAMAP-
Rule:MF_00110}.
METAL 245 245 Cobalt or zinc; via tele nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00110}.
METAL 262 262 Cobalt or zinc; via tele nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00110}.
BINDING 140 140 NAD; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_00110}.
BINDING 149 149 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}.
SEQUENCE 355 AA; 38718 MW; 1F7B08CEC01DB851 CRC64;
MTTLTVKLGE RSYPIFIQPS LLSQGNKLAD YIKTDKAVLV TNDLVDPLYS QTIIASLPDI
KIDKIVIADG EQHKNLASFE HVITQLLNMS AARDTTLIAL GGGVIGDLTG FVAASFQRGM
PFIQIPTTLL SQVDSSVGGK TAVNHPLGKN MIGAFYQPKA VFIDTKTLQT LPAKEFSAGM
AEVIKYGIIY DKAFFEWLEQ NTAQLISQDV DALQYAIARC CEIKAEIVAI DERESGLRAL
LNLGHTFGHA IEAEQGYGNW LHGEAVAAGM VLAAKAGQMK GWMQTEEVQR VIALIEAFAL
PITPPTDMGY DTFMQHMVHD KKVQAGKLNY IIPKAIGEAI VTPELDETLL KNLLN


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