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Q65M66 (AROD_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-dehydroquinate dehydratase

Short name=3-dehydroquinase
EC=4.2.1.10
Alternative name(s):
Type I DHQase
Gene names
Name:aroD
Ordered Locus Names:BLi00939, BL00001
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

3-dehydroquinate = 3-dehydroshikimate + H2O. HAMAP MF_00214

Pathway

Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. HAMAP MF_00214

Subunit structure

Homodimer By similarity. HAMAP MF_00214

Sequence similarities

Belongs to the type-I 3-dehydroquinase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Aromatic amino acid biosynthesis
   LigandSchiff base
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processaromatic amino acid family biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function3-dehydroquinate dehydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2542543-dehydroquinate dehydratase HAMAP MF_00214
PRO_0000325519

Sites

Active site1441Proton acceptor By similarity
Active site1711Schiff-base intermediate with substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65M66 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 80C9F8560A258A87

FASTA25427,695
        10         20         30         40         50         60 
MKKLVKVRGI TLGEGRPKIC VPLVGKNLAQ LKEEAAYFQT LDADIAEWRA DFYEDVDDVD 

        70         80         90        100        110        120 
QVCAALAEIR GLLKDTPLIF TFRSAAEGGE KEISTARYFS LNEAVVKTGL ADVIDIELFN 

       130        140        150        160        170        180 
DEEQVKALVE TAHGHEVSVI ISNHDFEKTP AAEEIVSRLR KAQELGADLP KIAVMPETTA 

       190        200        210        220        230        240 
DVLRLLEATC TMNEKYADRP IITMSMAGKG IISRLAGEVF GSAMTFGAAK KASAPGQIAA 

       250 
GELKEILHIL HRNL 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000002 Genomic DNA. Translation: AAU22502.1.
AE017333 Genomic DNA. Translation: AAU39848.1.
RefSeqYP_078140.1. NC_006270.3.
YP_090541.1. NC_006322.1.

3D structure databases

HSSPHSSP built from PDB template 1GQN based on UniProtKB P24670.
ProteinModelPortalQ65M66.
SMRQ65M66. Positions 3-252.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ65M66.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000054520; EBBACP00000053051; EBBACG00000054511.
EBBACT00000058723; EBBACP00000057156; EBBACG00000058714.
GeneID3029790.
3101155.
GenomeReviewsGene locus BLi00939 in contig AE017333_GR.
Gene locus BL00001 in contig CP000002_GR.
KEGGbld:BLi00939.
bli:BL00001.
NMPDRfig|279010.5.peg.1524.
PATRIC18947413. VBIBacLic203714_0912.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0710.
GeneTreeEBGT00050000001972.
HOGENOMHBG732926.
OMAIAKIAVM.
ProtClustDBPRK02412.

Enzyme and pathway databases

BioCycBLIC279010-1:BLI00939-MONOMER.
BLIC279010:BL00001-MONOMER.

Family and domain databases

HAMAPMF_00214. AroD.
[Tree]
InterProIPR018508. 3-dehydroquinate_DH_AS.
IPR013785. Aldolase_TIM.
IPR001381. DHquinase_I.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK03785.
PfamPF01487. DHquinase_I. 1 hit.
[Graphical view]
TIGRFAMsTIGR01093. AroD. 1 hit.
PROSITEPS01028. DEHYDROQUINASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAROD_BACLD
AccessionPrimary (citable) accession number: Q65M66
Secondary accession number(s): Q62XK6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families