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UniProtKB/Swiss-Prot entry P35146


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AROD_BACSU
Primary accession number P35146
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on February 1, 1994 (Sequence version 1)
Annotations were last modified on    October 14, 2008 (Entry version 68)
Name and origin of the protein
Protein name 3-dehydroquinate dehydratase
Synonyms 3-dehydroquinase
EC 4.2.1.10
Type I DHQase
Gene name
Name: aroC
OrderedLocusNames: BSU23080
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / Marburg;
PubMed=7934829 [NCBI, ExPASy, EBI, Israel, Japan]
Sorokin A.V., Zumstein E., Azevedo V., Ehrlich S.D., Serror P.;
"The organization of the Bacillus subtilis 168 chromosome region between the spoVA and serA genetic loci, based on sequence data.";
Mol. Microbiol. 10:385-395(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L09228; AAA67501.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99116; CAB14240.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S45563; S45563.
RefSeq NP_390189.1; -.
3D structure databases
HSSP P24670; 1L9W. [HSSP ENTRY / PDB]
ModBase P35146.
Enzyme and pathway databases
BioCyc BSUB224308:BSU2307-MON; -.
Organism-specific databases
SubtiList BG10538; aroC. [Micado]
Ontologies
GO
GO:0003855; Molecular function: 3-dehydroquinate dehydratase activity (inferred from electronic annotation from HAMAP).
GO:0009073; Biological process: aromatic amino acid family biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00214; -; 1.
PBIL [Tree]
InterPro IPR013785; Aldolase_TIM.
IPR001381; DHquinase_I.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
Pfam PF01487; DHquinase_I; 1.
Pfam graphical view of domain structure.
ProDom PD005337; DHquinase_I; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01093; aroD; 1.
PROSITE PS01028; DEHYDROQUINASE_I; 1.
ProtoNet P35146.
Genome annotation databases
GeneID 938963; -.
GenomeReviews AL009126_GR; BSU23080.
KEGG bsu:BSU23080; -.
NMPDR fig|224308.1.peg.2312; -.
Phylogenomic databases
HOGENOM P35146; -.
Genome annotation databases
CMR P35146; BSU23080.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Complete proteome; Lyase; Schiff base.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   255  255     3-dehydroquinate dehydratase. PRO_0000138793
ACT_SITE   143   143        Proton acceptor (By similarity). 
ACT_SITE   170   170        Schiff-base intermediate with substrate (By similarity). 
Sequence information
Length: 255 AA [This is the length of the unprocessed precursor] Molecular weight: 28132 Da [This is the MW of the unprocessed precursor] CRC64: 2B5E9833C6539726 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNVLTIKGVS IGEGMPKIII PLMGKTEKQI LNEAEAVKLL NPDIVEWRVD VFEKANDREA 

        70         80         90        100        110        120 
VTKLISKLRK SLEDKLFLFT FRTHKEGGSM EMDESSYLAL LESAIQTKDI DLIDIELFSG 

       130        140        150        160        170        180 
DANVKALVSL AEENNVYVVM SNHDFEKTPV KDEIISRLRK MQDLGAHIPK MAVMPNDTGD 

       190        200        210        220        230        240 
LLTLLDATYT MKTIYADRPI ITMSMAATGL ISRLSGEVFG SACTFGAGEE ASAPGQIPVS 

       250 
ELRSVLDILH KNTRG 

P35146 in FASTA format

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