P54721 (CADE_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Catechol-2,3-dioxygenase
EC=1.13.11.2

Alternative name(s):
Catechol-induced ring cleavage extradiol dioxygenase

Gene names

Name:	catE
Synonyms:	yfiE
Ordered Locus Names:	BSU08240

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	285 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the meta cleavage of catechol to 2-hydroxymuconic semialdehyde. Essential for growth and viability in the presence of catechol and probably involved in the detoxification of catechol. Ref.4
Catalytic activity	Catechol + O2 = 2-hydroxymuconate semialdehyde. Ref.4
Cofactor	Fe2+ ion By similarity.
Induction	Strongly induced by catechol, less strongly by 2-methylhydroquinone (2-MHQ) but only weakly by chromanon (6-brom-2-vinyl-chroman-4-on). Ref.4 Ref.5
Sequence similarities	Belongs to the extradiol ring-cleavage dioxygenase family.
Biophysicochemical properties	Kinetic parameters: Vmax=1.04 µmol/min/mg enzyme (at pH 7 and at 25 degrees Celsius) Ref.4

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism Detoxification
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW response to toxin Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	catechol 2,3-dioxygenase activity Inferred from electronic annotation. Source: EC ferrous iron binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 285	285	Catechol-2,3-dioxygenase		PRO_0000049525
Sites
	Metal binding	213	1	Iron By similarity
	Metal binding	264	1	Iron By similarity
Experimental info
	Sequence conflict	68	1	R → L in BAA09109. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P54721 [UniParc]. Last modified June 16, 2009. Version 2. Checksum: CCDA3E510D89C9FC	FASTA	285	31,565
	10 20 30 40 50 60 MTSIHEDTHI GYAKLTIRSL ERSLQFYCNV IGFQVLKKTD RQAELTADGK RVLLILEENP 70 80 90 100 110 120 SAVVLPERSV TGLYHFAILL PDRKELGIAL ARLIEHGIAI GHGDHAVSEA LYLSDPDGNG 130 140 150 160 170 180 IEMYADRPRS TWQRDREGNY VMTTTAVDIE GLLEEAGDER KTSLPNDTII GHIHLHVSDL 190 200 210 220 230 240 KEAKAFYTDV LGFDIVGNYA GMSALFVSAG GYHHHIGLNI WAGRNAPPKP TNASGLDYYT 250 260 270 280 VVLPHQEELD LVANRVKHAG YSIEETENSF RVKDPVSGAY ITFVI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Determination of a 12 kb nucleotide sequence around the 76 degrees region of the Bacillus subtilis chromosome." Yamamoto H., Uchiyama S., Fajar A.N., Ogasawara N., Sekiguchi J. Microbiology 142:1417-1421(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." 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. Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION TO 68.
[4]	"Differential gene expression in response to phenol and catechol reveals different metabolic activities for the degradation of aromatic compounds in Bacillus subtilis." Tam le T., Eymann C., Albrecht D., Sietmann R., Schauer F., Hecker M., Antelmann H. Environ. Microbiol. 8:1408-1427(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION. Strain: 168.
[5]	"Transcriptome and proteome analyses in response to 2-methylhydroquinone and 6-brom-2-vinyl-chroman-4-on reveal different degradation systems involved in the catabolism of aromatic compounds in Bacillus subtilis." Nguyen V.D., Wolf C., Maeder U., Lalk M., Langer P., Lindequist U., Hecker M., Antelmann H. Proteomics 7:1391-1408(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION, NOMENCLATURE. Strain: 168.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D50543 Genomic DNA. Translation: BAA09109.1. AL009126 Genomic DNA. Translation: CAB12653.2.
PIR	H69802.
RefSeq	NP_388705.2. NC_000964.3.
3D structure databases
ProteinModelPortal	P54721.
SMR	P54721. Positions 6-137, 167-283.
ModBase	Search...
Protein-protein interaction databases
STRING	224308.BSU08240.
Proteomic databases
PaxDb	P54721.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAB12653; CAB12653; BSU08240.
GeneID	936164.
KEGG	bsu:BSU08240.
PATRIC	18973298. VBIBacSub10457_0863.
Organism-specific databases
GenoList	BSU08240. [Micado]
Phylogenomic databases
eggNOG	COG2514.
HOGENOM	HOG000250737.
ProtClustDB	CLSK886889.
Enzyme and pathway databases
BioCyc	BSUB:BSU08240-MONOMER.
Family and domain databases
InterPro	IPR004360. Glyas_Fos-R_dOase_dom. IPR000486. Xdiol_ring_cleave_dOase_1/2. [Graphical view]
Pfam	PF00903. Glyoxalase. 2 hits. [Graphical view]
PROSITE	PS00082. EXTRADIOL_DIOXYGENAS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CADE_BACSU

Accession

Primary (citable) accession number: P54721

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	June 16, 2009
Last modified:	May 1, 2013
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program