Catalase-peroxidase - Escherichia coli O111:H- (strain 11128 / EHEC)

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Unreviewed, UniProtKB/TrEMBL C8UKK4 (C8UKK4_ECO1A)

Last modified March 2, 2010. Version 5. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequences · References · Cross-references · Entry information

Names and origin

Protein names

Recommended name:
Catalase-peroxidase RuleBase RU003451V0
EC=1.11.1.6 RuleBase RU003451V0

Gene names

Name:	katG EMBL BAI38514.1
Ordered Locus Names:	ECO111_4768

Organism

Escherichia coli O111:H- (strain 11128 / EHEC) [Complete proteome] [HAMAP]

Taxonomic identifier

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	726 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity

2 H₂O₂ = O₂ + 2 H₂O. RuleBase RU003451V0

Sequence similarities

Belongs to the peroxidase family.

Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide RuleBase RU003451V0
Ligand	Heme RuleBase RU003900V0 Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: InterPro response to oxidative stress Inferred from electronic annotation. Source: InterPro
Molecular function	catalase activity Inferred from electronic annotation. Source: HAMAP heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

Sequence

Length

Mass (Da)

Tools

C8UKK4-1 [UniParc].

Last modified November 3, 2009. Version 1.
Checksum: 24D32EA9DEB33A06
Show »

726

80,040

        10         20         30         40         50         60 
MSTSDDIHNT TATGKCPFHQ GGHDQSAGAG TTTRDWWPNQ LRVDLLNQHS NRSNPLGEDF 

        70         80         90        100        110        120 
DYRKEFSKLD YYGLKKDLKA LLTESQPWWP ADWGSYAGLF IRMAWHGAGT YRSIDGRGGA 

       130        140        150        160        170        180 
GRGQQRFAPL NSWPDNVSLD KARRLLWPIK QKYGQKISWA DLFILAGNVA LENSGFRTFG 

       190        200        210        220        230        240 
FGAGREDVWE PDLDVNWGDE KAWLTHRHPE ALAKAPLGAT EMGLIYVNPE GPDHSGEPLS 

       250        260        270        280        290        300 
AAAAIRATFG NMGMNDEETV ALIAGGHTLG KTHGAGPTSN VGPDPEAAPI EEQGLGWAST 

       310        320        330        340        350        360 
YGSGVGADAI TSGLEVVWTQ TPTQWSNYFF ENLFKYEWVQ TRSPAGAIQF EAVDAPEIIP 

       370        380        390        400        410        420 
DPFDPSKKRK PTMLVTDLTL RFDPEFEKIS RRFLNDPQAF NEAFARAWFK LTHRDMGPKS 

       430        440        450        460        470        480 
RYIGPEVPKE DLIWQDPLPQ PIYNPTEQDI IDLKFAIADS GLSVSELVSV AWASASTFRG 

       490        500        510        520        530        540 
GDKRGGANGA RLALMPQRDW DVNAAAVRAL PVLEKIQKES GKASLADIIV LAGVVGVEKA 

       550        560        570        580        590        600 
ASAAGLSIHV PFAPGRVDAR QDQTDIEMFE LLEPIADGFR NYRARLDVST TESLLIDKAQ 

       610        620        630        640        650        660 
QLTLTAPEMT ALVGGMRVLG ANFDGSKNGV FTDRVGVLSN DFFVNLLDMR YEWKATDESK 

       670        680        690        700        710        720 
ELFEGRDRET GEVKYTASRA DLVFGSNSVL RAVAEVYASS DAHEKFVKDF VAAWVKVMNL 


DRFDLL

References

[1]

"Comparative genomics reveal the mechanism of the parallel evolution of O157 and non-O157 enterohemorrhagic Escherichia coli."
Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., Hayashi T.
Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009) [PubMed: 19815525] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP010960 Genomic DNA. Translation: BAI38514.1.
RefSeq	YP_003237065.1.
3D structure databases
SMR	C8UKK4. Positions 30-725.
ModBase	Search...
Genome annotation databases
GeneID	8487254.
GenomeReviews	Gene locus ECO111_4768 in contig AP010960_GR.
KEGG	eoi:ECO111_4768.
Organism-specific databases
CMR	Search...
Phylogenomic databases
ProtClustDB	CLSK862766.
Family and domain databases
HAMAP	MF_01961. Catal-peroxid. [Tree]
InterPro	IPR000763. Catalase_peroxidase. IPR010255. Haem_peroxidase. IPR002016. Haem_peroxidase_pln/fun/bac. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view]
Pfam	PF00141. peroxidase. 2 hits. [Graphical view]
PRINTS	PR00460. BPEROXIDASE. PR00458. PEROXIDASE.
SUPFAM	SSF48113. Peroxidase_super. 2 hits.
TIGRFAMs	TIGR00198. cat_per_HPI. 1 hit.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

C8UKK4_ECO1A

Accession

Primary (citable) accession number: C8UKK4

Entry history

Integrated into UniProtKB/TrEMBL:	November 3, 2009
Last sequence update:	November 3, 2009
Last modified:	March 2, 2010
This is version 5 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequences · References · Cross-references · Entry information