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Q1RB63 (Q1RB63_ECOUT) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 63. Feed History...

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

Names and origin

Protein attributes

Sequence length753 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

2 H2O2 = O2 + 2 H2O. RuleBase RU000498

Cofactor

Heme group By similarity. PIRSR PIRSR038927-2

Sequence similarities

Belongs to the catalase family. RuleBase RU000498

Ontologies

Keywords
   Biological processHydrogen peroxide RuleBase RU000498
   LigandHeme RuleBase RU000498
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncatalase activity

Inferred from electronic annotation. Source: UniProtKB-EC

heme binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1281 By similarity
Active site2011 By similarity
Metal binding4151Iron (heme axial ligand) By similarity PIRSR PIRSR038927-2

Sequences

Sequence LengthMass (Da)Tools
Q1RB63 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 257B48341134D21E

FASTA75384,199
        10         20         30         40         50         60 
MSQHNEKNPH QHQSPLHDSS EAKPGMDSLA PEDGSHRPAA EPTPPGAQPT APGSLKAPDT 

        70         80         90        100        110        120 
RNEKLNSLED VRKGSENYAL TTNQGVRIAD DQNSLRAGSR GPTLLEDFIL REKITHFDHE 

       130        140        150        160        170        180 
RIPERIVHAR GSAAHGYFQP YKSLSDITKA DFLSDTNKIT PVFVRFSTVQ GGAGSADTVR 

       190        200        210        220        230        240 
DIRGFATKFY TEEGIFDLVG NNTPIFFIQD AHKFPDFVHA VKPEPHWAIP QGQSAHDTFW 

       250        260        270        280        290        300 
DYVSLQPETL HNVMWAMSDR GIPRSYRTME GFGIHTFRLI NAEGKATFVR FHWKPLAGKA 

       310        320        330        340        350        360 
SLVWDEAQKL TGRDPDFHRR ELWEAIEAGD FPEYELGFQL IPEEDEFKFD FDLLDPTKLI 

       370        380        390        400        410        420 
PEELVPVQRV GKMVLNRNPD NFFAENEQVA FHPGHIVPGL DFTNDPLLQG RLFSYTDTQI 

       430        440        450        460        470        480 
SRLGGPNFHE IPINRPTCPY HNFQRDGMHR MGIDTNPANY EPNSINDNWP RETPPGPKRG 

       490        500        510        520        530        540 
GFESYQERVE GNKVRERSPS FGEYYSHPRL FWLSQTPFEQ RHIVDGFSFE LSKVVRPYIR 

       550        560        570        580        590        600 
ERVVDQLAHI DLTLAQAVAK NLGIELTDDQ LNITPPPDVN GLKKDPSLSL YSIPDGDVKG 

       610        620        630        640        650        660 
RVVAILLNDE VRSADLLAIL KALKAKGVHA KLLYSRMGEV TADDGTVLPI AATFAGAPSL 

       670        680        690        700        710        720 
TVDAVIVPCG NIADIADNGD ANYYLMEAYK HLKPIALAGD ARKFKATIKV ADQGEEGIAE 

       730        740        750 
ADSADGSFMD ELLTLMTAHR VWSRIPKIDK IPA 

« Hide

References

[1]"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach."
Chen S.L., Hung C.S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UTI89 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000243 Genomic DNA. Translation: ABE07401.1.
RefSeqYP_540932.1. NC_007946.1.

3D structure databases

ProteinModelPortalQ1RB63.
SMRQ1RB63. Positions 27-753.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING364106.UTI89_C1925.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE07401; ABE07401; UTI89_C1925.
GeneID3990377.
KEGGeci:UTI89_C1925.
PATRIC18453442. VBIEscCol42261_1968.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0753.
HOGENOMHOG000087851.
KOK03781.
OMAHALTTNQ.
OrthoDBEOG6P5Z9F.
ProtClustDBPRK11249.

Enzyme and pathway databases

BioCycECOL364106:GHPQ-1910-MONOMER.

Family and domain databases

Gene3D2.40.180.10. 1 hit.
InterProIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024712. Catalase_clade2.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
[Graphical view]
PANTHERPTHR11465. PTHR11465. 1 hit.
PfamPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFPIRSF038927. Catalase_clade2. 1 hit.
PRINTSPR00067. CATALASE.
SMARTSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMSSF56634. SSF56634. 1 hit.
PROSITEPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ1RB63_ECOUT
AccessionPrimary (citable) accession number: Q1RB63
Entry history
Integrated into UniProtKB/TrEMBL: May 16, 2006
Last sequence update: May 16, 2006
Last modified: February 19, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)