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A2A136 (A2A136_9BACL) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

2 H2O2 = O2 + 2 H2O. RuleBase RU000498

Cofactor

Heme group By similarity. PIRSR PIRSR038928-2

Sequence similarities

Belongs to the catalase family. RuleBase RU000498

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site561 By similarity PIRSR PIRSR038928-1
Active site1291 By similarity
Metal binding3391Iron (heme axial ligand) PDB 2J2M
Metal binding3391Iron (heme axial ligand) By similarity PIRSR PIRSR038928-2

Sequences

Sequence LengthMass (Da)Tools
A2A136 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: 024092394EB49591

FASTA49156,523
        10         20         30         40         50         60 
MNENEKKLTT NQGVPIGDNQ NSRTAGRRGP TLLEDYQLIE KIAHFDRERV PERVVHARGF 

        70         80         90        100        110        120 
GAHGVFKVKN SMKKYTKAAF LQEEGTEVPV FARFSTVIHG THSPETLRDP RGFSVKFYTE 

       130        140        150        160        170        180 
EGNWDFVGNN LPVFFIRDAM KFPDMVHSLK PDPRTNIQDP DRYWDFMTLR PESTNMLMHI 

       190        200        210        220        230        240 
FTDEGIPASY RKMRGSSVHS FKWVNAHGNT VYIKLRWVPK EGVHNLSADE ATEVQGKDFN 

       250        260        270        280        290        300 
HASNDTFQAI ENGDFPEWDL FVQVLDPADV ENFDFDPLDA TKDWFEDVIP FQHVGTMTLN 

       310        320        330        340        350        360 
KNVDNYFAET ESVGFNPGVL VPGMLPSEDK LLQGRLFSYS DTQRHRIGPN YQQLPINCPF 

       370        380        390        400        410        420 
AQVNNYQRDG AMPFKQQTSS VNYEPNRYQD EPKQTPEYTE DTQPLHDDIH GRLEIEKTNN 

       430        440        450        460        470        480 
FGQAGEVYRR MTEEEQMALL NNLVNDLQQV RHENTVLLAI CNFYRADASL GEKLSEALNV 

       490 
DIKPFLQQMQ K 

« Hide

References

[1]"Relationship between the size of the bottleneck 15 A from iron in the main channel and the reactivity of catalase corresponding to the molecular size of substrates."
Hara I., Ichise N., Kojima K., Kondo H., Ohgiya S., Matsuyama H., Yumoto I.
Biochemistry 46:11-22(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB266484 Genomic DNA. Translation: BAF45371.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2J2MX-ray2.40A/B/C/D1-491[»]
ProteinModelPortalA2A136.
SMRA2A136. Positions 6-485.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.40.180.10. 1 hit.
InterProIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024711. Catalase_clade1/3.
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]
PIRSFPIRSF038928. Catalase_clade1-3. 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...

Other

EvolutionaryTraceA2A136.

Entry information

Entry nameA2A136_9BACL
AccessionPrimary (citable) accession number: A2A136
Entry history
Integrated into UniProtKB/TrEMBL: February 20, 2007
Last sequence update: February 20, 2007
Last modified: July 9, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)