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B8FZL5 (B8FZL5_DESHD) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 33. 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 namesRecommended name:
Catalase RuleBase RU000498
EC=1.11.1.6 RuleBase RU000498
Gene names
Ordered Locus Names:Dhaf_1029
OrganismDesulfitobacterium hafniense (strain DCB-2 / DSM 10664) [Complete proteome] [HAMAP] EMBL ACL19089.1
Taxonomic identifier272564 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Peptococcaceae › Desulfitobacterium ›

Protein attributes

Sequence length682 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: 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

Metal binding3591Iron (heme axial ligand) By similarity PIRSR PIRSR038927-2

Sequences

Sequence LengthMass (Da)Tools
B8FZL5 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 1F65D004D4AC86F9

FASTA68276,847
        10         20         30         40         50         60 
MKDNKPNKKR EQLEPFIHES EGKKMTSNEG ITISDDENTL TAGERGPTLI EDFLSREKLA 

        70         80         90        100        110        120 
HFDRERIPER VVHARGYGAH GEFQPYESLA DLTMADFLQD PNKKTPLFVR FSQVVGSKGC 

       130        140        150        160        170        180 
NETNRDVRGF SIKFYTDEGN FDLIAINMPV FFIQDAIKFP DLIHAVKPEP DNEYPQGQTD 

       190        200        210        220        230        240 
HNTFWDFMAN NKETAHMSLW IASNRAFPKS FRTMEGFGVH TFRLVNKDGK SHFVKFHIKP 

       250        260        270        280        290        300 
LLGVHSLIWD EAQRLGSDAD FHRRDLWENI EIGNYPEYEM AIQVIKEEDE FAYDFDLLDP 

       310        320        330        340        350        360 
TKLWPEEEIP LRRIGKIILN RNVENAFAET EQSAFHPGNI VRGIDFSNDP LLQGRLFSYT 

       370        380        390        400        410        420 
DAQQARLGPN HQQLPINRPV CPFANNQRDG ASRLVIDRGK VAYHRNGLAN NSPYTVPGTQ 

       430        440        450        460        470        480 
GGFVTYPSTV EGHKVRSTAP SFKDHYSQAK MFWNSMSEVE KRQIIGAYCF ELGKCGPFVR 

       490        500        510        520        530        540 
QEWVDVLAHI STELAKSVSK ELGTTVPADV EESPVTKSSP ALSLHNTIFV PDTLRVAVFL 

       550        560        570        580        590        600 
AQGFDGPGVS KVLETLAEAK LRVVIVHDTL GKVSGTEGVT YEVHDSFLTG SPLVYDGILI 

       610        620        630        640        650        660 
VGSGNITPYF TYTAQKFTTD IYNHFKPIGI IQKGDAVLEP LGLLADEGIV TDSGPDFAGR 

       670        680 
FIKAMAKQRF WNRPSFLYPA MV

« Hide

References

[1]"Complete sequence of Desulfitobacterium hafniense DCB-2."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Ovchinnikova G., Madsen T., Christiansen N., Ahring B., Marsh T., Harzman C., Davis J.K., Kim S.-H., Tiedje J.M.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DCB-2 / DSM 10664.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001336 Genomic DNA. Translation: ACL19089.1.
RefSeqYP_002457525.1. NC_011830.1.

3D structure databases

ProteinModelPortalB8FZL5.
SMRB8FZL5. Positions 20-241.
ModBaseSearch...

Protein-protein interaction databases

STRING272564.Dhaf_1029.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL19089; ACL19089; Dhaf_1029.
GeneID7257997.
KEGGdhd:Dhaf_1029.
PATRIC21659735. VBIDesHaf15223_1069.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0753.
HOGENOMHOG000087851.
KOK03781.
OMAECPRARA.
ProtClustDBCLSK904728.

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. Catalase_N. 1 hit.
PROSITEPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB8FZL5_DESHD
AccessionPrimary (citable) accession number: B8FZL5
Entry history
Integrated into UniProtKB/TrEMBL: March 3, 2009
Last sequence update: March 3, 2009
Last modified: May 1, 2013
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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