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A8M0Q3 (A8M0Q3_SALAI) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 50. 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 length748 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 site1311 By similarity
Active site2021 By similarity PIRSR PIRSR038927-1
Metal binding4171Iron (heme axial ligand) By similarity PIRSR PIRSR038927-2

Sequences

Sequence LengthMass (Da)Tools
A8M0Q3 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 7064F8928CF911F3

FASTA74880,718
        10         20         30         40         50         60 
MDPNKPAKAV EGVVQAAAEE GADVTRADVP GAPGSAPPSV EEPTEPHDPL PSRKEQGTPE 

        70         80         90        100        110        120 
TRTPTGATTG LPPAANGQQG AFLTTAQGAR LRDTDHSLKA GPRGPILMQD HHFREKITHF 

       130        140        150        160        170        180 
DHERIPERVV HARGAGAHGV FTSYGAAEVT RAGFLRKGKE TPVFVRFSTV LGSRGSADTV 

       190        200        210        220        230        240 
RDTRGFATKF YTDEGNFDLV GNNMPVFFIQ DAIKFPDIIH AGKPHPDREI PQAQSAHDTF 

       250        260        270        280        290        300 
WDFVSLHTEA QHHAMWNMSD RGIPRSFRMM EGFGVHTFRL VNAAGETALA KFHWKPKLGV 

       310        320        330        340        350        360 
HSLTWEEAQM ISGMDPDFHR RDLYDAIEAG AYPEWELGLQ IVPDSPEETF AGVDLLDPTK 

       370        380        390        400        410        420 
FVPEELAPVQ PVGMLVLNRM PTNFFAETEQ VAFHVGSLVA GIDVTNDPLL QGRLFSYVDT 

       430        440        450        460        470        480 
QLTRLAGPNF PQIPINRPHA PVNDLLRDGF HQQAVHTGVA PYRPNSLDGG NPFPAGDDEN 

       490        500        510        520        530        540 
AFLDVPVTVA EAPKVRANPV SFDDHFSQVR LFWLSMSPVE REHIIRAYTF ELSKCYHQEI 

       550        560        570        580        590        600 
KERQLRCLAN IDPVLCAQVA AGLGLPAPEP TVPPVDVEPS PALSQLGRTW PTDGRTVGIV 

       610        620        630        640        650        660 
VDADSDLDGV DGVRSAVFAA GMVPLLVAAH GGKVGELPVQ RTFATGRATE FDALLLAGAP 

       670        680        690        700        710        720 
APAPDALPAA DAGHATLVDP RVRLLVQESW RHAKAIGGWG AGVSVLEQAG VLGTPGVVTG 

       730        740 
GSGTDVLAGV QRLMAAHRVW ERFPTAVT 

« Hide

References

[1]"Complete sequence of Salinispora arenicola CNS-205."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K. expand/collapse author list , Jenkins C., Udwary D., Xiang L., Gontang E., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CNS-205 EMBL ABV98063.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000850 Genomic DNA. Translation: ABV98063.1.
RefSeqYP_001537054.1. NC_009953.1.

3D structure databases

ProteinModelPortalA8M0Q3.
SMRA8M0Q3. Positions 83-296.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391037.Sare_2202.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV98063; ABV98063; Sare_2202.
GeneID5708197.
KEGGsaq:Sare_2202.
PATRIC23432926. VBISalAre38676_2229.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0753.
HOGENOMHOG000087851.
KOK03781.
OMAESFGDHF.
OrthoDBEOG6P5Z9F.

Enzyme and pathway databases

BioCycSARE391037:GH66-2234-MONOMER.

Family and domain databases

Gene3D2.40.180.10. 1 hit.
3.40.50.880. 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.
IPR029062. Class_I_gatase-like.
[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]
SUPFAMSSF52317. SSF52317. 1 hit.
SSF56634. SSF56634. 1 hit.
PROSITEPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA8M0Q3_SALAI
AccessionPrimary (citable) accession number: A8M0Q3
Entry history
Integrated into UniProtKB/TrEMBL: December 4, 2007
Last sequence update: December 4, 2007
Last modified: July 9, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)