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P60355 (MCAT_LACPN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Manganese catalase

EC=1.11.1.6
Alternative name(s):
Pseudocatalase
OrganismLactobacillus plantarum
Taxonomic identifier1590 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length266 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

2 H2O2 = O2 + 2 H2O.

Cofactor

Binds 1 calcium ion per subunit.

Binds 2 manganese ions per subunit.

Subunit structure

Homohexamer. Ref.2

Sequence similarities

Belongs to the manganese catalase family.

Ontologies

Keywords
   LigandCalcium
Manganese
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Molecular_functioncatalase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 266266Manganese catalase
PRO_0000096155

Sites

Metal binding351Manganese 1
Metal binding571Calcium
Metal binding611Calcium
Metal binding661Manganese 1
Metal binding661Manganese 2
Metal binding691Manganese 1
Metal binding1481Manganese 2
Metal binding1811Manganese 2
Metal binding2181Calcium
Metal binding2201Calcium; via carbonyl oxygen
Metal binding2221Calcium; via carbonyl oxygen

Experimental info

Mutagenesis421Y → F: Loss of activity. Ref.3

Secondary structure

...................................... 266
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P60355 [UniParc].

Last modified February 16, 2004. Version 1.
Checksum: 2943A15DD7A60CB1

FASTA26629,743
        10         20         30         40         50         60 
MFKHTRKLQY NAKPDRSDPI MARRLQESLG GQWGETTGMM SYLSQGWAST GAEKYKDLLL 

        70         80         90        100        110        120 
DTGTEEMAHV EMISTMIGYL LEDAPFGPED LKRDPSLATT MAGMDPEHSL VHGLNASLNN 

       130        140        150        160        170        180 
PNGAAWNAGY VTSSGNLVAD MRFNVVRESE ARLQVSRLYS MTEDEGVRDM LKFLLARETQ 

       190        200        210        220        230        240 
HQLQFMKAQE ELEEKYGIIV PGDMKEIEHS EFSHVLMNFS DGDGSKAFEG QVAKDGEKFT 

       250        260 
YQENPEAMGG IPHIKPGDPR LHNHQG 

« Hide

References

[1]"Molecular cloning of manganese catalase from Lactobacillus plantarum."
Igarashi T., Kono Y., Tanaka K.
J. Biol. Chem. 271:29521-29524(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-32 AND 67-86.
Strain: ATCC 14431 / T-1043-5.
[2]"Crystal structure of manganese catalase from Lactobacillus plantarum."
Barynin V.V., Whittaker M.M., Antonyuk S.V., Lamzin V.S., Harrison P.M., Artymiuk P.J., Whittaker J.W.
Structure 9:725-738(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS), SUBUNIT.
[3]"Outer sphere mutagenesis of Lactobacillus plantarum manganese catalase disrupts the cluster core. Mechanistic implications."
Whittaker M.M., Barynin V.V., Igarashi T., Whittaker J.W.
Eur. J. Biochem. 270:1102-1116(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS), MUTAGENESIS OF TYR-42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D87070 Genomic DNA. Translation: BAA13239.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JKUX-ray1.84A/B/C/D/E/F1-266[»]
1JKVX-ray1.39A/B/C/D/E/F1-266[»]
1O9IX-ray1.33A/B/C/D/E/F1-266[»]
ProteinModelPortalP60355.
SMRP60355. Positions 1-266.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

PeroxiBase3978. LplMnCat01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.20.1260.10. 1 hit.
3.30.1530.10. 1 hit.
InterProIPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR007760. Mn_catalase.
IPR027407. Mn_catalase_dom2.
[Graphical view]
PfamPF05067. Mn_catalase. 1 hit.
[Graphical view]
SUPFAMSSF47240. SSF47240. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP60355.

Entry information

Entry nameMCAT_LACPN
AccessionPrimary (citable) accession number: P60355
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: February 16, 2004
Last modified: December 11, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references