P60355 (MCAT_LACPN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Manganese catalase EC=1.11.1.6 Alternative name(s): Pseudocatalase
Organism	Lactobacillus plantarum
Taxonomic identifier	1590 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	266 AA.
Sequence status	Complete.
Protein existence	Evidence 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
Ligand	Calcium Manganese Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular function	catalase activity Inferred from electronic annotation. Source: EC transition metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 266

266

Manganese catalase

PRO_0000096155

Sites

Metal binding

35

1

Manganese 1

Metal binding

57

1

Calcium

Metal binding

61

1

Calcium

Metal binding

66

1

Manganese 1

Metal binding

66

1

Manganese 2

Metal binding

69

1

Manganese 1

Metal binding

148

1

Manganese 2

Metal binding

181

1

Manganese 2

Metal binding

218

1

Calcium

Metal binding

220

1

Calcium; via carbonyl oxygen

Metal binding

222

1

Calcium; via carbonyl oxygen

Experimental info

Mutagenesis

42

1

Y → F: Loss of activity. Ref.3

Secondary structure

1

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266

Helix Strand Turn

Details...

Beta strand

2 – 4

3

Helix

19 – 30

12

Helix

35 – 48

14

Helix

53 – 80

28

Turn

81 – 83

3

Helix

88 – 93

6

Helix

97 – 103

7

Helix

106 – 110

5

Helix

128 – 130

3

Helix

137 – 159

23

Helix

165 – 196

32

Beta strand

198 – 201

4

Turn

205 – 207

3

Helix

210 – 212

3

Beta strand

215 – 217

3

Helix

224 – 228

5

Beta strand

240 – 244

5

Helix

259 – 261

3

Sequences

	Sequence		Length	Mass (Da)
	P60355 [UniParc]. Last modified February 16, 2004. Version 1. Checksum: 2943A15DD7A60CB1	FASTA	266	29,743
	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

References

[1]	"Molecular cloning of manganese catalase from Lactobacillus plantarum." Igarashi T., Kono Y., Tanaka K. J. Biol. Chem. 271:29521-29524(1996) [PubMed: 8939876] [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: 11587647] [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: 12631270] [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

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JKU	X-ray	1.84	A/B/C/D/E/F	1-266	[»]
1JKV	X-ray	1.39	A/B/C/D/E/F	1-266	[»]
1O9I	X-ray	1.33	A/B/C/D/E/F	1-266	[»]

ProteinModelPortal

P60355.

SMR

P60355. Positions 1-266.

ModBase

Search...

Protein family/group databases

PeroxiBase

3978. LplMnCat01.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR007760. Catalase_Mn.
IPR012347. Ferritin-rel.
IPR009078. Ferritin/RR-like.
[Graphical view]

Gene3D

G3DSA:1.20.1260.10. Ferritin_rel. 1 hit.

Pfam

PF05067. Mn_catalase. 1 hit.
[Graphical view]

SUPFAM

SSF47240. Ferritin/RR_like. 1 hit.

ProtoNet

Search...

Entry information

Entry name

MCAT_LACPN

Accession

Primary (citable) accession number: P60355

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 16, 2004
Last sequence update:	February 16, 2004
Last modified:	December 14, 2011
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program