Reviewed, UniProtKB/Swiss-Prot P11934 (CATA_PENJA)

Names and origin

Protein names	Recommended name:     Catalase     EC=1.11.1.6
Organism	Penicillium janthinellum (Penicillium vitale)
Taxonomic identifier	5079 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Penicillium

Protein attributes

Sequence length	670 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic activity	2 H2O2 = O2 + 2 H2O.
Cofactor	Heme group.
Subunit structure	Homotetramer.
Subcellular location	Peroxisome.
Sequence similarities	Belongs to the catalase family.
Caution	This is an X-ray determined sequence, alanine is indicated in position where no side chain could be observed.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Peroxisome
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	catalase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 670	670	Catalase		PRO_0000084924
Sites
	Active site	61	1
	Active site	132	1
	Metal binding	345	1	Iron (heme axial ligand) Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P11934-1 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 5EA0E355EC01BED6	FASTA	670	70,260
	10 20 30 40 50 60 AAAQRRQNDS SVFLAIMVAA AVESESSLTD GDAGALLLQD ISEWDEVFRF DRLEAVERAA 70 80 90 100 110 120 HAAAAAAFGA FVARGDWTAS AAAAFQAAGK QIAFMAAFST VAGAKGSATV RDADAFAAKF 130 140 150 160 170 180 ASAAALQELV GNNSPISFFI FDLLFAAILF ASKAKAANQA AFAAAAELAA ESLFVRLPSL 190 200 210 220 230 240 HQVSFFALAG FAAVAAHRHM NGYGSHTFKL VAKDGSVYCS KFWYKADQGQ AAEVWKDAEE 250 260 270 280 290 300 VAAEDVDYFR DLNFQAEAAG RYPLWELASQ VMTFSDFEID PFNENIPTKV VPRESVPLIV 310 320 330 340 350 360 DAELLLNRNP LNMFAEVEQV FMDVAAASKG ADEVEDPLIQ RQFAYIDTHL SELTASYGIP 370 380 390 400 410 420 VCRPYATVLN DQEDGARYDD VQDVLVIAPN AFSASAVEVQ IPAAAAFNLA AARVAAAGDV 430 440 450 460 470 480 RVNAVVEADQ RKQSRQFWAS DVNAQKKRLV DAFRMEVASA VSASIQVDVT VEFSFVAAAA 490 500 510 520 530 540 AARIAAAVGS AAAGALANRR QIKVIASLAV LAKADAKVRQ KNALESSSQA VAVDAKAAAQ 550 560 570 580 590 600 DIVDSSDAAN VVTVAREFAV LPQTAAADAA EFVAAASAKA FSSFPAMEVI SVAAAAGAVA 610 620 630 640 650 660 EPARASLDLN MAMFFSRIVA SRGAAANAIA ALVKASRDGV FVAAVLAKAA ANNRAAEAIF 670 KFEVRQAVDA

References

[1]	"Three-dimensional structure of catalase from Penicillium vitale at 2.0-A resolution." Vainshtein B.K., Melik-Adamyan W.R., Barynin V.V., Vagin A.A., Grebenko A.I., Borisov V.V., Bartels K.S., Fita I., Rossmann M.G. J. Mol. Biol. 188:49-61(1986) [PubMed: 3712443] [Abstract] Cited for: PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS).
[2]	"Comparison of beef liver and Penicillium vitale catalases." Melik-Adamyan W.R., Barynin V.V., Vagin A.A., Borisov V.V., Vainshtein B.K., Fita I., Murthy M.R.N., Rossmann M.G. J. Mol. Biol. 188:63-72(1986) [PubMed: 3712444] [Abstract] Cited for: SIMILARITY TO BOVINE CATALASE.

Cross-references

Sequence databases

PIR

A25001.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4CAT	X-ray	3.00	A/B	-	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.11.1.6. 18847.

Family and domain databases

InterPro

IPR002226. Catalase.
IPR011614. Catalase_N.
IPR018028. Catalase_rel_subgroup.
[Graphical view]

Gene3D

G3DSA:2.40.180.10. Catalase_N. 1 hit.

PANTHER

PTHR11465. Catalase. 1 hit.

Pfam

PF00199. Catalase. 1 hit.
[Graphical view]

PRINTS

PR00067. CATALASE.

ProDom

PD000510. Catalase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00437. CATALASE_1. False negative.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CATA_PENJA

Accession

Primary (citable) accession number: P11934

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)