P30263 (CATA_PICAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxisomal catalase
EC=1.11.1.6

Gene names

Name:	PXP9
Synonyms:	PXP-9

Organism

Pichia angusta (Yeast) (Hansenula polymorpha)

Taxonomic identifier

870730 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetales incertae sedis › Ogataea

Protein attributes

Sequence length	507 AA.
Sequence status	Complete.
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.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Peroxisome
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process 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 heme 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 – 507

507

Peroxisomal catalase

PRO_0000084926

Regions

Motif

505 – 507

3

Microbody targeting signal Potential

Sites

Active site

65

1

By similarity

Active site

138

1

By similarity

Metal binding

348

1

Iron (heme axial ligand) By similarity

Secondary structure

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507

Helix Strand Turn

Details...

Beta strand

21 – 23

3

Helix

45 – 54

10

Beta strand

74 – 76

3

Turn

82 – 84

3

Helix

88 – 90

3

Beta strand

99 – 102

4

Beta strand

116 – 118

3

Beta strand

123 – 126

4

Beta strand

133 – 136

4

Beta strand

139 – 141

3

Helix

148 – 150

3

Helix

151 – 158

8

Turn

162 – 164

3

Helix

169 – 178

10

Helix

180 – 182

3

Helix

183 – 190

8

Beta strand

210 – 213

4

Beta strand

219 – 228

10

Turn

237 – 239

3

Helix

250 – 260

11

Beta strand

266 – 274

9

Helix

276 – 279

4

Turn

295 – 297

3

Beta strand

306 – 310

5

Helix

315 – 318

4

Turn

319 – 321

3

Helix

339 – 355

17

Helix

360 – 362

3

Helix

364 – 366

3

Beta strand

425 – 427

3

Helix

433 – 436

4

Helix

437 – 445

9

Helix

453 – 464

12

Helix

469 – 479

11

Turn

480 – 482

3

Helix

489 – 499

11

Sequences

	Sequence		Length	Mass (Da)
	P30263 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 3536ED0A49539CC3	FASTA	507	57,849
	10 20 30 40 50 60 MSNPPVFTTS QGCPVSDPFT TQRIPLDSTG YKYAPPIGPL LLQDFKLIDT LSHFDRERIP 70 80 90 100 110 120 ERVVHAKGAG AYGVFEVTDD ITDVCSAKFL DTVGKKTRIF TRFSTVGGEK GSADTARDPR 130 140 150 160 170 180 GFATKFYTED GNLDLVYNNT PIFFIRDPIK FPHFIHTQKR NPATNLKDPN MFWDYLTAND 190 200 210 220 230 240 ESLHQVMYLF SNRGTPASYR TMNGYSGHTY KWYNSKGEWV YVQVHFIANQ GVHNLLDEEA 250 260 270 280 290 300 GRLAGEDPDH STRDLWEAIE KGDYPSWECY IQTMTLEQSK KLPFSVFDLT KVWPHKDFPL 310 320 330 340 350 360 RHFGRFTLNE NPKNYYAETE QIAFSPSHTV PGMEPSNDPV LQSRLFSYPD THRHRLGPNY 370 380 390 400 410 420 HQIPVNCPLK SGSFNPINRD GPMCVDGNLG GTPNYANAYN CPIQYAVSPK ASGNKPDEKY 430 440 450 460 470 480 TGEVVPYHWE HTDYDYFQPK MFWKVLGRTP GEQESLVKNV ANHVSAADEF IQDRVYEYFS 490 500 KAEPIIGDLI RKKVQELKRK ASSPSKI

References

[1]	"Targeting signal of the peroxisomal catalase in the methylotrophic yeast Hansenula polymorpha." Didion T., Roggenkamp R.O. FEBS Lett. 303:113-116(1992) [PubMed: 1607006] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL Y-5445.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X56501 Genomic DNA. Translation: CAA39856.1.

PIR

S23422.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2XQ1	X-ray	2.90	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P	3-507	[»]

ProteinModelPortal

P30263.

SMR

P30263. Positions 1-493.

ModBase

Search...

Protein family/group databases

PeroxiBase

5260. PangKat01.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024711. Catalase_clade1/3.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
[Graphical view]

Gene3D

G3DSA:2.40.180.10. Catalase_N. 1 hit.

PANTHER

PTHR11465. Catalase. 1 hit.

Pfam

PF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]

PIRSF

PIRSF038928. Catalase_clade1-3. 1 hit.

PRINTS

PR00067. CATALASE.

SMART

SM01060. Catalase. 1 hit.
[Graphical view]

SUPFAM

SSF56634. Catalase_N. 1 hit.

PROSITE

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

ProtoNet

Search...

Entry information

Entry name

CATA_PICAN

Accession

Primary (citable) accession number: P30263

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	January 25, 2012
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program