[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Petit Havana SR1; TISSUE=Leaf; DOI=10.1104/pp.106.1.399; PubMed=7972525 [NCBI, ExPASy, EBI, Israel, Japan] Schultes N.P., Zelitch I., McGonigle B., Nelson T.; "The primary leaf catalase gene from Nicotiana tabacum and Nicotiana sylvestris."; Plant Physiol. 106:399-400(1994).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 4-492, AND PARTIAL PROTEIN SEQUENCE. STRAIN=cv. SR1, and cv. Xanthi NC; TISSUE=Leaf; PubMed=8266079 [NCBI, ExPASy, EBI, Israel, Japan] Chen Z., Silva H., Klessig D.F.; "Active oxygen species in the induction of plant systemic acquired resistance by salicylic acid."; Science 262:1883-1886(1993).

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.
ENZYME REGULATION: Inhibited by salicylic acid.
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Peroxisome (By similarity). Glyoxysome (By similarity).
SIMILARITY: Belongs to the catalase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U07627; AAA57552.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03473; AAC48918.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A49388; A49388.

3D structure databases

HSSP

P46206; 1M7S. [HSSP ENTRY / PDB]

ModBase

P49319.

Ontologies

GO:0009514;	Cellular component: glyoxysome (inferred from electronic annotation from UniProtKB-KW).
GO:0005777;	Cellular component: peroxisome (inferred from electronic annotation from UniProtKB-KW).
GO:0004096;	Molecular function: catalase activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0042744;	Biological process: hydrogen peroxide catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002226; Catalase.
IPR011614; Catalase_N.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.180.10; Catalase_N; 1.

PANTHER

PTHR11465; Catalase; 1.

Pfam

PF00199; Catalase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00067; CATALASE.

ProDom

PD000510; Catalase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00437; CATALASE_1; 1.
PS00438; CATALASE_2; 1.
PS51402; CATALASE_3; 1.
PROSITE graphical view of domain structure (profiles).

Other

ProtoNet

P49319.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Glyoxysome; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Peroxisome.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 492`	`492`	`Catalase isozyme 1.`	`PRO_0000084966`
`ACT_SITE`	`65 65`		`By similarity.`
`ACT_SITE`	`138 138`		`By similarity.`
`METAL`	`348 348`		`Iron (heme axial ligand) (By similarity).`
`CONFLICT`	`140 140`		`V -> F (in Ref. 2; AA sequence).`
`CONFLICT`	`145 145`		`N -> I (in Ref. 2; AA sequence).`
`CONFLICT`	`171 171`		`K -> R (in Ref. 2; AAC48918).`
`CONFLICT`	`438 438`		`W -> F (in Ref. 2; AA sequence).`
`CONFLICT`	`439 439`		`E -> T (in Ref. 2; AA sequence).`
`CONFLICT`	`453 453`		`H -> A (in Ref. 2; AA sequence).`
`CONFLICT`	`469 470`		`SY -> CS (in Ref. 2; AAC48918).`

Sequence information

Length: 492 AA [This is the length of the unprocessed precursor]

Molecular weight: 56824 Da [This is the MW of the unprocessed precursor]

CRC64: 8AD3ED82F7CCE94E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDLSKFRPSS AYDSPFLTTN AGGPVYNNVS SLTVGPRGPV LLEDYHLIEK LATFDRERIP 

        70         80         90        100        110        120 
ERVVHARGAS AKGFFEVTHD ISHLTCADFL RAPGVQTPVI CRFSTVVHER GSPESLRDIR 

       130        140        150        160        170        180 
GFAVKFYTRE GNFDLVGNNV PVFFNRDAKS FPDTIRALKP NPKSHIQEYW KILDFFSFLP 

       190        200        210        220        230        240 
ESLHTFAWFF DDVCLPTDYR HMEGYGVHAY QLINKAGKAH YVKFHWKPTC GVKCMSEEEA 

       250        260        270        280        290        300 
IRVGGTNHSH ATKDLYDSIA AGNYPEWKLF IQIMDTEDVD KFDFDPLDVT KTWPEDILPL 

       310        320        330        340        350        360 
MPVGRLVLNR NIDNFFAENE QLAFNPGHIV PGLYYSEDKL LQTRIFAYAD TQRHRIGPNY 

       370        380        390        400        410        420 
MQLPVNAPKC AHHNNHRDGA MNFMHRDEEV DYLPSRFDPC RHAEQYPIPS RVLTGRREMC 

       430        440        450        460        470        480 
VIEKENNFKQ AGERYRSWEP DRQDRYVSKW VEHLSDPRVT YEIRSIWISY LSQADKSCGQ 

       490 
KVASRLTLKP TM

P49319 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools