Catalase isozyme 3 - Zea mays (Maize)

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P18123 (CATA3_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 85. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Catalase isozyme 3
EC=1.11.1.6

Gene names

Name:

CAT3

Organism

Zea mays (Maize)

Taxonomic identifier

4577 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › PACMAD clade › Panicoideae › Andropogoneae › Zea

Protein attributes

Sequence length	496 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Its levels are highest in the light period and are lowest in the dark period, hence it may be important for scavenging hydrogen peroxide at night, rather than during the day.
Catalytic activity	2 H₂O₂ = O₂ + 2 H₂O.
Cofactor	Heme group.
Subunit structure	Homotetramer.
Subcellular location	Mitochondrion.
Tissue specificity	Leaf mesophyll cells, pericarp, seedling roots and the coleoptile.
Sequence similarities	Belongs to the catalase family.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Mitochondrion
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion 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 – 496

496

Catalase isozyme 3

PRO_0000084948

Sites

Active site

By similarity

Active site

140

By similarity

Metal binding

351

Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict

A → D in AAA33441. Ref.2

Sequence conflict

A → D in CAA31057. Ref.2

Sequence conflict

C → S in AAA33441. Ref.2

Sequence conflict

C → S in CAA31057. Ref.2

Sequence conflict

107

T → Q in AAA33441. Ref.2

Sequence conflict

107

T → Q in CAA31057. Ref.2

Sequence conflict

110 – 116

HERGSPE → PEPGSGR in AAA33441. Ref.2

Sequence conflict

110 – 116

HERGSPE → PEPGSGR in CAA31057. Ref.2

Sequence conflict

121

P → A in AAA33441. Ref.2

Sequence conflict

121

P → A in CAA31057. Ref.2

Sequence conflict

194

D → H in AAA33441. Ref.2

Sequence conflict

234

V → E in AAA33441. Ref.2

Sequence conflict

234

V → E in CAA31057. Ref.2

Sequence conflict

236

C → S in AAA33441. Ref.2

Sequence conflict

244 – 245

AL → R in AAA33441. Ref.2

Sequence conflict

244 – 245

AL → R in CAA31057. Ref.2

Sequence conflict

254

Missing in AAA33441. Ref.2

Sequence conflict

254

Missing in CAA31057. Ref.2

Sequence conflict

264

A → AE in AAA33441. Ref.2

Sequence conflict

264

A → AE in CAA31057. Ref.2

Sequence conflict

280 – 281

DT → AQ in AAA33441. Ref.2

Sequence conflict

280 – 281

DT → AQ in CAA31057. Ref.2

Sequence conflict

282

E → Q in AAA33441. Ref.2

Sequence conflict

319

F → L in AAA33441. Ref.2

Sequence conflict

319

F → L in CAA31057. Ref.2

Sequence conflict

374 – 375

AH → GT in AAA33441. Ref.2

Sequence conflict

374 – 375

AH → GT in CAA31057. Ref.2

Sequence conflict

386

F → L in AAA33441. Ref.2

Sequence conflict

386

F → L in CAA31057. Ref.2

Sequence conflict

402 – 408

PLRQAAP → RRCGRAA in AAA33441. Ref.2

Sequence conflict

402 – 408

PLRQAAP → RRCGRAA in CAA31057. Ref.2

Sequence conflict

452 – 460

RRFADSLGH → KAIRRLART in AAA33441. Ref.2

Sequence conflict

452 – 460

RRFADSLGH → KAIRRLART in CAA31057. Ref.2

Sequence conflict

463

V → G in CAA31057. Ref.2

Sequence conflict

463

V → R in AAA33441. Ref.2

Sequence conflict

478

C → V in AAA33441. Ref.2

Sequence conflict

478

C → V in CAA31057. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P18123 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 566FFD05B3795B49
Show »

FASTA

496

56,796

        10         20         30         40         50         60 
MTMDPTKFRP SSSHDTTVTT TNAGAPVWND NEALTVGPRG PILLEDYHLI EKVAHFARER 

        70         80         90        100        110        120 
IPERVVHARG ASAKGFFECT HDVTSLTCAD FLRAPGVRTP VIVRFSTVIH ERGSPETIRD 

       130        140        150        160        170        180 
PRGFAVKFYT REGNWDLLGN NFPVFFIRDG IKFPDVIHAF KPNPRSHVQE YWRVFDFLSH 

       190        200        210        220        230        240 
LPESLHTFFF LFDDVGVPSD YRHMEGFGVN TYTFVSAAGK AQYVKFHWKP TCGVRCILTD 

       250        260        270        280        290        300 
EEAALVGGRN HSHATQDLYD SIAAGSFPEW TLYVQVMDPD TEEQYDFDPL DDTKTWPEDL 

       310        320        330        340        350        360 
LPLRPVGRLV LDRNVDNFFN ENEQLAFGPG LVVPGIYYSD DKMLQCRVFA YADTQRYRLG 

       370        380        390        400        410        420 
PNYLMLPVNA PRCAHHNNHY DGAMNFMHRD EEVDYYPSRH APLRQAAPPT PLPPRPVAGR 

       430        440        450        460        470        480 
REKATIRKPN DFKQPGERYR SWDADRQDRF VRRFADSLGH PKVSQELRSI WIDLLAKCDA 

       490 
SLGMKIATRL NMKANM

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References

[1]	"Isolation and characterization of a genomic sequence encoding the maize Cat3 catalase gene." Abler M.L., Scandalios J.G. Plant Mol. Biol. 22:1031-1038(1993) [PubMed: 8400123] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Wisconsin 64A. Tissue: Seedling leaf.
[2]	"Characterization of catalase transcripts and their differential expression in maize." Redinbaugh M.G., Wadsworth G.J., Scandalios J.G. Biochim. Biophys. Acta 951:104-116(1988) [PubMed: 2461221] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Wisconsin 64A. Tissue: Epicotyl.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L05934 Genomic DNA. Translation: AAC37357.1. M33103 mRNA. Translation: AAA33441.1. X12539 mRNA. Translation: CAA31057.1.
PIR	S37379.
RefSeq	NP_001105416.1. NM_001111946.1.
UniGene	Zm.93651.
3D structure databases
ProteinModelPortal	P18123.
ModBase	Search...
Protein family/group databases
PeroxiBase	6439. ZmKat3.
Proteomic databases
PRIDE	P18123.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	542370.
KEGG	zma:542370.
Organism-specific databases
Gramene	P18123.
MaizeGDB	13855.
Phylogenomic databases
GeneTree	EPGT00050000019328.
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.
KO	K03781.
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

CATA3_MAIZE

Accession

Primary (citable) accession number: P18123

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	February 1, 1996
Last modified:	January 25, 2012
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents