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P18122

- CATA1_MAIZE

UniProt

P18122 - CATA1_MAIZE

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Protein

Catalase isozyme 1

Gene

CAT1

Organism
Zea mays (Maize)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.

Catalytic activityi

2 H2O2 = O2 + 2 H2O.PROSITE-ProRule annotation

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei65 – 651PROSITE-ProRule annotation
Active sitei138 – 1381PROSITE-ProRule annotation
Metal bindingi348 – 3481Iron (heme axial ligand)By similarity

GO - Molecular functioni

  1. catalase activity Source: UniProtKB-EC
  2. heme binding Source: InterPro
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. hydrogen peroxide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding

Protein family/group databases

PeroxiBasei6437. ZmKat1.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase isozyme 1 (EC:1.11.1.6)
Gene namesi
Name:CAT1
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Organism-specific databases

GrameneiP18122.
MaizeGDBi13855.

Subcellular locationi

GO - Cellular componenti

  1. peroxisome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 492492Catalase isozyme 1PRO_0000084946Add
BLAST

Proteomic databases

PRIDEiP18122.

Expressioni

Tissue specificityi

Scutella, milky endosperm of immature kernels, leaves and epicotyls.

Interactioni

Subunit structurei

Homotetramer.

Structurei

3D structure databases

ProteinModelPortaliP18122.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.Curated

Phylogenomic databases

HOGENOMiHOG000087852.
KOiK03781.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. 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]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P18122-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDPYKHRPSS GSNSSFWTTN SGAPVWNNNS ALTVGQRGPI LLEDYHLIEK
60 70 80 90 100
LAQFDRERIP ERVVHARGAS AKGFFEVTHD VSHLTCADFL RAPGVQTPVI
110 120 130 140 150
VRFSTVVHER GSPETLRDPR GFAVKFYTRE GNFDLVGNNM PVFFIRDGMK
160 170 180 190 200
FPDMVHAFKP NPKTNLQENW RIVDFFSHHP ESLHMFTFLF DDVGIPLNYR
210 220 230 240 250
HMEGFGVNTY SLINRDGKPH LVKFHWKPTC GVKCLLDNEA VTVGGTCHSH
260 270 280 290 300
ATKDLYDSIA AGNYPEWKLY IQTIDLDHED KFDFDPLDVT KTWPEDIIPL
310 320 330 340 350
QPVGRMVLNK NVDNFFAENE QIAFCPAISV PAIHYSDDKL LQTRIFSYAD
360 370 380 390 400
TQRHRLGPNY LMLPVNAPKC AHHNNHHDGF MNFMHRDEEV NYFPSRFDPA
410 420 430 440 450
RHAEKVPIPP RVLTRCREKC IIQKENNFKQ AGERYRSFDP ARQDRFIQRW
460 470 480 490
VDALTHPRVT HEHRTIWISY WSQCDAALGQ KLPSRLNLKP SM
Length:492
Mass (Da):56,877
Last modified:November 1, 1990 - v1
Checksum:iCE10C93BEC1D9529
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti332 – 3321A → G in CAA31056. (PubMed:2461221)Curated
Sequence conflicti332 – 3321A → G in CAA42720. (PubMed:2461221)Curated
Sequence conflicti415 – 4151R → G in CAA31056. (PubMed:2461221)Curated
Sequence conflicti415 – 4151R → G in CAA42720. (PubMed:2461221)Curated
Sequence conflicti456 – 4561H → D in CAA31056. (PubMed:2461221)Curated
Sequence conflicti456 – 4561H → D in CAA42720. (PubMed:2461221)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti157 – 1571A → V in strain: cv. W64A.
Natural varianti211 – 2111S → T in strain: cv. W64A.
Natural varianti329 – 3291S → I in strain: cv. W64A.
Natural varianti483 – 4831P → A in strain: cv. W64A.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12538 mRNA. Translation: CAA31056.1.
X60135 Genomic DNA. Translation: CAA42720.1.
PIRiS48124.
RefSeqiNP_001105415.1. NM_001111945.1.
UniGeneiZm.160908.

Genome annotation databases

GeneIDi542369.
KEGGizma:542369.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12538 mRNA. Translation: CAA31056.1 .
X60135 Genomic DNA. Translation: CAA42720.1 .
PIRi S48124.
RefSeqi NP_001105415.1. NM_001111945.1.
UniGenei Zm.160908.

3D structure databases

ProteinModelPortali P18122.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

PeroxiBasei 6437. ZmKat1.

Proteomic databases

PRIDEi P18122.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 542369.
KEGGi zma:542369.

Organism-specific databases

Gramenei P18122.
MaizeGDBi 13855.

Phylogenomic databases

HOGENOMi HOG000087852.
KOi K03781.

Family and domain databases

Gene3Di 2.40.180.10. 1 hit.
InterProi 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 ]
PANTHERi PTHR11465. PTHR11465. 1 hit.
Pfami PF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view ]
PIRSFi PIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSi PR00067. CATALASE.
SMARTi SM01060. Catalase. 1 hit.
[Graphical view ]
SUPFAMi SSF56634. SSF56634. 1 hit.
PROSITEi PS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. R6-67.
    Tissue: Scutellum.
  2. "Characterization of the catalase antioxidant defense gene Cat1 of maize, and its developmentally regulated expression in transgenic tobacco."
    Guan L., Scandalios J.G.
    Plant J. 3:527-536(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Wisconsin 64A.
    Tissue: Leaf.

Entry informationi

Entry nameiCATA1_MAIZE
AccessioniPrimary (citable) accession number: P18122
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 26, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3