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Protein

Catalase A

Gene

catA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: 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 sitei93 – 931PROSITE-ProRule annotation
Active sitei166 – 1661PROSITE-ProRule annotation
Metal bindingi380 – 3801Iron (heme axial ligand)By similarity

GO - Molecular functioni

  • catalase activity Source: ASPGD
  • heme binding Source: InterPro
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cellular response to heat Source: ASPGD
  • cellular response to hydrogen peroxide Source: ASPGD
  • cellular response to iron ion starvation Source: ASPGD
  • hydrogen peroxide catabolic process Source: UniProtKB-KW
  • sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide, Sporulation

Keywords - Ligandi

Heme, Iron, Metal-binding

Protein family/group databases

PeroxiBasei5213. AniKat01.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase A (EC:1.11.1.6)
Alternative name(s):
Spore-specific catalase
Gene namesi
Name:catA
ORF Names:AN8637
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560 Componenti: Chromosome III

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 744744Catalase APRO_0000084921Add
BLAST

Expressioni

Developmental stagei

Sporulation-specific.

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00006410.

Structurei

3D structure databases

ProteinModelPortaliP55305.
SMRiP55305. Positions 44-744.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.Curated

Phylogenomic databases

eggNOGiCOG0753.
HOGENOMiHOG000087851.
InParanoidiP55305.
KOiK03781.
OMAiSMSEHEK.
OrthoDBiEOG7K9KBN.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
3.40.50.880. 1 hit.
InterProiIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024712. Catalase_clade2.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
IPR029062. Class_I_gatase-like.
[Graphical view]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038927. Catalase_clade2. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P55305-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSITAGLQ KAQQAVQDTA TKNKKIVDIS HDTVNVHTDQ EQRTDFGVAI
60 70 80 90 100
TDPDHWLRVT NETHSGPSLL EDHIARERIH RFDHERIPER VVHARGTGAY
110 120 130 140 150
GNFTLKESIE DLTYAGVLTD TSRNTPVFVR FSTVQGSRGS ADTVRDVRGF
160 170 180 190 200
AVKFYTDEGN WDIVGNNIPV FFIQDAIKFP DFVHAVKPEP HNEVPQAQTA
210 220 230 240 250
HNNFWDFVYL HPEATHMFMW AMSDRAIPRS YRMMQGFGVN TFSLVNKEGK
260 270 280 290 300
RHFVKFHWIP HLGVHSLVWD EALKLAGQDP DFHRKDLMEA IDNKAYPKWD
310 320 330 340 350
FAIQAIPEED QDKFEFDIFD ATKVWPEEQV PLRVVGELEL NRNIDEFFPE
360 370 380 390 400
TEQVAFCTSH IVPGIDFSDD PLLQGRNFSY QDTQISRLGV NWEEIPINRP
410 420 430 440 450
VCPFLNHNRD GAKRHRITKG TVNYWPNRFE ANPPASDKGF KSHPAPITGR
460 470 480 490 500
KRRDLTPKFK EYHNQAQLFY NSLSEVEKVH VKKAFSFELD HCDDPIVYER
510 520 530 540 550
LAGQRLAEID LPLAQAVAEM VGAPIPTKAL RDNHGKTSVR LSQFDFTPKA
560 570 580 590 600
PGIISRRIAI IIGDGYDKIA FNGMKAAILA AQALPFVIGT KRSAIYAQGE
610 620 630 640 650
DKNSSKGVIP DHMYDGMRST MFDATFIPGG SHIETLQKNG QIRYWIAETF
660 670 680 690 700
GHLKALGAMG EAAQLVKEVL GNVMGVQIAG ADSAEPVEWY GVVTARGPES
710 720 730 740
AESLSEGFKV LKDAGDFTSK FFYQISQHRN WQRELDGLAS TVAF
Length:744
Mass (Da):83,990
Last modified:May 26, 2009 - v2
Checksum:i3933E190CCBB0713
GO

Sequence cautioni

The sequence AAC49254.1 differs from that shown. Reason: Frameshift at positions 583 and 592. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti582 – 5821Q → A in AAC49254 (PubMed:8598056).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37803 Genomic DNA. Translation: AAC49254.1. Frameshift.
AACD01000158 Genomic DNA. Translation: EAA60671.1.
BN001303 Genomic DNA. Translation: CBF78282.1.
PIRiS68115.
RefSeqiXP_681906.1. XM_676814.1.

Genome annotation databases

EnsemblFungiiCADANIAT00006410; CADANIAP00006410; CADANIAG00006410.
GeneIDi2868532.
KEGGiani:AN8637.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37803 Genomic DNA. Translation: AAC49254.1. Frameshift.
AACD01000158 Genomic DNA. Translation: EAA60671.1.
BN001303 Genomic DNA. Translation: CBF78282.1.
PIRiS68115.
RefSeqiXP_681906.1. XM_676814.1.

3D structure databases

ProteinModelPortaliP55305.
SMRiP55305. Positions 44-744.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi162425.CADANIAP00006410.

Protein family/group databases

PeroxiBasei5213. AniKat01.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00006410; CADANIAP00006410; CADANIAG00006410.
GeneIDi2868532.
KEGGiani:AN8637.2.

Phylogenomic databases

eggNOGiCOG0753.
HOGENOMiHOG000087851.
InParanoidiP55305.
KOiK03781.
OMAiSMSEHEK.
OrthoDBiEOG7K9KBN.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
3.40.50.880. 1 hit.
InterProiIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024712. Catalase_clade2.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
IPR029062. Class_I_gatase-like.
[Graphical view]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038927. Catalase_clade2. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "catA, a new Aspergillus nidulans gene encoding a developmentally regulated catalase."
    Navarro R.E., Stringer M.A., Hansberg W., Timberlake W.E., Aguirre J.
    Curr. Genet. 29:352-359(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: FGSC 26.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiCATA_EMENI
AccessioniPrimary (citable) accession number: P55305
Secondary accession number(s): C8VAD2, Q5ASU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 26, 2009
Last modified: April 1, 2015
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.