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Protein

Catalase-peroxidase

Gene

katG

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.UniRule annotation

Catalytic activityi

Donor + H2O2 = oxidized donor + 2 H2O.UniRule annotation
2 H2O2 = O2 + 2 H2O.UniRule annotation

Cofactori

heme bUniRule annotationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei91 – 911Transition state stabilizerUniRule annotation
Active sitei95 – 951Proton acceptorUniRule annotation
Metal bindingi258 – 2581Iron (heme axial ligand)UniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  • cellular response to heat Source: ASPGD
  • cellular response to hydrogen peroxide Source: GO_Central
  • cellular response to starvation Source: ASPGD
  • hydrogen peroxide catabolic process Source: GO_Central
  • response to reactive oxygen species Source: ASPGD
  • sexual reproduction Source: ASPGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding

Protein family/group databases

PeroxiBasei1905. AniCP.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase-peroxidaseUniRule annotation (EC:1.11.1.21UniRule annotation)
Short name:
CPUniRule annotation
Alternative name(s):
Peroxidase/catalaseUniRule annotation
Gene namesi
Name:katGUniRule annotation
Synonyms:cpeA
ORF Names:AN7388
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000000560 Componenti: Chromosome IV
  • UP000005890 Componenti: Partially assembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:AN7388.

Subcellular locationi

  • Cytoplasm

  • Note: Found in sexual structures such as Huelle cells, but not in primordia, hyphae and conidiophores.

GO - Cellular componenti

  • cytoplasm Source: ASPGD
  • cytosol Source: GO_Central
  • extracellular region Source: ASPGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 739739Catalase-peroxidasePRO_0000354106Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki94 ↔ 217Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-243)UniRule annotation
Cross-linki217 ↔ 243Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-94)UniRule annotation

Post-translational modificationi

The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme.UniRule annotation

Proteomic databases

PRIDEiQ96VT4.

Expressioni

Inductioni

Induced by transcription factor stuA upon carbon starvation and during early sexual development.1 Publication

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ96VT4.
SMRiQ96VT4. Positions 19-726.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. Peroxidase/catalase subfamily.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000218110.
InParanoidiQ96VT4.
KOiK03782.
OMAiTESKCPF.
OrthoDBiEOG7BKD32.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid.
InterProiIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 2 hits.
TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96VT4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSNECPYSR QNANIGGGGQ NNRDWWPDDL KLNILRQHNS VSNPLDKGFD
60 70 80 90 100
YTAAFNSLDY FGLKRDLEAL MTDSQDWWPA DFGHYGGLFI RMAWHSAGTY
110 120 130 140 150
RVFDGRGGGG QGQQRFAPLN SWPDNVSLDK ARRLLWPIKQ KYGSKISWAD
160 170 180 190 200
LLILAGNVAL ESMGFKTFGF AGGRSDTWEA DQSVFWGGEK EWLGNDVRYL
210 220 230 240 250
NGELDNPLAA SHMGLIYVNP EGPNKNPDPV LAAKDIRITF GRMAMNDEET
260 270 280 290 300
VALIAGGHTF GKTHGAGPAT HLGKEPHGAG IELQGLGWES GFESGTGRHA
310 320 330 340 350
ITSGLEVIWT KTPTKWSNQF FEYLFKYDWE LTKSPAGAHQ YVAKGVEPFI
360 370 380 390 400
PDPFDPSIKH PPRMLTTDLS LRYDPEYEKI SRRFLENPDQ FADAFARAWF
410 420 430 440 450
KLTHRDVGPR VLYQGPEVPS EVLIWQDPVP PLDHPVIDND DIATLKKAIL
460 470 480 490 500
NSGISHTDLF STAWASASTF RGSDKRGGAN GARIRLSPQK NWKVNSQPWL
510 520 530 540 550
SESLAALEKI QKQFNDAQST DKRVSLADLI VLAGAASLEK AARDAGHNVS
560 570 580 590 600
VSFTPGRTDA TQEQTDVDSF NNLEPIADGF RNYGRGTPRV LTEDFLIDKA
610 620 630 640 650
QLLNLSPPEL TVLIGGLRVL NNNYDRSNLG VFTKRPGQLT NDFFVNLLDM
660 670 680 690 700
GVQWKPADDT NEIFIGSDRK TGQARWKASR ADLVFGSHAE LRAISEVYGS
710 720 730
SDGEAKFVKD FVAAWEKVSN LDRFDLKQTG LAQRIKPQL
Length:739
Mass (Da):82,110
Last modified:December 1, 2001 - v1
Checksum:i56D31ECCBA498FF5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ305225 Genomic DNA. Translation: CAC59821.1.
AACD01000128 Genomic DNA. Translation: EAA61759.1.
BN001304 Genomic DNA. Translation: CBF78482.1.
RefSeqiXP_680657.1. XM_675565.1.

Genome annotation databases

EnsemblFungiiCADANIAT00000040; CADANIAP00000040; CADANIAG00000040.
EAA61759; EAA61759; AN7388.2.
GeneIDi2869839.
KEGGiani:AN7388.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ305225 Genomic DNA. Translation: CAC59821.1.
AACD01000128 Genomic DNA. Translation: EAA61759.1.
BN001304 Genomic DNA. Translation: CBF78482.1.
RefSeqiXP_680657.1. XM_675565.1.

3D structure databases

ProteinModelPortaliQ96VT4.
SMRiQ96VT4. Positions 19-726.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei1905. AniCP.

Proteomic databases

PRIDEiQ96VT4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00000040; CADANIAP00000040; CADANIAG00000040.
EAA61759; EAA61759; AN7388.2.
GeneIDi2869839.
KEGGiani:AN7388.2.

Organism-specific databases

EuPathDBiFungiDB:AN7388.

Phylogenomic databases

HOGENOMiHOG000218110.
InParanoidiQ96VT4.
KOiK03782.
OMAiTESKCPF.
OrthoDBiEOG7BKD32.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid.
InterProiIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 2 hits.
TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Aspergillus nidulans catalase-peroxidase gene (cpeA) is transcriptionally induced during sexual development through the transcription factor StuA."
    Scherer M., Wei H., Liese R., Fischer R.
    Eukaryot. Cell 1:725-735(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 345-374 AND 448-459, INDUCTION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  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 nameiKATG_EMENI
AccessioniPrimary (citable) accession number: Q96VT4
Secondary accession number(s): C8VCF7, Q5AWE2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: December 1, 2001
Last modified: July 6, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.