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Protein

Catalase-peroxidase

Gene

katG

Organism
Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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
Sitei95 – 951Transition state stabilizerUniRule annotation
Active sitei99 – 991Proton acceptorUniRule annotation
Metal bindingi275 – 2751Iron (heme axial ligand)UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding

Protein family/group databases

PeroxiBasei2327. UmCP01.

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
ORF Names:UMAG_11067
OrganismiUstilago maydis (strain 521 / FGSC 9021) (Corn smut fungus)
Taxonomic identifieri237631 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaUstilaginomycotinaUstilaginomycetesUstilaginalesUstilaginaceaeUstilago
Proteomesi
  • UP000000561 Componentsi: Chromosome 9, Unassembled WGS sequence

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 749749Catalase-peroxidasePRO_0000354112Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki98 ↔ 234Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-260)UniRule annotation
Cross-linki234 ↔ 260Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-98)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

PRIDEiQ4P914.

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000218110.
InParanoidiQ4P914.
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. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4P914-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGECPFAHQA NVDRKRVPAA GFGTKNSDWW PNAVKLNVLR QHQAKSDPFN
60 70 80 90 100
AEFDYAAAFN SLDYDALKKD LTHLMTDSQD WWPADYGHYG GFFIRMSWHA
110 120 130 140 150
AGTYRVQDGR GGGGEGQQRF APLNSWPDNG NLDKARRLLW PIKQKYGNKI
160 170 180 190 200
SWADLLLLAG NVALESMGFK TFGFAGGRAD TWEADQSTYW GGETTWLAND
210 220 230 240 250
VRYEEGTKNG GDINDLKNRN LDHALAASHM GLIYVNPEGP NGEPDPVAAA
260 270 280 290 300
HDIRTTFGRM AMNDEETVAL IAGGHTFGKT HGAGNPDLVG PEPNGAPIEA
310 320 330 340 350
QGFGWTSKHG SGKAGDAITS GLEVVWTSKP TEWSNLYLKY LFEFEWEHDK
360 370 380 390 400
SPAGANQFVA KNADAIIPDP FDPSKKRRPT MLTTDLSLRY DPAYEKISRR
410 420 430 440 450
FLENHDEFAD AFARAWFQLL HRDMGPRARW LGPEVPKEIL IWEDPVPTAD
460 470 480 490 500
YALVDDRDLA GLKQAIFATG VEPSKFLATA WASAASYRDS DKRGGANGAR
510 520 530 540 550
IRLAPMKDWE VNNPQQLAEV IKALEGVQQQ FNSSNQGGKK ISIADLIVLA
560 570 580 590 600
GNAALEKASG LPVPFTPGRT DATQEQTEVD TFEFLKPVAD GFRNYGQSTD
610 620 630 640 650
RVCAEQILID RANLLTLTPP ELTVLIGGLR ALGLNYNGSS HGVLTHRRGQ
660 670 680 690 700
LSNDFFVNLL DMSTEWKAAD GGKGEVFDGV DRKSGQKKWS ATRADLVFGS
710 720 730 740
QAELRALAEN YAQADNADKF KKDFVTAWNK VMNLDRFDVK KSNIARARF
Length:749
Mass (Da):82,770
Last modified:November 25, 2008 - v2
Checksum:i6729BD2E6618AF85
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM003148 Genomic DNA. Translation: KIS68300.1.
RefSeqiXP_011390075.1. XM_011391773.1.

Genome annotation databases

GeneIDi23566997.
KEGGiuma:UMAG_11067.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM003148 Genomic DNA. Translation: KIS68300.1.
RefSeqiXP_011390075.1. XM_011391773.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei2327. UmCP01.

Proteomic databases

PRIDEiQ4P914.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi23566997.
KEGGiuma:UMAG_11067.

Phylogenomic databases

HOGENOMiHOG000218110.
InParanoidiQ4P914.
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. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis."
    Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J.
    , Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L., Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W.
    Nature 444:97-101(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 521 / FGSC 9021.
  2. Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.
    Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: 521 / FGSC 9021.

Entry informationi

Entry nameiKATG_USTMA
AccessioniPrimary (citable) accession number: Q4P914
Secondary accession number(s): A0A0D1E0R0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 25, 2008
Last modified: July 6, 2016
This is version 68 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

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.