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Protein

Catalase-peroxidase

Gene

katG

Organism
Serratia proteamaculans (strain 568)
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 dimer.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei93 – 931Transition state stabilizerUniRule annotation
Active sitei97 – 971Proton acceptorUniRule annotation
Metal bindingi264 – 2641Iron (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

Enzyme and pathway databases

BioCyciSPRO399741:GI55-3256-MONOMER.

Protein family/group databases

PeroxiBasei7335. SprCP01.

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
Ordered Locus Names:Spro_3192
OrganismiSerratia proteamaculans (strain 568)
Taxonomic identifieri399741 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia
Proteomesi
  • UP000007074 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 732732Catalase-peroxidasePRO_0000354912Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki96 ↔ 223Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-249)UniRule annotation
Cross-linki223 ↔ 249Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-96)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

PRIDEiA8GGQ0.

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi399741.Spro_3192.

Structurei

3D structure databases

ProteinModelPortaliA8GGQ0.
SMRiA8GGQ0. Positions 21-732.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiIAEVYAC.
OrthoDBiPOG091H05R1.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid. 1 hit.
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.

A8GGQ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTESKCPFS GGGKPNTPRR GPSNQDWWPN QLSLKPLHQH SSLSDPMDPD
60 70 80 90 100
FDYAKAFNSL DLAAVKQDLH ALMTDSQEWW PADFGHYGGL FIRMAWHSAG
110 120 130 140 150
TYRIGDGRGG AGEGQQRFAP LNSWPDNVSL DKARRLLWPI KQKYGRKISW
160 170 180 190 200
ADLIVLTGNV ALESMGFKTF GYAGGRADTW EPDDVYWGSE KIWLELSGGQ
210 220 230 240 250
NSRYSGDRDL EDPLAAVQMG LIYVNPEGPD GNPDPVAAAR DIRETFARMA
260 270 280 290 300
MNDEETVALI AGGHTFGKTH GAGPASHVGD DPETAGLERQ GLGWQSSFGT
310 320 330 340 350
GKGKDAITSG LEVTWTTTPT QWNHDFFKHL FEYEWELTQS PAGAHQWVAK
360 370 380 390 400
DVGETIPDAF DPAKKQRPTM LTTDLSLRFD PAYEKISRRF YEHPDQLADA
410 420 430 440 450
FSRAWYKLTH RDMGPRARYL GPEVPAEELI WQDPIPAVDH QLINDQDIAD
460 470 480 490 500
LKTSILTSGL PISVLVSTAW ASASTFRGSD KRGGANGARI RLAPQKDWAI
510 520 530 540 550
NQPAQLAQTL AKLEDIQQAF NNAQSGNKRV SLADLIVLAG AAAVEQAAAN
560 570 580 590 600
AGHPVSVPFT PGRMDATQEQ TDVDSFEAME PVADGFRNYL ERQFNIPAEA
610 620 630 640 650
LLVDKAQLLT LTAPEMTVLV GGLRVLNANV GQSQHGVLTQ RPQALSNDFF
660 670 680 690 700
VNLLDMGTTW KAAGEDGVFE GQDSQTGALK WTATRADLIF GSHSQLRALA
710 720 730
EVYGSSDAQA SFVYDFVAAW NKVMNLDRFD LA
Length:732
Mass (Da):80,366
Last modified:November 13, 2007 - v1
Checksum:iB426A424D961C8B3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000826 Genomic DNA. Translation: ABV42290.1.
RefSeqiWP_012145908.1. NC_009832.1.

Genome annotation databases

EnsemblBacteriaiABV42290; ABV42290; Spro_3192.
KEGGispe:Spro_3192.
PATRICi32419168. VBISerPro44537_3252.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000826 Genomic DNA. Translation: ABV42290.1.
RefSeqiWP_012145908.1. NC_009832.1.

3D structure databases

ProteinModelPortaliA8GGQ0.
SMRiA8GGQ0. Positions 21-732.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi399741.Spro_3192.

Protein family/group databases

PeroxiBasei7335. SprCP01.

Proteomic databases

PRIDEiA8GGQ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABV42290; ABV42290; Spro_3192.
KEGGispe:Spro_3192.
PATRICi32419168. VBISerPro44537_3252.

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiIAEVYAC.
OrthoDBiPOG091H05R1.

Enzyme and pathway databases

BioCyciSPRO399741:GI55-3256-MONOMER.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid. 1 hit.
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...

Entry informationi

Entry nameiKATG_SERP5
AccessioniPrimary (citable) accession number: A8GGQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 13, 2007
Last modified: September 7, 2016
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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.