Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Catalase-peroxidase

Gene

katG

Organism
Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377)
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
Sitei95 – 951Transition state stabilizerUniRule annotation
Active sitei99 – 991Proton acceptorUniRule annotation
Metal bindingi260 – 2601Iron (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

BioCyciABAU400667:GI0Q-400-MONOMER.

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:A1S_0412
OrganismiAcinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377)
Taxonomic identifieri400667 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 718718Catalase-peroxidasePRO_0000354712Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki98 ↔ 219Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-245)UniRule annotation
Cross-linki219 ↔ 245Tryptophyl-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

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.
KOiK03782.
OrthoDBiEOG6RRKKM.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid.
InterProiIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
[Graphical view]
PfamiPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 2 hits.
TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
PROSITEiPS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A3M1S3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNESKCPFS GHNSKPQVTV GGGTANLHWW PNQLRVDLLN QHSERSNPLG
60 70 80 90 100
KDFNYRQEFK KLDYYALKAD IKNVLTDSQD WWPADWGNYT GLFIRLAWHA
110 120 130 140 150
AGTYRMGDGR GGAGRGQQRF APLNSWPDNA SLDKARRLLW PVKQKYGQKI
160 170 180 190 200
SWADLFILAG NIALESSGFR TFGFGAGRED VWEPDNDVNW GDEKEWLAHR
210 220 230 240 250
NSEALAGSNL AATEMGLIYV NPEGPQASGD PRSAAPFIRA TFGNMAMDDE
260 270 280 290 300
EIVALIAGGH TLGKTHGAAP ADHVQADPEG APIEQMGFGW ANSYGTGVGK
310 320 330 340 350
DAITSGLEVI WSQTPTQWSN YFFENLFKYE WVQERSPAGA IQWVAADAEA
360 370 380 390 400
IIPDPFDPSI KRKPTMLTTD LTLRFDPEFE KISRRFLNDP QAFANAFARA
410 420 430 440 450
WFKLTHRDMG PKARYLGPEV PAEDLIWQDP LPAASATPSS ASIADAKAKI
460 470 480 490 500
VALGLSAGEL VSLAWASAST FRGGDKRGGA NGAHIALSPQ REWEVNKKAV
510 520 530 540 550
ETLTQIEELK ASTQLSLADL IVLAGNVGVE QAAQAAGFNI TVPFAPGRVD
560 570 580 590 600
ALQSQTDVES FQLLLGLADG FRNWKKQGVN TPAEVLLIDK AQQLTLTAPE
610 620 630 640 650
LTALIGGLRV LGTNWDGSQH GVFTQQVGVL STDFFTNLLD MSNVWAPVDS
660 670 680 690 700
TSEVFEGKDR KSGTVKFTAT RNDLVFGSNS ILRALAEVYA QADGKEKFVQ
710
DFVAAWTKVM NLDRFDLA
Length:718
Mass (Da):78,570
Last modified:September 2, 2008 - v2
Checksum:i923CFA296F1C4185
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000521 Genomic DNA. Translation: ABO10867.2.

Genome annotation databases

EnsemblBacteriaiABO10867; ABO10867; A1S_0412.
KEGGiacb:A1S_0412.
PATRICi20716936. VBIAciBau103176_0403.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000521 Genomic DNA. Translation: ABO10867.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABO10867; ABO10867; A1S_0412.
KEGGiacb:A1S_0412.
PATRICi20716936. VBIAciBau103176_0403.

Phylogenomic databases

HOGENOMiHOG000218110.
KOiK03782.
OrthoDBiEOG6RRKKM.

Enzyme and pathway databases

BioCyciABAU400667:GI0Q-400-MONOMER.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid.
InterProiIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
[Graphical view]
PfamiPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 2 hits.
TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
PROSITEiPS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis."
    Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M.
    Genes Dev. 21:601-614(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377.

Entry informationi

Entry nameiKATG_ACIBT
AccessioniPrimary (citable) accession number: A3M1S3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: September 2, 2008
Last modified: May 11, 2016
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.