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Q73WB6

- CRPE_MYCPA

UniProt

Q73WB6 - CRPE_MYCPA

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Protein

Catalase-related peroxidase

Gene
MAP_2744c
Organism
Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Has an organic peroxide-dependent peroxidase activity. Exhibits strong peroxidase activity using organic hydroperoxides as cosubstrates, weak peroxidase activity using hydrogen peroxide and negligible catalase activity. May have a role in elimination of reactive oxygen species, in particular by deactivating hydroperoxides.1 Publication

Cofactori

Heme group.2 Publications

Kineticsi

Kcat is 13 sec(-1) for H2O2. Kcat is 320 sec(-1) for t-butyl hydroperoxide. Kcat is 330 sec(-1) for cumene hydroperoxide. Kcat is 529 sec(-1) for 9S-HPODE.

  1. KM=30 mM for H2O2 in 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) (ABTS) oxidation assay (at pH 7.0)1 Publication
  2. KM=22 mM for t-butyl hydroperoxide in ABTS oxidation assay (at pH 7.0)
  3. KM=3 mM for cumene hydroperoxide in ABTS oxidation assay (at pH 7.0)
  4. KM=49 µM for 9S-hydroperoxy-octadecadienoic acid (9S-HPODE) used as a cosubstrate with ABTS (at pH 7.0)

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei28 – 281 By similarity
Metal bindingi294 – 2941Iron (heme axial ligand)

GO - Molecular functioni

  1. catalase activity Source: InterPro
  2. heme binding Source: UniProtKB
  3. iron ion binding Source: UniProtKB
  4. peroxidase activity Source: UniProtKB

GO - Biological processi

  1. hydrogen peroxide metabolic process Source: UniProtKB
  2. oxidation-reduction process Source: UniProtKB
  3. regulation of reactive oxygen species metabolic process Source: UniProtKB
  4. response to oxidative stress Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMAVI262316:GCQR-2780-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase-related peroxidase (EC:1.11.1.-)
Gene namesi
Ordered Locus Names:MAP_2744c
OrganismiMycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
Taxonomic identifieri262316 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)
ProteomesiUP000000580: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 313313Catalase-related peroxidasePRO_0000424152Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi262316.MAP2744c.

Structurei

Secondary structure

1
313
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 1610
Beta strandi26 – 283
Beta strandi30 – 4011
Helixi44 – 463
Helixi51 – 533
Beta strandi57 – 6913
Beta strandi81 – 888
Beta strandi94 – 1018
Helixi110 – 11910
Beta strandi121 – 1233
Helixi126 – 13611
Helixi138 – 1414
Helixi144 – 1507
Beta strandi153 – 1553
Helixi157 – 1593
Beta strandi162 – 17110
Beta strandi177 – 18812
Helixi195 – 1995
Helixi205 – 21612
Beta strandi219 – 2279
Beta strandi246 – 25712
Beta strandi260 – 2634
Beta strandi279 – 2813
Helixi285 – 30218

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3E4WX-ray1.80A/B1-313[»]
3E4YX-ray2.60A1-313[»]
ProteinModelPortaliQ73WB6.

Miscellaneous databases

EvolutionaryTraceiQ73WB6.

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.

Phylogenomic databases

KOiK03781.
OMAiGNDYLED.
OrthoDBiEOG6742T3.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR011614. Catalase_core.
IPR024168. Catalase_SrpA-type_pred.
[Graphical view]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
[Graphical view]
PIRSFiPIRSF000296. SrpA. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF56634. SSF56634. 1 hit.
PROSITEiPS51402. CATALASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q73WB6-1 [UniParc]FASTAAdd to Basket

« Hide

MSGGLTPDQA IDAIRGTGGA QPGCRALHAK GTLYRGTFTA TRDAVMLSAA    50
PHLDGSTVPA LIRFSNGSGN PKQRDGAPGV RGMAVKFTLP DGSTTDVSAQ 100
TARLLVSSTP EGFIDLLKAM RPGLTTPLRL ATHLLTHPRL LGALPLLREA 150
NRIPASYATT EYHGLHAFRW IAADGSARFV RYHLVPTAAE EYLSASDARG 200
KDPDFLTDEL AARLQDGPVR FDFRVQIAGP TDSTVDPSSA WQSTQIVTVG 250
TVTITGPDTE REHGGDIVVF DPMRVTDGIE PSDDPVLRFR TLVYSASVKL 300
RTGVDRGAQA PPV 313
Length:313
Mass (Da):33,321
Last modified:July 5, 2004 - v1
Checksum:i7EE2BE95125CD14E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016958 Genomic DNA. Translation: AAS05061.1.
RefSeqiNP_961678.1. NC_002944.2.

Genome annotation databases

EnsemblBacteriaiAAS05061; AAS05061; MAP_2744c.
GeneIDi2720786.
KEGGimpa:MAP2744c.
PATRICi17998202. VBIMycAvi108102_2915.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016958 Genomic DNA. Translation: AAS05061.1 .
RefSeqi NP_961678.1. NC_002944.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3E4W X-ray 1.80 A/B 1-313 [» ]
3E4Y X-ray 2.60 A 1-313 [» ]
ProteinModelPortali Q73WB6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 262316.MAP2744c.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAS05061 ; AAS05061 ; MAP_2744c .
GeneIDi 2720786.
KEGGi mpa:MAP2744c.
PATRICi 17998202. VBIMycAvi108102_2915.

Phylogenomic databases

KOi K03781.
OMAi GNDYLED.
OrthoDBi EOG6742T3.

Enzyme and pathway databases

BioCyci MAVI262316:GCQR-2780-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q73WB6.

Family and domain databases

Gene3Di 2.40.180.10. 1 hit.
InterProi IPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR011614. Catalase_core.
IPR024168. Catalase_SrpA-type_pred.
[Graphical view ]
PANTHERi PTHR11465. PTHR11465. 1 hit.
Pfami PF00199. Catalase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000296. SrpA. 1 hit.
PRINTSi PR00067. CATALASE.
SMARTi SM01060. Catalase. 1 hit.
[Graphical view ]
SUPFAMi SSF56634. SSF56634. 1 hit.
PROSITEi PS51402. CATALASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of Mycobacterium avium subspecies paratuberculosis."
    Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., Kanjilal S., Kapur V.
    Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-968 / K-10.
  2. "Coordination modes of tyrosinate-ligated catalase-type heme enzymes: magnetic circular dichroism studies of Plexaura homomalla allene oxide synthase, Mycobacterium avium ssp. paratuberculosis protein-2744c, and bovine liver catalase in their ferric and ferrous states."
    Bandara D.M., Sono M., Bruce G.S., Brash A.R., Dawson J.H.
    J. Inorg. Biochem. 105:1786-1794(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: MAGNETIC CIRCULAR DICHROISM, COFACTOR.
  3. "The structure and peroxidase activity of a 33-kDa catalase-related protein from Mycobacterium avium ssp. paratuberculosis."
    Pakhomova S., Gao B., Boeglin W.E., Brash A.R., Newcomer M.E.
    Protein Sci. 18:2559-2568(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

Entry informationi

Entry nameiCRPE_MYCPA
AccessioniPrimary (citable) accession number: Q73WB6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 67 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

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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