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O59651 (KATG2_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Catalase-peroxidase 2
Short name=CP 2
EC=1.11.1.21
Alternative name(s):
Peroxidase/catalase 2
Gene names
Name:katG2
Synonyms:Hmcp
Ordered Locus Names:rrnAC1171
OrganismHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) [Complete proteome] [HAMAP]
Taxonomic identifier272569 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloarcula ›

Protein attributes

Sequence length731 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity By similarity. HAMAP-Rule MF_01961

Catalytic activity

Donor + H2O2 = oxidized donor + 2 H2O. HAMAP-Rule MF_01961

2 H2O2 = O2 + 2 H2O. HAMAP-Rule MF_01961

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per subunit.

Subunit structure

Homodimer.

Post-translational modification

The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme By similarity. HAMAP-Rule MF_01961

Sequence similarities

Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Mass spectrometry

Molecular mass is 81292±9 Da from positions 2 - 731. Determined by MALDI. Ref.1

Sequence caution

The sequence AAV46121.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed HAMAP-Rule MF_01961
Chain2 – 731730Catalase-peroxidase 2 HAMAP-Rule MF_01961
PRO_0000055580

Sites

Active site961Proton acceptor
Metal binding2591Iron (heme axial ligand)
Site921Transition state stabilizer

Amino acid modifications

Cross-link95 ↔ 218Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-244) HAMAP-Rule MF_01961
Cross-link218 ↔ 244Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-95) HAMAP-Rule MF_01961

Secondary structure

1 .................................................................................................................................... 731
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O59651 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 0E12DE0CF72FF3A3

FASTA73181,384
        10         20         30         40         50         60 
MAETPNSDMS GATGGRSKRP KSNQDWWPSK LNLEILDQNA RDVGPVEDDF DYAEEFQKLD 

        70         80         90        100        110        120 
LEAVKSDLEE LMTSSQDWWP ADYGHYGPLF IRMAWHSAGT YRTADGRGGA AGGRQRFAPI 

       130        140        150        160        170        180 
NSWPDNANLD KARRLLLPIK QKYGQKISWA DLMILAGNVA IESMGFKTFG YAGGREDAFE 

       190        200        210        220        230        240 
EDKAVNWGPE DEFETQERFD EPGEIQEGLG ASVMGLIYVN PEGPDGNPDP EASAKNIRQT 

       250        260        270        280        290        300 
FDRMAMNDKE TAALIAGGHT FGKVHGADDP EENLGPEPEA APIEQQGLGW QNKNGNSKGG 

       310        320        330        340        350        360 
EMITSGIEGP WTQSPTEWDM GYINNLLDYE WEPEKGPGGA WQWAPKSEEL KNSVPDAHDP 

       370        380        390        400        410        420 
DEKQTPMMLT TDIALKRDPD YREVMETFQE NPMEFGMNFA KAWYKLTHRD MGPPERFLGP 

       430        440        450        460        470        480 
EVPDEEMIWQ DPLPDADYDL IGDEEIAELK EEILDSDLSV SQLVKTAWAS ASTYRDSDKR 

       490        500        510        520        530        540 
GGANGARLRL EPQKNWEVNE PEQLETVLGT LENIQTEFND SRSDGTQVSL ADLIVLGGNA 

       550        560        570        580        590        600 
AVEQAAANAG YDVEIPFEPG RVDAGPEHTD APSFDALKPK VDGVRNYIQD DITRPAEEVL 

       610        620        630        640        650        660 
VDNADLLNLT ASELTALIGG MRSIGANYQD TDLGVFTDEP ETLTNDFFVN LLDMGTEWEP 

       670        680        690        700        710        720 
AADSEHRYKG LDRDTGEVKW EATRIDLIFG SNDRLRAISE VYGSADAEKK LVHDFVDTWS 

       730 
KVMKLDRFDL E

« Hide

References

« Hide 'large scale' references
[1]"The protein sequence of an archaeal catalase-peroxidase."
Cannac-Caffrey V., Hudry-Clergeon G., Petillot Y., Gagnon J., Zaccai G., Franzetti B.
Biochimie 80:1003-1011(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY.
[2]"Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea."
Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., Hood L., Ng W.V.
Genome Res. 14:2221-2234(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[3]"The 2.0 A crystal structure of catalase-peroxidase from Haloarcula marismortui."
Yamada Y., Fujiwara T., Sato T., Igarashi N., Tanaka N.
Nat. Struct. Biol. 9:691-695(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 19-731.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y16851 Genomic DNA. Translation: CAA76423.1.
AY596297 Genomic DNA. Translation: AAV46121.1. Different initiation.
PIRT44846.
RefSeqYP_135827.1. NC_006396.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ITKX-ray2.00A/B1-731[»]
3UW8X-ray2.35A/B1-731[»]
3VLHX-ray1.73A/B1-731[»]
3VLIX-ray1.70A/B1-731[»]
3VLJX-ray1.70A/B1-731[»]
3VLKX-ray2.00A/B1-731[»]
3VLLX-ray2.00A/B1-731[»]
3VLMX-ray2.33A/B1-731[»]
ProteinModelPortalO59651.
SMRO59651. Positions 18-731.
ModBaseSearch...

Protein-protein interaction databases

STRING272569.rrnAC1171.

Protein family/group databases

PeroxiBase2440. HmaCP01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV46121; AAV46121; rrnAC1171.
GeneID3129320.
KEGGhma:rrnAC1171.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0376.
HOGENOMHOG000218110.
KOK03782.
ProtClustDBPRK15061.

Enzyme and pathway databases

BioCycHMAR272569:GJDH-1051-MONOMER.

Family and domain databases

HAMAPMF_01961. Catal-peroxid.
InterProIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMSSF48113. Peroxidase_super. 2 hits.
TIGRFAMsTIGR00198. cat_per_HPI. 1 hit.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO59651.

Entry information

Entry nameKATG2_HALMA
AccessionPrimary (citable) accession number: O59651
Secondary accession number(s): Q5V2Y1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 100 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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