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O59651

- KATG2_HALMA

UniProt

O59651 - KATG2_HALMA

Protein

Catalase-peroxidase 2

Gene

katG2

Organism
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei92 – 921Transition state stabilizer
    Active sitei96 – 961Proton acceptor
    Metal bindingi259 – 2591Iron (heme axial ligand)

    GO - Molecular functioni

    1. catalase activity Source: UniProtKB-HAMAP
    2. heme binding Source: InterPro
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. hydrogen peroxide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Hydrogen peroxide

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciHMAR272569:GJDH-1051-MONOMER.

    Protein family/group databases

    PeroxiBasei2440. HmaCP01.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Catalase-peroxidase 2UniRule annotation (EC:1.11.1.21UniRule annotation)
    Short name:
    CP 2UniRule annotation
    Alternative name(s):
    Peroxidase/catalase 2UniRule annotation
    Gene namesi
    Name:katG2UniRule annotation
    Synonyms:Hmcp
    Ordered Locus Names:rrnAC1171
    OrganismiHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
    Taxonomic identifieri272569 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula
    ProteomesiUP000001169: Chromosome I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 731730Catalase-peroxidase 2PRO_0000055580Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki95 ↔ 218Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-244)
    Cross-linki218 ↔ 244Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-95)

    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.

    Protein-protein interaction databases

    STRINGi272569.rrnAC1171.

    Structurei

    Secondary structure

    1
    731
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi23 – 264
    Helixi34 – 374
    Turni38 – 403
    Beta strandi44 – 463
    Beta strandi48 – 503
    Helixi52 – 587
    Helixi61 – 7212
    Helixi82 – 843
    Helixi87 – 9812
    Turni103 – 1053
    Beta strandi108 – 1103
    Helixi114 – 1163
    Helixi120 – 1223
    Helixi124 – 1263
    Helixi129 – 1357
    Helixi137 – 1437
    Helixi144 – 1463
    Helixi149 – 16315
    Beta strandi191 – 1944
    Beta strandi198 – 2014
    Beta strandi216 – 2194
    Helixi224 – 2263
    Helixi230 – 24213
    Turni243 – 2453
    Helixi248 – 25811
    Beta strandi266 – 2683
    Helixi270 – 2734
    Helixi278 – 2803
    Helixi283 – 2853
    Beta strandi303 – 3064
    Beta strandi309 – 3146
    Helixi321 – 3288
    Beta strandi331 – 3355
    Beta strandi341 – 3477
    Helixi348 – 3503
    Beta strandi354 – 3563
    Beta strandi359 – 3646
    Helixi370 – 3778
    Helixi379 – 39012
    Helixi392 – 40817
    Helixi414 – 4163
    Helixi428 – 4303
    Helixi443 – 45513
    Helixi460 – 47112
    Turni476 – 4794
    Helixi487 – 4893
    Helixi493 – 4953
    Helixi497 – 4993
    Helixi501 – 52121
    Beta strandi524 – 5263
    Helixi530 – 54819
    Helixi566 – 5683
    Helixi571 – 5744
    Helixi575 – 5773
    Beta strandi580 – 5823
    Turni583 – 5864
    Helixi596 – 60611
    Helixi611 – 62414
    Helixi628 – 6303
    Helixi646 – 6527
    Beta strandi656 – 6605
    Beta strandi668 – 6725
    Turni673 – 6753
    Beta strandi678 – 6825
    Helixi684 – 6874
    Helixi688 – 6903
    Helixi693 – 70210
    Helixi708 – 72316
    Turni724 – 7263
    Turni728 – 7303

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliO59651.
    SMRiO59651. Positions 18-731.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO59651.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0376.
    HOGENOMiHOG000218110.
    KOiK03782.

    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. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O59651-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAETPNSDMS GATGGRSKRP KSNQDWWPSK LNLEILDQNA RDVGPVEDDF    50
    DYAEEFQKLD LEAVKSDLEE LMTSSQDWWP ADYGHYGPLF IRMAWHSAGT 100
    YRTADGRGGA AGGRQRFAPI NSWPDNANLD KARRLLLPIK QKYGQKISWA 150
    DLMILAGNVA IESMGFKTFG YAGGREDAFE EDKAVNWGPE DEFETQERFD 200
    EPGEIQEGLG ASVMGLIYVN PEGPDGNPDP EASAKNIRQT FDRMAMNDKE 250
    TAALIAGGHT FGKVHGADDP EENLGPEPEA APIEQQGLGW QNKNGNSKGG 300
    EMITSGIEGP WTQSPTEWDM GYINNLLDYE WEPEKGPGGA WQWAPKSEEL 350
    KNSVPDAHDP DEKQTPMMLT TDIALKRDPD YREVMETFQE NPMEFGMNFA 400
    KAWYKLTHRD MGPPERFLGP EVPDEEMIWQ DPLPDADYDL IGDEEIAELK 450
    EEILDSDLSV SQLVKTAWAS ASTYRDSDKR GGANGARLRL EPQKNWEVNE 500
    PEQLETVLGT LENIQTEFND SRSDGTQVSL ADLIVLGGNA AVEQAAANAG 550
    YDVEIPFEPG RVDAGPEHTD APSFDALKPK VDGVRNYIQD DITRPAEEVL 600
    VDNADLLNLT ASELTALIGG MRSIGANYQD TDLGVFTDEP ETLTNDFFVN 650
    LLDMGTEWEP AADSEHRYKG LDRDTGEVKW EATRIDLIFG SNDRLRAISE 700
    VYGSADAEKK LVHDFVDTWS KVMKLDRFDL E 731
    Length:731
    Mass (Da):81,384
    Last modified:January 23, 2007 - v3
    Checksum:i0E12DE0CF72FF3A3
    GO

    Sequence cautioni

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

    Mass spectrometryi

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y16851 Genomic DNA. Translation: CAA76423.1.
    AY596297 Genomic DNA. Translation: AAV46121.1. Different initiation.
    PIRiT44846.
    RefSeqiYP_135827.1. NC_006396.1.

    Genome annotation databases

    EnsemblBacteriaiAAV46121; AAV46121; rrnAC1171.
    GeneIDi3129320.
    KEGGihma:rrnAC1171.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y16851 Genomic DNA. Translation: CAA76423.1 .
    AY596297 Genomic DNA. Translation: AAV46121.1 . Different initiation.
    PIRi T44846.
    RefSeqi YP_135827.1. NC_006396.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ITK X-ray 2.00 A/B 1-731 [» ]
    3UW8 X-ray 2.35 A/B 1-731 [» ]
    3VLH X-ray 1.73 A/B 1-731 [» ]
    3VLI X-ray 1.70 A/B 1-731 [» ]
    3VLJ X-ray 1.70 A/B 1-731 [» ]
    3VLK X-ray 2.00 A/B 1-731 [» ]
    3VLL X-ray 2.00 A/B 1-731 [» ]
    3VLM X-ray 2.33 A/B 1-731 [» ]
    ProteinModelPortali O59651.
    SMRi O59651. Positions 18-731.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272569.rrnAC1171.

    Protein family/group databases

    PeroxiBasei 2440. HmaCP01.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAV46121 ; AAV46121 ; rrnAC1171 .
    GeneIDi 3129320.
    KEGGi hma:rrnAC1171.

    Phylogenomic databases

    eggNOGi COG0376.
    HOGENOMi HOG000218110.
    KOi K03782.

    Enzyme and pathway databases

    BioCyci HMAR272569:GJDH-1051-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei O59651.

    Family and domain databases

    HAMAPi MF_01961. Catal_peroxid.
    InterProi IPR000763. Catalase_peroxidase.
    IPR010255. Haem_peroxidase.
    IPR002016. Haem_peroxidase_pln/fun/bac.
    IPR019794. Peroxidases_AS.
    IPR019793. Peroxidases_heam-ligand_BS.
    [Graphical view ]
    Pfami PF00141. peroxidase. 2 hits.
    [Graphical view ]
    PRINTSi PR00460. BPEROXIDASE.
    PR00458. PEROXIDASE.
    SUPFAMi SSF48113. SSF48113. 2 hits.
    TIGRFAMsi TIGR00198. cat_per_HPI. 1 hit.
    PROSITEi PS00435. PEROXIDASE_1. 1 hit.
    PS00436. PEROXIDASE_2. 1 hit.
    PS50873. PEROXIDASE_4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY.
    2. 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.

    Entry informationi

    Entry nameiKATG2_HALMA
    AccessioniPrimary (citable) accession number: O59651
    Secondary accession number(s): Q5V2Y1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 105 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference 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