UniProtKB - 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
Functioni
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.UniRule annotation
Catalytic activityi
Cofactori
heme bNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 92 | Transition state stabilizer | 1 | |
Active sitei | 96 | Proton acceptor | 1 | |
Metal bindingi | 259 | Iron (heme axial ligand) | 1 |
GO - Molecular functioni
- catalase activity Source: UniProtKB-UniRule
- heme binding Source: InterPro
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- hydrogen peroxide catabolic process Source: UniProtKB-KW
- response to oxidative stress Source: InterPro
Keywordsi
Molecular function | Oxidoreductase, Peroxidase |
Biological process | Hydrogen peroxide |
Ligand | Heme, Iron, Metal-binding |
Enzyme and pathway databases
BRENDAi | 1.11.1.21, 2549 |
Protein family/group databases
PeroxiBasei | 2440, 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 |
Organismi | Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) |
Taxonomic identifieri | 272569 [NCBI] |
Taxonomic lineagei | Archaea › Euryarchaeota › Stenosarchaea group › Halobacteria › Halobacteriales › Haloarculaceae › Haloarcula › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed | |||
ChainiPRO_0000055580 | 2 – 731 | Catalase-peroxidase 2Add BLAST | 730 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Cross-linki | 95 ↔ 218 | Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-244) | ||
Cross-linki | 218 ↔ 244 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-95) |
Post-translational modificationi
Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme.UniRule annotation
Interactioni
Subunit structurei
Homodimer.
Protein-protein interaction databases
STRINGi | 272569.rrnAC1171 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | O59651 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | O59651 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | arCOG04487, Archaea |
HOGENOMi | CLU_025424_2_0_2 |
Family and domain databases
HAMAPi | MF_01961, Catal_peroxid, 1 hit |
InterProi | View protein in InterPro IPR000763, Catalase_peroxidase IPR002016, Haem_peroxidase IPR010255, Haem_peroxidase_sf IPR019794, Peroxidases_AS IPR019793, Peroxidases_heam-ligand_BS |
PANTHERi | PTHR30555, PTHR30555, 1 hit |
Pfami | View protein in Pfam PF00141, peroxidase, 2 hits |
PRINTSi | PR00460, BPEROXIDASE PR00458, PEROXIDASE |
SUPFAMi | SSF48113, SSF48113, 2 hits |
TIGRFAMsi | TIGR00198, cat_per_HPI, 1 hit |
PROSITEi | View protein in PROSITE PS00435, PEROXIDASE_1, 1 hit PS00436, PEROXIDASE_2, 1 hit PS50873, PEROXIDASE_4, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
O59651-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MAETPNSDMS GATGGRSKRP KSNQDWWPSK LNLEILDQNA RDVGPVEDDF
60 70 80 90 100
DYAEEFQKLD LEAVKSDLEE LMTSSQDWWP ADYGHYGPLF IRMAWHSAGT
110 120 130 140 150
YRTADGRGGA AGGRQRFAPI NSWPDNANLD KARRLLLPIK QKYGQKISWA
160 170 180 190 200
DLMILAGNVA IESMGFKTFG YAGGREDAFE EDKAVNWGPE DEFETQERFD
210 220 230 240 250
EPGEIQEGLG ASVMGLIYVN PEGPDGNPDP EASAKNIRQT FDRMAMNDKE
260 270 280 290 300
TAALIAGGHT FGKVHGADDP EENLGPEPEA APIEQQGLGW QNKNGNSKGG
310 320 330 340 350
EMITSGIEGP WTQSPTEWDM GYINNLLDYE WEPEKGPGGA WQWAPKSEEL
360 370 380 390 400
KNSVPDAHDP DEKQTPMMLT TDIALKRDPD YREVMETFQE NPMEFGMNFA
410 420 430 440 450
KAWYKLTHRD MGPPERFLGP EVPDEEMIWQ DPLPDADYDL IGDEEIAELK
460 470 480 490 500
EEILDSDLSV SQLVKTAWAS ASTYRDSDKR GGANGARLRL EPQKNWEVNE
510 520 530 540 550
PEQLETVLGT LENIQTEFND SRSDGTQVSL ADLIVLGGNA AVEQAAANAG
560 570 580 590 600
YDVEIPFEPG RVDAGPEHTD APSFDALKPK VDGVRNYIQD DITRPAEEVL
610 620 630 640 650
VDNADLLNLT ASELTALIGG MRSIGANYQD TDLGVFTDEP ETLTNDFFVN
660 670 680 690 700
LLDMGTEWEP AADSEHRYKG LDRDTGEVKW EATRIDLIFG SNDRLRAISE
710 720 730
VYGSADAEKK LVHDFVDTWS KVMKLDRFDL E
Sequence cautioni
The sequence AAV46121 differs from that shown. Reason: Erroneous initiation.Curated
Mass spectrometryi
Molecular mass is 81292±9 Da. Determined by MALDI. 1 Publication
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Y16851 Genomic DNA Translation: CAA76423.1 AY596297 Genomic DNA Translation: AAV46121.1 Different initiation. |
PIRi | T44846 |
RefSeqi | WP_049938864.1, NZ_CP039138.1 |
Genome annotation databases
EnsemblBacteriai | AAV46121; AAV46121; rrnAC1171 |
GeneIDi | 40152166 |
KEGGi | hma:rrnAC1171 |
PATRICi | fig|272569.17.peg.1887 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Y16851 Genomic DNA Translation: CAA76423.1 AY596297 Genomic DNA Translation: AAV46121.1 Different initiation. |
PIRi | T44846 |
RefSeqi | WP_049938864.1, NZ_CP039138.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
SMRi | O59651 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 272569.rrnAC1171 |
Protein family/group databases
PeroxiBasei | 2440, HmaCP01 |
Genome annotation databases
EnsemblBacteriai | AAV46121; AAV46121; rrnAC1171 |
GeneIDi | 40152166 |
KEGGi | hma:rrnAC1171 |
PATRICi | fig|272569.17.peg.1887 |
Phylogenomic databases
eggNOGi | arCOG04487, Archaea |
HOGENOMi | CLU_025424_2_0_2 |
Enzyme and pathway databases
BRENDAi | 1.11.1.21, 2549 |
Miscellaneous databases
EvolutionaryTracei | O59651 |
Family and domain databases
HAMAPi | MF_01961, Catal_peroxid, 1 hit |
InterProi | View protein in InterPro IPR000763, Catalase_peroxidase IPR002016, Haem_peroxidase IPR010255, Haem_peroxidase_sf IPR019794, Peroxidases_AS IPR019793, Peroxidases_heam-ligand_BS |
PANTHERi | PTHR30555, PTHR30555, 1 hit |
Pfami | View protein in Pfam PF00141, peroxidase, 2 hits |
PRINTSi | PR00460, BPEROXIDASE PR00458, PEROXIDASE |
SUPFAMi | SSF48113, SSF48113, 2 hits |
TIGRFAMsi | TIGR00198, cat_per_HPI, 1 hit |
PROSITEi | View protein in PROSITE PS00435, PEROXIDASE_1, 1 hit PS00436, PEROXIDASE_2, 1 hit PS50873, PEROXIDASE_4, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | KATG2_HALMA | |
Accessioni | O59651Primary (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: | December 2, 2020 | |
This is version 132 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families