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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: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 bNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei92Transition state stabilizer1
Active sitei96Proton acceptor1
Metal bindingi259Iron (heme axial ligand)1

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

BRENDAi1.11.1.21. 2549.

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
Proteomesi
  • UP000001169 Componenti: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000555802 – 731Catalase-peroxidase 2Add BLAST730

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

1731
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi23 – 26Combined sources4
Helixi34 – 37Combined sources4
Turni38 – 40Combined sources3
Beta strandi44 – 46Combined sources3
Beta strandi48 – 50Combined sources3
Helixi52 – 58Combined sources7
Helixi61 – 72Combined sources12
Helixi82 – 84Combined sources3
Helixi87 – 98Combined sources12
Turni103 – 105Combined sources3
Beta strandi108 – 110Combined sources3
Helixi114 – 116Combined sources3
Helixi120 – 122Combined sources3
Helixi124 – 126Combined sources3
Helixi129 – 135Combined sources7
Helixi137 – 143Combined sources7
Helixi144 – 146Combined sources3
Helixi149 – 163Combined sources15
Beta strandi191 – 194Combined sources4
Beta strandi198 – 201Combined sources4
Beta strandi216 – 219Combined sources4
Helixi224 – 226Combined sources3
Helixi230 – 242Combined sources13
Turni243 – 245Combined sources3
Helixi248 – 258Combined sources11
Beta strandi266 – 268Combined sources3
Helixi270 – 273Combined sources4
Helixi278 – 280Combined sources3
Helixi283 – 285Combined sources3
Turni293 – 295Combined sources3
Helixi299 – 301Combined sources3
Beta strandi303 – 306Combined sources4
Beta strandi309 – 314Combined sources6
Helixi321 – 328Combined sources8
Beta strandi331 – 335Combined sources5
Beta strandi341 – 347Combined sources7
Helixi348 – 350Combined sources3
Beta strandi354 – 356Combined sources3
Beta strandi359 – 364Combined sources6
Helixi370 – 377Combined sources8
Helixi379 – 390Combined sources12
Helixi392 – 408Combined sources17
Helixi414 – 416Combined sources3
Helixi428 – 430Combined sources3
Helixi443 – 455Combined sources13
Helixi460 – 471Combined sources12
Turni476 – 479Combined sources4
Helixi487 – 489Combined sources3
Helixi493 – 495Combined sources3
Helixi497 – 499Combined sources3
Helixi501 – 521Combined sources21
Beta strandi524 – 526Combined sources3
Helixi530 – 548Combined sources19
Helixi566 – 568Combined sources3
Helixi571 – 574Combined sources4
Helixi575 – 577Combined sources3
Beta strandi580 – 582Combined sources3
Turni583 – 586Combined sources4
Helixi596 – 606Combined sources11
Helixi611 – 624Combined sources14
Helixi628 – 630Combined sources3
Helixi646 – 652Combined sources7
Beta strandi656 – 660Combined sources5
Beta strandi668 – 672Combined sources5
Turni673 – 675Combined sources3
Beta strandi678 – 682Combined sources5
Helixi684 – 687Combined sources4
Helixi688 – 690Combined sources3
Helixi693 – 702Combined sources10
Helixi708 – 723Combined sources16
Turni724 – 726Combined sources3
Turni728 – 730Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO59651.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiarCOG04487. Archaea.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid. 1 hit.
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

        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
Length:731
Mass (Da):81,384
Last modified:January 23, 2007 - v3
Checksum:i0E12DE0CF72FF3A3
GO

Sequence cautioni

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

Mass spectrometryi

Molecular mass is 81292±9 Da from positions 2 - 731. 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.
PIRiT44846.
RefSeqiWP_049938864.1. NC_006396.1.

Genome annotation databases

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

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.
PIRiT44846.
RefSeqiWP_049938864.1. NC_006396.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272569.rrnAC1171.

Protein family/group databases

PeroxiBasei2440. HmaCP01.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiarCOG04487. Archaea.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.

Enzyme and pathway databases

BRENDAi1.11.1.21. 2549.

Miscellaneous databases

EvolutionaryTraceiO59651.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid. 1 hit.
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]
ProtoNetiSearch...

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: November 2, 2016
This is version 117 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

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.