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O59651

- KATG2_HALMA

UniProt

O59651 - KATG2_HALMA

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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: 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)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
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        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 AAV46121.1 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.
RefSeqiYP_135827.1. 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.
PIRi T44846.
RefSeqi YP_135827.1. NC_006396.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 106 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