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Protein

Catalase-peroxidase

Gene

katG

Organism
Burkholderia pseudomallei (strain K96243)
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. Displays also NADH oxidase, isoniazid hydrazine lyase and isonicotinoyl-NAD synthase activity.UniRule annotation1 Publication

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.

Kineticsi

  1. KM=56 mM for H2O2 for the catalase reaction (at pH 5.5-6.0)2 Publications
  2. KM=4.5 mM for H2O2 for the catalase reaction (at pH 7.0)2 Publications
  3. KM=700 µM for H2O2 for the peroxidase reaction2 Publications
  4. KM=300 µM for ABTS for the peroxidase reaction2 Publications
  5. KM=12.5 µM for NADH for the oxidase reaction2 Publications
  1. Vmax=11900 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 5.5-6.0)2 Publications
  2. Vmax=4300 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 7.0)2 Publications
  3. Vmax=6.0 µmol/min/mg enzyme for ABTS for the peroxidase reaction2 Publications

pH dependencei

Optimum pH is 4.5 for the peroxidase reaction, 6.0 for the catalase reaction, and 8.75 for the NADH oxidase reaction.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei88Transition state stabilizer1
Active sitei92Proton 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. 1031.
SABIO-RKQ939D2.

Protein family/group databases

PeroxiBasei2303. BpCP01_K96243.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase-peroxidaseUniRule annotation (EC:1.11.1.21UniRule annotation)
Short name:
CPUniRule annotation
Alternative name(s):
Peroxidase/catalaseUniRule annotation
Gene namesi
Name:katGUniRule annotation
Ordered Locus Names:BPSL2865
OrganismiBurkholderia pseudomallei (strain K96243)
Taxonomic identifieri272560 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
Proteomesi
  • UP000000605 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00003450922 – 728Catalase-peroxidaseAdd BLAST727

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki91 ↔ 218Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-244)
Cross-linki218 ↔ 244Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-91)

Post-translational modificationi

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

Proteomic databases

PRIDEiQ939D2.

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

STRINGi272560.BPSL2865.

Structurei

Secondary structure

1728
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi19 – 22Combined sources4
Helixi29 – 32Combined sources4
Helixi37 – 39Combined sources3
Helixi48 – 53Combined sources6
Helixi57 – 68Combined sources12
Helixi78 – 80Combined sources3
Helixi83 – 94Combined sources12
Turni99 – 101Combined sources3
Helixi110 – 112Combined sources3
Helixi116 – 118Combined sources3
Helixi120 – 122Combined sources3
Helixi125 – 131Combined sources7
Helixi133 – 139Combined sources7
Helixi140 – 142Combined sources3
Helixi145 – 159Combined sources15
Beta strandi198 – 200Combined sources3
Turni201 – 203Combined sources3
Beta strandi211 – 213Combined sources3
Helixi224 – 226Combined sources3
Helixi230 – 242Combined sources13
Turni243 – 245Combined sources3
Helixi248 – 258Combined sources11
Beta strandi266 – 268Combined sources3
Helixi270 – 272Combined sources3
Helixi277 – 279Combined sources3
Helixi282 – 284Combined sources3
Helixi298 – 300Combined sources3
Beta strandi302 – 305Combined sources4
Helixi320 – 327Combined sources8
Beta strandi330 – 334Combined sources5
Beta strandi340 – 344Combined sources5
Helixi367 – 374Combined sources8
Helixi376 – 387Combined sources12
Helixi389 – 405Combined sources17
Helixi411 – 413Combined sources3
Helixi425 – 427Combined sources3
Helixi440 – 452Combined sources13
Helixi457 – 468Combined sources12
Turni473 – 476Combined sources4
Helixi484 – 486Combined sources3
Helixi490 – 492Combined sources3
Helixi494 – 496Combined sources3
Helixi498 – 517Combined sources20
Helixi527 – 545Combined sources19
Helixi568 – 571Combined sources4
Helixi572 – 574Combined sources3
Beta strandi577 – 579Combined sources3
Helixi580 – 582Combined sources3
Beta strandi584 – 587Combined sources4
Helixi593 – 603Combined sources11
Helixi608 – 621Combined sources14
Helixi625 – 627Combined sources3
Helixi643 – 648Combined sources6
Beta strandi653 – 657Combined sources5
Beta strandi664 – 669Combined sources6
Turni670 – 672Combined sources3
Beta strandi675 – 680Combined sources6
Helixi681 – 684Combined sources4
Helixi685 – 687Combined sources3
Helixi690 – 699Combined sources10
Helixi705 – 720Combined sources16
Turni721 – 723Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5L02X-ray1.90A/B1-728[»]
5L05X-ray1.70A/B15-728[»]
5SW4X-ray1.90A/B15-728[»]
5SW5X-ray2.05A/B15-728[»]
5SW6X-ray1.90A/B15-728[»]
5SX0X-ray2.00A/B15-728[»]
5SX1X-ray1.80A/B1-728[»]
5SX2X-ray2.15A/B1-728[»]
5SX3X-ray2.00A/B1-728[»]
5SX6X-ray1.90A/B1-728[»]
5SX7X-ray1.95A/B1-728[»]
5SXQX-ray2.10A/B1-728[»]
5SXRX-ray1.69A/B1-728[»]
5SXSX-ray1.89A/B1-728[»]
5SXTX-ray1.90A/B1-728[»]
5SXWX-ray1.60A/B1-728[»]
5SXXX-ray1.70A/B1-728[»]
5SYHX-ray1.65A/B15-728[»]
5SYIX-ray1.70A/B15-728[»]
5SYKX-ray1.80A/B1-728[»]
5SYLX-ray1.95A/B1-728[»]
5SYVX-ray1.75A/B1-728[»]
5SYXX-ray1.77A/B1-728[»]
ProteinModelPortaliQ939D2.
SMRiQ939D2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ939D2.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiIAEVYAC.

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.

Q939D2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNEAKCPFH QAAGNGTSNR DWWPNQLDLS ILHRHSSLSD PMGKDFNYAQ
60 70 80 90 100
AFEKLDLAAV KRDLHALMTT SQDWWPADFG HYGGLFIRMA WHSAGTYRTA
110 120 130 140 150
DGRGGAGEGQ QRFAPLNSWP DNANLDKARR LLWPIKQKYG RAISWADLLI
160 170 180 190 200
LTGNVALESM GFKTFGFAGG RADTWEPEDV YWGSEKIWLE LSGGPNSRYS
210 220 230 240 250
GDRQLENPLA AVQMGLIYVN PEGPDGNPDP VAAARDIRDT FARMAMNDEE
260 270 280 290 300
TVALIAGGHT FGKTHGAGPA SNVGAEPEAA GIEAQGLGWK SAYRTGKGAD
310 320 330 340 350
AITSGLEVTW TTTPTQWSHN FFENLFGYEW ELTKSPAGAH QWVAKGADAV
360 370 380 390 400
IPDAFDPSKK HRPTMLTTDL SLRFDPAYEK ISRRFHENPE QFADAFARAW
410 420 430 440 450
FKLTHRDMGP RARYLGPEVP AEVLLWQDPI PAVDHPLIDA ADAAELKAKV
460 470 480 490 500
LASGLTVSQL VSTAWAAAST FRGSDKRGGA NGARIRLAPQ KDWEANQPEQ
510 520 530 540 550
LAAVLETLEA IRTAFNGAQR GGKQVSLADL IVLAGCAGVE QAAKNAGHAV
560 570 580 590 600
TVPFAPGRAD ASQEQTDVES MAVLEPVADG FRNYLKGKYR VPAEVLLVDK
610 620 630 640 650
AQLLTLSAPE MTVLLGGLRV LGANVGQSRH GVFTAREQAL TNDFFVNLLD
660 670 680 690 700
MGTEWKPTAA DADVFEGRDR ATGELKWTGT RVDLVFGSHS QLRALAEVYG
710 720
SADAQEKFVR DFVAVWNKVM NLDRFDLA
Length:728
Mass (Da):79,446
Last modified:July 22, 2008 - v3
Checksum:iFB6EC6E5261F6740
GO

Sequence cautioni

The sequence AAK72466 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAH36875 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY040244 Genomic DNA. Translation: AAK72466.3. Different initiation.
BX571965 Genomic DNA. Translation: CAH36875.1. Different initiation.
RefSeqiWP_004522123.1. NZ_CP009538.1.
WP_011205232.1. NC_006350.1.
YP_109459.1. NC_006350.1.

Genome annotation databases

EnsemblBacteriaiCAH36875; CAH36875; BPSL2865.
GeneIDi3092072.
KEGGibps:BPSL2865.
PATRICi19266145. VBIBurPse99623_3268.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY040244 Genomic DNA. Translation: AAK72466.3. Different initiation.
BX571965 Genomic DNA. Translation: CAH36875.1. Different initiation.
RefSeqiWP_004522123.1. NZ_CP009538.1.
WP_011205232.1. NC_006350.1.
YP_109459.1. NC_006350.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5L02X-ray1.90A/B1-728[»]
5L05X-ray1.70A/B15-728[»]
5SW4X-ray1.90A/B15-728[»]
5SW5X-ray2.05A/B15-728[»]
5SW6X-ray1.90A/B15-728[»]
5SX0X-ray2.00A/B15-728[»]
5SX1X-ray1.80A/B1-728[»]
5SX2X-ray2.15A/B1-728[»]
5SX3X-ray2.00A/B1-728[»]
5SX6X-ray1.90A/B1-728[»]
5SX7X-ray1.95A/B1-728[»]
5SXQX-ray2.10A/B1-728[»]
5SXRX-ray1.69A/B1-728[»]
5SXSX-ray1.89A/B1-728[»]
5SXTX-ray1.90A/B1-728[»]
5SXWX-ray1.60A/B1-728[»]
5SXXX-ray1.70A/B1-728[»]
5SYHX-ray1.65A/B15-728[»]
5SYIX-ray1.70A/B15-728[»]
5SYKX-ray1.80A/B1-728[»]
5SYLX-ray1.95A/B1-728[»]
5SYVX-ray1.75A/B1-728[»]
5SYXX-ray1.77A/B1-728[»]
ProteinModelPortaliQ939D2.
SMRiQ939D2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272560.BPSL2865.

Protein family/group databases

PeroxiBasei2303. BpCP01_K96243.

Proteomic databases

PRIDEiQ939D2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAH36875; CAH36875; BPSL2865.
GeneIDi3092072.
KEGGibps:BPSL2865.
PATRICi19266145. VBIBurPse99623_3268.

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiIAEVYAC.

Enzyme and pathway databases

BRENDAi1.11.1.21. 1031.
SABIO-RKQ939D2.

Miscellaneous databases

EvolutionaryTraceiQ939D2.

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 nameiKATG_BURPS
AccessioniPrimary (citable) accession number: Q939D2
Secondary accession number(s): Q63R09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: July 22, 2008
Last modified: November 2, 2016
This is version 107 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.