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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)LengthDescriptionGraphical viewFeature identifierActions
Sitei88 – 881Transition state stabilizer
Active sitei92 – 921Proton acceptor
Metal bindingi259 – 2591Iron (heme axial ligand)

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

BioCyciBPSE272560:GJNI-2941-MONOMER.
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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 728727Catalase-peroxidasePRO_0000345092Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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.

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

STRINGi272560.BPSL2865.

Structurei

Secondary structure

1
728
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi19 – 224Combined sources
Helixi29 – 324Combined sources
Helixi37 – 393Combined sources
Helixi48 – 536Combined sources
Helixi57 – 6812Combined sources
Helixi78 – 803Combined sources
Helixi83 – 9412Combined sources
Turni99 – 1013Combined sources
Beta strandi104 – 1063Combined sources
Helixi110 – 1123Combined sources
Helixi116 – 1183Combined sources
Helixi120 – 1223Combined sources
Helixi125 – 1317Combined sources
Helixi133 – 1397Combined sources
Helixi140 – 1423Combined sources
Helixi145 – 15915Combined sources
Beta strandi192 – 1943Combined sources
Beta strandi198 – 2003Combined sources
Turni201 – 2033Combined sources
Beta strandi211 – 2133Combined sources
Beta strandi217 – 2193Combined sources
Helixi224 – 2263Combined sources
Helixi230 – 24213Combined sources
Turni243 – 2453Combined sources
Helixi248 – 25811Combined sources
Beta strandi266 – 2683Combined sources
Helixi270 – 2723Combined sources
Helixi277 – 2793Combined sources
Helixi282 – 2843Combined sources
Helixi298 – 3003Combined sources
Beta strandi302 – 3054Combined sources
Helixi320 – 3278Combined sources
Beta strandi330 – 3345Combined sources
Beta strandi340 – 3445Combined sources
Helixi367 – 3748Combined sources
Helixi376 – 38712Combined sources
Helixi389 – 40517Combined sources
Helixi411 – 4133Combined sources
Helixi425 – 4273Combined sources
Helixi440 – 45213Combined sources
Helixi457 – 46812Combined sources
Turni473 – 4753Combined sources
Helixi484 – 4863Combined sources
Helixi490 – 4923Combined sources
Helixi494 – 4963Combined sources
Helixi498 – 51720Combined sources
Helixi527 – 54519Combined sources
Helixi563 – 5653Combined sources
Helixi568 – 5714Combined sources
Helixi572 – 5743Combined sources
Beta strandi577 – 5793Combined sources
Helixi580 – 5823Combined sources
Beta strandi584 – 5874Combined sources
Helixi593 – 60311Combined sources
Helixi608 – 62114Combined sources
Helixi625 – 6273Combined sources
Helixi643 – 6486Combined sources
Beta strandi653 – 6575Combined sources
Beta strandi664 – 6696Combined sources
Turni670 – 6723Combined sources
Beta strandi675 – 6806Combined sources
Helixi681 – 6844Combined sources
Helixi685 – 6873Combined sources
Helixi690 – 69910Combined sources
Helixi705 – 72016Combined sources
Turni721 – 7233Combined sources
Helixi725 – 7273Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MWVX-ray1.70A/B15-728[»]
1X7UX-ray1.90A/B1-728[»]
2B2OX-ray1.90A/B15-728[»]
2B2QX-ray2.05A/B15-728[»]
2B2RX-ray1.90A/B15-728[»]
2B2SX-ray2.00A/B15-728[»]
2DV1X-ray1.80A/B1-728[»]
2DV2X-ray2.15A/B1-728[»]
2FXGX-ray2.00A/B1-728[»]
2FXHX-ray1.90A/B1-728[»]
2FXJX-ray1.95A/B1-728[»]
3N3NX-ray2.10A/B1-728[»]
3N3OX-ray1.69A/B1-728[»]
3N3PX-ray1.89A/B1-728[»]
3N3QX-ray1.90A/B1-728[»]
3N3RX-ray1.60A/B1-728[»]
3N3SX-ray1.70A/B1-728[»]
4KA5X-ray1.65A/B15-728[»]
4KA6X-ray1.70A/B15-728[»]
4MVPX-ray1.80A/B1-728[»]
4QZJX-ray1.95A/B1-728[»]
4QZLX-ray1.75A/B1-728[»]
4QZPX-ray1.77A/B1-728[»]
ProteinModelPortaliQ939D2.
SMRiQ939D2. Positions 14-728.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1MWVX-ray1.70A/B15-728[»]
1X7UX-ray1.90A/B1-728[»]
2B2OX-ray1.90A/B15-728[»]
2B2QX-ray2.05A/B15-728[»]
2B2RX-ray1.90A/B15-728[»]
2B2SX-ray2.00A/B15-728[»]
2DV1X-ray1.80A/B1-728[»]
2DV2X-ray2.15A/B1-728[»]
2FXGX-ray2.00A/B1-728[»]
2FXHX-ray1.90A/B1-728[»]
2FXJX-ray1.95A/B1-728[»]
3N3NX-ray2.10A/B1-728[»]
3N3OX-ray1.69A/B1-728[»]
3N3PX-ray1.89A/B1-728[»]
3N3QX-ray1.90A/B1-728[»]
3N3RX-ray1.60A/B1-728[»]
3N3SX-ray1.70A/B1-728[»]
4KA5X-ray1.65A/B15-728[»]
4KA6X-ray1.70A/B15-728[»]
4MVPX-ray1.80A/B1-728[»]
4QZJX-ray1.95A/B1-728[»]
4QZLX-ray1.75A/B1-728[»]
4QZPX-ray1.77A/B1-728[»]
ProteinModelPortaliQ939D2.
SMRiQ939D2. Positions 14-728.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272560.BPSL2865.

Protein family/group databases

PeroxiBasei2303. BpCP01_K96243.

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

BioCyciBPSE272560:GJNI-2941-MONOMER.
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: September 7, 2016
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

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.