NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND HEME-BINDING.
STRAIN=Tu45;
PubMed=10217488 [NCBI, ExPASy, EBI, Israel, Japan]
Zou P., Borovok I., Ortiz de Orue Lucana D., Muller D., Schrempf H.;
"The mycelium-associated Streptomyces reticuli catalase-peroxidase, its gene and regulation by FurS.";
Microbiology 145:549-559(1999).

Comments

FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
CATALYTIC ACTIVITY: 2 H₂O₂ = O₂ + 2 H₂O.
CATALYTIC ACTIVITY: Donor + H₂O₂ = oxidized donor + 2 H₂O.
COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per dimer.
SUBUNIT: Homodimer.
PTM: The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme (By similarity).
SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Y14317; CAA74698.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q939D2; 1MWV. [HSSP ENTRY / PDB]

ModBase

O87864.

Protein family/group databases

PeroxiBase

2330; SretCP01.

Ontologies

GO:0004096;	Molecular function: catalase activity (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0042744;	Biological process: hydrogen peroxide catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01961; -; 1.
PBIL [Tree]

InterPro

IPR000763; Catalase_proxase.
IPR002016; Haem_peroxidase_pln/fun/bac.
Graphical view of domain structure.

Pfam

PF00141; peroxidase; 2.
Pfam graphical view of domain structure.

PRINTS

PR00460; BPEROXIDASE.
PR00458; PEROXIDASE.

TIGRFAMs

TIGR00198; cat_per_HPI; 1.

PROSITE

PS00435; PEROXIDASE_1; 1.
PS00436; PEROXIDASE_2; 1.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

O87864.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 740`	`740`	`Catalase-peroxidase.`	`PRO_0000055577`
`ACT_SITE`	`109 109`		`Proton acceptor (By similarity).`
`METAL`	`272 272`		`Iron (heme axial ligand) (By similarity).`
`SITE`	`105 105`	`1`	`Transition state stabilizer (By similarity).`
`CROSSLNK`	`108 231`		`Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-257) (By similarity).`
`CROSSLNK`	`231 257`		`Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-108) (By similarity).`

Sequence information

Length: 740 AA [This is the length of the unprocessed precursor]

Molecular weight: 81346 Da [This is the MW of the unprocessed precursor]

CRC64: E21860AFE4B4A40E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTENHDAIVT DAKSEGSGGC PVAHDRALHP TQGGGNRQWW PERLNLKILA KNPAVANPLD 

        70         80         90        100        110        120 
EDFDYAEAFK ALDLAAVKRD IAEVLTTSQD WWPADFGNYG PLMIRMAWHS AGTYRISDGR 

       130        140        150        160        170        180 
GGAGAGQQRF APLNSWPDNG NLDKARRLLW PVKKKYGQSI SWADLLILTG NVALETMGFK 

       190        200        210        220        230        240 
TFGFGGGRAD VWEAEEDVYW GPETTWLDDR RYTGDRELEN PLGAVQMGLI YVNPEGPNGN 

       250        260        270        280        290        300 
PDPIAAARDI RETFRRMAMN DEETVALIAG GHTFGKTHGA GPADHVGADP EAASLEEQGL 

       310        320        330        340        350        360 
GWRSTYGTGK GADAITSGLE VTWTSTPTQW SNGFFKNLFE YEYELEQSPA GAHQWVAKNA 

       370        380        390        400        410        420 
PEIIPDAHDP SKKHRPRMLT TDLSLRFDPI YEPISRRFYE NPEEFADAFA RAWYKLTHRD 

       430        440        450        460        470        480 
MGPKSLYLGP EVPEETLLWQ DPLPEREGEL IDDADIAILK TKLLESGLSV SQLVTTAWAS 

       490        500        510        520        530        540 
ASTFRASDKR GGANGARIRL APQRGWEVND PDQLAQVLRT LENVQQEFNA SSGAKKVSLA 

       550        560        570        580        590        600 
DLIVLGGAAG VEKAAKEAGF EIQVPFTPGR VDATEEHTDV ESFEALEPTA DGFRNYLGKG 

       610        620        630        640        650        660 
NRLPAEYLLL DKANLLNLSA PEMTVLVGGL RVLGANHQQS QLGVFTKTPG VLTNDFFVNL 

       670        680        690        700        710        720 
LDMGTTWKAT SEDQTTFEGR DAATGEVKWA GSRADLVFGS NSELRALAEV YASDDAKEKF 

       730        740 
VKDFVAAWHK VMDADRFDLV

O87864 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools