NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 654-670, HEME-BINDING, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND INDUCTION.
DOI=10.1515/BC.2002.058; PubMed=12033445 [NCBI, ExPASy, EBI, Israel, Japan]
Peraza L., Hansberg W.;
"Neurospora crassa catalases, singlet oxygen and cell differentiation.";
Biol. Chem. 383:569-575(2002).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
DOI=10.1038/nature01554; PubMed=12712197 [NCBI, ExPASy, EBI, Israel, Japan]
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
"The genome sequence of the filamentous fungus Neurospora crassa.";
Nature 422:859-868(2003).

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 (By similarity).
ENZYME REGULATION: Inhibited by KCN.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=13.2 mM for H₂O₂ for the catalase reaction;
pH dependence: Optimum pH is 4.75 for the peroxidase reaction and 6.25 for the catalase reaction;
SUBUNIT: Homodimer or homotetramer (By similarity).
INDUCTION: Induced in late stationary growth phase.
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

AF459787; AAL66352.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AABX02000023; EAA30509.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_959745.1; -.

3D structure databases

HSSP

O59651; 1ITK. [HSSP ENTRY / PDB]

ModBase

Q8X182.

Protein family/group databases

PeroxiBase

2181; NcCP01.

Enzyme and pathway databases

BioCyc

NCRA-XX3-01:NCRA-XX3-01-009518-MON; -.

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

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

Q8X182.

Genome annotation databases

GeneID

3875883; -.

KEGG

ncr:NCU05770; -.

NMPDR

fig|5141.1.peg.3558; -.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 753`	`753`	`Catalase-peroxidase.`	`PRO_0000055582`
`ACT_SITE`	`91 91`		`Proton acceptor (By similarity).`
`METAL`	`279 279`		`Iron (heme axial ligand) (By similarity).`
`SITE`	`87 87`	`1`	`Transition state stabilizer (By similarity).`
`CROSSLNK`	`90 238`		`Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-264) (By similarity).`
`CROSSLNK`	`238 264`		`Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-90) (By similarity).`

Sequence information

Length: 753 AA [This is the length of the unprocessed precursor]

Molecular weight: 83380 Da [This is the MW of the unprocessed precursor]

CRC64: DED01DC6D10BA582 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSECPVRKSN VGGGGTRNHD WWPAQLRLNI LRQHTPVSNP LDKDFDYAAA FKSLDYEGLK 

        70         80         90        100        110        120 
KDLTKLMTDS QDWWPADFGH YGGLFIRMAW HSAGTYRVTD GRGGGGEGQQ RFAPLNSWPD 

       130        140        150        160        170        180 
NVSLDKARRL LWPIKQKYGN KISWSDLLLL TGNVALESMG FKTFGFAGGR PDTWEADESV 

       190        200        210        220        230        240 
YWGAETTWLG NEDRYSEGQE GHEGHGVVQG DESKKQHTDI HNRDLQSPLA SSHMGLIYVN 

       250        260        270        280        290        300 
PEGPDGIPDP VASAKDIRVT FGRMAMNDEE TVALIAGGHS FGKTHGAGPT HHVGKEPEAA 

       310        320        330        340        350        360 
PIEHQGLGWA NSFGQGKGPD TITSGLEVTW TPTPTKWGMG YLEYLYKFDW EPTKSPAGAN 

       370        380        390        400        410        420 
QWVAKNAEPT IPDAYDPNKK KLPTMLTTDI ALRMDPAYDK ICRDYLANPD KFADAFARAW 

       430        440        450        460        470        480 
FKLLHRDMGP RTRWIGPEVP SEILPWEDYI PPVDYQIIDD NDIAALKKEI LATGVAPKKL 

       490        500        510        520        530        540 
IFVAWSSASS FRGSDKRGGA NGARIRLAPQ NEWKVNDPST LREVLAALES VQQKFNDSSS 

       550        560        570        580        590        600 
GKKVSLADLI VLGGVAALEQ ASGLVVPFTP GRNDATQEHT DVHSFTHLEP HADGFRSYGK 

       610        620        630        640        650        660 
GTKRVRTEQF LIDRASLLTL SAPELTALIG GLRVLEANYD GSSYGVLTKT PGKLTNDYFV 

       670        680        690        700        710        720 
NLLDTNTAWK AADNEGEVFI GYDRKTHDKK WTATRADLIF GAHAELRALA EVYAAVDGEE 

       730        740        750 
KFKRDFVAAW HKVMNLDRFD LKQEGRGQNA PKL

Q8X182 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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