Reviewed, UniProtKB/Swiss-Prot Q8X182 (KATG_NEUCR)

Names and origin

Protein names

Recommended name:
    Catalase-peroxidase
      Short name=CP
    EC=1.11.1.6
    EC=1.11.1.7
Alternative name(s):
    Peroxidase/catalase
    Catalase-2

Gene names

Name:	katG
Synonyms:	cat-2
ORF Names:	NCU05770

Organism

Neurospora crassa [Complete proteome]

Taxonomic identifier

5141 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora

Protein attributes

Sequence length	753 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
Catalytic activity	2 H(2)O(2) = O(2) + 2 H(2)O. Donor + H(2)O(2) = oxidized donor + 2 H(2)O.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per dimer By similarity.
Enzyme regulation	Inhibited by KCN.
Subunit structure	Homodimer or homotetramer By similarity.
Induction	Induced in late stationary growth phase.
Post-translational modification	The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme By similarity.
Sequence similarities	Belongs to the peroxidase family. Peroxidase/catalase subfamily.
Biophysicochemical properties	Kinetic parameters: KM=13.2 mM for H(2)O(2) for the catalase reaction pH dependence: Optimum pH is 4.75 for the peroxidase reaction and 6.25 for the catalase reaction.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	catalase activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 753	753	Catalase-peroxidase		PRO_0000055582
Sites
	Active site	91	1	Proton acceptor By similarity
	Metal binding	279	1	Iron (heme axial ligand) By similarity
	Site	87	1	Transition state stabilizer By similarity
Amino acid modifications
	Cross-link	90 ↔ 238		Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-264) By similarity
	Cross-link	238 ↔ 264		Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-90) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8X182-1 [UniParc]. Last modified October 1, 2002. Version 2. Checksum: DED01DC6D10BA582	FASTA	753	83,380
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Neurospora crassa catalases, singlet oxygen and cell differentiation." Peraza L., Hansberg W. Biol. Chem. 383:569-575(2002) [PubMed: 12033445] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 654-670, HEME-BINDING, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, INDUCTION.
[2]	"The genome sequence of the filamentous fungus Neurospora crassa." 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. Nature 422:859-868(2003) [PubMed: 12712197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF459787 mRNA. Translation: AAL66352.2. AABX02000023 Genomic DNA. Translation: EAA30509.1.
RefSeq	XP_959745.1.
3D structure databases
HSSP	HSSP built from PDB template 1ITK based on UniProtKB O59651.
ModBase	Search...
Protein family/group databases
PeroxiBase	2181. NcCP01.
Genome annotation databases
GeneID	3875883.
KEGG	ncr:NCU05770.
NMPDR	fig|5141.1.peg.3558.
Enzyme and pathway databases
BioCyc	NCRA-XX3-01:NCRA-XX3-01-009518-MON.
Family and domain databases
InterPro	IPR000763. Catalase_proxase. IPR002016. Haem_peroxidase_pln/fun/bac. [Graphical view]
Pfam	PF00141. peroxidase. 2 hits. [Graphical view]
PRINTS	PR00460. BPEROXIDASE. PR00458. PEROXIDASE.
TIGRFAMs	TIGR00198. cat_per_HPI. 1 hit.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KATG_NEUCR

Accession

Primary (citable) accession number: Q8X182
Secondary accession number(s): Q7S4Q3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 9, 2003
Last sequence update:	October 1, 2002
Last modified:	November 25, 2008
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)