Reviewed, UniProtKB/Swiss-Prot Q6CW24 (CCPR_KLULA)

Names and origin

Protein names

Recommended name:
    Cytochrome c peroxidase, mitochondrial
      Short name=CCP
    EC=1.11.1.5

Gene names

Name:	CCP1
Ordered Locus Names:	KLLA0B07557g

Organism

Kluyveromyces lactis (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

28985 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces

Protein attributes

Sequence length	346 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Destroys radicals which are normally produced within the cells and which are toxic to biological systems By similarity.
Catalytic activity	2 ferrocytochrome c + H(2)O(2) = 2 ferricytochrome c + 2 H(2)O.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity.
Subunit structure	Forms a one-to-one complex with cytochrome c By similarity.
Subcellular location	Mitochondrion matrixBy similarity.
Sequence similarities	Belongs to the peroxidase family. Cytochrome c peroxidase subfamily.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to oxidative stress Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cytochrome-c peroxidase activity Inferred from electronic annotation. Source: EC 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
	Transit peptide	1 – 12	12	Mitochondrion
	Chain	13 – 346	334	Cytochrome c peroxidase, mitochondrial		PRO_0000045294
Sites
	Active site	105	1	Proton acceptor By similarity
	Active site	244	1	Tryptophan radical intermediate By similarity
	Metal binding	228	1	Iron (heme axial ligand)
	Site	101	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6CW24-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 8E0797BBB40B9AFB	FASTA	346	39,041
	10 20 30 40 50 60 MSTTFGNVFR RVNVKTLSFI VGAGALAGSA TGTVMEYQDM RNYNNRNYNK QKLAALAAAH 70 80 90 100 110 120 VAAKEKYDVA KYQKVYNDIA LKIRDEDEYD DFIGYGPVLV RLAWHCAGTW DAKDNTGGPY 130 140 150 160 170 180 GGTYRFAMET NDPSNNGLQN AAKFLEPIHE KYPWLSHGDL YSLAGVTAIQ EMQGPTIPWR 190 200 210 220 230 240 SGRVDQPEDT TPENGRLPDA SKDAKYVRCF FHRLNFEDRQ VVALLGAHAL GKTHLKNSGF 250 260 270 280 290 300 EGPWGAATNI FTNEFYNNLL NEKWDLITND AGNKQYVNDK GWMMLPTDMA LVQDPKYLPI 310 320 330 340 VKEFANDQDT FFKEFTKAFV VLLENGIDFP QENKPIKFKT LDAQDL

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR382122 Genomic DNA. Translation: CAH02258.1.
RefSeq	XP_451865.1.
3D structure databases
ModBase	Search...
Protein family/group databases
PeroxiBase	2358. KlCcP01.
Genome annotation databases
GeneID	2896897.
KEGG	kla:KLLA0B07557g.
Phylogenomic databases
HOGENOM	Q6CW24.
Family and domain databases
InterPro	IPR002207. Asc_perxdse. IPR002016. Haem_peroxidase_pln/fun/bac. [Graphical view]
Pfam	PF00141. peroxidase. 1 hit. [Graphical view]
PRINTS	PR00459. ASPEROXIDASE. PR00458. PEROXIDASE.
PROSITE	PS00435. PEROXIDASE_1. False negative. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CCPR_KLULA

Accession

Primary (citable) accession number: Q6CW24

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	August 16, 2004
Last modified:	November 25, 2008
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)