Reviewed, UniProtKB/Swiss-Prot Q6FMG7 (CCPR_CANGA)

Names and origin

Protein names

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

Gene names

Ordered Locus Names:

CAGL0K08184g

Organism

Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	357 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 – 23	23	Mitochondrion Potential
	Chain	24 – 357	334	Cytochrome c peroxidase, mitochondrial		PRO_0000045288
Regions
	Compositional bias	49 – 55	7	Poly-Asn
	Compositional bias	60 – 67	8	Poly-Ala
Sites
	Active site	116	1	Proton acceptor By similarity
	Active site	255	1	Tryptophan radical intermediate By similarity
	Metal binding	239	1	Iron (heme axial ligand)
	Site	112	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FMG7-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 721EAC06CEE4552F	FASTA	357	40,007
	10 20 30 40 50 60 MSATALRIAP IASRTFQRRL GYLLAGVATG AAATVAYKAQ KNNNYYKYNN NNNNNSGFKA 70 80 90 100 110 120 GALAAAAGVV HLAHEEDKKT ADYQKVYNLI AERLRDDDEY DNYIGYGPVL VRLAWHSSGT 130 140 150 160 170 180 WDKNDNTGGS YGGTYRYKKE SQDPSNAGLE NAAKFLEPVK KQFPWISYGD LYTLGGVVGI 190 200 210 220 230 240 QELQGPKIPW RSGRTDLPED MTPDNGRLPD GDKDANYVRN FYKRLDFNDR EVVALLGAHA 250 260 270 280 290 300 LGKTHLKNSG FEGPWGAANN IFTNEFYLNL LNEDWKLEKN DAGNLQYNSP KGYMMLPTDY 310 320 330 340 350 ALIQDSNYLK IVKEYAADQD AFFRDFSKAF AALLERGIDF PKNQPVHIFK TLDEQGL

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 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR380957 Genomic DNA. Translation: CAG61540.1.
RefSeq	XP_448577.1.
3D structure databases
SMR	Q6FMG7. Positions 69-357.
ModBase	Search...
Protein family/group databases
PeroxiBase	2366. CglCcP01.
Genome annotation databases
GeneID	2890345.
KEGG	cgr:CAGL0K08184g.
Phylogenomic databases
HOGENOM	Q6FMG7.
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. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CCPR_CANGA

Accession

Primary (citable) accession number: Q6FMG7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	July 19, 2004
Last modified:	November 25, 2008
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)