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Sequence of CCPR_YEAST

EC Number:1.11.1.5

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
cytochrome-c peroxidase
P00431
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
361
40353
Reaction
2 ferrocytochrome c + H2O2 + 2 H+ = 2 ferricytochrome c + 2 H2O
Other sequences found for EC No. 1.11.1.5

General information:

Sequence
show sequence in fasta format
  0 MTTAVRLLPS LGRTAHKRSL YLFSAAAAAA AAATFAYSQS QKRSSSSPGG GSNHGWNNWG
 60 KAAALASTTP LVHVASVEKG RSYEDFQKVY NAIALKLRED DEYDNYIGYG PVLVRLAWHT
120 SGTWDKHDNT GGSYGGTYRF KKEFNDPSNA GLQNGFKFLE PIHKEFPWIS SGDLFSLGGV
180 TAVQEMQGPK IPWRCGRVDT PEDTTPDNGR LPDADKDADY VRTFFQRLNM NDREVVALMG
240 AHALGKTHLK NSGYEGPWGA ANNVFTNEFY LNLLNEDWKL EKNDANNEQW DSKSGYMMLP
300 TDYSLIQDPK YLSIVKEYAN DQDKFFKDFS KAFEKLLENG ITFPKDAPSP FIFKTLEEQG
360 L
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
14851
Kaput J.,Goltz S.,Blobel G.
Nucleotide sequence of the yeast nuclear gene for cytochrome c peroxidase precursor. Functional implications of the pre sequence for protein transport into mitochondria.
J. Biol. Chem.
257
15054-15058
1982
14853
Dujon B.,Alexandraki D.,Andre B.,Ansorge W.,Baladron V.,Ballesta J.P.G.,Banrevi A.,Bolle P.-A.,Bolotin-Fukuhara M.,Bossier P.,Bou G.,Boyer J.,Buitrago M.J.,Cheret G.,Colleaux L.,Daignan-Fornier B.,del Rey F.,Dion C.,Domdey H.,Duesterhoeft A.,Duesterhus S.,Entian K.-D.,Erfle H.,Esteban P.F.,Feldmann H.,Fernandes L.,Fobo G.M.,Fritz C.,Fukuhara H.,Gabel C.,Gaillon L.,Garcia-Cantalejo J.M.,Garcia-Ramirez J.J.,Gent M.E.,Ghazvini M.,Goffeau A.,Gonzalez A.,Grothues D.,Guerreiro P.,Hegemann J.H.,Hewitt N.,Hilger F.,Hollenberg C.P.,Horaitis O.,Indge K.J.,Jacquier A.,James C.M.,Jauniaux J.-C.,Jimenez A.,Keuchel H.,Kirchrath L.,Kleine K.,Koetter P.,Legrain P.,Liebl S.,Louis E.J.,Maia e Silva A.,Marck C.,Monnier A.-L.,Moestl D.,Mueller S.,Obermaier B.,Oliver S.G.,Pallier C.,Pascolo S.,Pfeiffer F.,Philippsen P.,Planta R.J.,Pohl F.M.,Pohl T.M.,Poehlmann R.,Portetelle D.,Purnelle B.,Puzos V.,Ramezani Rad M.,Rasmussen S.W.,Remacha M.A.,Revuelta J.L.,Richard G.-F.,Rieger M.,Rodrigues-Pousada C.,Rose M.,Rupp T.,Santos M.A.,Schwager C.,Sensen C.,Skala J.,Soares H.,Sor F.,Stegemann J.,Tettelin H.,Thierry A.,Tzermia M.,Urrestarazu L.A.,van Dyck L.,van Vliet-Reedijk J.C.,Valens M.,Vandenbol M.,Vilela C.,Vissers S.,von Wettstein D.,Voss H.,Wiemann S.,Xu G.,Zimmermann J.,Haasemann M.,Becker I.,Mewes H.-W.
Complete DNA sequence of yeast chromosome XI.
Nature
369
371-378
1994
14854
Engel S.R.,Dietrich F.S.,Fisk D.G.,Binkley G.,Balakrishnan R.,Costanzo M.C.,Dwight S.S.,Hitz B.C.,Karra K.,Nash R.S.,Weng S.,Wong E.D.,Lloyd P.,Skrzypek M.S.,Miyasato S.R.,Simison M.,Cherry J.M.
The reference genome sequence of Saccharomyces cerevisiae: Then and now.
G3 (Bethesda)
4
389-398
2014
14855
Hu Y.,Rolfs A.,Bhullar B.,Murthy T.V.S.,Zhu C.,Berger M.F.,Camargo A.A.,Kelley F.,McCarron S.,Jepson D.,Richardson A.,Raphael J.,Moreira D.,Taycher E.,Zuo D.,Mohr S.,Kane M.F.,Williamson J.,Simpson A.J.G.,Bulyk M.L.,Harlow E.,Marsischky G.,Kolodner R.D.,LaBaer J.
Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.
Genome Res.
17
536-543
2007
14856
Takio K.,Titani K.,Ericsson L.H.,Yonetani T.
Primary structure of yeast cytochrome c peroxidase. II. The complete amino acid sequence.
Arch. Biochem. Biophys.
203
615-629
1980
14857
Goltz S.,Kaput J.,Blobel G.
Isolation of the yeast nuclear gene encoding the mitochondrial protein, cytochrome c peroxidase.
J. Biol. Chem.
257
11186-11190
1982
14858
Mauro J.M.,Fishel L.A.,Hazzard J.T.,Meyer T.E.,Tollin G.,Cusanovich M.A.,Kraut J.
Tryptophan-191-->phenylalanine, a proximal-side mutation in yeast cytochrome c peroxidase that strongly affects the kinetics of ferrocytochrome c oxidation.
Biochemistry
27
6243-6256
1988
14859
Ghaemmaghami S.,Huh W.-K.,Bower K.,Howson R.W.,Belle A.,Dephoure N.,O'Shea E.K.,Weissman J.S.
Global analysis of protein expression in yeast.
Nature
425
737-741
2003
14860
Albuquerque C.P.,Smolka M.B.,Payne S.H.,Bafna V.,Eng J.,Zhou H.
A multidimensional chromatography technology for in-depth phosphoproteome analysis.
Mol. Cell. Proteomics
7
1389-1396
2008
14861
Voegtle F.N.,Burkhart J.M.,Rao S.,Gerbeth C.,Hinrichs J.,Martinou J.C.,Chacinska A.,Sickmann A.,Zahedi R.P.,Meisinger C.
Intermembrane space proteome of yeast mitochondria.
Mol. Cell. Proteomics
11
1840-1852
2012
14862
Finzel B.C.,Poulos T.L.,Kraut J.
Crystal structure of yeast cytochrome c peroxidase refined at 1.7-A resolution.
J. Biol. Chem.
259
13027-13036
1984
14863
Wang J.M.,Mauro M.,Edwards S.L.,Oatley S.J.,Fishel L.A.,Ashford V.A.,Xuong N.-H.,Kraut J.
X-ray structures of recombinant yeast cytochrome c peroxidase and three heme-cleft mutants prepared by site-directed mutagenesis.
Biochemistry
29
7160-7173
1990
14864
Goodin D.B.,McRee D.E.
The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme.
Biochemistry
32
3313-3324
1993
14865
Fitzgerald M.M.,Musah R.A.,McRee D.E.,Goodin D.B.
A ligand-gated, hinged loop rearrangement opens a channel to a buried artificial protein cavity.
Nat. Struct. Biol.
3
626-631
1996
14866
Hirst J.,Goodin D.B.
Unusual oxidative chemistry of N(omega)-hydroxyarginine and N-hydroxyguanidine catalyzed at an engineered cavity in a heme peroxidase.
J. Biol. Chem.
275
8582-8591
2000
14867
Hirst J.,Wilcox S.K.,Williams P.A.,Blankenship J.,McRee D.E.,Goodin D.B.
Replacement of the axial histidine ligand with imidazole in cytochrome c peroxidase. 1. Effects on structure.
Biochemistry
40
1265-1273
2001