Cytochrome b2, mitochondrial (P00175)

Identification
NameCytochrome b2, mitochondrial
Synonyms
  • L-lactate dehydrogenase [Cytochrome]
  • L-lactate ferricytochrome C oxidoreductase
  • L-LCR
Gene NameCYB2
Enzyme Class
Biological Properties
General FunctionInvolved in catalytic activity
Specific Function(S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H(+)
Cellular LocationMitochondrion intermembrane space
SMPDB Pathways
Pyruvate metabolismPW002447 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Pyruvate metabolismec00620 Map00620
SMPDB ReactionsNot Available
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
YMDB00175Pyruvic acidShow
YMDB00247L-Lactic acidShow
YMDB00862hydronShow
GO Classification
Component
Not Available
Function
metal ion binding
transition metal ion binding
iron ion binding
oxidoreductase activity
heme binding
catalytic activity
binding
nucleotide binding
FMN binding
ion binding
cation binding
Process
oxidation reduction
metabolic process
Gene Properties
Chromosome Locationchromosome 13
LocusYML054C
Gene Sequence>1776 bp ATGCTAAAATACAAACCTTTACTAAAAATCTCGAAGAACTGTGAGGCTGCTATCCTCAGA GCGTCTAAGACTAGATTGAACACAATCCGCGCGTACGGTTCTACCGTTCCAAAATCCAAG TCGTTCGAACAAGACTCAAGAAAACGCACACAGTCATGGACTGCCTTGAGAGTCGGTGCA ATTCTAGCCGCTACTAGTTCCGTGGCGTATCTAAACTGGCATAATGGCCAAATAGACAAC GAGCCGAAACTGGATATGAATAAACAAAAGATTTCGCCCGCTGAAGTTGCCAAGCATAAC AAGCCCGATGATTGTTGGGTTGTGATCAATGGTTACGTATACGACTTAACGCGATTCCTA CCAAATCATCCAGGTGGGCAGGATGTTATCAAGTTTAATGCCGGGAAAGATGTCACTGCT ATTTTTGAACCATTACATGCTCCTAATGTCATCGATAAGTATATAGCTCCCGAGAAAAAA TTGGGTCCCCTTCAAGGATCCATGCCTCCTGAACTTGTCTGTCCTCCTTATGCTCCTGGT GAAACTAAGGAAGATATCGCTAGAAAAGAACAGCTAAAATCGCTGCTACCTCCTCTAGAT AATATTATTAACCTTTACGACTTTGAATACTTGGCCTCTCAAACTTTGACTAAACAAGCG TGGGCCTACTATTCCTCCGGTGCTAACGATGAAGTTACTCACAGAGAAAACCATAATGCG TATCATAGGATTTTTTTCAAACCAAAGATCCTTGTAGATGTACGCAAAGTAGACATTTCA ACTGACATGTTGGGTTCTCATGTGGATGTTCCCTTCTACGTGTCTGCTACAGCTTTGTGT AAACTGGGAAACCCCTTAGAAGGTGAAAAAGATGTCGCCAGAGGTTGTGGCCAAGGTGTG ACAAAAGTCCCACAAATGATATCTACTTTGGCTTCATGTTCCCCCGAGGAAATTATTGAA GCAGCACCCTCTGATAAACAAATTCAATGGTACCAACTATATGTTAACTCTGATAGAAAG ATCACTGATGATTTGGTTAAAAATGTAGAAAAACTGGGTGTAAAGGCATTATTTGTCACT GTGGATGCTCCAAGTTTAGGTCAAAGAGAAAAAGATATGAAGCTGAAATTTTCCAATACA AAGGCTGGTCCAAAAGCGATGAAGAAAACTAATGTAGAAGAATCTCAAGGTGCTTCGAGA GCGTTATCAAAGTTTATTGACCCCTCTTTGACTTGGAAAGATATAGAAGAGTTGAAGAAA AAGACAAAACTACCTATTGTTATCAAAGGTGTTCAACGTACCGAAGATGTTATCAAAGCA GCAGAAATCGGTGTAAGTGGGGTGGTTCTATCCAATCATGGTGGTAGACAATTAGATTTT TCAAGGGCTCCCATTGAAGTCCTGGCTGAAACCATGCCAATCCTGGAACAACGTAACTTG AAGGATAAGTTGGAAGTTTTCGTGGACGGTGGTGTTCGTCGTGGTACAGATGTCTTGAAA GCGTTATGTCTAGGTGCTAAAGGTGTTGGTTTGGGTAGACCATTCTTGTATGCGAACTCA TGCTATGGTCGTAATGGTGTTGAAAAAGCCATTGAAATTTTAAGAGATGAAATTGAAATG TCTATGAGACTATTAGGTGTTACTAGCATTGCGGAATTGAAGCCTGATCTTTTAGATCTA TCAACACTAAAGGCAAGAACAGTTGGAGTACCAAACGACGTGCTGTATAATGAAGTTTAT GAGGGACCTACTTTAACAGAATTTGAGGATGCATGA
Protein Properties
Pfam Domain Function
Protein Residues591
Protein Molecular Weight65538.79688
Protein Theoretical pI8.62
PDB Fileshow
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Cytochrome b2, mitochondrial MLKYKPLLKISKNCEAAILRASKTRLNTIRAYGSTVPKSKSFEQDSRKRTQSWTALRVGA ILAATSSVAYLNWHNGQIDNEPKLDMNKQKISPAEVAKHNKPDDCWVVINGYVYDLTRFL PNHPGGQDVIKFNAGKDVTAIFEPLHAPNVIDKYIAPEKKLGPLQGSMPPELVCPPYAPG ETKEDIARKEQLKSLLPPLDNIINLYDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNA YHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCKLGNPLEGEKDVARGCGQGV TKVPQMISTLASCSPEEIIEAAPSDKQIQWYQLYVNSDRKITDDLVKNVEKLGVKALFVT VDAPSLGQREKDMKLKFSNTKAGPKAMKKTNVEESQGASRALSKFIDPSLTWKDIEELKK KTKLPIVIKGVQRTEDVIKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAETMPILEQRNL KDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYANSCYGRNGVEKAIEILRDEIEM SMRLLGVTSIAELKPDLLDLSTLKARTVGVPNDVLYNEVYEGPTLTEFEDA
References
External Links
ResourceLink
Saccharomyces Genome Database CYB2
Uniprot IDP00175
Uniprot NameCYB2_YEAST
GenBank Gene IDX03215
Genebank Protein ID3633
PDB ID
1KBI
General Reference
  • Guiard, B. (1985). "Structure, expression and regulation of a nuclear gene encoding a mitochondrial protein: the yeast L(+)-lactate cytochrome c oxidoreductase (cytochrome b2)." EMBO J 4:3265-3272.3004948
  • Bowman, S., Churcher, C., Badcock, K., Brown, D., Chillingworth, T., Connor, R., Dedman, K., Devlin, K., Gentles, S., Hamlin, N., Hunt, S., Jagels, K., Lye, G., Moule, S., Odell, C., Pearson, D., Rajandream, M., Rice, P., Skelton, J., Walsh, S., Whitehead, S., Barrell, B. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Nature 387:90-93.9169872
  • Ghrir, R., Becam, A. M., Lederer, F. (1984). "Primary structure of flavocytochrome b2 from baker's yeast. Purification by reverse-phase high-pressure liquid chromatography and sequencing of fragment alpha cyanogen bromide peptides." Eur J Biochem 139:59-74.6365548
  • Lederer, F., Cortial, S., Becam, A. M., Haumont, P. Y., Perez, L. (1985). "Complete amino acid sequence of flavocytochrome b2 from baker's yeast." Eur J Biochem 152:419-428.3902473
  • Guiard, B., Lederer, F., Jacq, C. (1975). "More similarity between bakers'yeast L-(+)-lactate dehydrogenase and liver microsomal cytochrome b5." Nature 255:422-423.165435
  • Grandier-Vazeille, X., Bathany, K., Chaignepain, S., Camougrand, N., Manon, S., Schmitter, J. M. (2001). "Yeast mitochondrial dehydrogenases are associated in a supramolecular complex." Biochemistry 40:9758-9769.11502169
  • Guiard, B., Lederer, F. (1976). "Complete amino acid sequence of the heme-binding core in bakers' yeast cytochrome b2 (L-(+)-lactate dehydrogenase)." Biochimie 58:305-316.776230
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Xia, Z. X., Mathews, F. S. (1990). "Molecular structure of flavocytochrome b2 at 2.4 A resolution." J Mol Biol 212:837-863.2329585
  • Cunane, L. M., Barton, J. D., Chen, Z. W., Welsh, F. E., Chapman, S. K., Reid, G. A., Mathews, F. S. (2002). "Crystallographic study of the recombinant flavin-binding domain of Baker's yeast flavocytochrome b(2): comparison with the intact wild-type enzyme." Biochemistry 41:4264-4272.11914072