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P00175 (CYB2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome b2, mitochondrial

EC=1.1.2.3
Alternative name(s):
L-lactate dehydrogenase [Cytochrome]
L-lactate ferricytochrome C oxidoreductase
Short name=L-LCR
Gene names
Name:CYB2
Ordered Locus Names:YML054C
ORF Names:YM9958.08C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length591 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

(S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H+.

Cofactor

FMN (Ref.11).

Binds 1 heme B (iron-protoporphyrin IX) group non-covalently per subunit (Ref.11).

Subunit structure

Homotetramer.

Subcellular location

Mitochondrion intermembrane space Ref.7.

Induction

By L-lactate. Induced during respiratory adaptation.

Miscellaneous

Present with 4590 molecules/cell in log phase SD medium.

Sequence similarities

Contains 1 cytochrome b5 heme-binding domain.

Contains 1 FMN hydroxy acid dehydrogenase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 8080Mitochondrion Ref.4 Ref.6
Chain81 – 591511Cytochrome b2, mitochondrial
PRO_0000006480

Regions

Domain88 – 16578Cytochrome b5 heme-binding
Domain197 – 563367FMN hydroxy acid dehydrogenase
Region177 – 19014Hinge
Region567 – 59125Tail (wraps around the molecular 4-fold axis)

Sites

Active site4531Proton acceptor
Metal binding1231Iron (heme axial ligand)
Metal binding1461Iron (heme axial ligand)
Binding site1771Heme b
Binding site2191Heme b
Binding site2231Heme b
Binding site3761Heme b
Binding site4561Substrate

Experimental info

Sequence conflict1651Q → E AA sequence Ref.4
Sequence conflict1651Q → E AA sequence Ref.8
Sequence conflict4661E → Q AA sequence Ref.5
Sequence conflict5131R → E AA sequence Ref.5
Sequence conflict5701V → P AA sequence Ref.7

Secondary structure

.............................................................................................. 591
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00175 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: DBADA0751B3C5B83

FASTA59165,539
        10         20         30         40         50         60 
MLKYKPLLKI SKNCEAAILR ASKTRLNTIR AYGSTVPKSK SFEQDSRKRT QSWTALRVGA 

        70         80         90        100        110        120 
ILAATSSVAY LNWHNGQIDN EPKLDMNKQK ISPAEVAKHN KPDDCWVVIN GYVYDLTRFL 

       130        140        150        160        170        180 
PNHPGGQDVI KFNAGKDVTA IFEPLHAPNV IDKYIAPEKK LGPLQGSMPP ELVCPPYAPG 

       190        200        210        220        230        240 
ETKEDIARKE QLKSLLPPLD NIINLYDFEY LASQTLTKQA WAYYSSGAND EVTHRENHNA 

       250        260        270        280        290        300 
YHRIFFKPKI LVDVRKVDIS TDMLGSHVDV PFYVSATALC KLGNPLEGEK DVARGCGQGV 

       310        320        330        340        350        360 
TKVPQMISTL ASCSPEEIIE AAPSDKQIQW YQLYVNSDRK ITDDLVKNVE KLGVKALFVT 

       370        380        390        400        410        420 
VDAPSLGQRE KDMKLKFSNT KAGPKAMKKT NVEESQGASR ALSKFIDPSL TWKDIEELKK 

       430        440        450        460        470        480 
KTKLPIVIKG VQRTEDVIKA AEIGVSGVVL SNHGGRQLDF SRAPIEVLAE TMPILEQRNL 

       490        500        510        520        530        540 
KDKLEVFVDG GVRRGTDVLK ALCLGAKGVG LGRPFLYANS CYGRNGVEKA IEILRDEIEM 

       550        560        570        580        590 
SMRLLGVTSI AELKPDLLDL STLKARTVGV PNDVLYNEVY EGPTLTEFED A 

« Hide

References

« Hide 'large scale' references
[1]"Structure, expression and regulation of a nuclear gene encoding a mitochondrial protein: the yeast L(+)-lactate cytochrome c oxidoreductase (cytochrome b2)."
Guiard B.
EMBO J. 4:3265-3272(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., 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.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"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."
Ghrir R., Becam A.-M., Lederer F.
Eur. J. Biochem. 139:59-74(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 81-394.
[5]"Complete amino acid sequence of flavocytochrome b2 from baker's yeast."
Lederer F., Cortial S., Becam A.-M., Haumont P.-Y., Perez L.
Eur. J. Biochem. 152:419-428(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 395-591.
[6]"More similarity between bakers'yeast L-(+)-lactate dehydrogenase and liver microsomal sytochrome B5."
Guiard B., Lederer F., Jacq C.
Nature 255:422-423(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 81-94.
[7]"Yeast mitochondrial dehydrogenases are associated in a supramolecular complex."
Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.
Biochemistry 40:9758-9769(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 83-88 AND 564-570, SUBCELLULAR LOCATION.
Strain: ATCC 201238 / W303-1B.
[8]"Complete amino acid sequence of the heme-binding core in bakers' yeast cytochrome b2 (L-(+)-lactate dehydrogenase)."
Guiard B., Lederer F.
Biochimie 58:305-316(1976) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 88-183.
[9]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]"Molecular structure of flavocytochrome b2 at 2.4-A resolution."
Xia Z.-X., Mathews F.S.
J. Mol. Biol. 212:837-863(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[11]"Crystallographic study of the recombinant flavin-binding domain of Baker's yeast flavocytochrome b(2): comparison with the intact wild-type enzyme."
Cunane L.M., Barton J.D., Chen Z.-W., Welsh F.E., Chapman S.K., Reid G.A., Mathews F.S.
Biochemistry 41:4264-4272(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 81-591 IN COMPLEXES WITH HEME AND FMN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03215 Genomic DNA. Translation: CAA26959.1.
Z46729 Genomic DNA. Translation: CAA86721.1.
BK006946 Genomic DNA. Translation: DAA09844.1.
PIRCBBY2. A24583.
RefSeqNP_013658.1. NM_001182412.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FCBX-ray2.40A/B81-591[»]
1KBIX-ray2.30A/B81-591[»]
1KBJX-ray2.50A/B180-591[»]
1LCOX-ray2.90A/B81-591[»]
1LDCX-ray2.90A/B81-591[»]
1LTDX-ray2.60A/B86-591[»]
1QCWX-ray2.75A/B182-591[»]
1SZEX-ray3.00A/B81-591[»]
1SZFX-ray2.70A/B81-591[»]
1SZGX-ray2.70A/B81-591[»]
2OZ0X-ray2.80A/B81-591[»]
3KS0X-ray2.70A/B86-180[»]
ProteinModelPortalP00175.
SMRP00175. Positions 81-591.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35113. 29 interactions.
DIPDIP-5810N.
IntActP00175. 9 interactions.
MINTMINT-605329.
STRING4932.YML054C.

Proteomic databases

PaxDbP00175.
PeptideAtlasP00175.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYML054C; YML054C; YML054C.
GeneID854950.
KEGGsce:YML054C.

Organism-specific databases

CYGDYML054c.
SGDS000004518. CYB2.

Phylogenomic databases

eggNOGCOG1304.
GeneTreeENSGT00390000018717.
HOGENOMHOG000217463.
KOK00101.
OMAISKNCEA.
OrthoDBEOG7N63X3.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12911.
YEAST:YML054C-MONOMER.
ReactomeREACT_118590. Mitochondrial Protein Import (yeast).
REACT_85873. Metabolism of proteins.
SABIO-RKP00175.

Gene expression databases

GenevestigatorP00175.

Family and domain databases

Gene3D3.10.120.10. 1 hit.
3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]
PfamPF00173. Cyt-b5. 1 hit.
PF01070. FMN_dh. 1 hit.
[Graphical view]
PRINTSPR00363. CYTOCHROMEB5.
SUPFAMSSF55856. SSF55856. 1 hit.
PROSITEPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00175.
NextBio978016.

Entry information

Entry nameCYB2_YEAST
AccessionPrimary (citable) accession number: P00175
Secondary accession number(s): D6VZC0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: April 16, 2014
This is version 158 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references