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UniProtKB/Swiss-Prot entry P00175


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CYB2_YEAST
Primary accession number P00175
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on April 1, 1988 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 109)
Name and origin of the protein
Protein name Cytochrome b2, mitochondrial [Precursor]
Synonyms EC 1.1.2.3
L-lactate dehydrogenase [Cytochrome]
L-lactate ferricytochrome C oxidoreductase
L-LCR
Gene name
Name: CYB2
OrderedLocusNames: YML054C
ORFNames: YM9958.08C
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3004948 [NCBI, ExPASy, EBI, Israel, Japan]
Guiard B.;
"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(1985).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169872 [NCBI, ExPASy, EBI, Israel, Japan]
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., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
Nature 387:90-93(1997).
[3]
PROTEIN SEQUENCE OF 81-394.
PubMed=6365548 [NCBI, ExPASy, EBI, Israel, Japan]
Ghrir R., Becam A.-M., Lederer F.;
"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(1984).
[4]
PROTEIN SEQUENCE OF 395-591.
PubMed=3902473 [NCBI, ExPASy, EBI, Israel, Japan]
Lederer F., Cortial S., Becam A.-M., Haumont P.-Y., Perez L.;
"Complete amino acid sequence of flavocytochrome b2 from baker's yeast.";
Eur. J. Biochem. 152:419-428(1985).
[5]
PROTEIN SEQUENCE OF 81-94.
DOI=10.1038/255422a0; PubMed=165435 [NCBI, ExPASy, EBI, Israel, Japan]
Guiard B., Lederer F., Jacq C.;
"More similarity between bakers'yeast L-(+)-lactate dehydrogenase and liver microsomal sytochrome B5.";
Nature 255:422-423(1975).
[6]
PROTEIN SEQUENCE OF 83-88 AND 564-570, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 201238 / W303-1B;
DOI=10.1021/bi010277r; PubMed=11502169 [NCBI, ExPASy, EBI, Israel, Japan]
Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.;
"Yeast mitochondrial dehydrogenases are associated in a supramolecular complex.";
Biochemistry 40:9758-9769(2001).
[7]
PROTEIN SEQUENCE OF 88-183.
PubMed=776230 [NCBI, ExPASy, EBI, Israel, Japan]
Guiard B., Lederer F.;
"Complete amino acid sequence of the heme-binding core in bakers' yeast cytochrome b2 (L-(+)-lactate dehydrogenase).";
Biochimie 58:305-316(1976).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
DOI=10.1016/0022-2836(90)90240-M; PubMed=2329585 [NCBI, ExPASy, EBI, Israel, Japan]
Xia Z.-X., Mathews F.S.;
"Molecular structure of flavocytochrome b2 at 2.4-A resolution.";
J. Mol. Biol. 212:837-863(1990).
[10]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 180-591.
DOI=10.1021/bi0119870; PubMed=11914072 [NCBI, ExPASy, EBI, Israel, Japan]
Cunane L.M., Barton J.D., Chen Z.-W., Welsh F.E., Chapman S.K., Reid G.A., Mathews F.S.;
"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(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X03215; CAA26959.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z46729; CAA86721.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A24583; CBBY2.
RefSeq NP_013658.1; -.
3D structure databases
PDB
1FCB; X-ray; 2.40 A; A/B=81-591.[ExPASy / RCSB / EBI]
1KBI; X-ray; 2.30 A; A/B=81-591.[ExPASy / RCSB / EBI]
1KBJ; X-ray; 2.50 A; A/B=180-591.[ExPASy / RCSB / EBI]
1LCO; X-ray; 2.90 A; A/B=81-591.[ExPASy / RCSB / EBI]
1LDC; X-ray; 2.90 A; A/B=81-591.[ExPASy / RCSB / EBI]
1LTD; X-ray; 2.60 A; A/B=86-591.[ExPASy / RCSB / EBI]
1QCW; X-ray; 2.75 A; A/B=182-591.[ExPASy / RCSB / EBI]
1SZE; X-ray; 3.00 A; A/B=81-591.[ExPASy / RCSB / EBI]
1SZF; X-ray; 2.70 A; A/B=81-591.[ExPASy / RCSB / EBI]
1SZG; X-ray; 2.70 A; A/B=81-591.[ExPASy / RCSB / EBI]
2OZ0; X-ray; 2.80 A; A/B=81-591.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1FCB; -.
1KBI; -.
1KBJ; -.
1LCO; -.
1LDC; -.
1LTD; -.
1QCW; -.
1SZE; -.
1SZF; -.
1SZG; -.
2OZ0; -.
ModBase P00175.
Protein-protein interaction databases
DIP DIP:5810N; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-12911; -.
Organism-specific databases
CYGD YML054c; -.
SGD S000004518; CYB2.
Yeast-GFP YML054C.
Gene expression databases
GermOnline YML054C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005758; Cellular component: mitochondrial intermembrane space (inferred from direct assay from SGD).
GO:0004460; Molecular function: L-lactate dehydrogenase (cytochrome) activity (inferred from direct assay from SGD).
GO:0006089; Biological process: lactate metabolic process (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR013785; Aldolase_TIM.
IPR001199; Cyt_B5.
IPR008259; FMN_hydac_DHase_AS.
IPR000262; FMN_OHA_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
G3DSA:3.10.120.10; Cyt_B5; 1.
Pfam PF00173; Cyt-b5; 1.
PF01070; FMN_dh; 1.
Pfam graphical view of domain structure.
PRINTS PR00363; CYTOCHROMEB5.
ProDom PD000612; Cyt_B5; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00191; CYTOCHROME_B5_1; 1.
PS50255; CYTOCHROME_B5_2; 1.
PS00557; FMN_HYDROXY_ACID_DH_1; 1.
PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P00175.
Proteomic databases
PeptideAtlas P00175; -.
Genome annotation databases
Ensembl YML054C; Saccharomyces cerevisiae. [Contig view]
GeneID 854950; -.
GenomeReviews Z71257_GR; YML054C.
KEGG sce:YML054C; -.
NMPDR fig|4932.3.peg.4696; -.
Phylogenomic databases
HOGENOM P00175; -.
Other
LinkHub P00175; -.
ProtoNet P00175.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Direct protein sequencing; Electron transport; Flavoprotein; FMN; Heme; Iron; Metal-binding; Mitochondrion; Oxidoreductase; Respiratory chain; Transit peptide; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    80  80     Mitochondrion. 
CHAIN   81   591  511     Cytochrome b2, mitochondrial. PRO_0000006480
DOMAIN   88   165  78     Cytochrome b5 heme-binding. 
DOMAIN   197   563  367     FMN hydroxy acid dehydrogenase. 
REGION   177   190  14     Hinge. 
REGION   567   591  25     Tail (wraps around the molecular 4-fold axis). 
ACT_SITE   453   453        Proton acceptor. 
METAL   123   123        Iron (heme axial ligand) (By similarity). 
METAL   146   146        Iron (heme axial ligand) (By similarity). 
BINDING   456   456        Substrate. 
CONFLICT   165   165        Q -> E (in Ref. 3 and 7). 
CONFLICT   466   466        E -> Q (in Ref. 4; AA sequence). 
CONFLICT   513   513        R -> E (in Ref. 4; AA sequence). 
CONFLICT   570   570        V -> P (in Ref. 6; AA sequence). 
TURN   93    98  6      
HELIX   102   104  3      
STRAND   106   109  4      
STRAND   112   115  4      
TURN   117   119  3      
HELIX   120   122  3      
HELIX   128   131  4      
STRAND   135   137  3      
HELIX   139   142  4      
HELIX   143   145  3      
HELIX   150   154  5      
HELIX   157   159  3      
STRAND   160   166  7      
STRAND   170   173  4      
HELIX   185   191  7      
STRAND   192   194  3      
HELIX   199   201  3      
HELIX   206   215  10      
HELIX   218   225  8      
HELIX   232   239  8      
HELIX   240   243  4      
STRAND   261   263  3      
STRAND   266   274  9      
TURN   280   283  4      
TURN   285   288  4      
HELIX   289   297  9      
STRAND   298   301  4      
STRAND   305   308  4      
HELIX   315   320  6      
STRAND   325   327  3      
STRAND   329   333  5      
HELIX   339   351  13      
STRAND   357   360  4      
HELIX   370   376  7      
HELIX   412   420  9      
STRAND   426   431  6      
HELIX   434   442  9      
STRAND   446   450  5      
TURN   453   456  4      
HELIX   464   477  14      
HELIX   481   483  3      
STRAND   484   491  8      
HELIX   495   503  9      
STRAND   507   512  6      
HELIX   513   545  33      
HELIX   550   552  3      
HELIX   555   557  3      
TURN   561   564  4      
STRAND   566   569  4      
HELIX   574   579  6      
Sequence information
Length: 591 AA [This is the length of the unprocessed precursor] Molecular weight: 65539 Da [This is the MW of the unprocessed precursor] CRC64: DBADA0751B3C5B83 [This is a checksum on the sequence]
        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 

P00175 in FASTA format

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