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P09437 (CYB2_HANAN) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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
OrganismHansenula anomala (Yeast) (Candida pelliculosa)
Taxonomic identifier4927 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPhaffomycetaceaeWickerhamomyces

Protein attributes

Sequence length573 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 By similarity.

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

Subunit structure

Homotetramer.

Subcellular location

Mitochondrion intermembrane space.

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 – 7373Mitochondrion
Chain74 – 573500Cytochrome b2, mitochondrial
PRO_0000006479

Regions

Domain80 – 15778Cytochrome b5 heme-binding
Domain182 – 542361FMN hydroxy acid dehydrogenase

Sites

Active site4321Proton acceptor By similarity
Metal binding1151Iron (heme axial ligand) By similarity
Metal binding1381Iron (heme axial ligand) By similarity
Binding site2081Heme b By similarity
Binding site3571Heme b By similarity
Binding site4351Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P09437 [UniParc].

Last modified January 1, 1990. Version 2.
Checksum: 83EEF645C580BC8E

FASTA57364,202
        10         20         30         40         50         60 
MFKSQLRTAT ARSSFRSLAS KLNPQRFNSS KTPLLNATRG SNRSKNSLIA LAISLSAVSS 

        70         80         90        100        110        120 
SYYLYQKDKF ISADVPHWKD IELTPEIVSQ HNKKDDLWVV LNGQVYDLTD FLPNHPGGQK 

       130        140        150        160        170        180 
IIIRYAGKDA TKIFVPIHPP DTIEKFIPPE KHLGPLVGEF EQEEEELSDE EIDRLERIER 

       190        200        210        220        230        240 
KPPLSQMINL HDFETIARQI LPPPALAYYC SAADDEVTLR ENHNAYHRIF FNPKILIDVK 

       250        260        270        280        290        300 
DVDISTEFFG EKTSAPFYIS ATALAKLGHP EGEVAIAKGA GREDVVQMIS TLASCSFDEI 

       310        320        330        340        350        360 
ADARIPGQQQ WYQLYVNADR SITEKAVRHA EERGMKGLFI TVDAPSLGRR EKDMKMKFEA 

       370        380        390        400        410        420 
DSDVQGDDED IDRSQGASRA LSSFIDPSLS WKDIAFIKSI TKMPIVIKGV QRKEDVLLAA 

       430        440        450        460        470        480 
EHGLQGVVLS NHGGRQLDYT RAPVEVLAEV MPILKERGLD QKIDIFVDGG VRRGTDVLKA 

       490        500        510        520        530        540 
LCLGAKGVGL GRPFLYAMSS YGDKGVTKAI QLLKDEIEMN MRLLGVNKIE ELTPELLDTR 

       550        560        570 
SIHNRAVPVA KDYLYEQNYQ RMSGAEFRPG IED 

« Hide

References

[1]"Nucleotide sequence of the Hansenula anomala gene encoding flavocytochrome b2 (L-lactate:cytochrome c oxidoreductase)."
Risler Y., Tegoni M., Gervais M.
Nucleic Acids Res. 17:8381-8381(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structural basis for the kinetic differences between flavocytochromes b2 from the yeasts Hansenula anomala and Saccharomyces cerevisiae."
Black M.T., Gunn F.J., Chapman S.K., Reid G.A.
Biochem. J. 263:973-976(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Amino-acid sequence of the cytochrome-b5-like heme-binding domain from Hansenula anomala flavocytochrome b2."
Haumont P.-Y., Thomas M.-A., Labeyrie F., Lederer F.
Eur. J. Biochem. 169:539-546(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 80-163.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16051 Genomic DNA. Translation: CAA34183.1.
PIRS06600.

3D structure databases

ProteinModelPortalP09437.
SMRP09437. Positions 82-567.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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]
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...

Entry information

Entry nameCYB2_HANAN
AccessionPrimary (citable) accession number: P09437
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 1, 1990
Last modified: October 16, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families