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P09437

- CYB2_HANAN

UniProt

P09437 - CYB2_HANAN

Protein

Cytochrome b2, mitochondrial

Gene

CYB2

Organism
Hansenula anomala (Yeast) (Candida pelliculosa)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (01 Jan 1990)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi115 – 1151Iron (heme axial ligand)PROSITE-ProRule annotation
    Metal bindingi138 – 1381Iron (heme axial ligand)PROSITE-ProRule annotation
    Binding sitei208 – 2081Heme bBy similarity
    Binding sitei357 – 3571Heme bBy similarity
    Active sitei432 – 4321Proton acceptorPROSITE-ProRule annotation
    Binding sitei435 – 4351SubstratePROSITE-ProRule annotation

    GO - Molecular functioni

    1. FMN binding Source: InterPro
    2. heme binding Source: InterPro
    3. L-lactate dehydrogenase (cytochrome) activity Source: UniProtKB-EC
    4. metal ion binding Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Respiratory chain, Transport

    Keywords - Ligandi

    Flavoprotein, FMN, Heme, Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:CYB2
    OrganismiHansenula anomala (Yeast) (Candida pelliculosa)
    Taxonomic identifieri4927 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPhaffomycetaceaeWickerhamomyces

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial intermembrane space Source: UniProtKB-SubCell
    2. respiratory chain Source: UniProtKB-KW

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 7373MitochondrionAdd
    BLAST
    Chaini74 – 573500Cytochrome b2, mitochondrialPRO_0000006479Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    3D structure databases

    ProteinModelPortaliP09437.
    SMRiP09437. Positions 82-567.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini80 – 15778Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini182 – 542361FMN hydroxy acid dehydrogenasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation
    Contains 1 FMN hydroxy acid dehydrogenase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Family and domain databases

    Gene3Di3.10.120.10. 1 hit.
    3.20.20.70. 1 hit.
    InterProiIPR013785. 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]
    PfamiPF00173. Cyt-b5. 1 hit.
    PF01070. FMN_dh. 1 hit.
    [Graphical view]
    SUPFAMiSSF55856. SSF55856. 1 hit.
    PROSITEiPS00191. 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]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P09437-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFKSQLRTAT ARSSFRSLAS KLNPQRFNSS KTPLLNATRG SNRSKNSLIA    50
    LAISLSAVSS SYYLYQKDKF ISADVPHWKD IELTPEIVSQ HNKKDDLWVV 100
    LNGQVYDLTD FLPNHPGGQK IIIRYAGKDA TKIFVPIHPP DTIEKFIPPE 150
    KHLGPLVGEF EQEEEELSDE EIDRLERIER KPPLSQMINL HDFETIARQI 200
    LPPPALAYYC SAADDEVTLR ENHNAYHRIF FNPKILIDVK DVDISTEFFG 250
    EKTSAPFYIS ATALAKLGHP EGEVAIAKGA GREDVVQMIS TLASCSFDEI 300
    ADARIPGQQQ WYQLYVNADR SITEKAVRHA EERGMKGLFI TVDAPSLGRR 350
    EKDMKMKFEA DSDVQGDDED IDRSQGASRA LSSFIDPSLS WKDIAFIKSI 400
    TKMPIVIKGV QRKEDVLLAA EHGLQGVVLS NHGGRQLDYT RAPVEVLAEV 450
    MPILKERGLD QKIDIFVDGG VRRGTDVLKA LCLGAKGVGL GRPFLYAMSS 500
    YGDKGVTKAI QLLKDEIEMN MRLLGVNKIE ELTPELLDTR SIHNRAVPVA 550
    KDYLYEQNYQ RMSGAEFRPG IED 573
    Length:573
    Mass (Da):64,202
    Last modified:January 1, 1990 - v2
    Checksum:i83EEF645C580BC8E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16051 Genomic DNA. Translation: CAA34183.1.
    PIRiS06600.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16051 Genomic DNA. Translation: CAA34183.1 .
    PIRi S06600.

    3D structure databases

    ProteinModelPortali P09437.
    SMRi P09437. Positions 82-567.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.10.120.10. 1 hit.
    3.20.20.70. 1 hit.
    InterProi IPR013785. 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 ]
    Pfami PF00173. Cyt-b5. 1 hit.
    PF01070. FMN_dh. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55856. SSF55856. 1 hit.
    PROSITEi PS00191. 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 ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiCYB2_HANAN
    AccessioniPrimary (citable) accession number: P09437
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 109 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3