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P09437

- CYB2_HANAN

UniProt

P09437 - CYB2_HANAN

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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

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
Complete GO annotation...

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. mitochondrion Source: UniProtKB-KW
  2. respiratory chain Source: UniProtKB-KW
Complete GO annotation...

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

        10         20         30         40         50
MFKSQLRTAT ARSSFRSLAS KLNPQRFNSS KTPLLNATRG SNRSKNSLIA
60 70 80 90 100
LAISLSAVSS SYYLYQKDKF ISADVPHWKD IELTPEIVSQ HNKKDDLWVV
110 120 130 140 150
LNGQVYDLTD FLPNHPGGQK IIIRYAGKDA TKIFVPIHPP DTIEKFIPPE
160 170 180 190 200
KHLGPLVGEF EQEEEELSDE EIDRLERIER KPPLSQMINL HDFETIARQI
210 220 230 240 250
LPPPALAYYC SAADDEVTLR ENHNAYHRIF FNPKILIDVK DVDISTEFFG
260 270 280 290 300
EKTSAPFYIS ATALAKLGHP EGEVAIAKGA GREDVVQMIS TLASCSFDEI
310 320 330 340 350
ADARIPGQQQ WYQLYVNADR SITEKAVRHA EERGMKGLFI TVDAPSLGRR
360 370 380 390 400
EKDMKMKFEA DSDVQGDDED IDRSQGASRA LSSFIDPSLS WKDIAFIKSI
410 420 430 440 450
TKMPIVIKGV QRKEDVLLAA EHGLQGVVLS NHGGRQLDYT RAPVEVLAEV
460 470 480 490 500
MPILKERGLD QKIDIFVDGG VRRGTDVLKA LCLGAKGVGL GRPFLYAMSS
510 520 530 540 550
YGDKGVTKAI QLLKDEIEMN MRLLGVNKIE ELTPELLDTR SIHNRAVPVA
560 570
KDYLYEQNYQ RMSGAEFRPG IED
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 29, 2014
This is version 110 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