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Protein

Cytochrome b2, mitochondrial

Gene

CYB2

Organism
Wickerhamomyces anomalus (Yeast) (Hansenula anomala)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • FMNPROSITE-ProRule annotation
  • heme bBy similarityNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi115Iron (heme axial ligand)PROSITE-ProRule annotation1
Metal bindingi138Iron (heme axial ligand)PROSITE-ProRule annotation1
Binding sitei208Heme bBy similarity1
Binding sitei357Heme bBy similarity1
Active sitei432Proton acceptorPROSITE-ProRule annotation1
Binding sitei435SubstratePROSITE-ProRule annotation1

GO - Molecular functioni

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
OrganismiWickerhamomyces anomalus (Yeast) (Hansenula anomala)
Taxonomic identifieri4927 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPhaffomycetaceaeWickerhamomyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 73MitochondrionAdd BLAST73
ChainiPRO_000000647974 – 573Cytochrome b2, mitochondrialAdd BLAST500

Proteomic databases

PRIDEiP09437.

Interactioni

Subunit structurei

Homotetramer.

Structurei

3D structure databases

ProteinModelPortaliP09437.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini80 – 157Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd BLAST78
Domaini182 – 542FMN hydroxy acid dehydrogenasePROSITE-ProRule annotationAdd BLAST361

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]
SMARTiSM01117. Cyt-b5. 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:
EMBLi
GenBanki
DDBJi
Links Updated
X16051 Genomic DNA. Translation: CAA34183.1.
PIRiS06600.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16051 Genomic DNA. Translation: CAA34183.1.
PIRiS06600.

3D structure databases

ProteinModelPortaliP09437.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP09437.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]
SMARTiSM01117. Cyt-b5. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiCYB2_WICAO
AccessioniPrimary (citable) accession number: P09437
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 1, 1990
Last modified: October 5, 2016
This is version 119 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.