P09437 (CYB2_HANAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

CYB2

Organism

Hansenula anomala (Yeast) (Candida pelliculosa)

Taxonomic identifier

4927 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Phaffomycetaceae › Wickerhamomyces

Protein attributes

Sequence length	573 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	(S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H+.
Cofactor	FMN. Protoheme IX groups.
Subunit structure	Homotetramer.
Subcellular location	Mitochondrion intermembrane space.
Sequence similarities	Contains 1 cytochrome b5 heme-binding domain. Contains 1 FMN hydroxy acid dehydrogenase domain.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	FMN Flavoprotein Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrial intermembrane space Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	FMN binding Inferred from electronic annotation. Source: InterPro L-lactate dehydrogenase (cytochrome) activity Inferred from electronic annotation. Source: EC heme binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 73	73	Mitochondrion
	Chain	74 – 573	500	Cytochrome b2, mitochondrial		PRO_0000006479
Regions
	Domain	80 – 157	78	Cytochrome b5 heme-binding
	Domain	182 – 542	361	FMN hydroxy acid dehydrogenase
Sites
	Active site	432	1	Proton acceptor By similarity
	Metal binding	115	1	Iron (heme axial ligand) By similarity
	Metal binding	138	1	Iron (heme axial ligand) By similarity
	Binding site	435	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P09437 [UniParc]. Last modified January 1, 1990. Version 2. Checksum: 83EEF645C580BC8E	FASTA	573	64,202
	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

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.
PIR	S06600.
3D structure databases
ProteinModelPortal	P09437.
SMR	P09437. Positions 82-567.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.10.120.10. 1 hit. 3.20.20.70. 1 hit.
InterPro	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]
Pfam	PF00173. Cyt-b5. 1 hit. PF01070. FMN_dh. 1 hit. [Graphical view]
SUPFAM	SSF55856. Cyt_B5. 1 hit.
PROSITE	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]
ProtoNet	Search...

Entry information

Entry name

CYB2_HANAN

Accession

Primary (citable) accession number: P09437

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 1, 1990
Last modified:	April 3, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program