[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1093/nar/17.20.8381; PubMed=2813072 [NCBI, ExPASy, EBI, Israel, Japan] Risler Y., Tegoni M., Gervais M.; "Nucleotide sequence of the Hansenula anomala gene encoding flavocytochrome b2 (L-lactate:cytochrome c oxidoreductase)."; Nucleic Acids Res. 17:8381-8381(1989).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2688640 [NCBI, ExPASy, EBI, Israel, Japan] Black M.T., Gunn F.J., Chapman S.K., Reid G.A.; "Structural basis for the kinetic differences between flavocytochromes b2 from the yeasts Hansenula anomala and Saccharomyces cerevisiae."; Biochem. J. 263:973-976(1989).
[3]	PROTEIN SEQUENCE OF 80-163. PubMed=3319613 [NCBI, ExPASy, EBI, Israel, Japan] Haumont P.-Y., Thomas M.-A., Labeyrie F., Lederer F.; "Amino-acid sequence of the cytochrome-b5-like heme-binding domain from Hansenula anomala flavocytochrome b2."; Eur. J. Biochem. 169:539-546(1987).

Comments

CATALYTIC ACTIVITY: (S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H⁺.
COFACTOR: FMN.
COFACTOR: Protoheme IX groups.
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.
SIMILARITY: Contains 1 FMN hydroxy acid dehydrogenase domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X16051; CAA34183.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S06600; S06600.

3D structure databases

HSSP

P00175; 1LCO. [HSSP ENTRY / PDB]

ModBase

P09437.

Ontologies

GO:0005758;	Cellular component: mitochondrial intermembrane space (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004460;	Molecular function: L-lactate dehydrogenase (cytochrome) activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR013785; Aldolase_TIM.
IPR001199; Cyt_B5.
IPR008259; FMN_hydac_DHase_AS.
IPR000262; FMN_OHA_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.
G3DSA:3.10.120.10; Cyt_B5; 1.

Pfam

PF00173; Cyt-b5; 1.
PF01070; FMN_dh; 1.
Pfam graphical view of domain structure.

PRINTS

PR00363; CYTOCHROMEB5.

ProDom

PD000612; Cyt_B5; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00191; CYTOCHROME_B5_1; 1.
PS50255; CYTOCHROME_B5_2; 1.
PS00557; FMN_HYDROXY_ACID_DH_1; 1.
PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PROSITE graphical view of domain structure (profiles).

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Electron transport; Flavoprotein; FMN; Heme; Iron; Metal-binding; Mitochondrion; Oxidoreductase; Respiratory chain; Transit peptide; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 73`	`73`	`Mitochondrion.`
`CHAIN`	`74 573`	`500`	`Cytochrome b2, mitochondrial.`	`PRO_0000006479`
`DOMAIN`	`80 157`	`78`	`Cytochrome b5 heme-binding.`
`DOMAIN`	`182 542`	`361`	`FMN hydroxy acid dehydrogenase.`
`ACT_SITE`	`432 432`		`Proton acceptor (By similarity).`
`METAL`	`115 115`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`138 138`		`Iron (heme axial ligand) (By similarity).`
`BINDING`	`435 435`		`Substrate (By similarity).`

Sequence information

Length: 573 AA [This is the length of the unprocessed precursor]

Molecular weight: 64202 Da [This is the MW of the unprocessed precursor]

CRC64: 83EEF645C580BC8E [This is a checksum on the sequence]

        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

P09437 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools