Reviewed, UniProtKB/Swiss-Prot Q6CA86 (NCB5R_YARLI)

Names and origin

Protein names

Recommended name:
    NADH-cytochrome b5 reductase 1
    EC=1.6.2.2
Alternative name(s):
    Microsomal cytochrome b reductase

Gene names

Name:	CBR1
Ordered Locus Names:	YALI0D04983g

Organism

Yarrowia lipolytica (Candida lipolytica) [Complete proteome]

Taxonomic identifier

4952 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia

Protein attributes

Sequence length	290 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Electron donor reductase for cytochrome b5. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes By similarity.
Catalytic activity	NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5.
Cofactor	FAD By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane protein By similarity. Mitochondrion outer membrane; Single-pass membrane protein By similarity.
Sequence similarities	Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. Contains 1 FAD-binding FR-type domain.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Mitochondrion Mitochondrion outer membrane
Domain	Transmembrane
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cytochrome-b5 reductase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 290	290	NADH-cytochrome b5 reductase 1		PRO_0000330166
Regions
	Transmembrane	13 – 33	21	Potential
	Domain	47 – 151	105	FAD-binding FR-type
	Nucleotide binding	131 – 146	16	FAD By similarity
	Nucleotide binding	157 – 189	33	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6CA86-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: DFE44F6E2184F36B	FASTA	290	31,939
	10 20 30 40 50 60 MRSSSSRQPQ MQSYYAIATV WALIIGAATY YFFSNSKPKA VLQRGDTAFK EFPLIQKTVL 70 80 90 100 110 120 SHNSAIYRFG LPRPSHVLGL PIGQHVSLSA NIGGKEVLRS YTPTSSDLYD KGYFDILIKT 130 140 150 160 170 180 YPQGNISKYV SELAIGDTMK VRGPKGNFVY NHGLVESFGM VCGGTGITPM YQILRHIAAD 190 200 210 220 230 240 PADNTKVNLV YANVNHDDIL LKKELDAIAA ENDNIKIHYV LNNAPEDWTG SVGFVTKEIL 250 260 270 280 290 EKHCPPPGPN TKLLLCGPPP MISALKKASV ELGYEKARPV SKLEDQVFAF

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIB 122 / E 150.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR382130 Genomic DNA. Translation: CAG80614.1.
RefSeq	XP_502426.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2910663.
GenomeReviews	Gene locus YALI0D04983g in contig CR382130_GR.
KEGG	yli:YALI0D04983g.
Phylogenomic databases
HOGENOM	Q6CA86.
OMA	GNISRHV.
Family and domain databases
InterPro	IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR001834. NADH-Cyt_B5_reductase. IPR008333. OxRdtase_FAD-bd. IPR001433. OxRdtase_FAD/NAD_bd. [Graphical view]
Pfam	PF00970. FAD_binding_6. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00406. CYTB5RDTASE. PR00371. FPNCR.
PROSITE	PS51384. FAD_FR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NCB5R_YARLI

Accession

Primary (citable) accession number: Q6CA86

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	August 16, 2004
Last modified:	November 3, 2009
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)