Q6CID0 (NCB5R_KLULA) Reviewed, UniProtKB/Swiss-Prot

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:	KLLA0F27621g

Organism

Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

284590 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces

Protein attributes

Sequence length	281 AA.
Sequence status	Complete.
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 Transmembrane helix
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cytochrome-b5 reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 281	281	NADH-cytochrome b5 reductase 1		PRO_0000330154
Regions
	Transmembrane	2 – 22	21	Helical; Potential
	Domain	37 – 141	105	FAD-binding FR-type
	Nucleotide binding	121 – 136	16	FAD By similarity
	Nucleotide binding	147 – 179	33	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6CID0 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 1FCA8AE0D3425AD2	FASTA	281	31,220
	10 20 30 40 50 60 MVPGKFIFTA TFVLLCTIIA VVLEYQSKKD KPVLDKEKLQ EFPLVAKTVL THNTAIYRFG 70 80 90 100 110 120 LPKSTQVLGL PIGQHISVQA NINGKDILRS YTPTSLDSDA VGHFELLIKS YEKGNISKHF 130 140 150 160 170 180 AQLNIGDKIK VRGPKGFYHY QPNMNEEIGM IAGGTGIAPM YQIMKSIFAN DSDKTKVSLV 190 200 210 220 230 240 YGNQTEEDIL LKKELDAFVE RKPDQFKVYY LLDKAPEAWT GGVGYITVDT MKERLPAPAE 250 260 270 280 GVQLLVCGPP PMVSSIKRNA VTLGYEKAKP ISKMGDQIFV F

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: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382126 Genomic DNA. Translation: CAG99017.1.
RefSeq	XP_456309.1. XM_456309.1.
3D structure databases
HSSP	HSSP built from PDB template 2CND based on UniProtKB P17571.
ProteinModelPortal	Q6CID0.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2894868.
GenomeReviews	Gene locus KLLA0F27621g in contig CR382126_GR.
KEGG	kla:KLLA0F27621g.
Phylogenomic databases
eggNOG	fuNOG05226.
HOGENOM	HBG591994.
OMA	EEPLILM.
OrthoDB	EOG4FFH9R.
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_dom. IPR001433. OxRdtase_FAD/NAD-bd. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
KO	K00326.
Pfam	PF00970. FAD_binding_6. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00406. CYTB5RDTASE. PR00371. FPNCR.
SUPFAM	SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITE	PS51384. FAD_FR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NCB5R_KLULA

Accession

Primary (citable) accession number: Q6CID0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	August 16, 2004
Last modified:	December 14, 2011
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program