Q6FLT3 (NCB5R_CANGA) 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:	CAGL0L00847g

Organism

Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

284593 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length	285 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 – 285	285	NADH-cytochrome b5 reductase 1		PRO_0000330149
Regions
	Transmembrane	7 – 23	17	Helical; Potential
	Domain	40 – 144	105	FAD-binding FR-type
	Nucleotide binding	124 – 139	16	FAD By similarity
	Nucleotide binding	150 – 182	33	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FLT3 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 9F4507541EE084BC	FASTA	285	31,937
	10 20 30 40 50 60 MDGIKILATF SVLVLFYKLF TYSKKGGVSQ KEAVKALLKT EFREFELVEK EQLTHNTAKY 70 80 90 100 110 120 KFKLADESHV LGLPIGQHIT VKTIIGGKPV SRSYTPTSLD EECVGFFELL VKSYPEGNIS 130 140 150 160 170 180 KHIGDMKIGE KINISGPRGF YEYVPNVHKH LAMVAGGTGI TPMFQIMKAI ARDPSDKTRV 190 200 210 220 230 240 TLLYGNVLEE DILLKQELDD LVKQRPDQFK ITYLLDKPER DDWEGGVGYV TLDLMKESFP 250 260 270 280 SAEEDVQLLV CGPPGMVSSV KRNAVALGFP RAKPVSKMED RVFVF

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 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR380958 Genomic DNA. Translation: CAG61781.1.
RefSeq	XP_448811.1. XM_448811.1.
3D structure databases
HSSP	HSSP built from PDB template 1QX4 based on UniProtKB P20070.
ProteinModelPortal	Q6FLT3.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2890933.
GenomeReviews	Gene locus CAGL0L00847g in contig CR380958_GR.
KEGG	cgr:CAGL0L00847g.
Phylogenomic databases
eggNOG	fuNOG05226.
HOGENOM	HBG591994.
OMA	VRHFGMI.
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_CANGA

Accession

Primary (citable) accession number: Q6FLT3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	July 19, 2004
Last modified:	December 14, 2011
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program