Reviewed, UniProtKB/Swiss-Prot O74557 (NCB5R_SCHPO)

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
ORF Names:	SPCC970.03

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	301 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

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; Multi-pass membrane protein Potential. Mitochondrion outer membrane; Multi-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 vesicle-mediated transport Inferred by curator. Source: GeneDB_SPombe
Cellular component	endoplasmic reticulum membrane Inferred by curator. Source: GeneDB_SPombe 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 – 301	301	NADH-cytochrome b5 reductase 1		PRO_0000310844
Regions
	Transmembrane	8 – 28	21	Potential
	Transmembrane	32 – 49	18	Potential
	Domain	59 – 162	104	FAD-binding FR-type
	Nucleotide binding	142 – 157	16	FAD By similarity
	Nucleotide binding	168 – 199	32	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	O74557-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 455412A9AB47AA6B	FASTA	301	33,723
	10 20 30 40 50 60 MAKQTLLSTP LHGVYIPVFL IIFGTYIVKR EWVGYAIVVA FSLGFHKFWR GRVRKVLSDK 70 80 90 100 110 120 IQQFELSDKA VLNHNTAIYR FRLPRANDVL GLPIGQHLKV FVDVDGKEYS RSYTPLSSDA 130 140 150 160 170 180 DKGYFDLLVK SYPNGKVSKK FSELKIGDTI GVRGPKGNWK HRTGLARHFG MIAGGTGITP 190 200 210 220 230 240 MLQIIRAVLS NFEDPTEITL LYANVSEGDI VLRDEIDALA KKDPRFTVHY VLNNPPENWK 250 260 270 280 290 300 GSVGFVTQEL IKAHFPAPSP ETKVLICGPT PMVNSLREAT VALGYEKSRA ISKLEDQVFV F

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

[2]

"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329672 Genomic DNA. Translation: CAA20696.1.
PIR	T41677.
RefSeq	NP_587852.1.
3D structure databases
HSSP	HSSP built from PDB template 1I7P based on UniProtKB P20070.
ModBase	Search...
Protein-protein interaction databases
STRING	O74557.
Genome annotation databases
GeneID	2539526.
GenomeReviews	Gene locus cbr1 in contig CU329672_GR.
KEGG	spo:SPCC970.03.
NMPDR	fig|4896.1.peg.190.
Organism-specific databases
GeneDB_Spombe	SPCC970.03.
Phylogenomic databases
OMA	ARFKFAL.
Enzyme and pathway databases
BRENDA	1.6.2.2. 653.
Gene expression databases
ArrayExpress	O74557.
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_SCHPO

Accession

Primary (citable) accession number: O74557

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	November 1, 1998
Last modified:	November 3, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)