Q6CS27 (MCR1_KLULA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NADH-cytochrome b5 reductase 2
EC=1.6.2.2

Alternative name(s):
Mitochondrial cytochrome b reductase

Gene names

Name:	MCR1
Ordered Locus Names:	KLLA0D04488g

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	296 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	May mediate the reduction of outer membrane cytochrome b5 By similarity.
Catalytic activity	NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5.
Cofactor	FAD By similarity.
Subcellular location	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	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	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 – 296	296	NADH-cytochrome b5 reductase 2		PRO_0000330182
Regions
	Transmembrane	12 – 29	18	Helical; Potential
	Domain	47 – 151	105	FAD-binding FR-type
	Nucleotide binding	154 – 189	36	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6CS27 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 75C198B68CD53021	FASTA	296	33,013
	10 20 30 40 50 60 MFARLSRSNK FLPIALGVGA ASIATAIILQ RNYSIMNDTS KAFLGDNEWI DLPIIKIEKL 70 80 90 100 110 120 SHDTKRFTFA LPKKDQVSGL ITASCILAKF VTPKGSNVIR PYTPVSDNGT KGKMELVVKH 130 140 150 160 170 180 YENGKFTSHL FGLKENDTVS FKGPITKWEW KPNSYDSITL LGAGTGINPL YQLVHHIAEN 190 200 210 220 230 240 PEDNTKIHLY YGNKTPEDIL LKSELDNLQK KYPDQVKITY FVDKAEGNFE GETGFITKDY 250 260 270 280 290 LSHQAPKPSE KNQVFVCGPP PFMKAYSGPK VSPQDQGELT GILAELGYSK SNVFKF

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	CR382124 Genomic DNA. Translation: CAH00358.1.
RefSeq	XP_453262.1. XM_453262.1.
3D structure databases
HSSP	HSSP built from PDB template 1QX4 based on UniProtKB P20070.
ProteinModelPortal	Q6CS27.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6CS27.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2893331.
GenomeReviews	Gene locus KLLA0D04488g in contig CR382124_GR.
KEGG	kla:KLLA0D04488g.
Phylogenomic databases
eggNOG	fuNOG07850.
HOGENOM	HBG591994.
OMA	PVASCIT.
OrthoDB	EOG4FFH9V.
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

MCR1_KLULA

Accession

Primary (citable) accession number: Q6CS27

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	August 16, 2004
Last modified:	December 14, 2011
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program