A5E5C5 (MCR1_LODEL) 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
ORF Names:	LELG_04814

Organism

Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) [Complete proteome]

Taxonomic identifier

379508 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Lodderomyces

Protein attributes

Sequence length	300 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 – 300	300	NADH-cytochrome b5 reductase 2		PRO_0000330183
Regions
	Transmembrane	12 – 29	18	Helical; Potential
	Domain	49 – 153	105	FAD-binding FR-type
	Nucleotide binding	156 – 191	36	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5E5C5 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: 360834C12407A8C6	FASTA	300	33,537
	10 20 30 40 50 60 MSVSRLFSNP KFVYPLVGAT IGSIGLAYYS TQAQFYIANE TGKTFTGGDQ WIDLKLKKSE 70 80 90 100 110 120 DLTHNTKHLT FELLNPDDVS GLITASMLMT KYVTPKGNNV IRPYTPVSDP DQKGTLDFVI 130 140 150 160 170 180 KRYENGKMSN HIHNLKEGET LSFKGPVVKW KWEPNQFKSI ALIGGGTGIT PLYQLLREIT 190 200 210 220 230 240 SNPEDKTKVS LIYGNTSPED VLIKDRIDDI AAKHKDQVKV TYFVDENKAT KDWEGEVGFI 250 260 270 280 290 300 TKEFLEKELD KPSPDFKIFV CGPPGLYKAI SGVKVSPTDQ GEVEGALKDL GFSKEHVFKF

References

[1]

"Evolution of pathogenicity and sexual reproduction in eight Candida genomes." Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J. , Harris D., Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W., Kellis M., Cuomo C.A. Nature 459:657-662(2009) [PubMed: 19465905] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH981530 Genomic DNA. Translation: EDK46633.1.
RefSeq	XP_001524001.1. XM_001523951.1.
3D structure databases
ProteinModelPortal	A5E5C5.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5231247.
KEGG	lel:LELG_04814.
Phylogenomic databases
OMA	IKRYENG.
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_LODEL

Accession

Primary (citable) accession number: A5E5C5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	June 12, 2007
Last modified:	November 16, 2011
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program