Reviewed, UniProtKB/Swiss-Prot Q2UKB8 (MCR1_ASPOR)

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:	AO090003000873

Organism

Aspergillus oryzae [Complete proteome]

Taxonomic identifier

5062 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	323 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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
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
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 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 – 323	323	NADH-cytochrome b5 reductase 2		PRO_0000330173
Regions
	Transmembrane	30 – 46	17	Potential
	Domain	72 – 177	106	FAD-binding FR-type
	Nucleotide binding	180 – 215	36	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2UKB8-1 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: 35E61ADC5100DB2C	FASTA	323	36,322
	10 20 30 40 50 60 MFARQTFRCA QPLRQSFRKY STEAPKAKSL APIYTAVGLT GLSVGLYRYY YGAGATAEAP 70 80 90 100 110 120 VERAKVFTGG DQGWVDLKLS EIEVLSHNTK RLRFEFEDKE AVSGVTIASA LLTKFKPVGA 130 140 150 160 170 180 EKAVLRPYTP TSDEDQPGYL DLVVKVYPNG PMSEHLHSMN VDQRLSFKGP LPKYQWETNK 190 200 210 220 230 240 HEHIALIAGG TGITPMYQLI RQIFKNPDDK TKVTLVYGNV TEDDILLKKE LQDLENTYPQ 250 260 270 280 290 300 RFKAFYLLDK PPKEWTGGKG YINKELLKTV LPEPKEENQK IFVCGPPGLY NAVSGNKVSP 310 320 KDQGELSGIL KELGYNKDQV YKF

References

[1]

"Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H. Nature 438:1157-1161(2005) [PubMed: 16372010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AP007155 Genomic DNA. Translation: BAE57997.1.
RefSeq	XP_001819999.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5991982.
KEGG	aor:AO090003000873.
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

MCR1_ASPOR

Accession

Primary (citable) accession number: Q2UKB8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	January 24, 2006
Last modified:	June 16, 2009
This is version 24 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)