Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q5BG98 (MCR1_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADH-cytochrome b5 reductase 2

EC=1.6.2.2
Alternative name(s):
Mitochondrial cytochrome b reductase
Gene names
Name:mcr1
ORF Names:AN0432
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeEmericella

Protein attributes

Sequence length322 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 322322NADH-cytochrome b5 reductase 2
PRO_0000330181

Regions

Transmembrane30 – 4617Helical; Potential
Domain71 – 176106FAD-binding FR-type
Nucleotide binding179 – 21436FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5BG98 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: BF4D6CFE70E121E5

FASTA32236,073
        10         20         30         40         50         60 
MFSRYAFRCA QPLRQSARQY STEAPKSKSL APVYVAVGLA GLGVGLYRYQ SGAATAEAPA 

        70         80         90        100        110        120 
ERPKVFTGGD QGWVNLKLSD IEILSHNTKR LRFEFPDKEA VSGLHIASAL LTKYSPPDGS 

       130        140        150        160        170        180 
KPVIRPYTPT SDEDQPGYLE LVVKRYPNGP MSEHLHNMNV DQRLDFKGPL PKYPWEANKH 

       190        200        210        220        230        240 
KHICLVAGGT GITPMYQLAR EIFKNPEDKT KVTLVFGNVS EEDILLKREF EDLENTYPQR 

       250        260        270        280        290        300 
FRAFYVLDNP PEGWTGGKGY ITKELLKTVL PEPKEENIKI FVCGPPGMYK AISGPKVSPK 

       310        320 
DQGELTGILK ELGYSKDQVY KF 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed: 19146970] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACD01000007 Genomic DNA. Translation: EAA66531.1.
BN001308 Genomic DNA. Translation: CBF89495.1.
RefSeqXP_658036.1. XM_652944.1.

3D structure databases

HSSPHSSP built from PDB template 1QX4 based on UniProtKB P20070.
ProteinModelPortalQ5BG98.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00002263; CADANIAP00002263; CADANIAG00002263.
GeneID2876210.
KEGGani:AN0432.2.

Phylogenomic databases

OMARYSPNMK.
OrthoDBEOG4FFH9V.
PhylomeDBQ5BG98.

Family and domain databases

InterProIPR017927. 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]
KOK00326.
PfamPF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00406. CYTB5RDTASE.
PR00371. FPNCR.
SUPFAMSSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMCR1_EMENI
AccessionPrimary (citable) accession number: Q5BG98
Secondary accession number(s): C8VTF0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 26, 2005
Last modified: January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families