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Q5AZB4 (NCB5R_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
NADH-cytochrome b5 reductase 1
EC=1.6.2.2
Alternative name(s):
Microsomal cytochrome b reductase
Gene names
Name:cbr1
ORF Names:AN6366
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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; Single-pass membrane protein By similarity. 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 caution

The sequence EAA58750.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 310310NADH-cytochrome b5 reductase 1
PRO_0000330153

Regions

Transmembrane30 – 5021Helical; Potential
Domain61 – 166106FAD-binding FR-type
Nucleotide binding146 – 16015FAD By similarity
Nucleotide binding172 – 20938FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5AZB4 [UniParc].

Last modified November 16, 2011. Version 2.
Checksum: 7C6F0C17CB921D61

FASTA31033,823
        10         20         30         40         50         60 
MSALSLENIT GVYAPSALLV VGTFILKKEW VPFAVALAAG FVAWKLSVGG SSKPRKVLNP 

        70         80         90        100        110        120 
NEFQNFVLKE KNDISHNVTI YRFALPRPTD ILGLPIGQHI SLAATIEGQP KEVVRSYTPI 

       130        140        150        160        170        180 
SSDNEAGYFD LLVKAYPQGN ISKYLTTLKV GDTMKVRGPK GAMVYTPNMC RHIGMIAGGT 

       190        200        210        220        230        240 
GITPMLQIIK AIIRNRPRNG GNDTTQVDLI FANVNPDDIL LKDELEKLAA EDDGFRIYYV 

       250        260        270        280        290        300 
LNNPPEGWTG GVGFVTPDMI KERLPAPASD IKILLCGPPP MVSAMKKATE SLGYTKARPV 

       310 
SKLEDQVFCF

« 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		AACD01000107 Genomic DNA. Translation: EAA58750.1. Sequence problems.
BN001301 Genomic DNA. Translation: CBF69615.1.
RefSeqXP_663970.1. XM_658878.1.

3D structure databases

HSSPHSSP built from PDB template 1QX4 based on UniProtKB P20070.
ProteinModelPortalQ5AZB4.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2871257.
KEGGani:AN6366.2.

Phylogenomic databases

OrthoDBEOG4FFH9R.
PhylomeDBQ5AZB4.

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 nameNCB5R_EMENI
AccessionPrimary (citable) accession number: Q5AZB4
Secondary accession number(s): C8V0X3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: November 16, 2011
Last modified: January 25, 2012
This is version 48 of the entry and version 2 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents