NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 58785 / CBS 6054 / IFO 10063 / NRRL Y-11545;
DOI=10.1038/nbt1290; PubMed=17334359 [NCBI, ExPASy, EBI, Israel, Japan]
Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A., Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S., Passoth V., Richardson P.M.;
"Genome sequence of the lignocellulose-bioconverting and xylose-fermenting yeast Pichia stipitis.";
Nat. Biotechnol. 25:319-326(2007).

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).
SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
SIMILARITY: Contains 1 FAD-binding FR-type domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CP000498; ABN66017.2; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_001384046.2; -.

3D structure databases

ModBase

A3LT66.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005741;	Cellular component: mitochondrial outer membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0004128;	Molecular function: cytochrome-b5 reductase activity (inferred from electronic annotation from EC).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001834; Cyt_B5_reductase.
IPR001709; FPN_cyt_redctse.
IPR008333; OxRdtase_FAD-bd.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.

Pfam

PF00970; FAD_binding_6; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00406; CYTB5RDTASE.
PR00371; FPNCR.

PROSITE

PS51384; FAD_FR; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

A3LT66.

Genome annotation databases

GeneID

4838868; -.

KEGG

pic:PICST_44816; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane; NAD; Oxidoreductase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 298`	`298`	`NADH-cytochrome b5 reductase 2.`	`PRO_0000330189`
`TRANSMEM`	`15 38`	`24`	`Potential.`
`DOMAIN`	`49 153`	`105`	`FAD-binding FR-type.`
`NP_BIND`	`156 191`	`36`	`FAD (By similarity).`

Sequence information

Length: 298 AA [This is the length of the unprocessed precursor]

Molecular weight: 32581 Da [This is the MW of the unprocessed precursor]

CRC64: 2CD1C2AB00F2FD44 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSFSRSFSRL ASSKFVLPVA AAAVGLASYS FTSSSFIANE PSKAFKGGDE WIDLKLISSH 

        70         80         90        100        110        120 
DLSHDTKHLV FELPNKDDVS GLVTASLLMT KFVTPKGSNV IRPYTPVSDT EQAGTIDFVV 

       130        140        150        160        170        180 
KKYEGGKMSS HIHDLKPNDT LSFKGPFVKW KWEPNQFKSI ALIGGGTGIT PLYQLIHEIT 

       190        200        210        220        230        240 
KNPADKTQVS LFYGSQTPDD ILIKKELDAL AAKHKDQVKI VYFVDKADAS WKGETGYISK 

       250        260        270        280        290 
EFLQKNLPAP GPDNKIFVCG PPPLYKAVSG PKVSPTDQGE LTGSLAELGF SKENVFKF

A3LT66 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools