NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=VF5;
DOI=10.1038/32831; PubMed=9537320 [NCBI, ExPASy, EBI, Israel, Japan]
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
Nature 392:353-358(1998).

Comments

CATALYTIC ACTIVITY: Thioredoxin + NADP⁺ = thioredoxin disulfide + NADPH.
COFACTOR: Binds 1 FAD per subunit (By similarity).
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
MISCELLANEOUS: The active site is a redox-active disulfide bond.
SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.

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

AE000657; AAC06756.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B70345; B70345.

RefSeq

NP_213350.1; -.

3D structure databases

HSSP

P09625; 1TDE. [HSSP ENTRY / PDB]

ModBase

O66790.

Enzyme and pathway databases

BioCyc

AAEO224324:AQ_500-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0004791;	Molecular function: thioredoxin-disulfide reductase activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019430;	Biological process: removal of superoxide radicals (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000759; Adrndx_reductase.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
IPR000103; Pyridine_nuc-diS_OxRdtase_2.
IPR005982; Thioredox_reduct.
Graphical view of domain structure.

Pfam

PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.

PRINTS

PR00419; ADXRDTASE.
PR00368; FADPNR.
PR00469; PNDRDTASEII.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01292; TRX_reduct; 1.

PROSITE

PS00573; PYRIDINE_REDOX_2; 1.

Genome annotation databases

1193208; -.

AE000657_GR; aq_500.

aae:aq_500; -.

fig|224324.1.peg.365; -.

Phylogenomic databases

HOGENOM

O66790; -.

Genome annotation databases

CMR

O66790; aq_500.

Other

ProtoNet

O66790.

UniRef

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

Keywords

Complete proteome; Cytoplasm; FAD; Flavoprotein; NADP; Oxidoreductase; Redox-active center.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 323`	`323`	`Thioredoxin reductase.`	`PRO_0000166718`
`NP_BIND`	`42 49`	`8`	`FAD (By similarity).`
`NP_BIND`	`286 295`	`10`	`FAD (By similarity).`
`DISULFID`	`143 146`		`Redox-active (By similarity).`

Sequence information

Length: 323 AA [This is the length of the unprocessed precursor]

Molecular weight: 35101 Da [This is the MW of the unprocessed precursor]

CRC64: 363FC62EFDD03328 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVSLMQQPD KVYDVIIIGA GPAGTTAAIY TARAGWKTLV LYRAEADGAL GVTQKIENYP 

        70         80         90        100        110        120 
GVPGPLSGYE LLKIMREQAK SFGAEFVRGK VIATDLNSDP KKVYTIDGRE FRGKTIIVAS 

       130        140        150        160        170        180 
GAMERANKFK GEEEFLGRGV SYCGVCDAAF FKDQPVAVIG DDDYAIEEAE FIARFANKVF 

       190        200        210        220        230        240 
FVVPGSKIKA PPEVIEHFEK LPNVEILLRH RPIEIVGDQV VKGIKLKDLE KKEEKLLEVN 

       250        260        270        280        290        300 
GVFIFLGGTK PSVDFLMGQV EMTEGDCIVV NEEMMTSVPG VFAAGDVLCN EVKQAVVAAA 

       310        320 
MGCKAALAVD KFLSGKKKIV PQW

O66790 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