NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-29.
STRAIN=ATCC 9480 / CBS 307.48 / NRRL 1951 / GB8 / QM 941;
PubMed=8106340 [NCBI, ExPASy, EBI, Israel, Japan]
Cohen G., Argaman A., Schreiber R., Mislovati M., Aharonowitz Y.;
"The thioredoxin system of Penicillium chrysogenum and its possible role in penicillin biosynthesis.";
J. Bacteriol. 176:973-984(1994).

Comments

FUNCTION: Component of the thioredoxin-thioredoxin reductase system which may be involved in biosynthesis of penicillins and cephalosporins and may be important in determining the thiol-disulfide redox balance.
CATALYTIC ACTIVITY: Thioredoxin + NADP⁺ = thioredoxin disulfide + NADPH.
COFACTOR: Binds 1 FAD per subunit (By similarity).
SUBUNIT: Homodimer.
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

X76119; CAA53725.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B49888; B49888.

3D structure databases

HSSP

Q39243; 1VDC. [HSSP ENTRY / PDB]

ModBase

P43496.

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

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

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.

ProtoNet

P43496.

Other

UniRef

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

Keywords

Direct protein sequencing; FAD; Flavoprotein; NADP; Oxidoreductase; Redox-active center.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 334`	`333`	`Thioredoxin reductase.`	`PRO_0000166765`
`NP_BIND`	`33 45`	`13`	`FAD (By similarity).`
`NP_BIND`	`294 303`	`10`	`FAD (By similarity).`
`COMPBIAS`	`47 50`	`4`	`Poly-Thr.`
`DISULFID`	`145 148`		`Redox-active (By similarity).`

Sequence information

Length: 334 AA [This is the length of the unprocessed precursor]

Molecular weight: 35701 Da [This is the MW of the unprocessed precursor]

CRC64: 7A3A7457D7486341 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVHSKVVIIG SGAGAHTAAI YLSRAELQPV LYEGMLANGT AAGGQLTTTT DVENFPGFPS 

        70         80         90        100        110        120 
GIGGAELMDN MRAQSERFGT EIITETISKL DLSSRPFKMW TEWNDDEGSE PVRTADAVII 

       130        140        150        160        170        180 
ATGANARRLN LPGEETYWQN GISACAVCDG AVPIFRNKPL YVIGGGDSAA EEAMFLAKYG 

       190        200        210        220        230        240 
SSVTVLVRKD KLRASNIMAD RLLAHPKCKV RFNTVATEVI GENKPNGLMT HLRVKDVLSN 

       250        260        270        280        290        300 
AEEVVEANGL FYAVGHDPAS GLVKGQVELD DEGYIITKPG TSFTNVEGVF ACGDVQDKRY 

       310        320        330 
RQAITSAGSG CVAALEAEKF IAETETHQEA KPVL

P43496 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