NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CNRZ 368;
DOI=10.1016/0923-2508(96)80283-X; PubMed=8525054 [NCBI, ExPASy, EBI, Israel, Japan]
Pebay M., Holl A.-C., Simonet J.-M., Decaris B.;
"Characterization of the gor gene of the lactic acid bacterium Streptococcus thermophilus CNRZ368.";
Res. Microbiol. 146:371-383(1995).

Comments

FUNCTION: Maintains high levels of reduced glutathione in the cytosol (By similarity).
CATALYTIC ACTIVITY: 2 glutathione + NADP⁺ = glutathione disulfide + NADPH.
COFACTOR: Binds 1 FAD per subunit (By similarity).
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm.
MISCELLANEOUS: The active site is a redox-active disulfide bond.
SIMILARITY: Belongs to the class-I 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

L27672; AAB00353.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z29494; CAA82630.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S41386; S41386.

3D structure databases

HSSP

P00390; 1ALG. [HSSP ENTRY / PDB]

ModBase

Q60151.

Family and domain databases

InterPro

IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR006322; Glut_reduct_1.
IPR000815; Hg_reductase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR012999; Pyr_OxRdtase_I_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.390.30; Pyr_redox_dim; 1.

Pfam

PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.

PRINTS

PR00368; FADPNR.
PR00945; HGRDTASE.
PR00411; PNDRDTASEI.

ProDom

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

TIGRFAMs

TIGR01421; gluta_reduc_1; 1.

PROSITE

PS00076; PYRIDINE_REDOX_1; 1.

Other

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 450`	`450`	`Glutathione reductase.`	`PRO_0000067979`
`NP_BIND`	`34 42`	`9`	`FAD (By similarity).`
`ACT_SITE`	`439 439`		`Proton acceptor (By similarity).`
`DISULFID`	`42 47`		`Redox-active (By similarity).`

Sequence information

Length: 450 AA [This is the length of the unprocessed precursor]

Molecular weight: 48712 Da [This is the MW of the unprocessed precursor]

CRC64: 6A0DA46BEA828804 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVKEYDYIVI GGGSGGIASA NRAAMHGAKV ILFEGKEVGG TCVNVGCVPK KVMWYGAQVA 

        70         80         90        100        110        120 
ETLHRYAGEY GFDVTINNFD FATLKANRQA YIDRIHGSFE RGFDSNGVER VYEYARFVDP 

       130        140        150        160        170        180 
HTVEVAGELY TAPHILIATG GHPLYPNIPG SEYGITSDGF FELDEVPKRT AVIGAGYIAV 

       190        200        210        220        230        240 
EVAGVLNALG SDTHLFVRKD RPLRTFDKDI IDVLVDEMAK SGPTLHMHAN ATEVVKNADD 

       250        260        270        280        290        300 
SLTISFDNEE TITVDCLIWA VGRAANTSGF GLEKTGVELT ERGNIYSDEF ENTSVPGIYA 

       310        320        330        340        350        360 
LGDVTGKLDL TPVAVKAGRQ LSERLFNNKV DAKLDYTDVA TVVFSHPAIG AIGLTEEKAI 

       370        380        390        400        410        420 
AKYGAENIKV YKSSFTPMYT ALGDNRQLST MKLVTLGEDE KIIGLHGIGY GVDEMIQGFS 

       430        440        450 
VAIKMGATKA DFDNTVAIHP TGSEEFVTMR

Q60151 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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