ID A7KZX9_HUMLU Unreviewed; 174 AA.
AC A7KZX9;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 22-FEB-2023, entry version 38.
DE SubName: Full=Glutathione-disulfide reductase {ECO:0000313|EMBL:ABS72408.1};
DE Flags: Fragment;
OS Humulus lupulus (European hop).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Humulus.
OX NCBI_TaxID=3486 {ECO:0000313|EMBL:ABS72408.1};
RN [1] {ECO:0000313|EMBL:ABS72408.1}
RP NUCLEOTIDE SEQUENCE.
RA Costa J.C., Fortes A.M., Pais M.S.;
RT "Arginine decarboxylase expression, polyamines biosynthesis and reactive
RT oxygen species during organogenic nodule formation in hop.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABS72408.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18823540; DOI=10.1186/1471-2164-9-445;
RA Fortes A.M., Santos F., Choi Y.H., Silva M.S., Figueiredo A., Sousa L.,
RA Pessoa F., Santos B.A., Sebastiana M., Palme K., Malho R., Verpoorte R.,
RA Pais M.S.;
RT "Organogenic nodule development in hop (Humulus lupulus L.): transcript and
RT metabolic responses.";
RL BMC Genomics 9:445-445(2008).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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DR EMBL; EF633696; ABS72408.1; -; mRNA.
DR AlphaFoldDB; A7KZX9; -.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR046952; GSHR/TRXR-like.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR PANTHER; PTHR42737:SF4; GLUTATHIONE REDUCTASE; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 2: Evidence at transcript level;
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284}.
FT DOMAIN 80..173
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABS72408.1"
FT NON_TER 174
FT /evidence="ECO:0000313|EMBL:ABS72408.1"
SQ SEQUENCE 174 AA; 19084 MW; 08244A86F9025883 CRC64;
TQRADDACVT DKLSCEVDES HVQYLAYGYG DVQIEESTLW LMEGTSLLKL FLVGNLRKAD
YKDIPCAVFS IPPLLLWASV KRKQIEQSDG DILVFTSNFN PMKNTVSGRQ EKTVMKLVVD
AETDKVLGAS MCGPDAAEIM QGIGIALKCG ATKKQFDSTV GIHPSAAEEF VTMR
//
