ID A0A0D2AN08_9EURO Unreviewed; 319 AA.
AC A0A0D2AN08;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=GCS light chain {ECO:0000256|ARBA:ARBA00031732};
DE AltName: Full=Gamma-ECS regulatory subunit {ECO:0000256|ARBA:ARBA00030406};
DE AltName: Full=Gamma-glutamylcysteine synthetase regulatory subunit {ECO:0000256|ARBA:ARBA00032926};
DE AltName: Full=Glutamate--cysteine ligase modifier subunit {ECO:0000256|ARBA:ARBA00031154};
GN ORFNames=PV06_06923 {ECO:0000313|EMBL:KIW41356.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW41356.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW41356.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW41356.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 1/2. {ECO:0000256|ARBA:ARBA00005006}.
CC -!- SUBUNIT: Heterodimer of a catalytic heavy chain and a regulatory light
CC chain. {ECO:0000256|ARBA:ARBA00011532}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family.
CC Glutamate--cysteine ligase light chain subfamily.
CC {ECO:0000256|ARBA:ARBA00008612}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN847337; KIW41356.1; -; Genomic_DNA.
DR RefSeq; XP_016261572.1; XM_016408092.1.
DR AlphaFoldDB; A0A0D2AN08; -.
DR STRING; 215243.A0A0D2AN08; -.
DR GeneID; 27358997; -.
DR VEuPathDB; FungiDB:PV06_06923; -.
DR HOGENOM; CLU_055657_0_0_1; -.
DR OrthoDB; 1706825at2759; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000053342; Unassembled WGS sequence.
DR GO; GO:0035226; F:glutamate-cysteine ligase catalytic subunit binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR InterPro; IPR032963; Gclm.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR13295; GLUTAMATE CYSTEINE LIGASE REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR13295:SF4; GLUTAMATE--CYSTEINE LIGASE REGULATORY SUBUNIT; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
PE 3: Inferred from homology;
KW Glutathione biosynthesis {ECO:0000256|ARBA:ARBA00022684};
KW Reference proteome {ECO:0000313|Proteomes:UP000053342}.
FT DOMAIN 80..232
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
FT REGION 139..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..155
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 319 AA; 35365 MW; DEFAD00FA24905F0 CRC64;
MKLILSTSNI MSSGQSIVRR PLFSKSNIEL INSLRSNFAS FQHHPSASSE NADSTPDYKQ
WTTEEDDTLY VPSWRPTPLK EPRESYDVTV KLFFLPGIPS TRRCKHTREA IDLVLKELDI
ENIDLLIASY PGVTFDADDE EEVSADEDDE SARSDESEGL DAQIKTWQVL ESLHEKGVIS
QLGVSEFSSE RLDKFLPEVK VRPTVDQINV KDCCVVPKPL IVYAKENKIE LLTHADCMDI
LPPGTTRELL GPSKDGAGIL AACPNAGADE PGLKGDIEPQ WVVKYTAVVK NRGVVENKGY
FAVAQLGSCI EEKPDEEGL
//
