ID A0A084QVB1_STAC4 Unreviewed; 297 AA.
AC A0A084QVB1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=S40285_04079 {ECO:0000313|EMBL:KFA67896.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA67896.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA67896.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA67896.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
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}.
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DR EMBL; KL660079; KFA67896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084QVB1; -.
DR STRING; 1283841.A0A084QVB1; -.
DR HOGENOM; CLU_055657_0_0_1; -.
DR InParanoid; A0A084QVB1; -.
DR OMA; CTDILPR; -.
DR OrthoDB; 1706825at2759; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000028524; 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:UP000028524}.
FT DOMAIN 80..224
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
FT REGION 31..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 297 AA; 32792 MW; A78B2E5ADFB77ED1 CRC64;
MSAGPSIIRK SGTTRSNLEL VHGLRDNFTA AKQDYSPNSN GDPSGADHAT AARTPPELWT
ERIGDTLFVP RIDWQPAGLR DDADQYEITV KLFLLEGAAL AQREAYVKEA LELVRKELAI
ENIDLLVVSF PGMSFEGNCE WEADKINAQQ GNLEEEVETW KVFENLHRQG LVKRLGVAEF
GSEKLHAFMD RTSVHPTVDQ INLKNCCSVP PPLKKLAADS GIELNVHTDC TDILPRGTLR
ELLGPHGTAL LADTSSSDQG LKGEITPQWV VRYLAFVRDR GVIENKGYFA GAELLDN
//
