ID A0A2B7ZMZ2_9EURO Unreviewed; 325 AA.
AC A0A2B7ZMZ2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=GX50_02641 {ECO:0000313|EMBL:PGH34558.1};
OS Emmonsia crescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=73230 {ECO:0000313|EMBL:PGH34558.1, ECO:0000313|Proteomes:UP000226031};
RN [1] {ECO:0000313|EMBL:PGH34558.1, ECO:0000313|Proteomes:UP000226031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH4076 {ECO:0000313|EMBL:PGH34558.1,
RC ECO:0000313|Proteomes:UP000226031};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PGH34558.1}.
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DR EMBL; PDND01000038; PGH34558.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7ZMZ2; -.
DR STRING; 73230.A0A2B7ZMZ2; -.
DR VEuPathDB; FungiDB:EMCG_01387; -.
DR OrthoDB; 1706825at2759; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000226031; Unassembled WGS sequence.
DR GO; GO:0035226; F:glutamate-cysteine ligase catalytic subunit binding; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 Ligase {ECO:0000313|EMBL:PGH34558.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000226031}.
FT DOMAIN 83..245
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
FT REGION 141..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 325 AA; 35336 MW; 866B16C45BDB755B CRC64;
MSGGPSVIRR LTSDKSNVEL LNALRTNFVA AQHIEPSHTN GASLDIHDVP QRLSYSDYTT
WTSKQGDTLY VPAIDFSEPG LTEDRDQYDI TVKLFYLPGI PTSRRCAHTR EAIDLVLKEL
HVNSIDLLIV SFPGISFDAD DESEEEISDG DGNGNGNGNG NGNAAQSGGT PEMDGMIQTW
RVLESLKEQG MISQLGLSEF DSERLAKFLP HTKIRPAVDQ INVKDCCVVP RPLIVFAKKE
NIKLLTHNDC TDILPPGTTR DLLARGEKGA GILAASAAAE DGGLKGDIVP QWVVKYTAVV
KDRGVIENKG YFALAEVGNC IRDAE
//
