GSH1_JANMA
ID GSH1_JANMA Reviewed; 528 AA.
AC A6SX59;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Glutamate--cysteine ligase {ECO:0000255|HAMAP-Rule:MF_00578};
DE EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_00578};
DE AltName: Full=Gamma-ECS {ECO:0000255|HAMAP-Rule:MF_00578};
DE Short=GCS {ECO:0000255|HAMAP-Rule:MF_00578};
DE AltName: Full=Gamma-glutamylcysteine synthetase {ECO:0000255|HAMAP-Rule:MF_00578};
GN Name=gshA {ECO:0000255|HAMAP-Rule:MF_00578}; OrderedLocusNames=mma_1166;
OS Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=375286;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marseille;
RX PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA Drancourt M.;
RT "Genome analysis of Minibacterium massiliensis highlights the convergent
RT evolution of water-living bacteria.";
RL PLoS Genet. 3:1454-1463(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-
CC cysteine + H(+) + phosphate; Xref=Rhea:RHEA:13285, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00578};
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 1/2. {ECO:0000255|HAMAP-
CC Rule:MF_00578}.
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 1 family.
CC Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00578}.
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DR EMBL; CP000269; ABR88957.1; -; Genomic_DNA.
DR RefSeq; WP_012079023.1; NC_009659.1.
DR AlphaFoldDB; A6SX59; -.
DR SMR; A6SX59; -.
DR STRING; 375286.mma_1166; -.
DR PRIDE; A6SX59; -.
DR EnsemblBacteria; ABR88957; ABR88957; mma_1166.
DR KEGG; mms:mma_1166; -.
DR eggNOG; COG2918; Bacteria.
DR HOGENOM; CLU_020728_3_0_4; -.
DR OMA; RYSWLLM; -.
DR OrthoDB; 967793at2; -.
DR BioCyc; JSP375286:MMA_RS06075-MON; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000006388; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00578; Glu_cys_ligase; 1.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR007370; Glu_cys_ligase.
DR InterPro; IPR006334; Glut_cys_ligase.
DR PANTHER; PTHR38761; PTHR38761; 1.
DR Pfam; PF04262; Glu_cys_ligase; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR TIGRFAMs; TIGR01434; glu_cys_ligase; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glutathione biosynthesis; Ligase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..528
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_1000025174"
SQ SEQUENCE 528 AA; 60186 MW; 8177B1FB8370D386 CRC64;
MSNLFTRRLA LLADDAHRDL LNQGRRGIER ETLRVDLQGK LALGPHPVAL GSALTNPQIT
TDYSESLLEF ITPAEHDVAT ALEELDRIHR FANAKLDHEL LWSQSMPCTL PEEADIPIAW
YGTSHIGMIK HVYRRGLALR YGKAMQCIAG LHYNYSLSED LWRVIKQSEQ SRLDDKSYQS
ESYISLIRNF QRYSWLLMYL FGASPALSTH FLRGREHELQ TLSDDTLYLP YATSLRMSDL
GYQNNAQAGL MPPYNDLESY MRSLSRAVRQ AYPAYEAIGT RRNGEWIQLN TNLLQIENEY
YATIRPKRVI NSGERPVEAL CARGVQYIEV RCMDIDPFEP LGISLPTSRF LDAFLLFCAL
DDSPLTDEAN NRERTENFAR TVKEGRRPGL LLQRDGAAVK LQDWGLELLE RIQATADLLD
AQRADSQHAQ ALAAQKEKLL DAGLTPSARV LAELQATDKS FEQFGLRQSI AHAEYFRARP
LNAEENFYFE TLAKTSIAEQ EEMERTQSGD FDAFVEAYNQ RTPQQLCD
