ID A0A087VTB8_9BIFI Unreviewed; 424 AA.
AC A0A087VTB8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Glutamate--cysteine ligase {ECO:0000256|PIRNR:PIRNR017901};
DE EC=6.3.2.2 {ECO:0000256|PIRNR:PIRNR017901};
GN ORFNames=BINDI_0335 {ECO:0000313|EMBL:AIC91617.1};
OS Bifidobacterium indicum LMG 11587 = DSM 20214.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1341694 {ECO:0000313|EMBL:AIC91617.1, ECO:0000313|Proteomes:UP000028569};
RN [1] {ECO:0000313|EMBL:AIC91617.1, ECO:0000313|Proteomes:UP000028569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11587 {ECO:0000313|EMBL:AIC91617.1,
RC ECO:0000313|Proteomes:UP000028569};
RX PubMed=25085493; DOI=10.1128/AEM.02308-14;
RA Milani C., Lugli G.A., Duranti S., Turroni F., Bottacini F., Mangifesta M.,
RA Sanchez B., Viappiani A., Mancabelli L., Taminiau B., Delcenserie V.,
RA Barrangou R., Margolles A., van Sinderen D., Ventura M.;
RT "Genomic encyclopedia of type strains of the genus Bifidobacterium.";
RL Appl. Environ. Microbiol. 80:6290-6302(2014).
CC -!- FUNCTION: Catalyzes the synthesis of gamma-glutamylcysteine (gamma-GC).
CC {ECO:0000256|PIRNR:PIRNR017901}.
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:0000256|ARBA:ARBA00029283,
CC ECO:0000256|PIRNR:PIRNR017901};
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family.
CC EgtA subfamily. {ECO:0000256|PIRNR:PIRNR017901}.
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DR EMBL; CP006018; AIC91617.1; -; Genomic_DNA.
DR RefSeq; WP_033490759.1; NZ_JDUE01000001.1.
DR AlphaFoldDB; A0A087VTB8; -.
DR KEGG; bii:BINDI_0335; -.
DR HOGENOM; CLU_026610_1_1_11; -.
DR OrthoDB; 9780152at2; -.
DR Proteomes; UP000028569; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042398; P:cellular modified amino acid biosynthetic process; IEA:InterPro.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.590.20; -; 1.
DR InterPro; IPR035434; GCL_bact_plant.
DR InterPro; IPR006336; GCS2.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR PANTHER; PTHR34378; GLUTAMATE--CYSTEINE LIGASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR34378:SF1; GLUTAMATE--CYSTEINE LIGASE, CHLOROPLASTIC; 1.
DR Pfam; PF04107; GCS2; 1.
DR PIRSF; PIRSF017901; GCL; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR017901};
KW Ligase {ECO:0000256|PIRNR:PIRNR017901, ECO:0000313|EMBL:AIC91617.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR017901};
KW Reference proteome {ECO:0000313|Proteomes:UP000028569}.
SQ SEQUENCE 424 AA; 47796 MW; 57C7675F2A20757B CRC64;
MRENGRVGYA HLLTVPNPRH VDSLVDYFSR GAKPSSQWRF GVEIEHIPVS NDGSDAPVPY
EGERGIEALL SALEPYYDGD AEYREDGHLV GLSRPGCVVS LEPGSQVECS LGVVRDRQGF
EDLYRRFRAE VDPIAERLGF RLVEYGYRPA GSYADVGVNP KERYAVMNTY LGRIGQCGPM
MMRSTASTQI SIDYRDESDA IAKIRLGTAI GPILAYFFRN TPVFEGSPNR LPLRRQRIWD
WLDPQRTGLT PGLFDDGFGW EDYAVDVLST PLMVADVSRT PEVEGPEGKQ VFIAWHENAG
DIYPDRRLND AEIAHILTTH FNDVRLKNYI ELRHWDSLPM QRAGRLLEIV GGIFYDPDRF
TRLTGFLDGI DEENVLQTKA DLQVRGGQAC PYGRPLDFWR QVLGAEDTMD GLPGDPENTG
RFQD
//
