ID A0A1N7DQL5_9EURY Unreviewed; 362 AA.
AC A0A1N7DQL5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Glutamate--cysteine ligase {ECO:0000256|HAMAP-Rule:MF_01609};
DE EC=6.3.2.2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE AltName: Full=Gamma-glutamylcysteine synthetase {ECO:0000256|HAMAP-Rule:MF_01609};
DE Short=GCS {ECO:0000256|HAMAP-Rule:MF_01609};
DE Short=Gamma-GCS {ECO:0000256|HAMAP-Rule:MF_01609};
GN Name=gshA {ECO:0000256|HAMAP-Rule:MF_01609};
GN ORFNames=BB347_05480 {ECO:0000313|EMBL:APX96114.1}, SAMN05421809_2178
GN {ECO:0000313|EMBL:SIR78137.1};
OS Natronorubrum daqingense.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronorubrum.
OX NCBI_TaxID=588898 {ECO:0000313|EMBL:SIR78137.1, ECO:0000313|Proteomes:UP000185687};
RN [1] {ECO:0000313|EMBL:APX96114.1, ECO:0000313|Proteomes:UP000187321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JX313 {ECO:0000313|EMBL:APX96114.1,
RC ECO:0000313|Proteomes:UP000187321};
RA Shuang W.;
RT "Complete genome sequence of Haloterrigena daqingensis type strain
RT (JX313T).";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SIR78137.1, ECO:0000313|Proteomes:UP000185687}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8909 {ECO:0000313|EMBL:SIR78137.1,
RC ECO:0000313|Proteomes:UP000185687};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of gamma-glutamylcysteine (gamma-GC),
CC the main low-molecular-weight thiol compound instead of glutathione in
CC halophilic archaea. {ECO:0000256|HAMAP-Rule:MF_01609}.
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|HAMAP-Rule:MF_01609};
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family.
CC YbdK subfamily. {ECO:0000256|HAMAP-Rule:MF_01609}.
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DR EMBL; CP019327; APX96114.1; -; Genomic_DNA.
DR EMBL; FTNP01000003; SIR78137.1; -; Genomic_DNA.
DR RefSeq; WP_076581850.1; NZ_FTNP01000003.1.
DR AlphaFoldDB; A0A1N7DQL5; -.
DR STRING; 588898.BB347_05480; -.
DR GeneID; 30955373; -.
DR KEGG; hda:BB347_05480; -.
DR OrthoDB; 287652at2157; -.
DR Proteomes; UP000185687; Unassembled WGS sequence.
DR Proteomes; UP000187321; 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:0042398; P:cellular modified amino acid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.590.20; -; 1.
DR HAMAP; MF_01609; Glu_cys_ligase_2; 1.
DR InterPro; IPR006336; GCS2.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR011793; YbdK.
DR NCBIfam; TIGR02050; gshA_cyan_rel; 1.
DR PANTHER; PTHR36510; GLUTAMATE--CYSTEINE LIGASE 2-RELATED; 1.
DR PANTHER; PTHR36510:SF1; GLUTAMATE--CYSTEINE LIGASE 2-RELATED; 1.
DR Pfam; PF04107; GCS2; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_01609, ECO:0000313|EMBL:SIR78137.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000185687}.
SQ SEQUENCE 362 AA; 41442 MW; B0589466FD1E2C31 CRC64;
MERGSRESFT RMGTLGIEEE CFVVDDDGRP TSGTDELVYE HDPPEILDDR LDHELFKFVI
ETQTPLIEEP SDARESLLEI RRALVDHANE HGFQIAAAGL HPLAKWRELE HAEKPRYQSQ
LDRIQYPQHR NTTAGVHVHV GVDDADKAVW IANELRWYVP IMLALSANSP YWNGFDTGLQ
SARAKIFEAL PNTGMPTYFE DYEAFDQFER RMLETNAIED RGELWYDVRP HTAHGTVELR
TPDGQADPDI VMAFVEYAHA LVEALAAEYE DGAPGYGREH RRELLDENKW RAIRHGQDAS
FITRDLEGTV DLGEVVDREC ERLGIEGIKR VYERESGAER QRRLREEDGP DALCQSLLLG
TE
//
