ID A0A0W8IL17_9MICC Unreviewed; 387 AA.
AC A0A0W8IL17;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Putative glutamate--cysteine ligase 2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE EC=6.3.2.2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE AltName: Full=Gamma-glutamylcysteine synthetase 2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE Short=GCS 2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE Short=Gamma-GCS 2 {ECO:0000256|HAMAP-Rule:MF_01609};
GN ORFNames=AVL63_09125 {ECO:0000313|EMBL:KUG60515.1};
OS Nesterenkonia jeotgali.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Nesterenkonia.
OX NCBI_TaxID=317018 {ECO:0000313|EMBL:KUG60515.1, ECO:0000313|Proteomes:UP000054023};
RN [1] {ECO:0000313|Proteomes:UP000054023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD08_7 {ECO:0000313|Proteomes:UP000054023};
RA Nair G.R., Kaur G., Mayilraj S.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits weak
CC glutamate--cysteine ligase activity. {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|ARBA:ARBA00029283, ECO:0000256|HAMAP-
CC Rule:MF_01609};
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family.
CC YbdK subfamily. {ECO:0000256|HAMAP-Rule:MF_01609}.
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:KUG60515.1}.
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DR EMBL; LQBM01000001; KUG60515.1; -; Genomic_DNA.
DR RefSeq; WP_058887498.1; NZ_LQBM01000001.1.
DR AlphaFoldDB; A0A0W8IL17; -.
DR STRING; 317018.AVL63_09125; -.
DR OrthoDB; 9769628at2; -.
DR Proteomes; UP000054023; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-EC.
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:KUG60515.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000054023}.
SQ SEQUENCE 387 AA; 43425 MW; B765D18240C43CB0 CRC64;
MELPFAESRR STLGLEWELA LVDRQTGDLR SVADRVLRAC HQDLPELCSE DEHPYVKQEL
LTNTVELVTD VCPDVNTGVD QLRETARNVM RHCEPLDVEL YCQGSHPFAA PTAQEVTDKE
RYAELIRRTQ WWGRQMVIYG VHVHVGLDDV AQAMPAVNAL CNYNAHFQAL TASSPYWSGE
DTGYASQRAL VFQQLPTAGA SFQFEEWSGY EKAVSDLEYT GVINDVTEVR WDVRAVPRLG
TVELRVCDGL ATLEEIAGVA ALTQCIVHST VKDLENGGKV VSMPPWFVQE NKWRAARYGL
DAEIILNAEG DEMLVTDHLQ QELNRLEPVA KELGCADELA LVEQMMRDGA GYMRQRQVAE
THQGDLRQVV LDAAARTRMS INGPRRV
//
