ID A0A1Y5RJ79_9RHOB Unreviewed; 375 AA.
AC A0A1Y5RJ79;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 Name=ybdK {ECO:0000313|EMBL:SLN17486.1};
GN ORFNames=ROA7023_00308 {ECO:0000313|EMBL:SLN17486.1};
OS Roseisalinus antarcticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseisalinus.
OX NCBI_TaxID=254357 {ECO:0000313|EMBL:SLN17486.1, ECO:0000313|Proteomes:UP000193900};
RN [1] {ECO:0000313|EMBL:SLN17486.1, ECO:0000313|Proteomes:UP000193900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7023 {ECO:0000313|EMBL:SLN17486.1,
RC ECO:0000313|Proteomes:UP000193900};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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|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; FWFZ01000001; SLN17486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5RJ79; -.
DR OrthoDB; 9769628at2; -.
DR Proteomes; UP000193900; 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:SLN17486.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000193900}.
SQ SEQUENCE 375 AA; 41955 MW; F5E56FBC4CEFAE49 CRC64;
MKSPEFSLGI EEEYLLVDRE TLALHEAPEG LMEACQVVLG EQVSPEFLQC QIEVGTGVCS
TIQQARSDLR NLRSVVSEEA AKFGLAPIAA ACHPLADWKL VHHTDRARYN QLRTDLGGVA
RRMLICGMHV HVGLGEDALR ADLLNQMSYF LPHLLALSTS SPFWQGEDTG LASYRLSVFD
NLPRTGLPPK IDSWEEYQRS VSALVDLGVI EDSSKIWWDL RPSARFPTLE TRICDVCPRL
DHAISLAALV QCIARMLWRL RLRNQRWRRY DNFLIAENRW RAQRYGIGGG LIDFGRGEII
PVPALLEELF ELVAEDAEAL GCMTEILAAR DIVEGGTSSE RQRAVRDAAA TAGGDHAEQM
RTVVSHLIEE FHADL
//