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Database: UniProt
Entry: A0A1Y5RJ79_9RHOB
LinkDB: A0A1Y5RJ79_9RHOB
Original site: A0A1Y5RJ79_9RHOB 
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
//
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