ID   GCS22_ARTS2             Reviewed;         408 AA.
AC   A0K1R7;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Putative glutamate--cysteine ligase 2-2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE   AltName: Full=Gamma-glutamylcysteine synthetase 2-2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=GCS 2-2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=Gamma-GCS 2-2 {ECO:0000255|HAMAP-Rule:MF_01609};
GN   OrderedLocusNames=Arth_3862;
OS   Arthrobacter sp. (strain FB24).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=290399;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB24;
RX   PubMed=24501649; DOI=10.4056/sigs.4438185;
RA   Nakatsu C.H., Barabote R., Thompson S., Bruce D., Detter C., Brettin T.,
RA   Han C., Beasley F., Chen W., Konopka A., Xie G.;
RT   "Complete genome sequence of Arthrobacter sp. strain FB24.";
RL   Stand. Genomic Sci. 9:106-116(2013).
CC   -!- FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits weak
CC       glutamate--cysteine ligase activity. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01609};
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family.
CC       YbdK subfamily. {ECO:0000255|HAMAP-Rule:MF_01609}.
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DR   EMBL; CP000454; ABK05237.1; -; Genomic_DNA.
DR   RefSeq; WP_011693685.1; NC_008541.1.
DR   AlphaFoldDB; A0K1R7; -.
DR   SMR; A0K1R7; -.
DR   STRING; 290399.Arth_3862; -.
DR   EnsemblBacteria; ABK05237; ABK05237; Arth_3862.
DR   KEGG; art:Arth_3862; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_0_0_11; -.
DR   OMA; MLYWYAR; -.
DR   OrthoDB; 991285at2; -.
DR   Proteomes; UP000000754; Chromosome.
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   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   Pfam; PF04107; GCS2; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   TIGRFAMs; TIGR02050; gshA_cyan_rel; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..408
FT                   /note="Putative glutamate--cysteine ligase 2-2"
FT                   /id="PRO_0000291485"
FT   REGION          37..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   408 AA;  44724 MW;  A18A4D727D813861 CRC64;
     MRTFGVEEEL LIVDPVTGEP LALADALLTG RKLAADDAPD KPRILDPHDP TRDDGDTGLT
     AELKLEQIET QTRPCLNYEE LLLQIRQGRA LADTAAEKHN ARVAALATSP IASTTHTTPN
     PRYATMQERF GLTVHEQLTC GFHVHTFVES PEEGVAVIDR LRDKLAVLTA LSANSPYWNG
     VETGFESYRT QAWNRWPTSG PSQIFGTHSM YRRVVTRLLD SGVLLDEGMI YFDARLSRNH
     PTVEVRVADV CLQAEDAALI AVLVRALVES ASREWRAGVD PAPVPTVLLR MAAWQASNCG
     LRGDLLDFGT FRPAPAEEVV EALVDYVAPV LAEQDELELA WEGVRRILDR GTGSEQQRLA
     MQECLAGNPE AAAGLAAVVA HAVDVSMRRT EAVTAREKAP VLLRVRQS