GCS21_MYCSJ
ID GCS21_MYCSJ Reviewed; 376 AA.
AC A3PTZ8;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Putative glutamate--cysteine ligase 2-1 {ECO:0000255|HAMAP-Rule:MF_01609};
DE EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE AltName: Full=Gamma-glutamylcysteine synthetase 2-1 {ECO:0000255|HAMAP-Rule:MF_01609};
DE Short=GCS 2-1 {ECO:0000255|HAMAP-Rule:MF_01609};
DE Short=Gamma-GCS 2-1 {ECO:0000255|HAMAP-Rule:MF_01609};
GN OrderedLocusNames=Mjls_0563;
OS Mycobacterium sp. (strain JLS).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; unclassified Mycobacterium.
OX NCBI_TaxID=164757;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLS;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J.,
RA Sims R.C., Richardson P.;
RT "Complete sequence of Mycobacterium sp. JLS.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000580; ABN96375.1; -; Genomic_DNA.
DR AlphaFoldDB; A3PTZ8; -.
DR SMR; A3PTZ8; -.
DR STRING; 164757.Mjls_0563; -.
DR KEGG; mjl:Mjls_0563; -.
DR HOGENOM; CLU_044848_1_0_11; -.
DR OMA; LIFGLHV; -.
DR BioCyc; MSP164757:G1G8C-570-MON; -.
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.
FT CHAIN 1..376
FT /note="Putative glutamate--cysteine ligase 2-1"
FT /id="PRO_0000291495"
SQ SEQUENCE 376 AA; 42229 MW; A1606B5B492728FB CRC64;
MLSVPASSRI DFAGSPRPTV GVEWEFALVD AHTRDLSNEA ATVIAEIGET PHVHKELLRN
TVEVVTGICE NTGEAMADLH DTLQVVRRIV RDRGMELFCA GTHPFANWST QQLTDAPRYA
ELIKRTQWWG RQMLIWGVHV HVGISSAHKV MPIISSLLNQ YPHLLALSAS SPYWDGSDTG
YASNRAMMFQ QLPTAGLPFQ FQSWPEFERF VHDQKKTGII DHMNEIRWDI RPSPHLGTVE
IRVFDGVSNI AELGSLVALT HCLVVDLDRR LDAGEQLPVM PPWHVQENKW RAARYGLDAE
IILDADSNER LVTEDLDDLL TRLQPVARSL DCADELAGVA EIYRHGASYQ RQRRVAEEHD
GDLLAVVDAL VAELEL