ID GCS23_MYCS2 Reviewed; 365 AA.
AC A0R3T8; I7GEI1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Putative glutamate--cysteine ligase 2-3 {ECO:0000255|HAMAP-Rule:MF_01609};
DE EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE AltName: Full=Gamma-glutamylcysteine synthetase 2-3 {ECO:0000255|HAMAP-Rule:MF_01609};
DE Short=GCS 2-3 {ECO:0000255|HAMAP-Rule:MF_01609};
DE Short=Gamma-GCS 2-3 {ECO:0000255|HAMAP-Rule:MF_01609};
GN OrderedLocusNames=MSMEG_5590, MSMEI_5440;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
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; CP000480; ABK73440.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP41881.1; -; Genomic_DNA.
DR RefSeq; WP_011730643.1; NZ_SIJM01000034.1.
DR RefSeq; YP_889826.1; NC_008596.1.
DR AlphaFoldDB; A0R3T8; -.
DR SMR; A0R3T8; -.
DR STRING; 246196.MSMEG_5590; -.
DR PaxDb; 246196-MSMEI_5440; -.
DR GeneID; 66736888; -.
DR KEGG; msg:MSMEI_5440; -.
DR KEGG; msm:MSMEG_5590; -.
DR PATRIC; fig|246196.19.peg.5451; -.
DR eggNOG; COG2170; Bacteria.
DR OrthoDB; 9803842at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 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; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..365
FT /note="Putative glutamate--cysteine ligase 2-3"
FT /id="PRO_0000323507"
SQ SEQUENCE 365 AA; 39966 MW; 4E4A3BF4FE9C4B97 CRC64;
MSNNPTFGVE EEFLLVDPRT GEPIARNKAV AETAAAKGVD LQLELTSCQV ETATEVMDNS
DDLRKALLRL RRVATDAAET NGARLLAAGL PPTVPHKFPI TPTPRYRRIG HRFGMIAHEQ
GICGCHVHVE VPSRDAAIRV SNRLRPWLHL LLALTANSAI YRGSDSGYAT FRSVLWARWP
SAGPPPFFDS EAQYDATVAM LEDAGAALDD GMIYWDVRPS NKFPTVEVRV SDVPATVAET
VLFATLVRAA VMTATEAEKN GEPVVPLTDY VLKAAYWKSA RDGLDGRTID LAESHAVAPT
VELLTNFVEH LRPALEQLGE YDTVRGELAR VIETGNGAMR QRRAFERRRE AADVIDELAA
ATIAE
//
