GCS22_MYCS2
ID GCS22_MYCS2 Reviewed; 396 AA.
AC A0QXJ6; I7GB00;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=MSMEG_3326, MSMEI_3241;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFP39704.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK70098.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP39704.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_003894734.1; NZ_SIJM01000015.1.
DR RefSeq; YP_887634.1; NC_008596.1.
DR AlphaFoldDB; A0QXJ6; -.
DR SMR; A0QXJ6; -.
DR STRING; 246196.MSMEI_3241; -.
DR PRIDE; A0QXJ6; -.
DR EnsemblBacteria; ABK70098; ABK70098; MSMEG_3326.
DR EnsemblBacteria; AFP39704; AFP39704; MSMEI_3241.
DR GeneID; 66734720; -.
DR KEGG; msg:MSMEI_3241; -.
DR KEGG; msm:MSMEG_3326; -.
DR PATRIC; fig|246196.19.peg.3284; -.
DR eggNOG; COG2170; Bacteria.
DR OMA; LWQRWPT; -.
DR OrthoDB; 517836at2; -.
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 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..396
FT /note="Putative glutamate--cysteine ligase 2-2"
FT /id="PRO_0000323506"
SQ SEQUENCE 396 AA; 42680 MW; ACE4E634527705D5 CRC64;
MRECRSQEAS GQLTFAKTPR TVGIEEEFHL VDLTTRRLAT RAPELLPLLP DGYVAELQSC
VVETNGSVVS TLPELRADLT ARRRVLVDTA ATLGLGVVAA GAVPLSVPSE MRVTQTSRYQ
QMLADYQLLA REQLICGTQI HVGIDDPDES VLVAGRVAAY VPTLLALSAS SPFWSDGSDT
GYSSVRTLVW QRWPTTGLAP PATSAAEYDA LISDLIATGV ITDAGMSYFD VRPALRTPTL
ELRVCDSCPR ADTIVLIAAL FRALVEREIE GLRAGVPAAI VVPPLGRAAL WRAARSGLEG
DLVDLIHPAS RPAGDVVTDL VQMLRPQLEA SRDWQTVEEL ARRALAEGSS AARQRRAMRM
RNSLLDVVDH LIAETADVAT VANDALPTQR NGSDRG
