GCS2_CORJK
ID GCS2_CORJK Reviewed; 392 AA.
AC Q4JXP1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Putative glutamate--cysteine ligase 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 {ECO:0000255|HAMAP-Rule:MF_01609};
DE Short=GCS 2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE Short=Gamma-GCS 2 {ECO:0000255|HAMAP-Rule:MF_01609};
GN OrderedLocusNames=jk0264;
OS Corynebacterium jeikeium (strain K411).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=306537;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K411;
RX PubMed=15968079; DOI=10.1128/jb.187.13.4671-4682.2005;
RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT "Complete genome sequence and analysis of the multiresistant nosocomial
RT pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT human skin flora.";
RL J. Bacteriol. 187:4671-4682(2005).
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; CR931997; CAI36416.1; -; Genomic_DNA.
DR RefSeq; WP_011272981.1; NC_007164.1.
DR AlphaFoldDB; Q4JXP1; -.
DR SMR; Q4JXP1; -.
DR STRING; 306537.jk0264; -.
DR PRIDE; Q4JXP1; -.
DR EnsemblBacteria; CAI36416; CAI36416; jk0264.
DR KEGG; cjk:jk0264; -.
DR PATRIC; fig|306537.10.peg.274; -.
DR eggNOG; COG2170; Bacteria.
DR HOGENOM; CLU_044848_1_1_11; -.
DR OMA; LIFGLHV; -.
DR OrthoDB; 991285at2; -.
DR Proteomes; UP000000545; 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..392
FT /note="Putative glutamate--cysteine ligase 2"
FT /id="PRO_0000255798"
FT REGION 347..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 392 AA; 43904 MW; 748A67C776412DD6 CRC64;
MDFPGSAPSV GIEWEVALVD PETRDLVPRA AELIARMDEV HPGHKVVREF LANTVEMVSG
VHDTIPEAVE DLHVQAKQLM ECADDIGVNL FSAGTHPFAH WGDQKLSEKG SYQEIIERTQ
YWGRQMLIWG IHVHVGVGSK EKVWPIINAL MTHYPHILAM SASSPAWEGL DTGYSSNRTL
LYQQLPTAGM PYQFENWEQW EEFNRDQDLS GVINHTGSMH FDVRPTKYGT VETRFADATM
ELWELAAIAA YTHCLVVYFE RRLDAGHELP TLQPWHVAEN KWRAARYGLD ALIITDRETN
EALVTDELDA WVDRLAPLSE ELGCAAELQD VRKLIARGGD YALQRAAARK HGAAPEPGTR
TRGDDGVEGG FTQPEAWIAA VDLTVDSLRK SL