GCS2_SHIF8
ID GCS2_SHIF8 Reviewed; 372 AA.
AC Q0T746;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
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 Name=ybdK; OrderedLocusNames=SFV_0521;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
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 -!- SUBUNIT: Homodimer. {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; CP000266; ABF02780.1; -; Genomic_DNA.
DR RefSeq; WP_001130611.1; NC_008258.1.
DR AlphaFoldDB; Q0T746; -.
DR SMR; Q0T746; -.
DR EnsemblBacteria; ABF02780; ABF02780; SFV_0521.
DR KEGG; sfv:SFV_0521; -.
DR HOGENOM; CLU_044848_1_1_6; -.
DR OMA; LIFGLHV; -.
DR BioCyc; SFLE373384:SFV_RS02890-MON; -.
DR Proteomes; UP000000659; 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.
FT CHAIN 1..372
FT /note="Putative glutamate--cysteine ligase 2"
FT /id="PRO_0000291516"
SQ SEQUENCE 372 AA; 41655 MW; 0D4469A072DF4304 CRC64;
MPLPDFHVSE PFTLGIELEM QVVNPPGYDL NQDSSMLIDA VKNKITAGEV KHDITESMLE
LATDVCRDIN QAAGQFSAMQ KVVLQAAADH HLEICGGGTP PFQKWQRQEV CDNERYQRTL
ENFGYLIQQA TVFGQHVHVG CASGDDAIYL LHGLSRFVPH FIALSAASPY MQGTDTRFAP
SRPNIFSAFP DNGPMPWVSN WQQFEALFRC LSYTTMIDSI KDLHWDIRPS PHFGTVEVRV
MDTPLTLSHA VNMAGLIQAT AHWLLTERPF KHQEKDYLLY KFNRFQACRY GLEGVITDPH
TGDRRPLTED TLRLLEKIAP SAHKIGASSA IEALHRQVVS GLNEAQLMRD FVADGGSLIG
LVKKHCEIWA GD