GCS2_CORDI
ID GCS2_CORDI Reviewed; 359 AA.
AC Q6NF59;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=DIP2042;
OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS gravis).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=257309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX PubMed=14602910; DOI=10.1093/nar/gkg874;
RA Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA Parkhill J.;
RT "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT NCTC13129.";
RL Nucleic Acids Res. 31:6516-6523(2003).
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; BX248360; CAE50568.1; -; Genomic_DNA.
DR RefSeq; WP_010935524.1; NC_002935.2.
DR AlphaFoldDB; Q6NF59; -.
DR SMR; Q6NF59; -.
DR STRING; 257309.DIP2042; -.
DR PRIDE; Q6NF59; -.
DR EnsemblBacteria; CAE50568; CAE50568; DIP2042.
DR KEGG; cdi:DIP2042; -.
DR HOGENOM; CLU_044848_1_0_11; -.
DR OMA; LIFGLHV; -.
DR OrthoDB; 991285at2; -.
DR Proteomes; UP000002198; 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..359
FT /note="Putative glutamate--cysteine ligase 2"
FT /id="PRO_0000218192"
SQ SEQUENCE 359 AA; 40662 MW; ED768BE01392BE49 CRC64;
MIFPPSPPTL GVEWEVALAD PHSRDLVPRG HEVIEKATTH LEREFLANTV ELVTSVCTTV
PEAIEELREG IEEVKAIAAD MGLKVWAAGS HPFSDFRKQP VNEKGHYNEI IERTQYWGNQ
MLIWGIHVHV GISSKDRVWP IINAMLTYYP HLLALTASSP GWDGIDTGYA SNRTMLYQQL
PTAGLPYQFQ SWDEWEAYMA DQNKSGVINH TGSMHFDIRP TRYGTVEVRI CDSTNLRELS
AAVALTHCLI VDLERKLDRG EELPTLQDWH VAENKWRAAR YGMDAEIIIS RDTDEAWVTD
ELRSLVERLS PLARELGCYD ELQGVLTICQ TGASYQRQRA IYKETGSWLP VVDAVLAEM
