GCS23_PAEAT
ID GCS23_PAEAT Reviewed; 424 AA.
AC A1RAU1;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=AAur_3665;
OS Paenarthrobacter aurescens (strain TC1).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX NCBI_TaxID=290340;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC1;
RX PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V.,
RA Khouri H.M., Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT "Secrets of soil survival revealed by the genome sequence of Arthrobacter
RT aurescens TC1.";
RL PLoS Genet. 2:2094-2106(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 -!- 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; CP000474; ABM06492.1; -; Genomic_DNA.
DR AlphaFoldDB; A1RAU1; -.
DR SMR; A1RAU1; -.
DR STRING; 290340.AAur_3665; -.
DR EnsemblBacteria; ABM06492; ABM06492; AAur_3665.
DR KEGG; aau:AAur_3665; -.
DR eggNOG; COG2170; Bacteria.
DR HOGENOM; CLU_044848_0_0_11; -.
DR OMA; MLYWYAR; -.
DR Proteomes; UP000000637; 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..424
FT /note="Putative glutamate--cysteine ligase 2-3"
FT /id="PRO_0000291483"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 424 AA; 46183 MW; F9153D0879B4F623 CRC64;
MQMAGRGANR RGQHRSPVLV RPPDAEWSMR TFGVEEELLI VDPVTGEPLA LADALLAGQD
EPTSGLSHEL KLEQIETQTR PCHSYGELLQ QIRRGRAMAN QAARQHGARV AAIATSPLAS
NTHTTPDPRY AAMLDRFGII ATEQLTCGFH VHTSVESPEE GVVVLDHIRD KLAVLTALTA
NSPYWRGLPT GFDSYRTQAW NRWPTSGPSS VFGSLTAYRR IVKRLLETGV IMDEGMIYFD
ARISRNHPTV EVRVADVCLR AEDAALMAVL VRALVETASL EMLDGVEPTA VPTALLRMAS
WQASNSGLRG DLLDFGDFLP QPAADVVWAL VDYLSPVLDD QGELELVKAG ISDVLDRGNG
AHEQRETAVR YNKRQHDGQT QPGSPPTNEA LAAVVGHAAK VTVRGAAADA HKDPAPMLTR
VRRP
