ID A0A2S2BQ12_9NOCA Unreviewed; 795 AA.
AC A0A2S2BQ12;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Putative glutamate--cysteine ligase 2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE EC=6.3.2.2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE AltName: Full=Gamma-glutamylcysteine synthetase 2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE Short=GCS 2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE Short=Gamma-GCS 2 {ECO:0000256|HAMAP-Rule:MF_01609};
GN ORFNames=CBI38_03040 {ECO:0000313|EMBL:AWK70695.1};
OS Rhodococcus oxybenzonivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1990687 {ECO:0000313|EMBL:AWK70695.1, ECO:0000313|Proteomes:UP000245711};
RN [1] {ECO:0000313|EMBL:AWK70695.1, ECO:0000313|Proteomes:UP000245711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2-17 {ECO:0000313|EMBL:AWK70695.1,
RC ECO:0000313|Proteomes:UP000245711};
RA Lee Y., Kim K.H., Chun B.H., Jung H.S., Jeon C.O.;
RT "Isolation of Rhodococcus sp. S2-17 biodegrading of BP-3.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits weak
CC glutamate--cysteine ligase activity. {ECO:0000256|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:0000256|ARBA:ARBA00029283, ECO:0000256|HAMAP-
CC Rule:MF_01609};
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family.
CC YbdK subfamily. {ECO:0000256|HAMAP-Rule:MF_01609}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP021354; AWK70695.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S2BQ12; -.
DR KEGG; roz:CBI38_03040; -.
DR OrthoDB; 9803842at2; -.
DR Proteomes; UP000245711; 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:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0042398; P:cellular modified amino acid biosynthetic process; IEA:InterPro.
DR CDD; cd08014; M20_Acy1-like; 1.
DR Gene3D; 3.30.590.20; -; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR HAMAP; MF_01609; Glu_cys_ligase_2; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR006336; GCS2.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011793; YbdK.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR NCBIfam; TIGR02050; gshA_cyan_rel; 1.
DR PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR Pfam; PF04107; GCS2; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_01609, ECO:0000313|EMBL:AWK70695.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000245711}.
FT REGION 370..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 795 AA; 86110 MW; 2A523C3EAF486F0C CRC64;
MLASSPRKLG VEEEFHLIDL KTRRLTTRAP ELLARLPDDA YVDELQRCVV EVNSGVFTDL
ADLRSDLAWH RSLLVDAAEG LGVGVAAAGS MPLALPTEMQ VTGSLRYQRM LADYQMLARE
QLICGTQVHV DVPDRDEAVQ VANRIAPYLP VFLALSVSSP FRADGSDTGY ASARTLLWLR
WPSTGPAAPV SSAAEYDTLI DDLVSSGVIS DPGMAYFDIR PSAKLPTLEL RVCDSCPRLD
TVILVAALFR ALVEREVQGL RAGDKGLKVV STMTRAALWR AARSGLEADL VDVTVPRSRL
AADIVEDFVR SLRPQLEETG DWDTVRELSA AALATGSSAA RQRQAFQRRN RLTDVVDQLL
AETADRVSPL PEGETLVPSA HAGRSHSSVA TRPRRRWAAR FARRGSESEL TWTGSGELDE
QQLLAWRRDL HAHPELSFEE RRTTRVVRDH LASLGVEPVL MPGGTGLWCD IGPETEHCIA
LRADLDALPI TEATGLEFQS TVPGVSHACG HDAHTAMLMG AAAVLVKYPP TCRVRLIFQP
GEETTPGGSV DTIAAGALEG VSKIYALHCD PNLEVGKLAT RSGPITSSNA SVTVRLWSQG
GHTARPHLTG DLIHAGAVLI TGLASVLDRR IDARTATVLT WGKVSAGQVG NSVPESGELV
GTLRSASHET WANLEPLVTD TIGELLAPYH VRYELSYLQG VPPVVNDPDC TADLREAIES
VVGFDHLAEA EQSSGGEDFA WYLEQVPGAM ARLGVWEGVG ERQELHQPGF RLDERAMIHG
LRTLVALTRL GDQTE
//
