ID A0A2A3HPA7_9ACTN Unreviewed; 366 AA.
AC A0A2A3HPA7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=BX265_7866 {ECO:0000313|EMBL:PBC70443.1};
OS Streptomyces sp. TLI_235.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938860 {ECO:0000313|EMBL:PBC70443.1, ECO:0000313|Proteomes:UP000218662};
RN [1] {ECO:0000313|EMBL:PBC70443.1, ECO:0000313|Proteomes:UP000218662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TLI_235 {ECO:0000313|EMBL:PBC70443.1,
RC ECO:0000313|Proteomes:UP000218662};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PBC70443.1}.
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; NSGV01000003; PBC70443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3HPA7; -.
DR OrthoDB; 9803842at2; -.
DR Proteomes; UP000218662; Unassembled WGS sequence.
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 Gene3D; 3.30.590.20; -; 1.
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 NCBIfam; TIGR02050; gshA_cyan_rel; 1.
DR PANTHER; PTHR36510; GLUTAMATE--CYSTEINE LIGASE 2-RELATED; 1.
DR PANTHER; PTHR36510:SF1; GLUTAMATE--CYSTEINE LIGASE 2-RELATED; 1.
DR Pfam; PF04107; GCS2; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 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:PBC70443.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000218662}.
SQ SEQUENCE 366 AA; 39356 MW; 0E9522E39943A3C7 CRC64;
MLTIGVEEEY LLVSPATGVP VACAARVLAE AGLHPAVDRG EVQRELLQAQ LEVATPVCHG
LDELGGHLLR LRHCLSGAAE ACGCRLAACG SAPFTDRLPV PVTPSARYRR MRRDAPALTD
EQMINGMHVH IGVPGRAAGV AVLNGLRPWL PVLTALSANS PLWRGKDTGF ASWRTVVFGR
WPVSGVPPSF ADDADYDRRI HRLVATGLLR DTGQLYWQAR LSERYPTVEV RATDVQLRAD
EAVLLAGLVR ALAARSLDPR RATAVPPAPP ELLQTAAWYA ARHGLAERLS DPATGTLVPA
TEAAATTLAC VEPELRAGGD VERVGEGLRR LLAEGNGALR QRRELRQSGR KGLVRMITDE
TAGILH
//
