ID A0A1N7E441_9ACTN Unreviewed; 411 AA.
AC A0A1N7E441;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN05444858_12069 {ECO:0000313|EMBL:SIR82902.1};
OS Micromonospora avicenniae.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1198245 {ECO:0000313|EMBL:SIR82902.1, ECO:0000313|Proteomes:UP000186004};
RN [1] {ECO:0000313|EMBL:SIR82902.1, ECO:0000313|Proteomes:UP000186004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45758 {ECO:0000313|EMBL:SIR82902.1,
RC ECO:0000313|Proteomes:UP000186004};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-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}.
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DR EMBL; FTNF01000020; SIR82902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N7E441; -.
DR STRING; 1198245.SAMN05444858_12069; -.
DR Proteomes; UP000186004; 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:SIR82902.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000186004}.
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 44414 MW; 1B395760B4A34113 CRC64;
MADPERLPVE SAGTLIRPSS ATPGASPDET DAERMTYRPT VATAVPDLTT LTLGVEEEFL
LLDLRSGENL PVAQRVLTAL RGPARDQSRQ EFRHSMVEMV TPVTADLAEL RAHLVALRRS
AAEAAESAGA RLVAVGATPM HEPHRTVPDK PRYHAMSRRY GPVAHDPAVC GCHVHVGVPD
RELAIQVCNH LRPWLPVVHA IATNSPLHDG ADTGHASWRS MQLERWPSLG PTPYFASAAD
YDRTVEELIS AGVMLDAAMV YWYARPSAAY PTVEIRVGDV CPTVDDTVLV AALLRALVAT
VLDEARAGVP ASPVRDCLVS AAHWRAAHDG LDGTLIDLRR GGARPAWELV DELFATVSPA
LVRHGDLGYV LDQLTRLRGE GTGATRQRRV LDETGDLRAV LAELAAWTTA T
//
