ID A0A1I4ZQG5_9MICO Unreviewed; 389 AA.
AC A0A1I4ZQG5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN05216219_0987 {ECO:0000313|EMBL:SFN52388.1};
OS Mycetocola miduiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Mycetocola.
OX NCBI_TaxID=995034 {ECO:0000313|EMBL:SFN52388.1, ECO:0000313|Proteomes:UP000198867};
RN [1] {ECO:0000313|Proteomes:UP000198867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.11101 {ECO:0000313|Proteomes:UP000198867};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FOVM01000002; SFN52388.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4ZQG5; -.
DR STRING; 995034.SAMN05216219_0987; -.
DR OrthoDB; 9769628at2; -.
DR Proteomes; UP000198867; 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:SFN52388.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000198867}.
SQ SEQUENCE 389 AA; 43132 MW; FCFCA7F99C86B50C CRC64;
MGIDFARSER STVGIEWELA LVDRDSGELV SAADEVLQAL HQPDGSPHPH ITGELLLNTV
ELVSSVHTTV AEAVADLDGQ LQELREVTLG RGIDIIGSGS HPFGQWYDQP VANKERYHKL
IERTRWWGRN MMIWGVHVHV GIEDREKVIP ILNAMLSYIP HLQALSASSP YWGGVETGYA
SNRALMFQQL PTAGLPYQLA DWAAFENYVA DMTVPGIIDD YTEVRWDIRP SPHWGTLEVR
FCDGASTHHE LAAVAALIHC LVEHLSTRID EGKPLTVLQP WYVRENKWRA ARYGLDAHII
LDTEGNERLV TDDIRDLLVT LAPIARRLGC AEELASIEGI LENGASYSRQ LSVAKANDGD
LTSVVTALAR ELHDGSRQAR QLPSAQLPG
//
