ID A0A1H5T6J2_9BACT Unreviewed; 367 AA.
AC A0A1H5T6J2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-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=SAMN05421819_0496 {ECO:0000313|EMBL:SEF58400.1};
OS Bryocella elongata.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Bryocella.
OX NCBI_TaxID=863522 {ECO:0000313|EMBL:SEF58400.1, ECO:0000313|Proteomes:UP000236728};
RN [1] {ECO:0000313|EMBL:SEF58400.1, ECO:0000313|Proteomes:UP000236728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22489 {ECO:0000313|EMBL:SEF58400.1,
RC ECO:0000313|Proteomes:UP000236728};
RA de Groot N.N.;
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|HAMAP-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; FNVA01000001; SEF58400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5T6J2; -.
DR OrthoDB; 9769628at2; -.
DR Proteomes; UP000236728; 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:SEF58400.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000236728}.
SQ SEQUENCE 367 AA; 42657 MW; 732200438DA78D8F CRC64;
MRPSFTLGIE EEYQTIDPVT RDLRSHVATE MLEHGKLQLQ ERVKAEMHQS VVEVGTRVCH
NIEEAREDLY DLRRSMIRLA EEHGLVLVAG ATHPFADWRQ QEIYPDPRYA KVVEDLQLVA
RSNLIFGLHV HVGIEDKESA IRVMNSMRYF LPHILALSTN SPFWLGMETG YKSYRAKVFE
NFPRTNIPDE FATYSEFEAY VNLLIKTNTI DNAKKIWWDI RPHPYFSTIE VRICDIPLRA
EESIAIAALI QATACTLWKL HARNMDFRRY SRALLMENKF RAVRYGLEGK LIDFGKQLEV
PEHDLIHEYL AFVEDAVDEL GSREAINYIR QMLRQGSGAD RQLKVWRETG DLKKVVDFMA
EETRAGL
//
