ID A0A0Q8F6W3_9GAMM Unreviewed; 378 AA.
AC A0A0Q8F6W3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=ASD77_11340 {ECO:0000313|EMBL:KRA52271.1};
OS Pseudoxanthomonas sp. Root65.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1736576 {ECO:0000313|EMBL:KRA52271.1, ECO:0000313|Proteomes:UP000051430};
RN [1] {ECO:0000313|EMBL:KRA52271.1, ECO:0000313|Proteomes:UP000051430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root65 {ECO:0000313|EMBL:KRA52271.1,
RC ECO:0000313|Proteomes:UP000051430};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA52271.1, ECO:0000313|Proteomes:UP000051430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root65 {ECO:0000313|EMBL:KRA52271.1,
RC ECO:0000313|Proteomes:UP000051430};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
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:KRA52271.1}.
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DR EMBL; LMHA01000002; KRA52271.1; -; Genomic_DNA.
DR RefSeq; WP_055941586.1; NZ_LMHA01000002.1.
DR AlphaFoldDB; A0A0Q8F6W3; -.
DR STRING; 1736576.ASD77_11340; -.
DR OrthoDB; 9769628at2; -.
DR Proteomes; UP000051430; 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};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000051430}.
SQ SEQUENCE 378 AA; 42591 MW; 80F31E4EDB7998B5 CRC64;
MAAEPDSHPY TFGLEEEYFL VRRNGRRLRH MPRRFFDACR AALGERFGSE MLQTQVEVQT
AVHDDPRAAE HDLLTLRRTI GGIARAHGLD ILSAGTHPSA PWRGQRSTDK PHYDQVMDEL
QMLGHRNLLC GLHVHVQPAD PAQRVHLMAR MQPFLPLLLA LSTSSPFWMG QATGLMGYRQ
TAYQEIPRTG LPPLFRGQDE YDDYVRRMID ARAIRDASFL WWALRPSLAF PTLELRVTDA
CTDPRDALAI AQLFRCVVRY LERTPRLHAA LDAGAQAVIE ENLWRAQRHG FDAGLIDIGS
GDLVSVREML ESTLEIIAAD VAALDCARQI DHAWRILDGG TSAHGQQRHY QQRRLAGDTH
GEALVHVVRW LAAASVPD
//
