ID A0A126PGA2_9BACT Unreviewed; 365 AA.
AC A0A126PGA2;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-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=AXW84_12060 {ECO:0000313|EMBL:AMJ68154.1};
OS Hymenobacter sp. PAMC 26628.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1484118 {ECO:0000313|EMBL:AMJ68154.1, ECO:0000313|Proteomes:UP000059956};
RN [1] {ECO:0000313|EMBL:AMJ68154.1, ECO:0000313|Proteomes:UP000059956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC26628 {ECO:0000313|EMBL:AMJ68154.1,
RC ECO:0000313|Proteomes:UP000059956};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-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}.
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; CP014304; AMJ68154.1; -; Genomic_DNA.
DR RefSeq; WP_068239327.1; NZ_CP014304.1.
DR AlphaFoldDB; A0A126PGA2; -.
DR STRING; 1484118.AXW84_12060; -.
DR KEGG; hyz:AXW84_12060; -.
DR OrthoDB; 9769628at2; -.
DR Proteomes; UP000059956; Chromosome.
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:AMJ68154.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000059956}.
SQ SEQUENCE 365 AA; 42081 MW; 8DF4BEFE34C471F2 CRC64;
MPTFTLGIEE EFQTIDPDTR ELRSHMSKIV ENGKITLLEQ VKAEMHESVV EVGTNICQNI
HEARAEVLHL RRQVIELAGN VGLRIGAAGT HPFSRWQDQP ITPDARYDKI VEELQEAARS
NLVFGMHVHV GIENRDIGVY MMNALRYFLP HLFALSTNSP FWEGRETGYK SFRTKVFERF
PRTGIPSYFT SASDYDEFIQ LLIKTGCIDN GKKIWWDLRL HPFFDTIEYR ICDMMMRPDE
TIAVAAIMQA LVAKIYKLKR QNLNFRLYRS ALIKENKWRA ARYGIDGTMI DFGKQQEVPT
RALILELLDF VDDVLDELGS RHEVEYVLKM LEMGTGADRQ LAVFRETGDL TKVVDYILAE
TTHGL
//
