ID A0A1L7CI67_9CORY Unreviewed; 378 AA.
AC A0A1L7CI67;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, 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=CAQU_11210 {ECO:0000313|EMBL:APT85518.1};
OS Corynebacterium aquilae DSM 44791.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1431546 {ECO:0000313|EMBL:APT85518.1, ECO:0000313|Proteomes:UP000185478};
RN [1] {ECO:0000313|EMBL:APT85518.1, ECO:0000313|Proteomes:UP000185478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S-613 {ECO:0000313|EMBL:APT85518.1,
RC ECO:0000313|Proteomes:UP000185478};
RA Ruckert C., Albersmeier A., Winkler A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium aquilae S-613T(T) (=DSM
RT 44791(T)), isolated from the choana of a healthy golden eagle.";
RL Submitted (AUG-2014) 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; CP009245; APT85518.1; -; Genomic_DNA.
DR RefSeq; WP_075727671.1; NZ_CP009245.1.
DR AlphaFoldDB; A0A1L7CI67; -.
DR STRING; 1431546.CAQU_11210; -.
DR KEGG; caqu:CAQU_11210; -.
DR Proteomes; UP000185478; 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:APT85518.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000185478}.
SQ SEQUENCE 378 AA; 42506 MW; 96FE7835D24A8A4B CRC64;
MAHIFKGSPQ PTIGVEWELA LVDPDTGDLV GRAAELIEKT PKPHDKVRFD LEFLDNTVEI
VTGVCTNTAE AFEQLQASRA ALDKAAREMG LRLWTSGSHP TTDFRTQDVS DKPHYKEIIE
RTQYWGRQML IWGLHVHVGV KDEDRVWPII GGLMTLMPVM LAYSASSPAW ISEDTGYASN
RSMLYQQLPT AGIPYGFDTW AEYESFMKDQ ETSGVVSHTG SMHFDIRPAC EHGTIEVRVC
DSPATLWEVA ALTAFIHCAV VYFDSLIDAG EAVPKLPYWH NVENKWRAAR YGDETLMITD
GDTHEATVDV VLEDYLQRFA PIAKDLGCED ELAMMRTLAK VRPGYVRQRE AFAQHNDWVE
VVHHTVDELA SGDVPPRL
//
