ID A0A1C9WLN4_9MICC Unreviewed; 383 AA.
AC A0A1C9WLN4;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=ASPU41_00465 {ECO:0000313|EMBL:AOT02031.1};
OS Arthrobacter sp. U41.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1849032 {ECO:0000313|EMBL:AOT02031.1, ECO:0000313|Proteomes:UP000095776};
RN [1] {ECO:0000313|EMBL:AOT02031.1, ECO:0000313|Proteomes:UP000095776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U41 {ECO:0000313|EMBL:AOT02031.1,
RC ECO:0000313|Proteomes:UP000095776};
RA Fomenkov A., Akimov V.N., Vasilyeva L.V., Andersen D., Vincze T.,
RA Roberts R.J.;
RT "Complete Genome and Methylome Analysis of Psychrotrophic Bacterial
RT Isolates from Antarctic Lake Untersee.";
RL Submitted (MAY-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}.
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; CP015732; AOT02031.1; -; Genomic_DNA.
DR RefSeq; WP_069949242.1; NZ_CP015732.1.
DR AlphaFoldDB; A0A1C9WLN4; -.
DR STRING; 1849032.ASPU41_00465; -.
DR KEGG; aru:ASPU41_00465; -.
DR OrthoDB; 9769628at2; -.
DR Proteomes; UP000095776; 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:AOT02031.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000095776}.
SQ SEQUENCE 383 AA; 42229 MW; F91269DF4F7A6AE7 CRC64;
MKIDFASSRQ STLGVEWELA LVDAETGELA SVAQEVLRGV AARHPELNED DEHPHIKQEL
LLNTVELVTG ICNTVAEAKA DLSSSLAAVR DVTDPMGVEI FCAGSHPFSP PQLQPVTDKE
RYAKLIDRTQ WWGRQMVIYG VHVHVGLDSR DKVLPVLDGL VNYFPQFQAL SASSPFWGGE
DTGYASQRAL MFQQLPTAGL PFQFASWEDF ESYAQDMFTT GVIDSLSEIR WDIRPVPHFG
TIEMRICDGL ATLEEVGAIA ALTQCLVDEF STTLDNGGTI PTMPPWHVQE NKWRAARYGL
DAIIILDAAG NEQLVTDHIR ETVARLEPVA VKLGCAAELA DVLKIIERGA GYQRQRRVAA
EHGGDLRAVV LDLVQQMRKG PEA
//
