ID A0A1I6KEW2_9MICO Unreviewed; 375 AA.
AC A0A1I6KEW2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=SAMN04487846_0383 {ECO:0000313|EMBL:SFR89782.1};
OS Microbacterium sp. cf046.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1761803 {ECO:0000313|EMBL:SFR89782.1, ECO:0000313|Proteomes:UP000199422};
RN [1] {ECO:0000313|EMBL:SFR89782.1, ECO:0000313|Proteomes:UP000199422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF046 {ECO:0000313|EMBL:SFR89782.1,
RC ECO:0000313|Proteomes:UP000199422};
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|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; FOZJ01000001; SFR89782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6KEW2; -.
DR STRING; 1761803.SAMN04487846_0383; -.
DR OrthoDB; 9769628at2; -.
DR Proteomes; UP000199422; 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:SFR89782.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000199422}.
SQ SEQUENCE 375 AA; 42751 MW; ABAB1C442DB4DC1E CRC64;
MERPEFTMGI EEEYLLVDRD SRALGVAPED FIEDCRADLQ DQVSPEYKQC QVEIGTKVCR
NVAEARDDLR RLRSTISRHA ARYGLAPIAA SCHPFSDWKH QHHTDKERYR GLERDLAGVA
RRLLICGCHV HIGIGDNALR SDLLRQMPYF LPHLLALSTS SPFWQGEDTG LASYRISVFD
NLPRTGLPPD YQSWAELQRS VGVLVDLGII EDSSKIWWDI RPSNRYPTLE TRIMDVSPRA
VDALTLAAVT QCLMRMLWRL RIRNQRWRIY DRFLVGENRW RAQRYGVTEG LIDFGANTIV
PFPQLMAELV EMIAEDAEAL DCRDEMVRVL SIATDGTSAQ RQRAVVAEAT AAGADQDQAM
TAVVDHLIEE FHQDL
//