ID A0A2N6UMJ8_9ACTO Unreviewed; 398 AA.
AC A0A2N6UMJ8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-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=CJ187_06030 {ECO:0000313|EMBL:PMC84527.1};
OS Gleimia hominis.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Gleimia.
OX NCBI_TaxID=595468 {ECO:0000313|EMBL:PMC84527.1};
RN [1] {ECO:0000313|EMBL:PMC84527.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0859 {ECO:0000313|EMBL:PMC84527.1};
RA Thomas-White K., Kumar N., Forster S., Putonti C., Lawley T., Wolfe A.J.;
RT "Bacterial strain isolated from the female urinary microbiota.";
RL Submitted (SEP-2017) 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 -!- 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:PMC84527.1}.
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DR EMBL; PNHU01000002; PMC84527.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N6UMJ8; -.
DR OrthoDB; 9769628at2; -.
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:PMC84527.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609}.
SQ SEQUENCE 398 AA; 44444 MW; 39620B98A47FC743 CRC64;
MSIKFADSER STIGIEWELQ LIDRDSLDLR QCGDLVVDRA RELNPDSELI HGEMLRNTVE
LVSGKQTNVA ACAEDLQRGV DMLAPVIDPL RIDLASAGSH PFANPEFQRV SDSERYAKLV
NRTQYWGRQM LLYGTHVHVG VEDFRKVLPI LNYLLTKLGL MQALSASSPF WGGVDTRYCD
NRAMVFQQLP TAGTPRQFTE WHQLEEYTAG LRKTGVIGSF NEVRWDIRPS PALGTIEVRV
CDAASNLTEV RAAAALIHAL VETASRRLDA GEELPTIPPW FLDENKWRAA RYGMDATLIE
NANGDEASVK ETLPALLEQL APAARDLNCL EDLEALYDIA ASGVGYQRQR AVVERTGTLE
AVVEHMCAEF ESGKPVSAYD FEYDPRGMRF PDSGNRGW
//
