ID A0A2I1J9H0_9MICC Unreviewed; 382 AA.
AC A0A2I1J9H0;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-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=CJ193_04040 {ECO:0000313|EMBL:PMC78192.1}, CYJ35_07245
GN {ECO:0000313|EMBL:PKY80009.1};
OS Pseudoglutamicibacter albus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Pseudoglutamicibacter.
OX NCBI_TaxID=98671 {ECO:0000313|EMBL:PKY80009.1, ECO:0000313|Proteomes:UP000234591};
RN [1] {ECO:0000313|EMBL:PMC78192.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0715 {ECO:0000313|EMBL:PMC78192.1};
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.
RN [2] {ECO:0000313|EMBL:PKY80009.1, ECO:0000313|Proteomes:UP000234591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0722 {ECO:0000313|EMBL:PKY80009.1,
RC ECO:0000313|Proteomes:UP000234591};
RA Thomas-White K., Wolfe A.J.;
RT "Phylogenetic diversity of female urinary microbiome.";
RL Submitted (DEC-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:PKY80009.1}.
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DR EMBL; PKGR01000007; PKY80009.1; -; Genomic_DNA.
DR EMBL; PNHO01000008; PMC78192.1; -; Genomic_DNA.
DR OrthoDB; 9769628at2; -.
DR Proteomes; UP000234591; 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:PKY80009.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609}.
SQ SEQUENCE 382 AA; 42755 MW; 8F60B3CCE11248E6 CRC64;
MSIEFTPSKP STLGIEWEIA LVDRETGDLR PEAPRILDEL EKQDRITHPD GSPRLTRELL
QNTVECVTGV HNTVADAVAD LASTARHVSD ILDPLNTSLY CAGSHPFAEP TLQEVSDKDR
YATLIDRTQW WGRQMVIYGV HVHVGIDHRD KALPIVDGLI NKQPHLLALT SSSPFWGGTD
TGYGSQRSLM FQQLPTAGLP FHFSKWFEYE SYVADMLHTG VVDVLDEIRW DARPVPKYGT
VEMRICDGLP DLDDIAAVAA YTQCLVTEMS DILDGGWSIP VMTPWFRVEN KWRAARYGRE
AIIIVNSAGD ELLVTDHIAQ DVERLTPIAE RLGCAEELNH ITTMMQQPCE YERQRNVAEA
NGGDLAAVVK DNSERLHASL DR
//
