ID A0A2S7WWX0_9FLAO Unreviewed; 364 AA.
AC A0A2S7WWX0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=BTO16_05720 {ECO:0000313|EMBL:PQJ82100.1};
OS Polaribacter glomeratus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=102 {ECO:0000313|EMBL:PQJ82100.1, ECO:0000313|Proteomes:UP000239068};
RN [1] {ECO:0000313|EMBL:PQJ82100.1, ECO:0000313|Proteomes:UP000239068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43844 {ECO:0000313|EMBL:PQJ82100.1,
RC ECO:0000313|Proteomes:UP000239068};
RA Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
RL Submitted (DEC-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|HAMAP-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:PQJ82100.1}.
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DR EMBL; MSCM01000001; PQJ82100.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7WWX0; -.
DR OrthoDB; 9769628at2; -.
DR Proteomes; UP000239068; 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:PQJ82100.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000239068}.
SQ SEQUENCE 364 AA; 41938 MW; 59EA63514C8177E8 CRC64;
MKFTLGIEEE YQVIDPITRE LVSHDQQIVM NASKVLNDQV KAEMHQAVVE VGTNICNDIQ
DAREQITHLR KSISTFAGEL GYKIGAAGTH PFSKWETQLI TPNPRYHEII DELQDTARSN
LIFGLHVHVG MEDKNMAMHL VNAMRYFLPH LYALSTNSPF WEGRNTGFKS FRSKVFDKFP
RTGIPGVFNS YAQYENYVNL LVKTKCIDNP KKIWWDIRIH PVFPTIEVRI CDVPLTVDET
ICIAALIQAL VAKLHKLRSQ NLNFMNYHRA LINENKWRAG RYGIDGKMID FGLEKEVETK
LLMREFVDFV DDVLDELGSR KEVEYVFEIL KNGTGADRQL KVFEETNDLI KVVDFITEQT
ILGL
//
