ID A0A239WV92_9FLAO Unreviewed; 367 AA.
AC A0A239WV92;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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 Name=ybdK {ECO:0000313|EMBL:SNV37708.1};
GN ORFNames=SAMEA4412677_00696 {ECO:0000313|EMBL:SNV37708.1};
OS Chryseobacterium taklimakanense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=536441 {ECO:0000313|EMBL:SNV37708.1, ECO:0000313|Proteomes:UP000215196};
RN [1] {ECO:0000313|EMBL:SNV37708.1, ECO:0000313|Proteomes:UP000215196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13490 {ECO:0000313|EMBL:SNV37708.1,
RC ECO:0000313|Proteomes:UP000215196};
RG Pathogen Informatics;
RL Submitted (JUN-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|HAMAP-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; LT906465; SNV37708.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239WV92; -.
DR KEGG; ctak:4412677_00696; -.
DR Proteomes; UP000215196; Chromosome 1.
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:SNV37708.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000215196}.
SQ SEQUENCE 367 AA; 42844 MW; 54C28C9C07823BE4 CRC64;
MHRFTIGVEE EYQIIDAESR DLVSHVSKII EGGKATLEEH LKHEMHESVV EMETGICQNI
KQAKEELYSL RKRLIKIAHE QNLRVSGGGT HPFSQWRTNK ITSADRYDKI VDDMGDVARG
NLIFGLHVHI GIPNREEGIK IQNVMRYFLP HIYALSTNSP FWIGRNTGFK SYRQQVFAKF
PRTGIPSYFS SVSEFDEYIN LMIKTGTIDN AKKIWWDLRV HPFYPTIEFR ICDMPLRIDE
TVCLAAIMQA LTAKIYKLHQ QNITFRSYRR LMITENKWRA AKKGIQSELI DFGKEESVPF
IDLLRELLLF IDDVVDELES RDEINYVWEI IRRGTGADRQ LQVFNDTRDL RSVVDYMIAE
TEYGITE
//
