ID A0A3S9PB73_9BACT Unreviewed; 763 AA.
AC A0A3S9PB73;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=glutamate--cysteine ligase {ECO:0000256|ARBA:ARBA00012220};
DE EC=6.3.2.2 {ECO:0000256|ARBA:ARBA00012220};
GN Name=gshB {ECO:0000313|EMBL:AZQ65427.1};
GN ORFNames=EI427_24770 {ECO:0000313|EMBL:AZQ65427.1};
OS Flammeovirga pectinis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae;
OC Flammeovirga.
OX NCBI_TaxID=2494373 {ECO:0000313|EMBL:AZQ65427.1, ECO:0000313|Proteomes:UP000267268};
RN [1] {ECO:0000313|EMBL:AZQ65427.1, ECO:0000313|Proteomes:UP000267268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L12M1 {ECO:0000313|EMBL:AZQ65427.1,
RC ECO:0000313|Proteomes:UP000267268};
RA Bae J.-W., Jeong Y.-S., Kang W.;
RT "Flammeovirga pectinis sp. nov., isolated from the gut of the Korean
RT scallop, Patinopecten yessoensis.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 1/2. {ECO:0000256|ARBA:ARBA00005006}.
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DR EMBL; CP034563; AZQ65427.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S9PB73; -.
DR KEGG; fll:EI427_24770; -.
DR OrthoDB; 9803907at2; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000267268; Chromosome 2.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.590.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR HAMAP; MF_00782; Glut_biosynth; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR007370; Glu_cys_ligase.
DR InterPro; IPR006335; Glut_biosynth.
DR InterPro; IPR006334; Glut_cys_ligase.
DR InterPro; IPR040657; GshAB_ATP-grasp.
DR NCBIfam; TIGR01435; glu_cys_lig_rel; 1.
DR PANTHER; PTHR38761; GLUTAMATE--CYSTEINE LIGASE; 1.
DR PANTHER; PTHR38761:SF1; GLUTAMATE--CYSTEINE LIGASE; 1.
DR Pfam; PF18419; ATP-grasp_6; 1.
DR Pfam; PF04262; Glu_cys_ligase; 2.
DR Pfam; PF08443; RimK; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Glutathione biosynthesis {ECO:0000256|ARBA:ARBA00022684};
KW Ligase {ECO:0000313|EMBL:AZQ65427.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000267268}.
FT DOMAIN 506..762
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 763 AA; 86913 MW; 87F9EF02EA13458F CRC64;
MKALDSIINN YKSSHLFEGS FGLEKENIRI DKNGKIALTP HPSRLGSKLT HPYITTDFSE
SQIEMITPPL PSIHEALGFL ETIHDIVSEQ LGDEYLWPQS TPPDLPENDN DIPIANYGEG
GEVNEEYRNH LATKYGKKKQ LLSGIHYNFS LLEKNLKFLY DKSEEKAQPY AQFKEAVYLK
IARNFLKYRW YLVTLLGDSP ALHSSYMKCC IDTLPKATSD AHHFTEATSM RTSVCGYKNQ
EDLLLDYTSM EGYHNSIQNA IDKGQLESAK ENYSPIRLKE INGQLEYLEI RLLDLDPSVK
LGITKETADI VHMFLLFCLL KEETIFDATV QLTANENQEI AATMGLSKTA KIEFEGKGMN
LQEAVARITR QIEHTLDKLL PESYVNSLEH LIKISDDIND RPAAKTLTAI QGTSFLAWHL
QKAQLYKQES LNHSYKFYGL EDMELSTQLL LREAVLRGII FEIMDRSENF VRLEKDGKEE
YVMQATRTSL DNYVSVLMME NKVMTKKLIE RVGIRTPKGE QYIDHYKAKE DFLFYKNKSV
VVKPKSTNFG LGISILKNNT KKEVFDRAIE IAFEHDNSIL VEEFVSGKEY RIFIIKNEVV
GILHRVPANV KGDGEATIRE LVIEKNKDPL RGKGYKTPLE KIALGEAEEM FLQSQGLDFD
FVPSKNQIVY LRENSNISTG GDSLDFTDDI PESYKKIAVD AAKALDVEIT GLDMMIDDIS
EEANDSNYAI IEMNFNPAIH IHCYPYKGKN RRLNAKVLDA LGY
//
