ID   A0A6N8S223_9BURK        Unreviewed;       509 AA.
AC   A0A6N8S223;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 1.
DT   14-DEC-2022, entry version 9.
DE   RecName: Full=Glutamate--cysteine ligase {ECO:0000256|HAMAP-Rule:MF_00578};
DE            EC=6.3.2.2 {ECO:0000256|HAMAP-Rule:MF_00578};
DE   AltName: Full=Gamma-ECS {ECO:0000256|HAMAP-Rule:MF_00578};
DE            Short=GCS {ECO:0000256|HAMAP-Rule:MF_00578};
DE   AltName: Full=Gamma-glutamylcysteine synthetase {ECO:0000256|HAMAP-Rule:MF_00578};
GN   Name=gshA {ECO:0000256|HAMAP-Rule:MF_00578,
GN   ECO:0000313|EMBL:MXN32001.1};
GN   ORFNames=GRX31_25585 {ECO:0000313|EMBL:MXN32001.1};
OS   Delftia sp. CH05.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=2692194 {ECO:0000313|EMBL:MXN32001.1, ECO:0000313|Proteomes:UP000438180};
RN   [1] {ECO:0000313|EMBL:MXN32001.1, ECO:0000313|Proteomes:UP000438180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH05 {ECO:0000313|EMBL:MXN32001.1,
RC   ECO:0000313|Proteomes:UP000438180};
RA   Sbano A., Succar J.B., Ferreira J.V.R., Berbert L.C., Flores V.R.,
RA   Direito I.C.C., Cardoso A.M.;
RT   "Draft genome sequence of Delftia sp. strain CH05, isolated from the
RT   chicory (Cichorium endivia L.) rhizosphere.";
RL   Submitted (DEC-2019) 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, ECO:0000256|HAMAP-
CC         Rule:MF_00578, ECO:0000256|RuleBase:RU004391};
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC       L-cysteine and L-glutamate: step 1/2. {ECO:0000256|ARBA:ARBA00005006,
CC       ECO:0000256|HAMAP-Rule:MF_00578, ECO:0000256|RuleBase:RU004391}.
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 1 family.
CC       Type 1 subfamily. {ECO:0000256|ARBA:ARBA00008772, ECO:0000256|HAMAP-
CC       Rule:MF_00578}.
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:MXN32001.1}.
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DR   EMBL; WUMG01000048; MXN32001.1; -; Genomic_DNA.
DR   RefSeq; WP_034348046.1; NZ_WUMG01000048.1.
DR   AlphaFoldDB; A0A6N8S223; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000438180; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00578; Glu_cys_ligase; 1.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR007370; Glu_cys_ligase.
DR   InterPro; IPR006334; Glut_cys_ligase.
DR   PANTHER; PTHR38761; GLUTAMATE--CYSTEINE LIGASE; 1.
DR   Pfam; PF04262; Glu_cys_ligase; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR   TIGRFAMs; TIGR01434; glu_cys_ligase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00578};
KW   Glutathione biosynthesis {ECO:0000256|ARBA:ARBA00022684, ECO:0000256|HAMAP-
KW   Rule:MF_00578};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00578, ECO:0000313|EMBL:MXN32001.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00578}.
FT   DOMAIN          14..362
FT                   /note="Glu_cys_ligase"
FT                   /evidence="ECO:0000259|Pfam:PF04262"
SQ   SEQUENCE   509 AA;  57021 MW;  216858C99DFDDC91 CRC64;
     MKTSQASMAV PGPERLKGIR RGIEKEGLRV LPSGSLALTP HPLALGSALT HPHITTDYSE
     SQIELITGAR LGVQECLDEL VQIHQFVLRS LRDAGGEMLW SSSMPCQLPT DETIPLARYG
     SSHSGRSKSV YRMGLGHRYG RRMQTISGIH YNWSLPGVTS DQYFSLIRNF RRHAFVLLYL
     YGASPALCPC FVEGREHRLQ PLGNTGQALY LPHATSLRMG RLGYQSDAQA SINVSYNGLE
     GYANSLYDAL TQPYPAYEML GVRNPGGDYN QLGTGLLQIE NEFYGTIRPK RTVSRGERPL
     HALRERGVEY VEVRLMDLDP FEDVGIAAPT MRMLDVFLLH CLNADSPPDT PDEIAELKHN
     QHLTAERGRE PGLQLVRAGR EVPLRDWAHE VLDQCRPYAQ ALDSTHGTQD YSAALAQALE
     RLEHPERTPS AHVLGELTGA YGNSFANFTL ARSEQARDSL LALPWSQAQQ QRFEQWSAQS
     VQEQRDIEAA DTLSFEEWRL RYMAPENLR
//