ID   A0A1D8IZT4_9BURK        Unreviewed;       509 AA.
AC   A0A1D8IZT4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   28-FEB-2018, entry version 10.
DE   RecName: Full=Glutamate--cysteine ligase {ECO:0000256|RuleBase:RU004391, ECO:0000256|SAAS:SAAS00997187};
DE            EC=6.3.2.2 {ECO:0000256|RuleBase:RU004391, ECO:0000256|SAAS:SAAS00997172};
GN   Name=gshA {ECO:0000256|HAMAP-Rule:MF_00578};
GN   ORFNames=BI380_11915 {ECO:0000313|EMBL:AOV01999.1};
OS   Delftia tsuruhatensis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=180282 {ECO:0000313|EMBL:AOV01999.1, ECO:0000313|Proteomes:UP000095607};
RN   [1] {ECO:0000313|EMBL:AOV01999.1, ECO:0000313|Proteomes:UP000095607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM13 {ECO:0000313|EMBL:AOV01999.1,
RC   ECO:0000313|Proteomes:UP000095607};
RA   Saffarian A.;
RT   "Complete genome sequence of Deltia acidovorans CM13 isolated from
RT   murine proximal colonic tissue.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + L-cysteine = ADP +
CC       phosphate + gamma-L-glutamyl-L-cysteine.
CC       {ECO:0000256|RuleBase:RU004391, ECO:0000256|SAAS:SAAS00963680}.
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
CC       from L-cysteine and L-glutamate: step 1/2.
CC       {ECO:0000256|RuleBase:RU004391, ECO:0000256|SAAS:SAAS00963683}.
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 1
CC       family. Type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_00578,
CC       ECO:0000256|SAAS:SAAS00997183}.
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DR   EMBL; CP017420; AOV01999.1; -; Genomic_DNA.
DR   RefSeq; WP_034348046.1; NZ_CP017420.1.
DR   EnsemblBacteria; AOV01999; AOV01999; BI380_11915.
DR   KEGG; dts:BI380_11915; -.
DR   KO; K01919; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000095607; Chromosome.
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; PTHR38761; 1.
DR   Pfam; PF04262; Glu_cys_ligase; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   TIGRFAMs; TIGR01434; glu_cys_ligase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00578,
KW   ECO:0000256|SAAS:SAAS00963666};
KW   Complete proteome {ECO:0000313|Proteomes:UP000095607};
KW   Glutathione biosynthesis {ECO:0000256|HAMAP-Rule:MF_00578,
KW   ECO:0000256|SAAS:SAAS00963671};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00578,
KW   ECO:0000256|SAAS:SAAS00963674, ECO:0000313|EMBL:AOV01999.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00578,
KW   ECO:0000256|SAAS:SAAS00963669}.
FT   DOMAIN       14    362       Glu_cys_ligase. {ECO:0000259|Pfam:
FT                                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
//