ID A0A1D8IZT4_9BURK Unreviewed; 509 AA. AC A0A1D8IZT4; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 27-SEP-2017, entry version 7. 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 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. {ECO:0000256|HAMAP- CC Rule:MF_00578, ECO:0000256|RuleBase:RU004391, CC ECO:0000256|SAAS:SAAS00073839}. CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione CC from L-cysteine and L-glutamate: step 1/2. {ECO:0000256|HAMAP- CC Rule:MF_00578, ECO:0000256|RuleBase:RU004391, CC ECO:0000256|SAAS:SAAS00376196}. 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:SAAS00566831}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; IPR007370; Glu_cys_ligase. DR InterPro; IPR006334; Glut_cys_ligase. DR Pfam; PF04262; Glu_cys_ligase; 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:SAAS00073841}; KW Complete proteome {ECO:0000313|Proteomes:UP000095607}; KW Glutathione biosynthesis {ECO:0000256|HAMAP-Rule:MF_00578, KW ECO:0000256|SAAS:SAAS00073856}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00578, KW ECO:0000256|SAAS:SAAS00073847, ECO:0000313|EMBL:AOV01999.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00578, KW ECO:0000256|SAAS:SAAS00073833}. 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 //