ID GSH1_SACD2 Reviewed; 530 AA. AC Q21EP1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 1. DT 16-JUN-2009, entry version 20. DE RecName: Full=Glutamate--cysteine ligase; DE EC=6.3.2.2; DE AltName: Full=Gamma-glutamylcysteine synthetase; DE AltName: Full=Gamma-ECS; DE Short=GCS; GN Name=gshA; OrderedLocusNames=Sde_3583; OS Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Saccharophagus. OX NCBI_TaxID=203122; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Saunders E.H., Brettin T., Bruce D., RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., RA Kyrpides N., Lykidis A., Richardson P., Weiner R.; RT "Complete sequence of Saccharophagus degradans 2-40."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + L-cysteine = ADP + CC phosphate + gamma-L-glutamyl-L-cysteine. CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione CC from L-cysteine and L-glutamate: step 1/2. CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 1 CC family. Type 1 subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000282; ABD82838.1; -; Genomic_DNA. DR RefSeq; YP_529050.1; -. DR GeneID; 3966445; -. DR GenomeReviews; CP000282_GR; Sde_3583. DR KEGG; sde:Sde_3583; -. DR NMPDR; fig|203122.1.peg.1595; -. DR HOGENOM; Q21EP1; -. DR OMA; Q21EP1; DTLYLPY. DR BioCyc; SDEG203122:SDE_3583-MON; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:HAMAP. DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00578; -; 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; Complete proteome; Glutathione biosynthesis; Ligase; KW Nucleotide-binding. FT CHAIN 1 530 Glutamate--cysteine ligase. FT /FTId=PRO_1000025185. SQ SEQUENCE 530 AA; 60265 MW; C55176AC2B39CD30 CRC64; MYEIQSFHAG LYDSKNAPVL TGIMRGIERE GLRIDRDGKL AQTPHPVALG SALTHPQITT DFSEALLEFI TPPTHRVEDL FKQLYDIQGY TLSKLDDELI WSSSMPCVLN DDATIPVAQY GSSNNGTMKT VYRVGLGHRY GRAMQTVAGL HYNFSLPDAF WSFLHREEYS LLDLQDFKDQ KYFALIRNFR RYYWLLVYLF GASPALCGSF IKGREHNLQP LIDERTLHLP YATSLRMGDL GYQSSAQESL YVCYNDKQSY ITTLCAAITT PIDEYKAIGL QDEKGEFKQL NTSLLQIENE FYSSIRPKRT AKHGETALSA LRNRGVEYIE VRCLDIDPFD PLGVNKPQVR FLDTFLLYCA LQDSPDTSPE ESANILRNQK TVVTEGRSPK ALIESFTKGK IPLKQAGEAL IKAMRPVAEL LDIAHETEEH TQSLETQLAA ILNPELTPSA RIISHLSAKK LPYAHYALAQ SRHHHETLLA KKPSNNTMQQ FEKMAAESLD KQTRLEQKNS GNFSEFLQEY YKQYQMCCDK //