ID   GSH1_TOBAC              Reviewed;         522 AA.
AC   Q1W2L8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   16-JUN-2009, entry version 18.
DE   RecName: Full=Glutamate--cysteine ligase, chloroplastic;
DE            EC=6.3.2.2;
DE   AltName: Full=Gamma-glutamylcysteine synthetase;
DE   AltName: Full=Gamma-ECS;
DE            Short=GCS;
DE   Flags: Precursor;
GN   Name=GSH1;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Gromes R., Rausch T.;
RT   "Regulation of plant and bacterial gamma-glutamylcysteine
RT   synthetase.";
RL   Submitted (AUG-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   -!- SUBUNIT: Homodimer or monomer when oxidized or reduced,
CC       respectively (By similarity).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast (By similarity).
CC   -!- PTM: The Cys-186-Cys-406 disulfide bridge is known to modulate the
CC       enzyme activity according to the redox status. The oxidized form
CC       constitutes the active enzyme (By similarity).
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2
CC       family.
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DR   EMBL; DQ444219; ABD98695.2; -; mRNA.
DR   SMR; Q1W2L8; 87-522.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:EC.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006336; GCS2.
DR   InterPro; IPR011556; Glut_cys_lig_pln.
DR   Pfam; PF04107; GCS2; 1.
DR   TIGRFAMs; TIGR01436; glu_cys_lig_pln; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chloroplast; Disulfide bond; Glutathione biosynthesis;
KW   Ligase; Nucleotide-binding; Plastid; Transit peptide.
FT   TRANSIT       1     45       Chloroplast (Potential).
FT   CHAIN        46    522       Glutamate--cysteine ligase,
FT                                chloroplastic.
FT                                /FTId=PRO_0000333025.
FT   DISULFID    186    406       By similarity.
SQ   SEQUENCE   522 AA;  58962 MW;  590EBC7DE01FEEDC CRC64;
     MALMSQAGSS HCIYSEKMKC ISGHSSITSN MEMLKMKDIC FGNISSRNSS KPMQGIYLDR
     VGVERRRGRL AIVAASPPTE DAVVAAEPLT KEDLVAYLAS GCKSKEKWRI GTEHEKFGFE
     FGTLRPMKYE QIAELLNGIA ERFDWEKVME GDNIIGLKQG KQSISLEPGG QFELSGAPLE
     TLHQTCAEVN SHLYQVKAVA EEMGIGFLGT GFQPKWGLKD IPVMPKGRYE IMRNYMPKVG
     SLGLDMMFRT CTVQVNLDFS SEADMIRKFR AGLALQPIAT ALFANSPFTE GKPNGYLSMR
     SHIWTDTDNN RAGMLPFVFD DSFGFEQYVD YALDVPMYFV YRKKKYIDCA GMSFRDFMNG
     KLSPIPGDYP TLNDWENHLT TIFPEVRLKR YLEMRGADGG PWRRLCALPA FWVGILYDEV
     SLQTVLDMTS DWTAEEREML RNKVPTSGLK TPFRDGLLKH VAQDVVKLAK EGLERRGYKE
     TGFLNEVTEV VRTGVTPAEK LLELYHGKWG RSVDPVFEEL LY
//