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Glutathione biosynthesis bifunctional protein GshAB (Gamma-GCS-GS) (GCS-GS) [Includes: Glutamate--cysteine ligase (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase); Glutathione synthetase (EC 6.3.2.3) (GSH synthetase) (GS) (GSH-S) (GSHase) (Glutathione synthase)]

 A0A0A3IXG2_9BACI        Unreviewed;       754 AA.
A0A0A3IXG2;
04-FEB-2015, integrated into UniProtKB/TrEMBL.
04-FEB-2015, sequence version 1.
08-MAY-2019, entry version 37.
RecName: Full=Glutathione biosynthesis bifunctional protein GshAB {ECO:0000256|HAMAP-Rule:MF_00782};
AltName: Full=Gamma-GCS-GS {ECO:0000256|HAMAP-Rule:MF_00782};
Short=GCS-GS {ECO:0000256|HAMAP-Rule:MF_00782};
Includes:
RecName: Full=Glutamate--cysteine ligase {ECO:0000256|HAMAP-Rule:MF_00782};
EC=6.3.2.2 {ECO:0000256|HAMAP-Rule:MF_00782};
AltName: Full=Gamma-glutamylcysteine synthetase {ECO:0000256|HAMAP-Rule:MF_00782};
AltName: Full=Gamma-ECS {ECO:0000256|HAMAP-Rule:MF_00782};
Short=GCS {ECO:0000256|HAMAP-Rule:MF_00782};
Includes:
RecName: Full=Glutathione synthetase {ECO:0000256|HAMAP-Rule:MF_00782};
EC=6.3.2.3 {ECO:0000256|HAMAP-Rule:MF_00782};
AltName: Full=Glutathione synthase {ECO:0000256|HAMAP-Rule:MF_00782};
AltName: Full=GSH synthetase {ECO:0000256|HAMAP-Rule:MF_00782};
Short=GS {ECO:0000256|HAMAP-Rule:MF_00782};
Short=GSH-S {ECO:0000256|HAMAP-Rule:MF_00782};
Short=GSHase {ECO:0000256|HAMAP-Rule:MF_00782};
Name=gshAB {ECO:0000256|HAMAP-Rule:MF_00782};
Synonyms=gshF {ECO:0000256|HAMAP-Rule:MF_00782};
ORFNames=CD30_17105 {ECO:0000313|EMBL:KGR89381.1};
Lysinibacillus massiliensis 4400831 = CIP 108448 = CCUG 49529.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae;
Lysinibacillus.
NCBI_TaxID=1211035 {ECO:0000313|EMBL:KGR89381.1, ECO:0000313|Proteomes:UP000030595};
[1] {ECO:0000313|EMBL:KGR89381.1, ECO:0000313|Proteomes:UP000030595}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CCUG 49529 {ECO:0000313|EMBL:KGR89381.1,
ECO:0000313|Proteomes:UP000030595};
Zhang F., Wang G., Zhang L.;
"Draft genome sequence of Lysinibacillus massiliensis CCUG 49529.";
Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Synthesizes glutathione from L-glutamate and L-cysteine
via gamma-L-glutamyl-L-cysteine. {ECO:0000256|HAMAP-
Rule:MF_00782}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-cysteine + L-glutamate = ADP + H(+) + L-gamma-
glutamyl-L-cysteine + phosphate; Xref=Rhea:RHEA:13285,
ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
ChEBI:CHEBI:35235, ChEBI:CHEBI:43474, ChEBI:CHEBI:58173,
ChEBI:CHEBI:456216; EC=6.3.2.2; Evidence={ECO:0000256|HAMAP-
Rule:MF_00782, ECO:0000256|SAAS:SAAS01123335};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + glycine + L-gamma-glutamyl-L-cysteine = ADP +
glutathione + H(+) + phosphate; Xref=Rhea:RHEA:13557,
ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
ChEBI:CHEBI:57305, ChEBI:CHEBI:57925, ChEBI:CHEBI:58173,
ChEBI:CHEBI:456216; EC=6.3.2.3; Evidence={ECO:0000256|HAMAP-
Rule:MF_00782};
-!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
from L-cysteine and L-glutamate: step 1/2. {ECO:0000256|HAMAP-
Rule:MF_00782, ECO:0000256|SAAS:SAAS01089095}.
-!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
from L-cysteine and L-glutamate: step 2/2. {ECO:0000256|HAMAP-
Rule:MF_00782}.
-!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00782}.
-!- SIMILARITY: In the N-terminal section; belongs to the glutamate--
cysteine ligase type 1 family. Type 2 subfamily.
{ECO:0000256|HAMAP-Rule:MF_00782}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KGR89381.1}.
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EMBL; JPVQ01000048; KGR89381.1; -; Genomic_DNA.
RefSeq; WP_036179340.1; NZ_JPVQ01000048.1.
STRING; 1211035.CD30_17105; -.
EnsemblBacteria; KGR89381; KGR89381; CD30_17105.
OrthoDB; 250578at2; -.
UniPathway; UPA00142; UER00209.
UniPathway; UPA00142; UER00210.
Proteomes; UP000030595; Unassembled WGS sequence.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro.
GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-UniRule.
GO; GO:0004363; F:glutathione synthase activity; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:InterPro.
Gene3D; 3.30.1490.20; -; 1.
HAMAP; MF_00782; Glut_biosynth; 1.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR011095; Dala_Dala_lig_C.
InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
InterPro; IPR007370; Glu_cys_ligase.
InterPro; IPR006335; Glut_biosynth.
InterPro; IPR006334; Glut_cys_ligase.
InterPro; IPR040657; GshAB_ATP-grasp.
PANTHER; PTHR38761; PTHR38761; 1.
Pfam; PF18419; ATP-grasp_6; 1.
Pfam; PF07478; Dala_Dala_lig_C; 1.
Pfam; PF04262; Glu_cys_ligase; 1.
SUPFAM; SSF55931; SSF55931; 1.
TIGRFAMs; TIGR01435; glu_cys_lig_rel; 1.
PROSITE; PS50975; ATP_GRASP; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00782, ECO:0000256|PROSITE-
ProRule:PRU00409, ECO:0000256|SAAS:SAAS01089093};
Complete proteome {ECO:0000313|Proteomes:UP000030595};
Glutathione biosynthesis {ECO:0000256|HAMAP-Rule:MF_00782,
ECO:0000256|SAAS:SAAS01089077};
Ligase {ECO:0000256|HAMAP-Rule:MF_00782,
ECO:0000256|SAAS:SAAS01089084, ECO:0000313|EMBL:KGR89381.1};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00782};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00782,
ECO:0000256|PROSITE-ProRule:PRU00409, ECO:0000256|SAAS:SAAS01089093};
Reference proteome {ECO:0000313|Proteomes:UP000030595}.
DOMAIN 491 748 ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
REGION 1 336 Glutamate--cysteine ligase.
{ECO:0000256|HAMAP-Rule:MF_00782}.
SEQUENCE 754 AA; 87148 MW; E4462528CC65D5B9 CRC64;
MDIKKMLVND HVKPYLLNAR YGIEKESNRV DLSGNLAKTD HPKSISLRDE HPYIQRDFSE
LQMEIITPVS NTLEELFNYL AAIHDVAYRS MGKNEMLWPL SMPPQLPEKE ENIVIAKLKN
VENVLYRQTL SDTYGRRKQM ICGVHFNFEF GDELIRALFN AQSEIKDFHH FKTEIYLKAT
RNYIHYRWLV TYFYGASPSS EKNFFEEDSL NGPVRSIRNS KYGYTNSAGV EVSYSSIQNY
LSDLSLMVKR GLLSKEKEFY SPVRLRGGQQ VSDLAVHGIN YIELRNIDLN PFETYGVSYE
QAEFLHLFLI YLLWKDEGEN CDEWVKMGDY YNDVVALEHP LEHTKFKKDA ENMIDEMEHL
VQILDLPISD TLFIHLREML MDPSKTLAGR LYKESGKSSQ CQVATSIAKE NYKKSWDKPY
QLTGFTDMEL STQILMFDAI QQGIQVEILD RQDQFLKLKL KDHVEYVKNG NMTSVDNYVS
TLIMENKTVT KKILHQHAFR VPKGEEFQTI EQALRSYDFF STKPFVVKPK TTNYGLGISI
FKEGANEEDY HKAITLAFKE DNTILIEEFI KGTEYRFFVI NDQVYAVLLR IPANVKGDGK
HTIQELVNQK NNDSLRGSDH RTPLERIQLG ELEKLMLKGQ GYQIDSIPKK DEIIFLRENS
NISTGGDSID VTDQIPDDYK KIAVDAVAAL GAKICGIDLI IEDTNVPATN KNAYGIIEAN
FNPSMYMHIY PYKGKSRRLT MHIIHYLFPE LLQS


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