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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)]

 GSHAB_STRA5             Reviewed;         750 AA.
Q8DXM9;
24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
25-OCT-2017, entry version 95.
RecName: Full=Glutathione biosynthesis bifunctional protein GshAB {ECO:0000255|HAMAP-Rule:MF_00782};
AltName: Full=Gamma-GCS-GS {ECO:0000255|HAMAP-Rule:MF_00782};
Short=GCS-GS {ECO:0000255|HAMAP-Rule:MF_00782};
Includes:
RecName: Full=Glutamate--cysteine ligase {ECO:0000255|HAMAP-Rule:MF_00782};
EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_00782};
AltName: Full=Gamma-ECS {ECO:0000255|HAMAP-Rule:MF_00782};
Short=GCS {ECO:0000255|HAMAP-Rule:MF_00782};
AltName: Full=Gamma-glutamylcysteine synthetase {ECO:0000255|HAMAP-Rule:MF_00782};
Includes:
RecName: Full=Glutathione synthetase {ECO:0000255|HAMAP-Rule:MF_00782};
EC=6.3.2.3 {ECO:0000255|HAMAP-Rule:MF_00782};
AltName: Full=GSH synthetase {ECO:0000255|HAMAP-Rule:MF_00782};
Short=GS {ECO:0000255|HAMAP-Rule:MF_00782};
Short=GSH-S {ECO:0000255|HAMAP-Rule:MF_00782};
Short=GSHase {ECO:0000255|HAMAP-Rule:MF_00782};
AltName: Full=Glutathione synthase {ECO:0000255|HAMAP-Rule:MF_00782};
Name=gshAB {ECO:0000255|HAMAP-Rule:MF_00782};
Synonyms=gshF {ECO:0000255|HAMAP-Rule:MF_00782};
OrderedLocusNames=SAG1821;
Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=208435;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-611 / 2603 V/R;
PubMed=12200547; DOI=10.1073/pnas.182380799;
Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R.,
Radune D., Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S.,
Carty H.A., Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M.,
Iacobini E.T., Brettoni C., Galli G., Mariani M., Vegni F., Maione D.,
Rinaudo D., Rappuoli R., Telford J.L., Kasper D.L., Grandi G.,
Fraser C.M.;
"Complete genome sequence and comparative genomic analysis of an
emerging human pathogen, serotype V Streptococcus agalactiae.";
Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
[2]
CHARACTERIZATION.
STRAIN=ATCC BAA-611 / 2603 V/R;
PubMed=15642737; DOI=10.1074/jbc.M414326200;
Janowiak B.E., Griffith O.W.;
"Glutathione synthesis in Streptococcus agalactiae. One protein
accounts for gamma-glutamylcysteine synthetase and glutathione
synthetase activities.";
J. Biol. Chem. 280:11829-11839(2005).
-!- FUNCTION: Synthesizes glutathione from L-glutamate and L-cysteine
via gamma-L-glutamyl-L-cysteine.
-!- CATALYTIC ACTIVITY: ATP + L-glutamate + L-cysteine = ADP +
phosphate + gamma-L-glutamyl-L-cysteine. {ECO:0000255|HAMAP-
Rule:MF_00782}.
-!- CATALYTIC ACTIVITY: ATP + gamma-L-glutamyl-L-cysteine + glycine =
ADP + phosphate + glutathione. {ECO:0000255|HAMAP-Rule:MF_00782}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 magnesium or manganese ions per subunit.
{ECO:0000250};
-!- ENZYME REGULATION: Inhibited by L-buthionine-S-sulfoximine (L-S-
BSO).
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=22 mM for L-glutamate;
KM=156 uM for L-cysteine;
KM=8.2 mM for alpha-L-aminobutyrate;
KM=64 uM for ATP (in the reaction with gamma-GCS);
KM=5.9 mM for gamma-L-glutamyl-L-cysteine;
KM=11.5 mM for gamma-L-glutamyl-L-alpha-aminobutyrate;
KM=6.3 mM for glycine;
KM=420 uM for ATP (in the reaction with GS);
-!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
from L-cysteine and L-glutamate: step 1/2. {ECO:0000255|HAMAP-
Rule:MF_00782}.
-!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
from L-cysteine and L-glutamate: step 2/2. {ECO:0000255|HAMAP-
Rule:MF_00782}.
-!- SUBUNIT: Monomer. {ECO:0000305}.
-!- SIMILARITY: In the N-terminal section; belongs to the glutamate--
cysteine ligase type 1 family. Type 2 subfamily.
{ECO:0000255|HAMAP-Rule:MF_00782}.
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EMBL; AE009948; AAN00684.1; -; Genomic_DNA.
RefSeq; NP_688811.1; NC_004116.1.
RefSeq; WP_000582678.1; NC_004116.1.
PDB; 3LN6; X-ray; 2.95 A; A=1-750.
PDBsum; 3LN6; -.
ProteinModelPortal; Q8DXM9; -.
SMR; Q8DXM9; -.
EnsemblBacteria; AAN00684; AAN00684; SAG1821.
GeneID; 1014630; -.
KEGG; sag:SAG1821; -.
PATRIC; fig|208435.3.peg.1829; -.
HOGENOM; HOG000156471; -.
KO; K01919; -.
OMA; EANFNPM; -.
BRENDA; 6.3.2.3; 5917.
SABIO-RK; Q8DXM9; -.
UniPathway; UPA00142; UER00209.
UniPathway; UPA00142; UER00210.
Proteomes; UP000000821; Chromosome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-EC.
GO; GO:0004363; F:glutathione synthase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
Gene3D; 3.30.1490.20; -; 1.
HAMAP; MF_00782; Glut_biosynth; 1.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
InterPro; IPR007370; Glu_cys_ligase.
InterPro; IPR006335; Glut_biosynth.
InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
Pfam; PF01071; GARS_A; 1.
Pfam; PF04262; Glu_cys_ligase; 1.
SUPFAM; SSF55931; SSF55931; 1.
TIGRFAMs; TIGR01435; glu_cys_lig_rel; 1.
PROSITE; PS50975; ATP_GRASP; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome;
Glutathione biosynthesis; Ligase; Magnesium; Manganese; Metal-binding;
Multifunctional enzyme; Nucleotide-binding; Reference proteome.
CHAIN 1 750 Glutathione biosynthesis bifunctional
protein GshAB.
/FTId=PRO_0000192559.
DOMAIN 489 747 ATP-grasp. {ECO:0000255|HAMAP-
Rule:MF_00782}.
NP_BIND 516 574 ATP. {ECO:0000255|HAMAP-Rule:MF_00782}.
REGION 1 333 Glutamate--cysteine ligase.
METAL 696 696 Magnesium or manganese 1.
{ECO:0000255|HAMAP-Rule:MF_00782}.
METAL 717 717 Magnesium or manganese 1.
{ECO:0000255|HAMAP-Rule:MF_00782}.
METAL 717 717 Magnesium or manganese 2.
{ECO:0000255|HAMAP-Rule:MF_00782}.
METAL 719 719 Magnesium or manganese 2.
{ECO:0000255|HAMAP-Rule:MF_00782}.
HELIX 7 9 {ECO:0000244|PDB:3LN6}.
STRAND 19 31 {ECO:0000244|PDB:3LN6}.
TURN 32 35 {ECO:0000244|PDB:3LN6}.
STRAND 44 46 {ECO:0000244|PDB:3LN6}.
TURN 49 51 {ECO:0000244|PDB:3LN6}.
STRAND 53 67 {ECO:0000244|PDB:3LN6}.
STRAND 71 73 {ECO:0000244|PDB:3LN6}.
HELIX 74 91 {ECO:0000244|PDB:3LN6}.
STRAND 96 98 {ECO:0000244|PDB:3LN6}.
STRAND 101 103 {ECO:0000244|PDB:3LN6}.
TURN 109 111 {ECO:0000244|PDB:3LN6}.
HELIX 120 133 {ECO:0000244|PDB:3LN6}.
HELIX 136 139 {ECO:0000244|PDB:3LN6}.
STRAND 143 149 {ECO:0000244|PDB:3LN6}.
HELIX 151 161 {ECO:0000244|PDB:3LN6}.
HELIX 166 191 {ECO:0000244|PDB:3LN6}.
STRAND 199 201 {ECO:0000244|PDB:3LN6}.
TURN 206 208 {ECO:0000244|PDB:3LN6}.
STRAND 212 214 {ECO:0000244|PDB:3LN6}.
STRAND 217 221 {ECO:0000244|PDB:3LN6}.
HELIX 234 243 {ECO:0000244|PDB:3LN6}.
TURN 246 248 {ECO:0000244|PDB:3LN6}.
HELIX 253 255 {ECO:0000244|PDB:3LN6}.
STRAND 259 264 {ECO:0000244|PDB:3LN6}.
TURN 268 274 {ECO:0000244|PDB:3LN6}.
STRAND 278 281 {ECO:0000244|PDB:3LN6}.
HELIX 296 311 {ECO:0000244|PDB:3LN6}.
HELIX 318 334 {ECO:0000244|PDB:3LN6}.
HELIX 347 361 {ECO:0000244|PDB:3LN6}.
HELIX 365 379 {ECO:0000244|PDB:3LN6}.
HELIX 381 383 {ECO:0000244|PDB:3LN6}.
HELIX 385 392 {ECO:0000244|PDB:3LN6}.
HELIX 399 413 {ECO:0000244|PDB:3LN6}.
HELIX 421 423 {ECO:0000244|PDB:3LN6}.
HELIX 428 440 {ECO:0000244|PDB:3LN6}.
STRAND 443 447 {ECO:0000244|PDB:3LN6}.
STRAND 449 451 {ECO:0000244|PDB:3LN6}.
STRAND 453 458 {ECO:0000244|PDB:3LN6}.
STRAND 461 466 {ECO:0000244|PDB:3LN6}.
TURN 467 469 {ECO:0000244|PDB:3LN6}.
HELIX 477 481 {ECO:0000244|PDB:3LN6}.
TURN 482 484 {ECO:0000244|PDB:3LN6}.
HELIX 486 494 {ECO:0000244|PDB:3LN6}.
TURN 507 510 {ECO:0000244|PDB:3LN6}.
HELIX 511 517 {ECO:0000244|PDB:3LN6}.
STRAND 518 521 {ECO:0000244|PDB:3LN6}.
STRAND 523 527 {ECO:0000244|PDB:3LN6}.
STRAND 532 535 {ECO:0000244|PDB:3LN6}.
STRAND 537 541 {ECO:0000244|PDB:3LN6}.
HELIX 545 558 {ECO:0000244|PDB:3LN6}.
STRAND 560 566 {ECO:0000244|PDB:3LN6}.
STRAND 570 578 {ECO:0000244|PDB:3LN6}.
STRAND 581 589 {ECO:0000244|PDB:3LN6}.
STRAND 592 594 {ECO:0000244|PDB:3LN6}.
HELIX 601 608 {ECO:0000244|PDB:3LN6}.
STRAND 614 618 {ECO:0000244|PDB:3LN6}.
STRAND 621 623 {ECO:0000244|PDB:3LN6}.
HELIX 629 637 {ECO:0000244|PDB:3LN6}.
STRAND 651 654 {ECO:0000244|PDB:3LN6}.
TURN 660 663 {ECO:0000244|PDB:3LN6}.
STRAND 665 668 {ECO:0000244|PDB:3LN6}.
TURN 670 672 {ECO:0000244|PDB:3LN6}.
HELIX 675 687 {ECO:0000244|PDB:3LN6}.
STRAND 694 700 {ECO:0000244|PDB:3LN6}.
STRAND 702 704 {ECO:0000244|PDB:3LN6}.
TURN 708 711 {ECO:0000244|PDB:3LN6}.
STRAND 714 721 {ECO:0000244|PDB:3LN6}.
HELIX 725 728 {ECO:0000244|PDB:3LN6}.
STRAND 731 733 {ECO:0000244|PDB:3LN6}.
HELIX 739 746 {ECO:0000244|PDB:3LN6}.
SEQUENCE 750 AA; 85603 MW; 97829C2C5B44174A CRC64;
MIIDRLLQRS HSHLPILQAT FGLERESLRI HQPTQRVAQT PHPKTLGSRN YHPYIQTDYS
EPQLELITPI AKDSQEAIRF LKAISDVAGR SINHDEYLWP LSMPPKVREE DIQIAQLEDA
FEYDYRKYLE KTYGKLIQSI SGIHYNLGLG QELLTSLFEL SQADNAIDFQ NQLYMKLSQN
FLRYRWLLTY LYGASPVAEE DFLDQKLNNP VRSLRNSHLG YVNHKDIRIS YTSLKDYVND
LENAVKSGQL IAEKEFYSPV RLRGSKACRN YLEKGITYLE FRTFDLNPFS PIGITQETVD
TVHLFLLALL WIDSSSHIDQ DIKEANRLND LIALSHPLEK LPNQAPVSDL VDAMQSVIQH
FNLSPYYQDL LESVKRQIQS PELTVAGQLL EMIEGLSLET FGQRQGQIYH DYAWEAPYAL
KGYETMELST QLLLFDVIQK GVNFEVLDEQ DQFLKLWHNS HIEYVKNGNM TSKDNYIVPL
AMANKVVTKK ILDEKHFPTP FGDEFTDRKE ALNYFSQIQD KPIVVKPKST NFGLGISIFK
TSANLASYEK AIDIAFTEDS AILVEEYIEG TEYRFFVLEG DCIAVLLRVA ANVVGDGIHT
ISQLVKLKNQ NPLRGYDHRS PLEVIELGEV EQLMLEQQGY TVNSIPPEGT KIELRRNSNI
STGGDSIDVT NTMDPTYKQL AAEMAEAMGA WVCGVDLIIP NATQAYSKDK KNATCIELNF
NPLMYMHTYC QEGPGQSITP RILAKLFPEL


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