ID B0BR08_ACTPJ Unreviewed; 757 AA.
AC B0BR08;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 19-FEB-2014, entry version 43.
DE RecName: Full=Glutathione biosynthesis bifunctional protein GshAB;
DE AltName: Full=Gamma-GCS-GS;
GN Name=gshA; Synonyms=gshAB, gshF; OrderedLocusNames=APJL_1439;
OS Actinobacillus pleuropneumoniae serotype 3 (strain JL03).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=434271;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JL03;
RX PubMed=18197260; DOI=10.1371/journal.pone.0001450;
RA Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K.,
RA Li W., Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y.,
RA Zhang L., Xu T., Zheng H., Pu S., Wang B., Gu W., Zhang X.L.,
RA Zhu G.F., Wang S., Zhao G.P., Chen H.;
RT "Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of
RT serotype 3 prevalent in China.";
RL PLoS ONE 3:E1450-E1450(2008).
CC -!- FUNCTION: Synthesizes glutathione from L-glutamate and L-cysteine
CC via gamma-L-glutamyl-L-cysteine (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + L-cysteine = ADP +
CC phosphate + gamma-L-glutamyl-L-cysteine.
CC -!- CATALYTIC ACTIVITY: ATP + gamma-L-glutamyl-L-cysteine + glycine =
CC ADP + phosphate + glutathione.
CC -!- COFACTOR: Binds 2 magnesium or manganese ions per subunit (By
CC similarity).
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
CC from L-cysteine and L-glutamate: step 1/2.
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
CC from L-cysteine and L-glutamate: step 2/2.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SIMILARITY: Contains 1 ATP-grasp domain.
CC -!- SIMILARITY: In the N-terminal section; belongs to the glutamate--
CC cysteine ligase type 1 family. Type 2 subfamily.
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DR EMBL; CP000687; ABY69993.1; -; Genomic_DNA.
DR RefSeq; YP_001652437.1; NC_010278.1.
DR ProteinModelPortal; B0BR08; -.
DR STRING; 434271.APJL_1439; -.
DR EnsemblBacteria; ABY69993; ABY69993; APJL_1439.
DR GeneID; 5851148; -.
DR KEGG; apj:APJL_1439; -.
DR PATRIC; 20752160; VBIActPle136345_1431.
DR eggNOG; COG1181; -.
DR HOGENOM; HOG000156471; -.
DR KO; K01919; -.
DR OMA; PYIQTDF; -.
DR OrthoDB; EOG6BKJ7H; -.
DR ProtClustDB; PRK02471; -.
DR BioCyc; APLE434271:GIX7-1459-MONOMER; -.
DR UniPathway; UPA00142; UER00209.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-HAMAP.
DR GO; GO:0004363; F:glutathione synthase activity; IEA:UniProtKB-HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.30.470.20; -; 3.
DR HAMAP; MF_00782; Glut_biosynth; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR013816; ATP_grasp_subdomain_2.
DR InterPro; IPR007370; Glu_cys_ligase.
DR InterPro; IPR006335; Glut_biosynth.
DR Pfam; PF04262; Glu_cys_ligase; 1.
DR TIGRFAMs; TIGR01435; glu_cys_lig_rel; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Glutathione biosynthesis; Ligase;
KW Magnesium; Manganese; Metal-binding; Multifunctional enzyme;
KW Nucleotide-binding.
FT DOMAIN 494 753 ATP-grasp (By similarity).
FT NP_BIND 521 580 ATP (By similarity).
FT REGION 1 337 Glutamate--cysteine ligase (By
FT similarity).
FT METAL 702 702 Magnesium or manganese 1 (By similarity).
FT METAL 723 723 Magnesium or manganese 1 (By similarity).
FT METAL 723 723 Magnesium or manganese 2 (By similarity).
FT METAL 725 725 Magnesium or manganese 2 (By similarity).
SQ SEQUENCE 757 AA; 85384 MW; C13B124E7E70A8D0 CRC64;
MKLQQLIKTH HLGLLFQQGK FGIEKESQRI DNKGNIVTTA HPSVFGNRSY HPYIQTDFAE
SQLELITPPN DKLENTYRWL SAIHEVTLRS LPDDEYIFPF SMPAGLPPES EIKEAQLDNE
WDVKYREHLS AIYGKYKQMV SGIHYNFQIS DEFVESAFAL QTEYPNKIAF RNALYMKLAN
NFLRYQWILV YLLAATPTVE AQYFGENRPL AEGQLVRSLR SGPYGYVNAP HIVINHDSLQ
QYVESLEHFV ATGDLLAEKE FYSNVRLRGA KKARELLEKG VKYAEFRLFD LNPFSPYGIE
LADAKFIHLF LLAMLWMDET SGQREVEIGT QKLYQVALED PRSHTAFQAE GEAILNLMLA
MLDDLSVPQN EKDLLQQKLA QFADPSQTVN GRLLAAIEQA GSYKALGAQL AQQYKAQAFE
RFYAISAFDN MELSTQALLF DAIQQGLQIE LLDENDQFLA LKFGDHLEYV KNGNMTSHDQ
YISPLIMENK VVTKKVLAKA GFNVPKSIEF TSVEQAVAHY PLFEGKAMVI KPKSTNYGLG
ITIFQQGVTD KADFAKAIEI AFREDKEVMV EDYLVGTEYR FFVLGDETLA VLLRVPANVK
GDGIHTVREL VEAKNSDPLR GDGSRSPLKK IALGDIELLQ LKEQGLTPDS IPADGQIVQL
RANSNISTGG DSIDMTDQMH DSYKQLAVGI AKEMGAKVCG VDLIIPDLTK AAEPSLRSWG
VIEANFNPMM MMHIFPYQGK SRRLTKAVLK MLFPELP
//
