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Database: UniProt/TrEMBL
Entry: B0BR08_ACTPJ
LinkDB: B0BR08_ACTPJ
Original site: B0BR08_ACTPJ 
ID   B0BR08_ACTPJ            Unreviewed;       757 AA.
AC   B0BR08;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   26-NOV-2014, entry version 50.
DE   RecName: Full=Glutathione biosynthesis bifunctional protein GshAB {ECO:0000256|HAMAP-Rule:MF_00782};
DE   AltName: Full=Gamma-GCS-GS {ECO:0000256|HAMAP-Rule:MF_00782};
GN   Name=gshA {ECO:0000313|EMBL:ABY69993.1};
GN   Synonyms=gshAB {ECO:0000256|HAMAP-Rule:MF_00782}, gshF
GN   {ECO:0000256|HAMAP-Rule:MF_00782};
GN   OrderedLocusNames=APJL_1439 {ECO:0000313|EMBL:ABY69993.1};
OS   Actinobacillus pleuropneumoniae serotype 3 (strain JL03).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=434271 {ECO:0000313|EMBL:ABY69993.1, ECO:0000313|Proteomes:UP000008547};
RN   [1] {ECO:0000313|EMBL:ABY69993.1, ECO:0000313|Proteomes:UP000008547}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JL03 {ECO:0000313|EMBL:ABY69993.1,
RC   ECO:0000313|Proteomes:UP000008547};
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. {ECO:0000256|HAMAP-
CC       Rule:MF_00782}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + L-cysteine = ADP +
CC       phosphate + gamma-L-glutamyl-L-cysteine. {ECO:0000256|HAMAP-
CC       Rule:MF_00782}.
CC   -!- CATALYTIC ACTIVITY: ATP + gamma-L-glutamyl-L-cysteine + glycine =
CC       ADP + phosphate + glutathione. {ECO:0000256|HAMAP-Rule:MF_00782}.
CC   -!- COFACTOR:
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_00782};
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
CC       from L-cysteine and L-glutamate: step 1/2. {ECO:0000256|HAMAP-
CC       Rule:MF_00782}.
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
CC       from L-cysteine and L-glutamate: step 2/2. {ECO:0000256|HAMAP-
CC       Rule:MF_00782}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00782}.
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000256|HAMAP-
CC       Rule:MF_00782}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the glutamate--
CC       cysteine ligase type 1 family. Type 2 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00782}.
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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; WMDETSS; -.
DR   OrthoDB; EOG6BKJ7H; -.
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 {ECO:0000256|HAMAP-Rule:MF_00782};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008547};
KW   Glutathione biosynthesis {ECO:0000256|HAMAP-Rule:MF_00782};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00782};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00782};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_00782};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00782};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00782};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00782}.
FT   DOMAIN      494    753       ATP-grasp. {ECO:0000256|HAMAP-Rule:
FT                                MF_00782}.
FT   NP_BIND     521    580       ATP. {ECO:0000256|HAMAP-Rule:MF_00782}.
FT   REGION        1    337       Glutamate--cysteine ligase.
FT                                {ECO:0000256|HAMAP-Rule:MF_00782}.
FT   METAL       702    702       Magnesium or manganese 1.
FT                                {ECO:0000256|HAMAP-Rule:MF_00782}.
FT   METAL       723    723       Magnesium or manganese 1.
FT                                {ECO:0000256|HAMAP-Rule:MF_00782}.
FT   METAL       723    723       Magnesium or manganese 2.
FT                                {ECO:0000256|HAMAP-Rule:MF_00782}.
FT   METAL       725    725       Magnesium or manganese 2.
FT                                {ECO:0000256|HAMAP-Rule:MF_00782}.
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
//
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