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Database: UniProt/TrEMBL
Entry: C6AKC8_AGGAN
LinkDB: C6AKC8_AGGAN
Original site: C6AKC8_AGGAN 
ID   C6AKC8_AGGAN            Unreviewed;       757 AA.
AC   C6AKC8;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   01-MAY-2013, entry version 30.
DE   RecName: Full=Glutathione biosynthesis bifunctional protein GshAB;
DE   AltName: Full=Gamma-GCS-GS;
GN   Name=gshAB; Synonyms=gshF; OrderedLocusNames=NT05HA_0176;
OS   Aggregatibacter aphrophilus (strain NJ8700) (Haemophilus aphrophilus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Aggregatibacter.
OX   NCBI_TaxID=634176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJ8700;
RX   PubMed=19447908; DOI=10.1128/JB.00447-09;
RA   Di Bonaventura M.P., DeSalle R., Pop M., Nagarajan N., Figurski D.H.,
RA   Fine D.H., Kaplan J.B., Planet P.J.;
RT   "Complete genome sequence of Aggregatibacter (Haemophilus) aphrophilus
RT   NJ8700.";
RL   J. Bacteriol. 191:4693-4694(2009).
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   -!- 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; CP001607; ACS96614.1; -; Genomic_DNA.
DR   RefSeq; YP_003006701.1; NC_012913.1.
DR   STRING; 634176.NT05HA_0176; -.
DR   EnsemblBacteria; ACS96614; ACS96614; NT05HA_0176.
DR   GeneID; 8121538; -.
DR   KEGG; aap:NT05HA_0176; -.
DR   PATRIC; 31915474; VBIAggAph86045_0170.
DR   eggNOG; COG1181; -.
DR   HOGENOM; HOG000156471; -.
DR   KO; K01919; -.
DR   OMA; PYIQTDF; -.
DR   ProtClustDB; PRK02471; -.
DR   BioCyc; AAPH634176:GHVL-173-MONOMER; -.
DR   UniPathway; UPA00142; UER00209.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:HAMAP.
DR   GO; GO:0004363; F:glutathione synthase activity; IEA:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR   Gene3D; 3.30.470.20; -; 2.
DR   HAMAP; MF_00782; Glut_biosynth; 1; -.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR007370; Glu_cys_ligase.
DR   InterPro; IPR006335; Glut_cys-rel.
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;  85093 MW;  0EA68ECF97BA7512 CRC64;
     MNIQQVIKEN RLELLFQQGS FGIEKESQRV HADGSIVVTE HPKCFGSRSY HPYIQTDFAE
     SQLELITPPN KKIEDSLRWL SAIHEVVLCS LPEDEFIFPL SMPAGLPPED QIKVAQLENP
     ADVAYREHLV ASYGKNKQMV SGIHYNFQLE PTFIQQLFAQ QNTYQSAVDF QNDLYLKVAR
     NFLRYQWILV YLLAATPTVD ANYFRHGTPL KAGQYVRSLR SSQYGYVNDP SVKVSYDSLN
     DYVKTLEHAV SSGQLIAEKE FYSNVRLRGA KHARELLQNG IQYLEFRLFD LNPFEAYGIA
     LNDAKFVHYF ILLMAWLDEE SLASAVDLGK EKLAQVAWEN PLSATAFQAE GERILQQLLA
     MLTEINADVE IEAIVKDKLV QFAEPSQTLG ARLVKAIEAH GGYQKLGAEL AIRYKQRAFE
     RFYALSAFDN MELSTQALMF DAIQKGLKME ILDERDQFLS LQFGDHLEYV KNGNMTSHDS
     YISPLIMENK VVTKKVLAKA GFNVPQSVEF TSVEQAVANY ALFAGRAVVI KPKSTNYGLG
     ISIFQQGVHD REDFAKAIEI AFREDKEVMV EDYLTGTEYR FFVLGDETLA VLLRVPANVI
     GDSVHTVAEL VAQKNDHPLR GDGSRTPLKK IALGDIEQLQ LKEQGLTVDS VPAKDQLVQL
     RANSNISTGG DSIDMTDQMH PSYKALAVGI TKAMGAAVCG VDLIIPDLTK PAEPSLQSWG
     VIEANFNPMM MMHIFPYAGQ SRRVTQNVLK MLFPELK
//
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