(data stored in ACNUC7421 zone)

SWISSPROT: GCS22_LEGPC

ID   GCS22_LEGPC             Reviewed;         373 AA.
AC   A5IGU3;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   11-DEC-2019, entry version 64.
DE   RecName: Full=Putative glutamate--cysteine ligase 2-2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE   AltName: Full=Gamma-glutamylcysteine synthetase 2-2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=GCS 2-2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=Gamma-GCS 2-2 {ECO:0000255|HAMAP-Rule:MF_01609};
GN   OrderedLocusNames=LPC_2680;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits weak
CC       glutamate--cysteine ligase activity. {ECO:0000255|HAMAP-Rule:MF_01609}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-cysteine + L-glutamate = ADP + H(+) + L-gamma-
CC         glutamyl-L-cysteine + phosphate; Xref=Rhea:RHEA:13285,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:43474, ChEBI:CHEBI:58173,
CC         ChEBI:CHEBI:456216; EC=6.3.2.2; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01609};
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family.
CC       YbdK subfamily. {ECO:0000255|HAMAP-Rule:MF_01609}.
DR   EMBL; CP000675; ABQ56593.1; -; Genomic_DNA.
DR   RefSeq; WP_011945778.1; NC_009494.2.
DR   SMR; A5IGU3; -.
DR   EnsemblBacteria; ABQ56593; ABQ56593; LPC_2680.
DR   KEGG; lpc:LPC_2680; -.
DR   HOGENOM; HOG000220942; -.
DR   KO; K06048; -.
DR   OMA; LIFGLHV; -.
DR   BioCyc; LPNE400673:LPC_RS03535-MONOMER; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042398; P:cellular modified amino acid biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_01609; Glu_cys_ligase_2; 1.
DR   InterPro; IPR006336; GCS2.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR011793; YbdK.
DR   Pfam; PF04107; GCS2; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   TIGRFAMs; TIGR02050; gshA_cyan_rel; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5IGU3.
DR   SWISS-2DPAGE; A5IGU3.
KW   ATP-binding; Ligase; Nucleotide-binding.
FT   CHAIN           1..373
FT                   /note="Putative glutamate--cysteine ligase 2-2"
FT                   /id="PRO_0000323503"
SQ   SEQUENCE   373 AA;  42911 MW;  7DDD697FD9394FA5 CRC64;
     MPLQPFKTSN LLTMGVELEL QLISLSNFDL TAASPDILEL LGRSSFPGSF TPEITESMLE
     IATDVHEEYD QLLKQLFHIR DALVTVGDRL NIGICGGGTH PFQMWSDQRI FNKTRFIEVS
     ELYGYLTKQF TIFGQHIHIG CEDGNQALFL LHSLNRYIPH FIALSASSPF VQSKDTLYNS
     ARLNSVFAFP LSGRAPFVLN WDEFSLGYFE KMEHTGIVKS MKDFYWDLRP KPEFGTIEMR
     VCDSPLTVER AAALACYMQA LCSYLLENKE PLPHEDDYLV YNYNRFQACR FGLDGTLVHP
     KTYEQILLRE DILTTLRRLK PYANQLNSTM ALEHIYEITH KGSDASFLRE KYAEHRTLES
     VVNESLKQFR RSK
//

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