ID   GCS2_BDEBA              Reviewed;         378 AA.
AC   Q6MKW4;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Putative glutamate--cysteine ligase 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 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=GCS 2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=Gamma-GCS 2 {ECO:0000255|HAMAP-Rule:MF_01609};
GN   OrderedLocusNames=Bd2263;
OS   Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS   HD100).
OC   Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC   Bdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=264462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX   PubMed=14752164; DOI=10.1126/science.1093027;
RA   Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA   Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA   Schuster S.C.;
RT   "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT   genomic perspective.";
RL   Science 303:689-692(2004).
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 + gamma-L-glutamyl-L-
CC         cysteine + H(+) + phosphate; Xref=Rhea:RHEA:13285, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:35235,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01609};
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family.
CC       YbdK subfamily. {ECO:0000255|HAMAP-Rule:MF_01609}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX842652; CAE80093.1; -; Genomic_DNA.
DR   RefSeq; WP_011164695.1; NC_005363.1.
DR   AlphaFoldDB; Q6MKW4; -.
DR   SMR; Q6MKW4; -.
DR   STRING; 264462.Bd2263; -.
DR   EnsemblBacteria; CAE80093; CAE80093; Bd2263.
DR   KEGG; bba:Bd2263; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_0_7; -.
DR   OMA; LIFGLHV; -.
DR   OrthoDB; 991285at2; -.
DR   Proteomes; UP000008080; Chromosome.
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;
KW   ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..378
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000218184"
SQ   SEQUENCE   378 AA;  43760 MW;  F2DAB46367C6B40E CRC64;
     MTKPQPIPFG KSDLFSLGVE VELQIIHPET RNLFPISPDI LEEWSLQSPH LKPEVFQSML
     EIDTPICKNV QEVEYELLLT SRELLRICKK HGARLASNGT HPFAKWHHRI FYPSDRYEYL
     LERNQHIARR LMIYGLHVHL GMKDGDHCIA MMNEFLYYLP HMLAMSASSP FWTGHDTGLA
     SSRITVFEAH PAGGTPCRVE NWAQFEDIVQ KLTRSNSIGS FKDIWWDIRP SPNYGTLEIR
     ICDGVPGIRK TTRLVAFIHL LAKHLQKRLE QGIRRQTPDD WMVRENKWRA SRHGLDCEVL
     IDNDGMTKNL REDIKDLLAA MKEDAAEMGY TEYLKQLVEE DLTHPSYEIQ RALFEKTGSL
     EHVVDSLCDV FEKDLDVV