ID   GCS2_BORA1              Reviewed;         403 AA.
AC   Q2L0C4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, 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=BAV0234;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N;
RX   PubMed=16885469; DOI=10.1128/jb.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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}.
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DR   EMBL; AM167904; CAJ47839.1; -; Genomic_DNA.
DR   RefSeq; WP_012415937.1; NC_010645.1.
DR   AlphaFoldDB; Q2L0C4; -.
DR   SMR; Q2L0C4; -.
DR   STRING; 360910.BAV0234; -.
DR   EnsemblBacteria; CAJ47839; CAJ47839; BAV0234.
DR   GeneID; 41392163; -.
DR   KEGG; bav:BAV0234; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_1_4; -.
DR   OMA; LIFGLHV; -.
DR   OrthoDB; 991285at2; -.
DR   Proteomes; UP000001977; 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..403
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000255792"
FT   REGION          370..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   403 AA;  44789 MW;  6DFAACEF6768492A CRC64;
     MEQIPFVSSS PNTLGIELEL QLIDPAGFDL AAASDELLAQ LANHPVADRI KPEITRSMIE
     LNSSVHEHPA GLLAEMREMR DALCEAADAV GVSVSGGGTH PFMRWQERTI SDTPRFQYLA
     EMYGYLARQF TVFGQHIHLG VPSGDAAVRL VHGLSPYVPH FIALSASSPY REGVDTLFSC
     ARLNAVNSFP LAGHLPPEVA DWYHFEAHIA QLRASGLAES IKDLYWDIRP KPEFGTVEIR
     VCDTPLTVER ACQLAAFAQA LAVLLEREPS PPTQAWLAYR SNHFQACRFG LHGSYVTPGG
     QRVRLADHLK ALFVRLMPVA EELGTTDILQ SLRDEMQRGG NDARWLRAQF HRTRELSGTV
     EAMTQVFRGE SAAQRRAPQA ARRRIRASSE PLGPMSMWPE RLH