ID   GCS2_PSEAE              Reviewed;         377 AA.
AC   Q9I1T4;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=PA2181;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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; AE004091; AAG05569.1; -; Genomic_DNA.
DR   PIR; C83372; C83372.
DR   RefSeq; NP_250871.1; NC_002516.2.
DR   RefSeq; WP_003113671.1; NZ_QZGE01000014.1.
DR   AlphaFoldDB; Q9I1T4; -.
DR   SMR; Q9I1T4; -.
DR   STRING; 287.DR97_6243; -.
DR   PaxDb; Q9I1T4; -.
DR   PRIDE; Q9I1T4; -.
DR   DNASU; 877967; -.
DR   EnsemblBacteria; AAG05569; AAG05569; PA2181.
DR   GeneID; 877967; -.
DR   KEGG; pae:PA2181; -.
DR   PATRIC; fig|208964.12.peg.2284; -.
DR   PseudoCAP; PA2181; -.
DR   HOGENOM; CLU_044848_0_1_6; -.
DR   InParanoid; Q9I1T4; -.
DR   OMA; LIFGLHV; -.
DR   PhylomeDB; Q9I1T4; -.
DR   BioCyc; PAER208964:G1FZ6-2222-MON; -.
DR   Proteomes; UP000002438; 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:0016879; F:ligase activity, forming carbon-nitrogen bonds; IBA:GO_Central.
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..377
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000218211"
SQ   SEQUENCE   377 AA;  42358 MW;  194A3749530486CE CRC64;
     MTHDLAASGL RFGIEEEFFL LDASDLDIVR SAPAGFVAAC RDTLGEHFAE EMFECQVEVA
     SPVFSTLAEA ARFHGQARQR LAHLAMDFGL RSLCVGTHPF ADWRRARSNP AAHFARLFED
     QGRVARRSLV CGLHVHVEIP PSHDRMAVLQ RVLPWLPLLL ALSASSPFRG GRRSGLASYR
     RALCGEWPRM NIPPALPDED AYRRHLALLR ETGCIREDGQ VWWMIRPSSH VPTLELRICD
     ACPRLADALS LAGLFRALVG EALGADPRAL PVARDACLEE NYWQALRYGC AGRYLVEGRC
     VGAGDWLEMA WRQCRPQARQ GNEWAYQHAC GLLEETSAAR QLRRYRRLRE AGQERHPALR
     RLVEELLEEN LQPALAG