ID   GCS2_RHORT              Reviewed;         389 AA.
AC   Q2RRI3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=Rru_A2462;
OS   Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS   NCIMB 8255 / S1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX   PubMed=21886856; DOI=10.4056/sigs.1804360;
RA   Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA   Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA   Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA   Roberts G.P., Reslewic S., Schwartz D.C.;
RT   "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL   Stand. Genomic Sci. 4:293-302(2011).
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; CP000230; ABC23262.1; -; Genomic_DNA.
DR   RefSeq; WP_011390215.1; NC_007643.1.
DR   RefSeq; YP_427549.1; NC_007643.1.
DR   AlphaFoldDB; Q2RRI3; -.
DR   SMR; Q2RRI3; -.
DR   STRING; 269796.Rru_A2462; -.
DR   EnsemblBacteria; ABC23262; ABC23262; Rru_A2462.
DR   KEGG; rru:Rru_A2462; -.
DR   PATRIC; fig|269796.9.peg.2566; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_0_5; -.
DR   OMA; LIFGLHV; -.
DR   OrthoDB; 991285at2; -.
DR   PhylomeDB; Q2RRI3; -.
DR   Proteomes; UP000001929; 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..389
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000255810"
SQ   SEQUENCE   389 AA;  43078 MW;  D043AA8300EDA6A7 CRC64;
     MREPAFTVGI EEEYLLVDRQ SRALAADPPE ALMTRLAAAF GDTNHGAVTP EFLRAQIEVG
     TKVCDSLAEA GEALGALRRV LAEEAKGFGL APIAASTHPF AEWADLKHTP KERYDLLAED
     LQAVVRRLVI CGMHVHVGIE DPDLRMDLMA QVSYFLPHLL ALTTSSPFWR GEDSGLKSYR
     IAVFSALPRT GLPDSFSSFA EYQRHVEVLV SAGLIEDSTR IWWDIRPSHR FPTLEMRIAD
     VCTRLDDALC VAALFRCLLR MLYRLRRANQ RWRHYARLLI AENRWRAQRY GLDGGLVDFG
     RGEVVPFADL IEELLELIAP DAAVFGCQAE VLHARTILHR GTSAHNQLRV FAEARAGGMT
     RDEALVAVVD HLIAQTVAPL GADAGAPGP