ID   GCS2_RHOBA              Reviewed;         372 AA.
AC   Q7USI0;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=RB4485;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294140; CAD73816.1; -; Genomic_DNA.
DR   RefSeq; NP_866130.1; NC_005027.1.
DR   RefSeq; WP_011119935.1; NC_005027.1.
DR   AlphaFoldDB; Q7USI0; -.
DR   SMR; Q7USI0; -.
DR   STRING; 243090.RB4485; -.
DR   EnsemblBacteria; CAD73816; CAD73816; RB4485.
DR   KEGG; rba:RB4485; -.
DR   PATRIC; fig|243090.15.peg.2093; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_0_0; -.
DR   InParanoid; Q7USI0; -.
DR   OMA; LIFGLHV; -.
DR   OrthoDB; 991285at2; -.
DR   Proteomes; UP000001025; 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..372
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000218214"
SQ   SEQUENCE   372 AA;  41488 MW;  818DB10DDD718869 CRC64;
     MSFQVPTVGV EEEYQLVDPR SGALIPNCKE VMRTIRRNGG SEEAHSEIQH ELHLNQIEMA
     SDVCSSLEEV RDALTQTRRM LIDAARSNET ELASAGTNPL PIPTDDALTP KDRYQAMTDR
     YQQIARDLFI FGCHVHVAME DRELGIQVMN RCRRWLPILQ AITANSPYWD GVDTGYASYR
     RELWAQWPMA GPPAHFDSLA DYQSCVDDLV ACGAIKDESF LYWDIRLPTR VPTIEFRAAD
     VMTRVEETVG YVGMIRAIVM LAISEEEQGK PIVPIRPSVL SYAIWHAARY GMNEQLVDPE
     SREMIPASEL LNRLMTAIDP ALKATGEARP VEAFANQLIK SGTGADRQRR GGELSSVVAN
     VVAETVPSAI LA