ID   GCS2_HERA2              Reviewed;         385 AA.
AC   A9B2Z8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=Haur_4831;
OS   Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC   Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC   Herpetosiphon.
OX   NCBI_TaxID=316274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23779 / DSM 785 / 114-95;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000875; ABX07461.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9B2Z8; -.
DR   SMR; A9B2Z8; -.
DR   STRING; 316274.Haur_4831; -.
DR   EnsemblBacteria; ABX07461; ABX07461; Haur_4831.
DR   KEGG; hau:Haur_4831; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_0_0; -.
DR   OMA; LIFGLHV; -.
DR   BioCyc; HAUR316274:GHYA-4890-MON; -.
DR   Proteomes; UP000000787; 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..385
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_1000148222"
SQ   SEQUENCE   385 AA;  44162 MW;  A10FBBFD46A62B4E CRC64;
     MEYRDPGHPH FPFTIGIEEE YQIIDPETRE LKSYITQILD EGQLILREQM KPEMHQSIVE
     VGTHVCRTVE EARAEIIRLR GAIGSLAASK GLRIAAAGTH PFSSWQKQDI YPHERYYGVI
     EEMQEAARRL LIFGMHVHIG MPDNETCIEI MNVARYFLPH LLALSTSSPF WMGRKTGFQS
     YRSIIFTNFP RTGIPDTFQS YAEFEQYINI LLKTHSIDNG KKVWWDARPH PMFGTLEVRI
     CDIATKVDEA IMIAGLVQAI FVKIYSLFRQ NQTFRVYSRA LINENKWRAA RYGMGGKLID
     FGRREELSAH DLMAELREFV DDVVDDLGSR AAVDYIDQVL KHGTSAERQL RTYEETGDIK
     AVVDQLIRET MEGVPLDQAT QVVSG