GCS23_FRAAA
ID GCS23_FRAAA Reviewed; 858 AA.
AC Q0RHA0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Putative glutamate--cysteine ligase 2-3;
DE EC=6.3.2.2;
DE AltName: Full=Gamma-glutamylcysteine synthetase 2-3;
DE Short=GCS 2-3;
DE Short=Gamma-GCS 2-3;
GN OrderedLocusNames=FRAAL4489;
OS Frankia alni (strain ACN14a).
OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=326424;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACN14a;
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
CC -!- FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits weak
CC glutamate--cysteine ligase activity. {ECO:0000250}.
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 -!- SIMILARITY: In the N-terminal section; belongs to the glutamate--
CC cysteine ligase type 2 family. YbdK subfamily. {ECO:0000305}.
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DR EMBL; CT573213; CAJ63131.1; -; Genomic_DNA.
DR RefSeq; WP_011605610.1; NC_008278.1.
DR AlphaFoldDB; Q0RHA0; -.
DR SMR; Q0RHA0; -.
DR STRING; 326424.FRAAL4489; -.
DR KEGG; fal:FRAAL4489; -.
DR eggNOG; COG2170; Bacteria.
DR eggNOG; COG2308; Bacteria.
DR HOGENOM; CLU_017048_0_0_11; -.
DR OMA; DSAWFEH; -.
DR OrthoDB; 517836at2; -.
DR Proteomes; UP000000657; 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; IPR025841; CP_ATPgrasp_2.
DR InterPro; IPR006336; GCS2.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR011793; YbdK.
DR Pfam; PF14403; CP_ATPgrasp_2; 1.
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..858
FT /note="Putative glutamate--cysteine ligase 2-3"
FT /id="PRO_0000323509"
FT REGION 1..372
FT /note="Carboxylate-amine ligase"
FT REGION 373..858
FT /note="Unknown"
SQ SEQUENCE 858 AA; 92396 MW; E9CD6E07935765D5 CRC64;
MSDARNVAVG VEEEFHILDL TTRQLVPRAE EILQRLDKDS FSPELLKSVV ETNSQPTVDL
LALRSNLLDL RRRLAEAAGE LGLGPAASGT VPILDMDLLD VSRDARYEQM TEDYQIVARE
QLICGAQVHV DVADRDLAMA VVAWTAPWLP MLLALSASSP YWLGADSGYA SMRTLVWQRW
PTAGVAGSFQ TAAEYDQLIA DLIKSGVISD PGMVYFDVRP SAHLPTVELR ICDACPDVDN
VILIAGLFRA LVGRAIEEIE AGGQAPPPRA ELLRAATWRA ARSGLEGDLV DIFGAGPVPA
RAMLRRMLEE VRPQLERYDD WELIDNLAEQ AAGRGSSALR QRRAFARRGL LTDVADLILA
ETRDVPPAGA SLGVAPAVSA PDQIAPILLE RYQPAGYDEV VDEHGAVRPQ YRAVMRTLER
LGPDTLDERV GAREAEQTDR GITFRVNGDS ASRPFPFDIV PRIVAADDWA VLGRGLGQRV
RALEAFLHDV YGERAAVADG IVPPWVVNDA PGLRHGGRAP GRDAIRITTA GIDLVRGGDG
GWLVLEDNLR VPSGIAYAVE GRRLAESVLP ELGPPPGILR LGTVPALLHD ALVAAAPPAV
TGEPAVAVLT SGPADSAYFE HAMLAEEMGV PLVEPGALLV DDDVAYRVDD GRRRRVDVLY
RRIDEDELFA APGADGAPLG PALLRAVRAG QVSVANAPGN GIGDDKVVYA YVPRMVTYYL
GEQPVLDDVP TYVCGDPEQC EHVLANLDQL VVKPVDGFGG SGVVIGPHAE PYQLTAVREQ
ILADPRRWIG QEVVALSTHP TWHDSHLEPC AVDLRVFVYA GVEPVVVPAA LSRVAPPGSL
IVNSSQGGGS KDTWIPRR