ID   D5G474_TUBMM            Unreviewed;       861 AA.
AC   D5G474;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Glutamate--ammonia ligase {ECO:0000256|ARBA:ARBA00030668};
GN   ORFNames=GSTUM_00003979001 {ECO:0000313|EMBL:CAZ79317.1};
OS   Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ79317.1, ECO:0000313|Proteomes:UP000006911};
RN   [1] {ECO:0000313|EMBL:CAZ79317.1, ECO:0000313|Proteomes:UP000006911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mel28 {ECO:0000313|EMBL:CAZ79317.1,
RC   ECO:0000313|Proteomes:UP000006911};
RX   PubMed=20348908; DOI=10.1038/nature08867;
RA   Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA   Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA   Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA   Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA   Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA   Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA   Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA   Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA   Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA   Ottonello S., Wincker P.;
RT   "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT   of symbiosis.";
RL   Nature 464:1033-1038(2010).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01331, ECO:0000256|RuleBase:RU000384}.
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DR   EMBL; FN429986; CAZ79317.1; -; Genomic_DNA.
DR   RefSeq; XP_002835196.1; XM_002835150.1.
DR   AlphaFoldDB; D5G474; -.
DR   STRING; 656061.D5G474; -.
DR   EnsemblFungi; CAZ79317; CAZ79317; GSTUM_00003979001.
DR   GeneID; 9184293; -.
DR   KEGG; tml:GSTUM_00003979001; -.
DR   eggNOG; KOG0683; Eukaryota.
DR   HOGENOM; CLU_017290_6_3_1; -.
DR   InParanoid; D5G474; -.
DR   OMA; LEGCPRT; -.
DR   OrthoDB; 10308at2759; -.
DR   Proteomes; UP000006911; Unassembled WGS sequence.
DR   GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR036651; Gln_synt_N_sf.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR008146; Gln_synth_cat_dom.
DR   InterPro; IPR027303; Gln_synth_gly_rich_site.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR   PANTHER; PTHR43785:SF2; TYPE-1 GLUTAMINE SYNTHETASE 1; 1.
DR   Pfam; PF04909; Amidohydro_2; 1.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
DR   PROSITE; PS51987; GS_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006911}.
FT   DOMAIN          541..861
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   861 AA;  95457 MW;  E0E92750D7B0C88F CRC64;
     MAPPHPPTTI AELRGLINTH PIIDNHAHNL LRDVDSTSSP LESIVSEASG LALSDATRTL
     AHARAVTQLS GLLGCAPTWE AIKDKRRTID YEAWAKKCLS GTQCLLIDDG LDGEGVHPYD
     WHDRYASSPS KRLVRVETLA EQTLREFAPE FQEDESNNSR EAELFNRWSE RFSGLINAAV
     QDPVVAGFKS IICYRSGLDI AGETTGGLLL EAVKNALRGS RRDGGRYKIR DKILGDFLVC
     EVARIIAKSG SWKPFQFHTG LGDNDLNIRK ANPAYLQDFI KENPDVPIVL LHSSYPFTRE
     AGYLASVYKN VYLDIGEVFP MISKDGQKSV VKQCLECTPS NKLLWSTDGH WFPEGFALAN
     MQIREVLGEV LPKCVAKGQL TVPQAAGFVK DLLFENSNKL YRLNLIPIFA STIDLVDHSP
     PINQGTQMLS EFLHKNPHVK YFRLQWVDYT NTLRLRLVTL AQMNKMVSKG TFLTVTKAVL
     SLLQDDSPTD DFTPAGRYNL VPDWSSLRIC PGEPGLLEKP SKYASVMCFF RDNEEEVDTC
     PRTILSRAVR RAKEEHKVDF LIGWETEVVF LNKTDLEAAS KTHAWSTSRS LHNRCLTALE
     QIVDALEASG IEVLLFHPES APSQYEIVTG PLPPLESIDA LYHTRETIMR ICSYHNLRAT
     LHPKPFKGAA GTAAHMHVSM APPTESLQNA FFAGVLSHLG SLAALTLPQA ASYERLGDSC
     WTGGTWIAWG EENRETPLRR VSKGEAHWEI RCIDGLANAY LAATGIISAG CMGMLDGMKL
     PGESCNSDPS KMTSRERNGL GITRQLPDGL GKAMDLLRAD KKLRSRIGEA CVAKYIILKK
     AETAALEANG PSVRAWIMDR Y
//