ID A0A395RIQ9_9HYPO Unreviewed; 664 AA.
AC A0A395RIQ9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Glutamate--ammonia ligase {ECO:0000256|ARBA:ARBA00030668};
GN ORFNames=FLONG3_11036 {ECO:0000313|EMBL:RGP59981.1};
OS Fusarium longipes.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=694270 {ECO:0000313|EMBL:RGP59981.1, ECO:0000313|Proteomes:UP000266234};
RN [1] {ECO:0000313|EMBL:RGP59981.1, ECO:0000313|Proteomes:UP000266234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 20695 {ECO:0000313|EMBL:RGP59981.1,
RC ECO:0000313|Proteomes:UP000266234};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01330, ECO:0000256|RuleBase:RU000384}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RGP59981.1}.
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DR EMBL; PXOG01000356; RGP59981.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395RIQ9; -.
DR STRING; 694270.A0A395RIQ9; -.
DR Proteomes; UP000266234; Unassembled WGS sequence.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR CDD; cd03424; ADPRase_NUDT5; 1.
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; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR008147; Gln_synt_N.
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; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR PANTHER; PTHR43785:SF15; TYPE-1 GLUTAMINE SYNTHETASE 2; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000266234}.
FT DOMAIN 16..112
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 120..535
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT DOMAIN 511..648
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 664 AA; 73872 MW; F2A9EBB1C7A7BC1A CRC64;
MSSQTVTVDN LAQVLENDNM VKLAGVDVDG ILRGKLVSKK KFLSIAEAGF GFCSVIFGWD
MHDRTYVREL KISNADNGYH DLLAIPDLST FRRIPWEDNV PLFLVDFLDP DTQKPICACP
RGLVKTQLAK LKEHGYGAMA GAEYEFYQFK SPDPSSSSPA AYLQENPPHQ LPALTEGMFG
YSLTRPVHNQ DYYYDVFNTC AKFSCDIEGW HTESGPGVFE AALEFGEIAQ MADRAALFKY
VVKSVSTKYG ITPCFMAKPK QGLPGNSGHM HVSIVDKDGK NLFARETKDE NPKWSDIANL
SDMGRHFLAG ILVGLPDIMP ILAPTINSYK RLVENFWAPV TVSWGLEHRA ASIRLICPKP
SATRFEVRVP GADTNPHLVL SAILGCGWRG VEKKLEIPTP PLAMGQDVGG DADQGERLAK
SLKEATVRFM AKDSIAREVF GDDFVEHFGG TREHEVRLFD EAVTDCHFNR ASAQSEEDAR
WVKLKKITYG DARGVQRTWE SAERLTRPKD ASIDGVGIVA ILEKHTGPEI VLQKQYRPPV
DKVVIEVPAG LIDEGETAEE CAVRELREET GYVGVATETS PIMFNDPGFC NTNLKMVHVS
IDMDLKENQD PQPQLEEGEY IEVFTVKLKD LWDECEKLEK QGHVIDARVG TLAEGILLAQ
RFKL
//
