ID A0A167XY18_9EURO Unreviewed; 442 AA.
AC A0A167XY18;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Glutamate--ammonia ligase {ECO:0000256|ARBA:ARBA00030668};
GN ORFNames=AAP_03709 {ECO:0000313|EMBL:KZZ90614.1};
OS Ascosphaera apis ARSEF 7405.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ascosphaeraceae; Ascosphaera.
OX NCBI_TaxID=392613 {ECO:0000313|EMBL:KZZ90614.1, ECO:0000313|Proteomes:UP000242877};
RN [1] {ECO:0000313|EMBL:KZZ90614.1, ECO:0000313|Proteomes:UP000242877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 7405 {ECO:0000313|EMBL:KZZ90614.1,
RC ECO:0000313|Proteomes:UP000242877};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01331, 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:KZZ90614.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AZGZ01000016; KZZ90614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167XY18; -.
DR VEuPathDB; FungiDB:AAP_03709; -.
DR OrthoDB; 2783297at2759; -.
DR Proteomes; UP000242877; Unassembled WGS sequence.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 2.
DR InterPro; IPR036651; Gln_synt_N_sf.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR008146; Gln_synth_cat_dom.
DR PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR PANTHER; PTHR43785:SF15; TYPE-1 GLUTAMINE SYNTHETASE 2; 1.
DR Pfam; PF00120; Gln-synt_C; 2.
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 PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:KZZ90614.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000242877};
KW Transferase {ECO:0000313|EMBL:KZZ90614.1}.
FT DOMAIN 124..442
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 442 AA; 49412 MW; 4F23768A4D51287A CRC64;
MPDTQEQQSP SISYITDALA NDTQVKVAGV DADGILRGKL VSKKKFLSIA EDGFGFCSVI
FGWDMHDQTY FRELTISNKE NGYRDIVAVP DLKSFRRIPW EDNVPFFLVH FLDPDTKEPI
APCPRGLVKS AAKGLEAKGY KAMAGAEFEF YQFRVPTDQP PNERNSSATA TFLKTHPVEQ
LPSLTEGMFG YSLSRPVQNQ GYYYDVFNYC REFKCDIESW HTESGPGVFE AALEFGEAKE
IADRASLFKG SADPNPPYPD VTYLSDLGRH FLAGILEGLP DIMPILAPTI NSYKRLVENF
WAPVTVSWGL EHRAASIRLI TPPTASPKGT RLEIRTPGAD VNPHYVLAAI IALGWRGVEK
KLEIPVPPLA KGEDVGGASD QGERLAKSLK EATQRFMRKD SIAREVLGDG FVEHFGGTRE
HEVRLWEEAV TDWEVRRYIE TV
//
