ID A0A165QU49_9AGAM Unreviewed; 473 AA.
AC A0A165QU49;
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=NEOLEDRAFT_1097114 {ECO:0000313|EMBL:KZT22877.1};
OS Neolentinus lepideus HHB14362 ss-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Neolentinus.
OX NCBI_TaxID=1314782 {ECO:0000313|EMBL:KZT22877.1, ECO:0000313|Proteomes:UP000076761};
RN [1] {ECO:0000313|EMBL:KZT22877.1, ECO:0000313|Proteomes:UP000076761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB14362 ss-1 {ECO:0000313|EMBL:KZT22877.1,
RC ECO:0000313|Proteomes:UP000076761};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01331, ECO:0000256|RuleBase:RU000384}.
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; KV425591; KZT22877.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165QU49; -.
DR STRING; 1314782.A0A165QU49; -.
DR InParanoid; A0A165QU49; -.
DR OrthoDB; 2534858at2759; -.
DR Proteomes; UP000076761; 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; 1.
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:SF2; TYPE-1 GLUTAMINE SYNTHETASE 1; 1.
DR Pfam; PF00120; Gln-synt_C; 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 PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:KZT22877.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076761};
KW Transferase {ECO:0000313|EMBL:KZT22877.1}.
FT DOMAIN 135..473
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 473 AA; 51669 MW; 6C47F654A4743A8F CRC64;
MSQTTSYGIA YSPTVDSTHT SLTLEQLGDQ GVRYIRLTWV DLVNNIRYRV IPLPYFDKLL
KSSRPGITIG KIVFGLVFLD TAEGFGPTGE YLYVPDMKTL RRCPYAEGHA MVLGYFEHKD
KYSSGMDSLE VDLCPRTVLR RVMQEAKETC DVDFLVGFET EFILLKSVDP IEAMNNHGWS
NSPALPSGAV ETKVLEEIAD SLQTSSIELQ MYHAEAAPGQ YEVVTGPLSP LEACDALIFT
RETIFNTASK YGLRATLAPR VFGTSCGSGA HTHISIHSKK NLSLPPSTSN HLSPIEAAFL
SGILTALPAL CALTLPTAAS YARMADGVWS GGTYVAWGVD NRETPIRLCP SSSHHFEVKC
LDGTANPYVA IAGLLGAGLQ GVEKQVGLKV RECSVVAPAE LSEEERRKVG ATVRMPRTIK
EARERLAGGE GMTVREVLGE VFVEAYINVN KTLEKSLGEG SEADIMRRMI ENY
//
