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Database: UniProt
Entry: W6QDK6_PENRF
LinkDB: W6QDK6_PENRF
Original site: W6QDK6_PENRF 
ID   W6QDK6_PENRF            Unreviewed;       481 AA.
AC   W6QDK6;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Glutamate--ammonia ligase {ECO:0000256|ARBA:ARBA00030668};
GN   ORFNames=PROQFM164_S03g000885 {ECO:0000313|EMBL:CDM34161.1};
OS   Penicillium roqueforti (strain FM164).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM34161.1};
RN   [1] {ECO:0000313|EMBL:CDM34161.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FM164 {ECO:0000313|EMBL:CDM34161.1};
RX   PubMed=24407037; DOI=10.1038/ncomms3876;
RA   Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA   Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA   Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT   "Multiple recent horizontal transfers of a large genomic region in cheese
RT   making fungi.";
RL   Nat. Commun. 5:2876-2876(2014).
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01331, ECO:0000256|RuleBase:RU000384}.
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DR   EMBL; HG792017; CDM34161.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6QDK6; -.
DR   STRING; 1365484.W6QDK6; -.
DR   OMA; CNPGQHE; -.
DR   OrthoDB; 2783297at2759; -.
DR   GO; GO:0004356; F:glutamine synthetase 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   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; 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;
FT   DOMAIN          119..481
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   481 AA;  53269 MW;  8B9ABDE067600109 CRC64;
     MTTPTIITLE SLPSLLADDI KVKVAGIDSD GVLRGKVMAK EKFLGIAEKG FGFSSALFGW
     DMHDMLWTTD ARIAPPESGY ADFLAVPDLN SFRRLPWEEN IPFFLVRFLD DTRPVSADGR
     SMLRSLCDRL AGEGLHALAG VELEFMNFQT PSEDGYGSAG SQHPNLATFL EKNPPSALRP
     ITAGMFCYSS TRPVVNKKYF YDIFNTSAQI NCGIEGWHTE GGPGVYEAAL KVSEISEMAD
     KVALFKLLTK SLGVDHGITP CFMAKPMQGM PGSSGHIHIS LSDKDGNNLF ARETPEANPQ
     WSDIAYLSET GRHFLAGLLE ALPDIMPLFA PTVNSYKRLV ENYWAPVHIS WGLEDRIASI
     RLITPPVCKP GATRFEVRIP GADLHPHYAL SVILAAGWRG VQKKLEIKVP PMSARTPEDR
     PELLPNTLDK ALDRFSAPGS IAREILSSEF VDFFTATRQH ELGLWREAVT DWELKRYIEI
     V
//
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