ID A0A2H3HQG4_FUSOX Unreviewed; 515 AA.
AC A0A2H3HQG4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Glutamate--ammonia ligase {ECO:0000256|ARBA:ARBA00030668};
GN ORFNames=AU210_000104 {ECO:0000313|EMBL:PCD44647.1};
OS Fusarium oxysporum f. sp. radicis-cucumerinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=327505 {ECO:0000313|EMBL:PCD44647.1, ECO:0000313|Proteomes:UP000219602};
RN [1] {ECO:0000313|EMBL:PCD44647.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD44647.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=27387256; DOI=10.1111/1462-2920.13445;
RA van Dam P., Fokkens L., Schmidt S.M., Linmans J.H., Kistler H.C., Ma L.J.,
RA Rep M.;
RT "Effector profiles distinguish formae speciales of Fusarium oxysporum.";
RL Environ. Microbiol. 18:4087-4102(2016).
RN [2] {ECO:0000313|EMBL:PCD44647.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD44647.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=28831051; DOI=10.1038/s41598-017-07995-y;
RA van Dam P., Fokkens L., Ayukawa Y., van der Gragt M., Ter Horst A.,
RA Brankovics B., Houterman P.M., Arie T., Rep M.;
RT "A mobile pathogenicity chromosome in Fusarium oxysporum for infection of
RT multiple cucurbit species.";
RL Sci. Rep. 7:9042-9042(2017).
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:PCD44647.1}.
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DR EMBL; MABQ02000001; PCD44647.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3HQG4; -.
DR STRING; 327505.A0A2H3HQG4; -.
DR OrthoDB; 2783297at2759; -.
DR Proteomes; UP000219602; Chromosome 1.
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; 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; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000219602}.
FT DOMAIN 136..515
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 515 AA; 56799 MW; EF6B1B31EE5FEBB5 CRC64;
MANYGDKTHD AIANNAVNGE IAESPIDRIA KLLTGDKKVK VAGIDCDGIL RGKIIHKTKF
LSSLESGFGM SSAIFGWDMH DVLYTEETGL TSADSGYQDF TAVIDLNSFR RLPFEDNIAF
FLLHFYIQDK PVFADGRGLV KALTNNLADS GYKGLAGVEL EFLNFQTPSQ DGYSNSADRP
NLAAFLANNA PKALRPVTAG AFGYSATRPI MAKQYFHDIF DQSLEIECPI EGWHTESGPC
VYEAALAVSQ LSHMADNVAL FKSVFSANAV KSTGLTYLSR LVCKSVGVQH NITPCFMAKP
IQGLPGNSGH IHVSLTTKEG QNVFVRETPD VDPRWPDMAN LSDTGRHFLA GIISALPDIM
PLLAPNVNSY KRLVENYWAP VSVSWGFEDR LASIRLVAPP SCKPSATRFE IRVPGADIHP
HYALSAIFYA GLRGIKNKMQ ITIPPESARP KETPAERLPN TLEAALGRFS AKDSVARQIL
GDEFVDFFTV SRRHELRQWR EAVTDWEFSR YIETV
//
