ID   C7ZN98_FUSV7            Unreviewed;       513 AA.
AC   C7ZN98;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
GN   ORFNames=NECHADRAFT_54444 {ECO:0000313|EMBL:EEU34530.1};
OS   Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL
OS   45880 / 77-13-4) (Fusarium solani subsp. pisi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex; Fusarium vanettenii.
OX   NCBI_TaxID=660122 {ECO:0000313|EMBL:EEU34530.1, ECO:0000313|Proteomes:UP000005206};
RN   [1] {ECO:0000313|EMBL:EEU34530.1, ECO:0000313|Proteomes:UP000005206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4
RC   {ECO:0000313|Proteomes:UP000005206};
RX   PubMed=19714214; DOI=10.1371/journal.pgen.1000618;
RA   Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C.,
RA   Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C.,
RA   Freitag M., Ma L.J., Danchin E.G., Henrissat B., Coutinho P.M.,
RA   Nelson D.R., Straney D., Napoli C.A., Barker B.M., Gribskov M., Rep M.,
RA   Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L.,
RA   Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E.,
RA   Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E.,
RA   Vanetten H.D.;
RT   "The genome of Nectria haematococca: contribution of supernumerary
RT   chromosomes to gene expansion.";
RL   PLoS Genet. 5:E1000618-E1000618(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC         Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC         Evidence={ECO:0000256|RuleBase:RU361171};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; GG698964; EEU34530.1; -; Genomic_DNA.
DR   RefSeq; XP_003040243.1; XM_003040197.1.
DR   AlphaFoldDB; C7ZN98; -.
DR   STRING; 660122.C7ZN98; -.
DR   EnsemblFungi; NechaT54444; NechaP54444; NechaG54444.
DR   GeneID; 9678065; -.
DR   KEGG; nhe:NECHADRAFT_54444; -.
DR   VEuPathDB; FungiDB:NECHADRAFT_54444; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_019582_2_2_1; -.
DR   InParanoid; C7ZN98; -.
DR   OMA; VGWVFWR; -.
DR   OrthoDB; 2783360at2759; -.
DR   Proteomes; UP000005206; Unassembled WGS sequence.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006536; P:glutamate metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.160; -; 1.
DR   Gene3D; 4.10.280.50; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   NCBIfam; TIGR01788; Glu-decarb-GAD; 1.
DR   PANTHER; PTHR43321; GLUTAMATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43321:SF6; GLUTAMATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005206}.
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          489..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         287
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   513 AA;  57769 MW;  EBCC64C53D6B5B2D CRC64;
     MSHLSTVHSH KTQPGKAPRV ELSTDEEDTF KTSDYGSRFA CMELPRHQLP NGEMPRDIAY
     RLIKDELSLD NNPALNLASF VTTYMEDEVE KLMTESFSKN FIDYEEYPQS ADIQNRCVSI
     IGNLFHAPAG VSVGTSTVGS SEAIMLAVLA MKKRWKTRRL ADGKSVDKPN MIMSSAVQVV
     WEKAMRYFEI EERFIYCDPD RYVIDPDQAV DLCDENTIGI CAILGTTYTG QYEDIKALNG
     LLIDRKVDVP IHVDAASGGF VAPFVVPELE WDFRCEKVVS INVSGHKYGL VYPGVGWVIW
     RAPEYLPQEL VFNINYLGAN QSSFTLNFSK SACQVIGQYY QLIRLGRHGY HSIMSNLTRN
     SDYLADAIEK QGFIVMSERN GAGLPLVAFR FSTPEEDGSD EQGRHYDEFA LAHHLRSRGW
     VVPAYTMAPK SGVKMLRIVV REDFTRSRCD SLISDIALCC RLLQDMDKES SKRFEAYINK
     HLTALGKSDG AHPEYKNETH SLQGKTGKTH AVC
//