ID   A1D6V6_NEOFI            Unreviewed;       572 AA.
AC   A1D6V6;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 84.
DE   SubName: Full=Glutamate decarboxylase, putative {ECO:0000313|EMBL:EAW21450.1};
GN   ORFNames=NFIA_066140 {ECO:0000313|EMBL:EAW21450.1};
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW21450.1, ECO:0000313|Proteomes:UP000006702};
RN   [1] {ECO:0000313|Proteomes:UP000006702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027690; EAW21450.1; -; Genomic_DNA.
DR   RefSeq; XP_001263347.1; XM_001263346.1.
DR   AlphaFoldDB; A1D6V6; -.
DR   STRING; 331117.A1D6V6; -.
DR   EnsemblFungi; EAW21450; EAW21450; NFIA_066140.
DR   GeneID; 4589867; -.
DR   KEGG; nfi:NFIA_066140; -.
DR   VEuPathDB; FungiDB:NFIA_066140; -.
DR   eggNOG; KOG0629; Eukaryota.
DR   HOGENOM; CLU_011856_0_0_1; -.
DR   OMA; RHATYHA; -.
DR   OrthoDB; 888358at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.170; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
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:UP000006702}.
FT   REGION          551..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..565
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         328
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   572 AA;  62270 MW;  E03338D456F279EC CRC64;
     MSVSPPSSRA EEVRKLLSAV EDLLIPFIQS ADENPLGLSL QQNGVNGTNG ANGANGHLKR
     PRTALVDYKK PGELRDILQL SLPEKGTRQD GLIEVLRRVL KYSVNTWHQG FLDKLYASTN
     APGVASELIL AALNTNVHVY QVSPALTIIE KYTGEKLASL FGLNGPRAGG ISVQGGSASN
     TTSIVIARNN LYPDTKKNGN GDYKFVIFTS DHGHYSIEKA AQMLGLGSSS VWAVPVDKQG
     RMIPEELEKL VRKALQEKRT PFYVNATAGT TVMGSFDPFN EIAAICQKYN LWFHVDGSWG
     GSFVFSKRQK HKLAGVDKAN SIAINPHKML GVPVTCSFLL AADIRQFHRA NTLPAGYLFH
     SDDTEPQPNG DLSTAENELS VDSPEVWDLA DLTLQCGRRA DSLKLFLGWT YYGTEGYEQQ
     IDTACDIAAH LATLVSENPN FILISENPPP CLQVCFYYAP GGQLVHPRGV VSNETERAKA
     NSKVTEEVTH ALVHKGFMVD FAPPSGDDDA VGNGKFFRCV VNVQTTRETI EALVRAIEEV
     GPAITERLKA EAASVPKRRP GERGHGPVVH QG
//