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Database: UniProt/TrEMBL
Entry: A1DP70_NEOFI
LinkDB: A1DP70_NEOFI
Original site: A1DP70_NEOFI 
ID   A1DP70_NEOFI            Unreviewed;       515 AA.
AC   A1DP70;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   20-JUN-2018, entry version 63.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=NFIA_059440 {ECO:0000313|EMBL:EAW16591.1};
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC
OS   A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW16591.1, 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.,
RA   Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA   Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA   Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA   Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA   Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA   Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA   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   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC       {ECO:0000256|RuleBase:RU361171}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; DS027698; EAW16591.1; -; Genomic_DNA.
DR   RefSeq; XP_001258488.1; XM_001258487.1.
DR   ProteinModelPortal; A1DP70; -.
DR   STRING; 36630.CADNFIAP00004507; -.
DR   PRIDE; A1DP70; -.
DR   EnsemblFungi; EAW16591; EAW16591; NFIA_059440.
DR   GeneID; 4585004; -.
DR   KEGG; nfi:NFIA_059440; -.
DR   EuPathDB; FungiDB:NFIA_059440; -.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; FTTSVYG; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000006702; 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; 3.40.640.10; -; 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   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006702};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006702}.
FT   MOD_RES     295    295       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   515 AA;  58974 MW;  92398ABA742A22AB CRC64;
     MVHLATVKRD SENFEPLVKR VDSIKLETTD DDDFYSTVYG TRFAAEQLPQ NEMPEREMPR
     EVAYRMIKDE LSLDGNPMLN LASFVTTYME EEAEKLMTDS FSKNFIDYEE YPQSAEIQNR
     CVNMIARLFN APIDSDNEHP VGTSTVGSSE AIMLGTLAMK RRWQNKRKAE GKDTTRPNII
     MNSAVQVCWE KAARYFDVEE RYVYCTEDRY VIDPKQAVDL VDENTIGICA ILGTTYTGEY
     EDVKAINDLL VERGLDIPIH VDAASGGFVV PFINPNLLWD FRLEKVVSIN VSGHKYGLVY
     PGVGWVVWRS PEYLPKELIF NINYLGAEQA SFTLNFSKGA SQVIGQYYQM IRLGKRGYRS
     IMVNITRIAD YLAQQLEQLG FIIMSQQRGR GLPLVAFRLP SDRNEQFDEF ALAHQLRERG
     WIVPAYTMAP HSNELKLMRV VVREDFSMNR CDALLTDIKL ALKTLSDMDK AMLEKYTLHV
     QKHAVNSHKS KHNHSHYKNE KHSLQGKTGK THGVC
//
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