ID Q4WXY4_ASPFU Unreviewed; 572 AA. AC Q4WXY4; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 24-JAN-2024, entry version 100. DE SubName: Full=Glutamate decarboxylase, putative {ECO:0000313|EMBL:EAL92469.1}; DE EC=4.1.1.15 {ECO:0000313|EMBL:EAL92469.1}; GN ORFNames=AFUA_3G11120 {ECO:0000313|EMBL:EAL92469.1}; OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / OS Af293) (Neosartorya fumigata). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Fumigati. OX NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL92469.1, ECO:0000313|Proteomes:UP000002530}; RN [1] {ECO:0000313|EMBL:EAL92469.1, ECO:0000313|Proteomes:UP000002530} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100 RC {ECO:0000313|Proteomes:UP000002530}; RX PubMed=16372009; DOI=10.1038/nature04332; RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P., RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M., RA Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A., RA Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., RA Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H., RA Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., RA Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P., RA Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., RA Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S., RA Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., RA Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., RA Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., RA Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., RA Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., RA Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H., RA Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B., RA Denning D.W.; RT "Genomic sequence of the pathogenic and allergenic filamentous fungus RT Aspergillus fumigatus."; RL Nature 438:1151-1156(2005). 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}. 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:EAL92469.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAHF01000002; EAL92469.1; -; Genomic_DNA. DR RefSeq; XP_754507.1; XM_749414.1. DR AlphaFoldDB; Q4WXY4; -. DR STRING; 330879.Q4WXY4; -. DR EnsemblFungi; EAL92469; EAL92469; AFUA_3G11120. DR GeneID; 3512083; -. DR KEGG; afm:AFUA_3G11120; -. DR VEuPathDB; FungiDB:Afu3g11120; -. DR eggNOG; KOG0629; Eukaryota. DR HOGENOM; CLU_011856_0_0_1; -. DR InParanoid; Q4WXY4; -. DR OMA; RHATYHA; -. DR OrthoDB; 888358at2759; -. DR Proteomes; UP000002530; Chromosome 3. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central. DR GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC. 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:UP000002530}. FT MOD_RES 328 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50" SQ SEQUENCE 572 AA; 62271 MW; D8C14E8DECB794EE CRC64; MSVSPPSSRA EEVRKLLGAV EDLLIPFIQS ADENPLGLAL QQNGVNGTND TNGTNGHLKS PRTALVDYKN PEELRDILQL SLPEKGTRQE GLIEVLRKVL KYSVNTWHQG FLDKLYASTN APGVASELIL AALNTNVHVY QVSPALTIIE KFTGEKLASL FGLNGPRAGG ISVQGGSASN TTSIVIARNN LYPDTKKNGN GDYKFVVFTS DHGHYSIEKA AQMLGLGSSS VWVVPVDKQG RMIPEELEKL VRKALQENRT PFYVNATAGT TVMGSFDPFN EIAAICQKYN LWFHVDGSWG GSFVFSKRQK HKLAGVDKAN SIAINPHKML GVPVTCSFLL AADIRQFHRA NTLPAGYLFH NNDTEPQPNG DLGTSENELS VDSPEVWDLA DLTLQCGRRA DSLKLFLGWT YYGTEGYEQQ IDTACDIAAH LATLVSESPN FILISENPPP CLQVCFYYAP GGQLVHPRGV VSNETERAKA NSKVTEELTH ALVHKGFMVD FAPPSGDEDA AGDGKFFRCV VNVQTTRETV EALVRAIEEA GPAIIERLKA EAASIPKRRP GERGHGPVVH QG //