ID   C1H8W9_PARBA            Unreviewed;       604 AA.
AC   C1H8W9;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:EEH36792.1};
GN   ORFNames=PAAG_07210 {ECO:0000313|EMBL:EEH36792.1};
OS   Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS   brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH36792.1, ECO:0000313|Proteomes:UP000002059};
RN   [1] {ECO:0000313|EMBL:EEH36792.1, ECO:0000313|Proteomes:UP000002059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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; KN294013; EEH36792.1; -; Genomic_DNA.
DR   RefSeq; XP_002790974.1; XM_002790928.1.
DR   AlphaFoldDB; C1H8W9; -.
DR   STRING; 502779.C1H8W9; -.
DR   GeneID; 9094151; -.
DR   KEGG; pbl:PAAG_07210; -.
DR   VEuPathDB; FungiDB:PAAG_07210; -.
DR   eggNOG; KOG0629; Eukaryota.
DR   HOGENOM; CLU_011856_0_0_1; -.
DR   OMA; RHATYHA; -.
DR   OrthoDB; 888358at2759; -.
DR   Proteomes; UP000002059; Partially assembled 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:UP000002059}.
FT   REGION          540..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         322
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   604 AA;  65466 MW;  8B513A1A710853DF CRC64;
     MSSKDPTIAS GGDLLERSEE VRNLLNAVQE RLVSFIRAAD HDDFSSSKAG DAPRQPSALV
     QYVKPEELQA TMNLQIPSSG EGQRGLLRIL DQVLQYSVNT WHQGFLDKLY ASTNAPGLAA
     ELIIAALNTN VHIYPVSPAL TVIEKYTSKQ LANLFGFDGP NSGGISVQGG SAANATSIVI
     ARNTLFPKTK KDGCDGSKFV IFTSTHGHYS IKKAAWMLGF GGSAVWSVPV DEKGQMIPQS
     LEELVIKAKN EGRTTFYVNA TAGTTVLGSF DPLEHIALIC RKYNLWLHVD ASWGGSFAFS
     KKKRGKLAGS HLADSLTVNP HKMLGVPVTC SFLLGADMTQ FHRANTLPAG YLFHDDYLEA
     GLNGNDVKCP EVWDLADLTL QCGRRADSLK FYLSWIYYGS EGYERQIDSA CDVAADLAAA
     ISNSPNFILI SENPPPCLQV AFYYAPNKQL VFPRGKEVGG KQLDEEERGK RNSKITQEIT
     KRLVSRGFMI DYAPPAEGDP SAGDGKFFRC VVNVQTKKET VEALLAAILD IGPEVVEQSA
     RGDSIDDPDP FAGAEPFRMG NPAKHGYGPV AHPPDPFAGA KPFRMGNPAE HGHGPVVHQI
     HTSS
//