ID   C4JZ82_UNCRE            Unreviewed;       550 AA.
AC   C4JZ82;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Glutamate decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=UREG_07483 {ECO:0000313|EMBL:EEP82618.1};
OS   Uncinocarpus reesii (strain UAMH 1704).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX   NCBI_TaxID=336963 {ECO:0000313|EMBL:EEP82618.1, ECO:0000313|Proteomes:UP000002058};
RN   [1] {ECO:0000313|Proteomes:UP000002058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 1704 {ECO:0000313|Proteomes:UP000002058};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; CH476619; EEP82618.1; -; Genomic_DNA.
DR   RefSeq; XP_002582710.1; XM_002582664.1.
DR   AlphaFoldDB; C4JZ82; -.
DR   STRING; 336963.C4JZ82; -.
DR   GeneID; 8439951; -.
DR   KEGG; ure:UREG_07483; -.
DR   VEuPathDB; FungiDB:UREG_07483; -.
DR   eggNOG; KOG0629; Eukaryota.
DR   HOGENOM; CLU_011856_0_0_1; -.
DR   InParanoid; C4JZ82; -.
DR   OMA; RHATYHA; -.
DR   OrthoDB; 888358at2759; -.
DR   Proteomes; UP000002058; 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:UP000002058}.
FT   MOD_RES         311
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   550 AA;  60597 MW;  E97D471375AF9970 CRC64;
     MERADEVRNL LNPVQERILQ FIQSADQGSQ ALVQRHASNE SGPFKSGLLD LKKPTELQEE
     LQVELPAHGQ GVDGLLQVLD KLLRYSVNTW HQGFLDKLYA STNAPGLAAE LIIATLNTNV
     HIYQVAPVLT IIEKTTAARL ASLFGLTGQY AGGISAQGGT ASNTTAIVIA RNTLFPETKT
     EGVSNNQFVL FTSAHGHYSI EKAAQMLGFG SKAVWPVPVD EKGQMIPEKL DELITTAKEQ
     GKKPFFVNAT AGTTVVGSFD PLPEIHQICL KHNLWFHVDA SWGGSFIFSK KQRSKLRGSH
     LADSITFNPH KMLGVPLTCS FLLAADIRQF HRANTLPAGY LFHNEEYTNG FWDLGDLTLQ
     CGRRADSLKL FLSWMYYGSE GYEQQIDSAC SIAEQLSTLV GASPHLKLLT ENPPPCLQVC
     FYYAPLGRMA YPPEREINGK RLSEEERAKL NGKVTEEVVR ELVDQGFMVD YAPPSEDDTF
     ARDGKFFRCV VNVLTKKETI EALVDIIVKL GSKLVQRQLG SELKVPTASV MSGFQPKNPA
     EMGHGPVVHG
//