ID   B2AKT3_PODAN            Unreviewed;       531 AA.
AC   B2AKT3;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:CDP29970.1};
DE   SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 5, supercontig 9 {ECO:0000313|EMBL:CAP64573.1};
GN   ORFNames=PODANS_5_8480 {ECO:0000313|EMBL:CAP64573.1};
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC   Podospora anserina.
OX   NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP64573.1};
RN   [1] {ECO:0000313|EMBL:CAP64573.1, ECO:0000313|Proteomes:UP000001197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC   {ECO:0000313|EMBL:CAP64573.1};
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA   Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA   Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA   Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA   de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA   El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2] {ECO:0000313|EMBL:CAP64573.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP64573.1};
RA   Genoscope - CEA;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000001197}
RP   GENOME REANNOTATION.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197};
RX   PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA   Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA   Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
RN   [4] {ECO:0000313|EMBL:CDP29970.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA   Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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; CU633865; CAP64573.1; -; Genomic_DNA.
DR   EMBL; FO904940; CDP29970.1; -; Genomic_DNA.
DR   RefSeq; XP_001904666.1; XM_001904631.1.
DR   AlphaFoldDB; B2AKT3; -.
DR   STRING; 515849.B2AKT3; -.
DR   GeneID; 6188910; -.
DR   KEGG; pan:PODANSg1688; -.
DR   VEuPathDB; FungiDB:PODANS_5_8480; -.
DR   eggNOG; KOG0629; Eukaryota.
DR   HOGENOM; CLU_011856_0_0_1; -.
DR   OrthoDB; 888358at2759; -.
DR   Proteomes; UP000001197; Chromosome 5.
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; -; 2.
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:UP000001197}.
FT   MOD_RES         344
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   531 AA;  57098 MW;  A52E842857916CA7 CRC64;
     MNGTNGVKKQ TLDRASEVEH LIDAVKSLII PFIQAADDAV PSRAAGELLP NRNGVVRNAL
     VESKGPEELV KELALSLPQV GRGEEGLLQT IQDVLKHSVN TWDQGFMDKL YASTNPVCCC
     SKTFVRQSSN SVTQVGVISE LVLAVLNTNV HVYQVSPALA VIEKHTAKTF ASLFGFNGPR
     AGGVTCQGGS SSNLTSIVIA RNTLYPESKL NGNSAAPNGP FVLFTSSHGH YSVEKAAVTC
     GFGSSSVWTV PVDASGRIIP SELRRLVQKS LDQGLTPFYV NATAGTTVLG SYDPFEEISA
     VCKEFNLWMH IDASWGGPAI FSAAHKHKLV GSHLADSLTV NPHKMLNCPV TCSFLLGPDM
     SVFHKANTLP AGYLFHSSAP SDVWDLADLT LQCGRRADSL KLALAWIYYG AEGFGRQIEA
     AFELAAYFAG LLERSGNFVL VSENPPPCLQ VCFYYAPGGR LRGTGEGNTE VTRGMVERLV
     RRGYMVDYAP DVSKESRGSF FRVVVNAQTL RGTVEGLVKG LEAVGREVVP Q
//