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Database: UniProt/TrEMBL
Entry: B2B163_PODAN
LinkDB: B2B163_PODAN
Original site: B2B163_PODAN 
ID   B2B163_PODAN            Unreviewed;       518 AA.
AC   B2B163;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 60.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=PODANS_3_9440 {ECO:0000313|EMBL:CAP70886.1};
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Lasiosphaeriaceae;
OC   Podospora.
OX   NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP70886.1};
RN   [1] {ECO:0000313|EMBL:CAP70886.1, 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:CAP70886.1};
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O.,
RA   Porcel B.M., Couloux A., Aury J.-M., Segurens B., Poulain J.,
RA   Anthouard V., Grossetete S., Khalili H., Coppin E.,
RA   Dequard-Chablat M., Picard M., Contamine V., Arnaise S., Bourdais A.,
RA   Berteaux-Lecellier V., Gautheret D., de Vries R.P., Battaglia E.,
RA   Coutinho P.M., Danchin E.G.J., Henrissat B., El Khoury R.,
RA   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
RT   anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2] {ECO:0000313|EMBL:CAP70886.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP70886.1};
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.,
RA   Benkhali J.A., Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and
RT   its role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
RN   [4] {ECO:0000313|EMBL:CDP27482.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:CDP27482.1}
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
RT   its role in heterokaryosis in Podospora anserina.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; CU638743; CAP70886.1; -; Genomic_DNA.
DR   EMBL; FO904938; CDP27482.1; -; Genomic_DNA.
DR   RefSeq; XP_001909753.1; XM_001909718.1.
DR   ProteinModelPortal; B2B163; -.
DR   STRING; 515849.XP_001909753.1; -.
DR   PRIDE; B2B163; -.
DR   EnsemblFungi; CAP70886; CAP70886; PODANS_3_9440.
DR   GeneID; 6193873; -.
DR   KEGG; pan:PODANSg6789; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   KO; K01580; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000001197; Chromosome 3.
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   Gene3D; 3.90.1150.10; -; 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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
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:UP000001197};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {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     298    298       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   518 AA;  58333 MW;  19AC468B8BF23057 CRC64;
     MVHLSTIPDE NQVVNGKLAG GIKKAHLQLV NDDDSFTTSV YGSRFAARDL PKHEMPEAEM
     SKDVAYRLIK DHLSLDGNPI LNLASFVTTY MEEEAEKLMT ESFSKNFIDY EEYPQSADIQ
     NRCVSMIGRL FHAPIGVEDD VGAIGTSCVG SSEAIMLAVL AMKRRWKNKR IEEGKPYDRP
     NIVMSSAVQV CWEKAARYFE VEEKLVYCTE ERYVIDPEET VNLVDENTIG ICVILGTTYT
     GEYEDVKAVD DLLTKKGLNT PIHVDAASGG FVAPFVVPDL EWDFRLEHVV SINVSGHKYG
     LVYPGVGWVV WRSAEFLPQE LVFNINYLGA DQASFTLNFS KGASQVIGQY YQLIRLGKHG
     YRAIMSNLTR TANYLSDSLE ALGFIIMSKK SGEGLPLVAF RLPPQEDRNY DEFALAHQLR
     VRGWVVPAYT MAPNTENLKM LRVVVREDFT RSRCDSLITD IKQSQQLLGQ MDQDSIKKQQ
     DFIHKHNTSS GKASHNHPKY RKEKHSLQGK TGKTHAIC
//
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