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Database: UniProt/TrEMBL
Entry: B0D3H6_LACBS
LinkDB: B0D3H6_LACBS
Original site: B0D3H6_LACBS 
ID   B0D3H6_LACBS            Unreviewed;       537 AA.
AC   B0D3H6;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   25-OCT-2017, entry version 49.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=LACBIDRAFT_315921 {ECO:0000313|EMBL:EDR10921.1};
OS   Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured
OS   deceiver) (Laccaria laccata var. bicolor).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Tricholomataceae;
OC   Laccaria.
OX   NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN   [1] {ECO:0000313|EMBL:EDR10921.1, ECO:0000313|Proteomes:UP000001194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX   PubMed=18322534; DOI=10.1038/nature06556;
RA   Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA   Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A.,
RA   Shapiro H.J., Wuyts J., Blaudez D., Buee M., Brokstein P.,
RA   Canbaeck B., Cohen D., Courty P.E., Coutinho P.M., Delaruelle C.,
RA   Detter J.C., Deveau A., DiFazio S., Duplessis S.,
RA   Fraissinet-Tachet L., Lucic E., Frey-Klett P., Fourrey C.,
RA   Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P., Kilaru S.,
RA   Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R., Melayah D.,
RA   Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA   Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA   Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA   Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA   Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA   Tuskan G., Grigoriev I.V.;
RT   "The genome of Laccaria bicolor provides insights into mycorrhizal
RT   symbiosis.";
RL   Nature 452:88-92(2008).
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:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; DS547096; EDR10921.1; -; Genomic_DNA.
DR   RefSeq; XP_001878222.1; XM_001878187.1.
DR   ProteinModelPortal; B0D3H6; -.
DR   STRING; 486041.XP_001878222.1; -.
DR   EnsemblFungi; EDR10921; EDR10921; LACBIDRAFT_315921.
DR   GeneID; 6073940; -.
DR   KEGG; lbc:LACBIDRAFT_315921; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   InParanoid; B0D3H6; -.
DR   KO; K01580; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000001194; Unassembled WGS sequence.
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:UP000001194};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171, ECO:0000313|EMBL:EDR10921.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001194}.
FT   MOD_RES     298    298       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   537 AA;  59454 MW;  97441FD1A73AD534 CRC64;
     MALSKHVNAD HLIQKSHDKH ATHGEFAAEQ AQEATYSYGS RYGTNPVPKY RISSKGVSAD
     AAYQIIHDEL SLDGSTVLNL ASFVHTWMPP QADKLVHENI TKNLIDTDEY PATQIIHTRC
     ISILADVWHA PSSKQAIGTA TTGSSEAIQL GGLAMKKIWQ AKRKAAGKSI HEPGPNIVMG
     ANAQVALEKF ARYFDVECRL VPISVQSKYR LDPKEAIKYV DENTIGVFVI LGSTYTGHYE
     PVKEISDLLD EYEAKTGNSV PIHVDAASGG FIAPFAHPKL LWDFKLPRVV SINTSGHKFG
     LSYVGVGWVV WRDKAHLPKD LIFELHYLGS VEYSFSLNFS RPAAPIIAQY FNLLHLGFEG
     YREVALDDLK NARLLSRALE NTGYYTVLSD VHRSVGAVGG KGIDTHDVEA YEPGLPVVAF
     RFSDEFQQKN PEVEQKWIQT LLRAKGWIVP NYELAPDLQQ VQILRVVIRE NVTEVLLDKL
     IADIVEITEE LASKASSEHA LNVLGQMHGA RKKHEHKTST FDAGEGSEAS GTYARSC
//
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