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Database: UniProt/TrEMBL
Entry: A0A1U8QKD6_EMENI Q5B1Y3_EMENI
LinkDB: A0A1U8QKD6_EMENI Q5B1Y3_EMENI
Original site: A0A1U8QKD6_EMENI Q5B1Y3_EMENI 
ID   A0A1U8QKD6_EMENI        Unreviewed;       515 AA.
AC   A0A1U8QKD6;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   25-OCT-2017, entry version 5.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=AN5447.2 {ECO:0000313|EMBL:EAA62607.1};
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321 {ECO:0000313|EMBL:EAA62607.1, ECO:0000313|Proteomes:UP000005890};
RN   [1] {ECO:0000313|EMBL:EAA62607.1, ECO:0000313|Proteomes:UP000005890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000005890};
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R.,
RA   Batzoglou S., Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M., Hynes M., Paoletti M., Fischer R., Miller B., Dyer P.,
RA   Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EAA62607.1}.
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DR   EMBL; AACD01000094; EAA62607.1; -; Genomic_DNA.
DR   RefSeq; XP_663051.1; XM_657959.1.
DR   GeneID; 2871735; -.
DR   KEGG; ani:AN5447.2; -.
DR   KO; K01580; -.
DR   Proteomes; UP000005890; 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:UP000005890};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171}.
FT   MOD_RES     294    294       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   515 AA;  58898 MW;  6638DB0638482AC7 CRC64;
     MVHLASIKKD DDFEPVVNRV DSIKLDTIEE DDYSATVYGT RFATQQLPHA EMPDREMPRE
     VAYRMIKDEL SLDGNPMLNL ASFVTTYMED EAEKLMAESF SKNFIDYEEY PQSAEIQNRC
     VNMIARLFNA PTDSDTDHPM GTSTVGSSEA IMLGTLAMKK RWQNKRKAEG KDYSRPNIVM
     NSAVQVCWEK AARYFDVEER YVYCTEERYV IDPQQAVDLV DENTIGICAI LGTTYTGEYE
     DVKAINDLLV ERGLDCPIHV DAASGGFVAP FIHPTLQWDF RLEKVVSINV SGHKYGLVYP
     GVGWVVWRSP EFLPKELIFN INYLGAEQAS FTLNFSKGAS HVIGQYYQMI RLGKRGYRSV
     MVNITRIADY LADQLEQLGF IIMSQRRGRG LPLVAFRLPA DRADETFDEF AIAHQLRERG
     WIVPAYTMAP HSNNLKLMRV VVREDFSMSR CDQLLSDIKL ALKSLREMDQ AMLERYTQHV
     RSHTTKSHRA KHTHPHYKNE THSLQGRTGK THGVC
//
  All links  
Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (6)   
   InterPro (5)   
   Pfam (1)   
Literature (1)   
   PubMed (1)   
All databases (16)   

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ID   Q5B1Y3_EMENI            Unreviewed;       515 AA.
AC   Q5B1Y3; C8VGH3;
DT   26-APR-2005, integrated into UniProtKB/TrEMBL.
DT   26-APR-2005, sequence version 1.
DT   25-OCT-2017, entry version 87.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=ANIA_05447 {ECO:0000313|EMBL:CBF81894.1};
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF81894.1, ECO:0000313|Proteomes:UP000000560};
RN   [1] {ECO:0000313|Proteomes:UP000000560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R.,
RA   Batzoglou S., Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M., Hynes M., Paoletti M., Fischer R., Miller B., Dyer P.,
RA   Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2] {ECO:0000313|Proteomes:UP000000560}
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BN001305; CBF81894.1; -; Genomic_DNA.
DR   RefSeq; XP_663051.1; XM_657959.1.
DR   STRING; 162425.CADANIAP00003642; -.
DR   EnsemblFungi; CADANIAT00003642; CADANIAP00003642; CADANIAG00003642.
DR   EnsemblFungi; EAA62607; EAA62607; AN5447.2.
DR   GeneID; 2871735; -.
DR   KEGG; ani:AN5447.2; -.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; FTTSVYG; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000000560; Chromosome V.
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:UP000000560};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000560}.
FT   MOD_RES     294    294       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   515 AA;  58898 MW;  6638DB0638482AC7 CRC64;
     MVHLASIKKD DDFEPVVNRV DSIKLDTIEE DDYSATVYGT RFATQQLPHA EMPDREMPRE
     VAYRMIKDEL SLDGNPMLNL ASFVTTYMED EAEKLMAESF SKNFIDYEEY PQSAEIQNRC
     VNMIARLFNA PTDSDTDHPM GTSTVGSSEA IMLGTLAMKK RWQNKRKAEG KDYSRPNIVM
     NSAVQVCWEK AARYFDVEER YVYCTEERYV IDPQQAVDLV DENTIGICAI LGTTYTGEYE
     DVKAINDLLV ERGLDCPIHV DAASGGFVAP FIHPTLQWDF RLEKVVSINV SGHKYGLVYP
     GVGWVVWRSP EFLPKELIFN INYLGAEQAS FTLNFSKGAS HVIGQYYQMI RLGKRGYRSV
     MVNITRIADY LADQLEQLGF IIMSQRRGRG LPLVAFRLPA DRADETFDEF AIAHQLRERG
     WIVPAYTMAP HSNNLKLMRV VVREDFSMSR CDQLLSDIKL ALKSLREMDQ AMLERYTQHV
     RSHTTKSHRA KHTHPHYKNE THSLQGRTGK THGVC
//
  All links  
Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (6)   
   InterPro (5)   
   Pfam (1)   
Literature (2)   
   PubMed (2)   
All databases (17)   

Download RDF
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