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Database: UniProt/TrEMBL
Entry: A0A0D1DNE1_USTMA
LinkDB: A0A0D1DNE1_USTMA
Original site: A0A0D1DNE1_USTMA 
ID   A0A0D1DNE1_USTMA        Unreviewed;       585 AA.
AC   A0A0D1DNE1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   20-DEC-2017, entry version 20.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=UMAG_06063 {ECO:0000313|EMBL:KIS65974.1};
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS65974.1, ECO:0000313|Proteomes:UP000000561};
RN   [1] {ECO:0000313|EMBL:KIS65974.1, ECO:0000313|Proteomes:UP000000561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H.,
RA   Wosten H.A., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbrugge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C.,
RA   Molina L., Schirawski J., Mendoza-Mendoza A., Greilinger D., Munch K.,
RA   Rossel N., Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U.,
RA   Sandrock B., Meng S., Ho E.C., Cahill M.J., Boyce K.J., Klose J.,
RA   Klosterman S.J., Deelstra H.J., Ortiz-Castellanos L., Li W.,
RA   Sanchez-Alonso P., Schreier P.H., Hauser-Hahn I., Vaupel M.,
RA   Koopmann E., Friedrich G., Voss H., Schluter T., Margolis J.,
RA   Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V., Mannhaupt G.,
RA   Guldener U., Munsterkotter M., Haase D., Oesterheld M., Mewes H.W.,
RA   Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S., Jaffe D.B.,
RA   Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen
RT   Ustilago maydis.";
RL   Nature 444:97-101(2006).
RN   [2] {ECO:0000313|Proteomes:UP000000561}
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G.,
RA   Kahmann R.;
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; CM003160; KIS65974.1; -; Genomic_DNA.
DR   RefSeq; XP_011392424.1; XM_011394122.1.
DR   ProteinModelPortal; A0A0D1DNE1; -.
DR   STRING; 5270.UM06063P0; -.
DR   EnsemblFungi; KIS65974; KIS65974; UMAG_06063.
DR   GeneID; 23565775; -.
DR   KEGG; uma:UMAG_06063; -.
DR   EuPathDB; FungiDB:UMAG_06063; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   Proteomes; UP000000561; Chromosome 21.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR   GO; GO:0006538; P:glutamate catabolic process; IEA:EnsemblFungi.
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; 2.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000561};
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:UP000000561}.
FT   MOD_RES     308    308       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   585 AA;  65161 MW;  0E1FD8D97B5764DD CRC64;
     MSLSQHIDPE ELIEQAADHP ILGLLEHPAG KHARAYHSGA HAGRYVTEPI PKYKIPQKGT
     DAEATYELLS SELSLDGKPT LNLASFVHTW MPKEATKLMS ETMMVNLCDQ DEYPATMSFH
     NRAVSMLADL WKAPTEKDEN GKRKPAMGVA TTGSSEAIML ACLAAKKRWQ HRMKAQGKSF
     KEPGPNMVFG SNAQVAIEKF ARYFDVEERL VPVSHESRYC LDINKAIEMV DENTICVVVI
     LGSTYTGHYE DVEGMSKLLD EYESKTGISI PIHVDGASGA MVAPFATPEL KWSFEIARVA
     SINTSGHKFG MVYPGLGWVL FRDNEQVPKE LIFELHYLGS VEYSFGLNFS RPAHPVIGQL
     FNFINLGFEG YRRVMQSDLQ NARLLSRALE NSGLYQVLSE IHKPVSSPSA ATGAAALIQQ
     AGSKLTSSTQ SHEQLNQHSA EMYRPGLPVV SFRWSEDFRK RNPNLEQRWM QTLLRAKGWI
     VPNYNLSPDL EHIDILRVVV RENLSETMIE QLVYDIITIT QSLEKQANDG GFRHLAELTS
     SKHDDSTAAK DAEKSTGHHN AAHDKHRGGL PKDSGVQAKG YAKQC
//
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