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Database: UniProt/TrEMBL
Entry: A0A0S2JD41_9GAMM
LinkDB: A0A0S2JD41_9GAMM
Original site: A0A0S2JD41_9GAMM 
ID   A0A0S2JD41_9GAMM        Unreviewed;       543 AA.
AC   A0A0S2JD41;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   28-FEB-2018, entry version 10.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:ALO33954.1};
GN   ORFNames=CMT41_03835 {ECO:0000313|EMBL:ALO33954.1};
OS   Colwellia sp. MT41.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=58049 {ECO:0000313|EMBL:ALO33954.1, ECO:0000313|Proteomes:UP000065319};
RN   [1] {ECO:0000313|EMBL:ALO33954.1, ECO:0000313|Proteomes:UP000065319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MT41 {ECO:0000313|EMBL:ALO33954.1,
RC   ECO:0000313|Proteomes:UP000065319};
RA   Kyaw T.S., Ugalde J., Peoples L., Narasingarao P., Chastain R.A.,
RA   Yayanos A., Methe B.A., Bartlett D.H.;
RT   "Distinctive Gene and Protein Characteristics of Extremely Piezophilic
RT   Colwellia.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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; CP013145; ALO33954.1; -; Genomic_DNA.
DR   RefSeq; WP_057179869.1; NZ_CP013145.1.
DR   EnsemblBacteria; ALO33954; ALO33954; CMT41_03835.
DR   KEGG; com:CMT41_03835; -.
DR   KO; K01580; -.
DR   Proteomes; UP000065319; Chromosome.
DR   GO; GO:0016831; F:carboxy-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; 3.40.640.10; -; 1.
DR   InterPro; IPR022517; Asp_decarboxylase_pyridox.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03799; NOD_PanD_pyr; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000065319};
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:UP000065319}.
FT   MOD_RES     338    338       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   543 AA;  60419 MW;  E8892DEAB1596093 CRC64;
     MRATKRIAEA TQESLHRIFT IAEAPDSTLG RLEQEMSQNL VGFLNNHIVA SKNALSDIEK
     DFVNPHIPEQ PEFVSDHMHH LLDKLVAQSV HTSSPSFIGH MTSALPAFIL PLSKLMVGLN
     QNLVKVETSK AFTPLERQVI GMMHNLIYQQ DDDFYKSWMH SAQHSLGTFC SGGTVANITA
     LWVARNKLLQ ADGDFRGVAR EGLHRAMRHY GYQDLAILVS ERGHYSLKKS ADILGIGQEN
     VIAIATDENN KIDCQKLAEK CQQLSAKNIK VLAIVGVAGT TETGNVDPLD KMAVIAQKIQ
     CHFHVDAAWG GATLLSNKYR PLLKGIEQAD SVTIDAHKQM YVPMGAGIVI FKDPGSVSAI
     EHHAEYILRK GSKDLGSHTL EGSRPGMAML VYASLHIISR PGYEMLINQA IEKAEYFAEI
     INQHDSFELI TRPELCLLTY RYAPKSVQAL LARNDNDANK SVNLLLGQLT KFIQKRQRED
     GRSFVSRTRI EVGKYGGEKV IVFRVVLANP LTTKEILQDI LEQQCQLALE SENFLPELLQ
     IAK
//
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