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Database: UniProt/TrEMBL
Entry: Q5QVR3_IDILO
LinkDB: Q5QVR3_IDILO
Original site: Q5QVR3_IDILO 
ID   Q5QVR3_IDILO            Unreviewed;       549 AA.
AC   Q5QVR3;
DT   04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT   04-JAN-2005, sequence version 1.
DT   20-JUN-2018, entry version 76.
DE   SubName: Full=Glutamate decarboxylase putative {ECO:0000313|EMBL:AAV83088.1};
GN   Name=gadB {ECO:0000313|EMBL:AAV83088.1};
GN   OrderedLocusNames=IL2256 {ECO:0000313|EMBL:AAV83088.1};
OS   Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=283942 {ECO:0000313|EMBL:AAV83088.1, ECO:0000313|Proteomes:UP000001171};
RN   [1] {ECO:0000313|EMBL:AAV83088.1, ECO:0000313|Proteomes:UP000001171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR
RC   {ECO:0000313|Proteomes:UP000001171};
RX   PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA   Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA   Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA   Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S.,
RA   Campbell S., Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT   "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT   loihiensis reveals amino acid fermentation as a source of carbon and
RT   energy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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; AE017340; AAV83088.1; -; Genomic_DNA.
DR   RefSeq; WP_011235483.1; NC_006512.1.
DR   ProteinModelPortal; Q5QVR3; -.
DR   STRING; 283942.IL2256; -.
DR   DNASU; 3173263; -.
DR   EnsemblBacteria; AAV83088; AAV83088; IL2256.
DR   KEGG; ilo:IL2256; -.
DR   eggNOG; ENOG4105DY8; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000282553; -.
DR   KO; K01580; -.
DR   OMA; FHKHFFQ; -.
DR   OrthoDB; POG091H05DC; -.
DR   BioCyc; ILOI283942:IL_RS11570-MONOMER; -.
DR   Proteomes; UP000001171; 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:UP000001171};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES     338    338       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   549 AA;  61069 MW;  D4C420D99625E7A0 CRC64;
     MSPKTDIAEV NQESLYRIFT IPEAPDSTLG KIEKHLSENL MGFLGEHIVA REKPLQEIER
     DFDKSQIPEE PAFVSDHTEF LLDKLVAHSV HTASPRFIGH MTSALPYFLL PLAKLMVGLN
     QNLVKIETSK AFTPLERNVI GMMHHLVYQQ DAPFYNRWMH SAQHSLGAFC SGGTIANMTA
     LWVARNRLLQ ADGDFAGISA DGLAAGLQHY GYSKLTVVVS ERGHYSLSKA ADVLGIGRRN
     LVSVATDSDN RIRIDELRKT CEKIAKEGGK VLALVGVAGT TETGHIDPLD EMATVAEEVD
     AHFHVDAAWG GATLLSEQHR PLLAGIERAD SVTIDAHKQM YVPMGAGLVL FKNPALVKSI
     EYHAEYIIRQ GSKDLGSHTM EGSRAGMAMM VFSAMHVIGR RGYELLINNS IDKARYFSKL
     ISEQDDFEVI TEPELCILTY RFVPIKVKTV LDKATPEQLA RLTPHLNALT RYIQKRQRET
     GQSFVSRTKL TPAQYHHEPT VVFRVVLANP LTTNEMLQEV LCEQRKIAAK ATSLRGALHT
     EMRELGMLI
//
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