GenomeNet

Database: UniProt/TrEMBL
Entry: A0A0H4IG43_9ALTE
LinkDB: A0A0H4IG43_9ALTE
Original site: A0A0H4IG43_9ALTE 
ID   A0A0H4IG43_9ALTE        Unreviewed;       551 AA.
AC   A0A0H4IG43;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   07-JUN-2017, entry version 8.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:AKO53887.1};
GN   ORFNames=ABA45_16805 {ECO:0000313|EMBL:AKO53887.1};
OS   Marinobacter psychrophilus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Marinobacter.
OX   NCBI_TaxID=330734 {ECO:0000313|EMBL:AKO53887.1, ECO:0000313|Proteomes:UP000036406};
RN   [1] {ECO:0000313|EMBL:AKO53887.1, ECO:0000313|Proteomes:UP000036406}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20041 {ECO:0000313|EMBL:AKO53887.1,
RC   ECO:0000313|Proteomes:UP000036406};
RA   Song L., Ren L., Yu Y., Wang X.;
RT   "Complete genome of Marinobacter psychrophilus strain 20041T isolated
RT   from sea-ice of the Canadian Basin.";
RL   Submitted (MAY-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}.
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; CP011494; AKO53887.1; -; Genomic_DNA.
DR   RefSeq; WP_048388076.1; NZ_CP011494.1.
DR   EnsemblBacteria; AKO53887; AKO53887; ABA45_16805.
DR   KEGG; mpq:ABA45_16805; -.
DR   PATRIC; fig|330734.3.peg.3531; -.
DR   KO; K01580; -.
DR   Proteomes; UP000036406; 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   Gene3D; 3.90.1150.10; -; 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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
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:UP000036406};
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   551 AA;  60991 MW;  154A46B969151738 CRC64;
     MTGIKKSAQA SVEAMYRVFT IPEAPDSTLS RIDQDISRNL AGFLQDHIVA VERDLADVEK
     NFSEYSVPEK PIFVSEQTQF LLDKLVANSV HTASPAFIGH MTSALPYFML PLSKIMIALN
     QNLVKTETSK AFTPLERQVL GMIHRLVFEQ DGSFYRKWMH NPRYALGAMC SGGTVANLTA
     LWVARNHAFP AEGNFRGLQQ EGLFRALKYY GYEGAAIVVS RRGHYSLSKA ADILGLGRDA
     LVTVATDSNN RIQIDALREK CLQLQKQKIK VIALCGVAGT TETGNVDPLE AMADIAREFG
     AHFHVDAAWG GPTLFSRRYR SLLKGIEKAD SVTFDAHKQL YVPMGVGLVV FRDPSLASAV
     EHHAQYVIRK GSRDLGSTTL EGSRPGMAML IHSGLKILAR EGYELLIDTG IGKARTFAAM
     IDEAEDFELI TRPELNILTY RYCPAQVRQA LESADEMLAE KINTSLNRVT KFIQKTQRER
     GKAFVSRTRL EPDNYYNFPC IVFRVVLANP LTTADILSDI LAEQRLLAGE NGIADEMAIL
     NNLAAGARAR A
//
DBGET integrated database retrieval system