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Database: UniProt/TrEMBL
Entry: A0A193KC98_9VIBR
LinkDB: A0A193KC98_9VIBR
Original site: A0A193KC98_9VIBR 
ID   A0A193KC98_9VIBR        Unreviewed;       549 AA.
AC   A0A193KC98;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   07-JUN-2017, entry version 8.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:ANO33036.1};
GN   ORFNames=A6E01_07370 {ECO:0000313|EMBL:ANO33036.1};
OS   Vibrio breoganii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=553239 {ECO:0000313|EMBL:ANO33036.1, ECO:0000313|Proteomes:UP000092018};
RN   [1] {ECO:0000313|EMBL:ANO33036.1, ECO:0000313|Proteomes:UP000092018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FF50 {ECO:0000313|EMBL:ANO33036.1,
RC   ECO:0000313|Proteomes:UP000092018};
RA   Hehemann J.-H., Arevalo P., Datta M.S., Yu X., Corzett C.,
RA   Henschel A., Preheim S.P., Timberlake S., Alm E.J., Polz M.F.;
RT   "Adaptive Radiation by Waves of Gene Transfer Leads to Fine-Scale
RT   Resource Partitioning in Marine Microbes.";
RL   Submitted (JUN-2016) 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; CP016177; ANO33036.1; -; Genomic_DNA.
DR   RefSeq; WP_065209949.1; NZ_MAKG01000218.1.
DR   EnsemblBacteria; ANO33036; ANO33036; A6E01_07370.
DR   KEGG; vbr:A6E01_07370; -.
DR   KO; K01580; -.
DR   Proteomes; UP000092018; Chromosome 1.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000092018};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   COILED      247    274       {ECO:0000256|SAM:Coils}.
FT   MOD_RES     338    338       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   549 AA;  61170 MW;  5F42A8B3723FFD64 CRC64;
     MVSQDKTAKV DFESLLRIFT VPEGPESTLT QIEDRLSLNL NEFLKEHIVA EEKPLREIEK
     DFNDSLLPES PTFVSEHTQH LLDTLVSHSV HTSSPSFIGH MTSALPYFLM PLSKIMIALN
     QNLVKIETSK AFTPLERQVL GMLHSLIYAQ TDDFYSQWMH SAQHSLGAFC SGGTIANITA
     LWVARNNAFP ADGEFKGIEQ QGIFKALKHY GYEGIAILVS ERGHYSLKKA ADVLGIGRES
     LIAVKTNENN KICLDDLEAK LVELEESRIK TIAVVGIAGT TETGNIDPLE DIAKQCQKHQ
     CHFHVDAAWG GATLMSNKHR HMLAGIELAD SVTIDAHKQL YIPMGAGMVL FKDPHAMASV
     EHHAAYILRK GSKDLGSHSL EGSRSGMAML VYSSMHIISR PGYELLINEG LDKAQYFADL
     VSQQDDFELI TDPELCLLTY RYIPARVRLA LEKASGKSKH KLNELLNGLT QFIQKRQREN
     GLSFVSRTTL TPKQWDSMTT IVFRVVLANP LTTHDILNSV LNEQREIAKM APSLNKQIDA
     LVSTIESEL
//
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