ID A0A193KC98_9VIBR Unreviewed; 549 AA.
AC A0A193KC98;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 28-FEB-2018, entry version 9.
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 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 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
//
