ID E3BKW3_9VIBR Unreviewed; 548 AA.
AC E3BKW3;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:EFP96307.1};
GN ORFNames=VIBC2010_12099 {ECO:0000313|EMBL:EFP96307.1};
OS Vibrio caribbeanicus ATCC BAA-2122.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=796620 {ECO:0000313|EMBL:EFP96307.1, ECO:0000313|Proteomes:UP000002943};
RN [1] {ECO:0000313|EMBL:EFP96307.1, ECO:0000313|Proteomes:UP000002943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2122 {ECO:0000313|EMBL:EFP96307.1,
RC ECO:0000313|Proteomes:UP000002943};
RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT Scleritoderma cyanea.";
RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFP96307.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEIU01000075; EFP96307.1; -; Genomic_DNA.
DR RefSeq; WP_009601690.1; NZ_AEIU01000075.1.
DR AlphaFoldDB; E3BKW3; -.
DR STRING; 796620.VIBC2010_12099; -.
DR eggNOG; COG0076; Bacteria.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000002943; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR03799; NOD_PanD_pyr; 1.
DR PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000002943}.
FT MOD_RES 338
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 548 AA; 61309 MW; E9D4F1F295B01EA4 CRC64;
MISEHKTAEV SLEHLIRIFT VPEGPDSTLT EIEEKLSQNL NRFLREHIAA EEKPLIDIEK
DFAKATIPES PEFVSQHTQH LLDKLVAHSV HTSSPSFVGH MTSALPYFLM PLSKIMIALN
QNLVKIETSK AFTPLERQVL GMLHRLIYSQ EDSFYARWMH SANHSLGAFC SGGTIANITA
LWVARNNALR AKNEFTGVEK EGLYKAMKYY GYEGLAILVS ERGHYSLKKA ADVLGIGQEG
LVSVATDTNN RICPIALQEK IAQLKNNNIM PFAVVGVAGT TETGNIDPLD EVAKICLQEG
CHFHVDAAWG GATLMSNNYR GLLKGIELAD SVTIDAHKQL YIPMGAGMVL FKNPNAMKSI
EHHAQYILRK GSKDLGSHTL EGSRSGMAML VYAAMHIISR PGYELLIDQS IEKAQYFASM
IENQPDFELI SHPELCLLTY RYIPESVCNA LLVASNERKA ELNDHLNQLT MFIQKKQREA
GKSFVSRTRL NPEKWNKLDT IVFRVVLANP LTNHEVLHLV LEEQRRIAQQ APRLMNSIEQ
LCNDILAS
//
