ID C9P436_VIBME Unreviewed; 550 AA.
AC C9P436;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Glutamate decarboxylase eukaryotic type {ECO:0000313|EMBL:EEX36940.1};
DE EC=4.1.1.15 {ECO:0000313|EMBL:EEX36940.1};
GN ORFNames=VIB_001047 {ECO:0000313|EMBL:EEX36940.1};
OS Vibrio metschnikovii CIP 69.14.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=675813 {ECO:0000313|EMBL:EEX36940.1, ECO:0000313|Proteomes:UP000005604};
RN [1] {ECO:0000313|EMBL:EEX36940.1, ECO:0000313|Proteomes:UP000005604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 69.14 {ECO:0000313|EMBL:EEX36940.1,
RC ECO:0000313|Proteomes:UP000005604};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., Bartels D.,
RA Vonstein V.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
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; ACZO01000006; EEX36940.1; -; Genomic_DNA.
DR RefSeq; WP_004395037.1; NZ_ACZO01000006.1.
DR AlphaFoldDB; C9P436; -.
DR STRING; 675813.VIB_001047; -.
DR GeneID; 79888022; -.
DR eggNOG; COG0076; Bacteria.
DR Proteomes; UP000005604; Unassembled WGS sequence.
DR GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
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:UP000005604}.
FT MOD_RES 338
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 550 AA; 61347 MW; CE695E5C152B0F3D CRC64;
MVSEHKIADA SFESLLRIFT VPEGPDSTLT RIEEELSRNL NQFLREHIVA EEKPLKEIEK
DFSNPHIPEA PEFVSEHTQH LMDTLVAQSV HTASPSFIGH MTSALPYFLM PLSKIMIALN
QNLVKIETSK AFTPLERQVL GMLHRLIYAQ QDEFYQQWMH SAAHSLGAFC SGGTIANITA
LWVARNNALQ AREGFGGVEK EGLFKAMLHY GYQGLAILVS ERGHYSLKKA ADILGIGQQG
LVTVRTDNNN RLCPDDLQLK INQLKSQNIH PFAVVGVAGT TETGNVDPLR AIGEICQKEQ
CHFHVDAAWG GATLMSSTYR HLLDGIELAD SVTIDAHKQM YIPMGAGMVL FKDPHAMNAI
EHHAQYILRK GSKDLGSHTL EGSRSGMAML VYASMHIISR AGYQLLIDQS IEKARYFADL
IQSQTDFELV SEPELCLLTY RYAPDNAIKA LTIADEKEKT ALNHLLNELT KYIQKKQRET
GKSFVSRTQL NPARWQGLDT LVFRVVLANP LTTRSILHSV LQEQRDIAQT ATQLLAQINQ
SSQSIISSQA
//
