ID D4ZAE7_SHEVD Unreviewed; 550 AA. AC D4ZAE7; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAR-2024, entry version 63. DE SubName: Full=Glutamate decarboxylase, putative {ECO:0000313|EMBL:BAJ02992.1}; GN OrderedLocusNames=SVI_3021 {ECO:0000313|EMBL:BAJ02992.1}; OS Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / DSS12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=637905 {ECO:0000313|EMBL:BAJ02992.1, ECO:0000313|Proteomes:UP000002350}; RN [1] {ECO:0000313|Proteomes:UP000002350} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12 RC {ECO:0000313|Proteomes:UP000002350}; RX PubMed=20458400; DOI=10.1039/c000396d; RA Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E., Toyonaga H., RA Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M., Kato C., Oshima T., RA Nakasone K., Mori H.; RT "Complete genome sequence and comparative analysis of Shewanella violacea, RT a psychrophilic and piezophilic bacterium from deep sea floor sediments."; RL Mol. Biosyst. 6:1216-1226(2010). 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; AP011177; BAJ02992.1; -; Genomic_DNA. DR AlphaFoldDB; D4ZAE7; -. DR STRING; 637905.SVI_3021; -. DR KEGG; svo:SVI_3021; -. DR eggNOG; COG0076; Bacteria. DR HOGENOM; CLU_011856_0_4_6; -. DR Proteomes; UP000002350; Chromosome. 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:UP000002350}. FT MOD_RES 338 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50" SQ SEQUENCE 550 AA; 61088 MW; C0C217B220F60E5E CRC64; MSMTPRRATA SEEALLRIFT VPEAPDSTLS VIEKNISQNL MGFLQESVVA VEKPLSEIEL DFQQHQIPSA PQFVSDYADE MMKTLVAHSV HTSSPSFIGH MTSALPYFVL PLSKMMVGLN QNLVKIETSK AFTPLERQVL GMMHHLIYSE DDKFYKNWMH SANYSLGAFC SGGTIANITA LWTARNQLLK ADGDFKGVSA QGLMKGLRHY GYDDLAILVS ERGHYSLAKT ADLLGIGRDN IIQVPTSSDN KVDVDKMRAM AKQLDLDNIK VMAIVGVAGT TETGNIDPLD ELATLAVELN CHFHVDAAWG GASLLSNKYR HLLKGIERAD SVTIDAHKQM YVPMGAGMVI FKDPAFANAI KHHAEYILRK GSKDLGSQTL EGSRPGMAML VHACLQIIGR DGYEILINNS LEKARYFAEL IHGQDDFQLV SEPELCLLTY RYVPKSVQEA MQETRESGNT EKLIEFNSLL DGLTKFVQKR QREQGTSFVS RTRINPESRA SLNIQSVVFR VVLANPLTTR EILQQVLAEQ IEIAQQDNEF LPQLLALASN //