ID A1AMJ0_PELPD Unreviewed; 567 AA. AC A1AMJ0; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 91. DE SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ABK98560.1}; GN OrderedLocusNames=Ppro_0931 {ECO:0000313|EMBL:ABK98560.1}; OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1). OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales; OC Desulfuromonadaceae; Pelobacter. OX NCBI_TaxID=338966 {ECO:0000313|EMBL:ABK98560.1, ECO:0000313|Proteomes:UP000006732}; RN [1] {ECO:0000313|EMBL:ABK98560.1, ECO:0000313|Proteomes:UP000006732} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1 RC {ECO:0000313|Proteomes:UP000006732}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D., RA Richardson P.; RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379."; RL Submitted (OCT-2006) 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; CP000482; ABK98560.1; -; Genomic_DNA. DR RefSeq; WP_011734869.1; NC_008609.1. DR AlphaFoldDB; A1AMJ0; -. DR STRING; 338966.Ppro_0931; -. DR KEGG; ppd:Ppro_0931; -. DR eggNOG; COG0076; Bacteria. DR HOGENOM; CLU_011856_0_4_7; -. DR OrthoDB; 9803665at2; -. DR Proteomes; UP000006732; 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:UP000006732}. FT REGION 547..567 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 338 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50" SQ SEQUENCE 567 AA; 63406 MW; F601AEAB63FE23B3 CRC64; MPKKRDAARA NLETLYRIFT VPEAPDSTLG AIDQAIADDV IGFLQTHIVA VEHDLEEIEA YYSSPVIPEE PTYVSEYTEF VKRNLVAQSV HTAAPGFVGH MTSALPYFML PLARLMTALN QNLVKVETSK AFTPMERQVL AMLHRLVYRR PDDFYPPWIH NSQHALGAFC SGGTIANVTA LWVARNRLFA PSRTFGGIAR EGLFRALKHH GCDGIAVLVS ERGHYSFGKA TDLLGFGRDN LIKVKTDGHN RIDLKLLREE YRRLRDRNIL PLALVGIAGT TETGNVDPLE AMADFAQEIG CHFHVDAAWG GPTLFSDRYR SLLAGIERAD SVTIDGHKQL YVPMGAGMVV FKDPTAQSAI EHHANYILRR GSKDLGSHTL EGSRPGMAML VHAGFCIIGR KGYELLIDRG IERARTFAEM VRSHPDFELT SEPELNILTY RFSPAKVQQA LARATDEQRP YINALLDQVN QQLQKHQREA GKTFVSRTRL CVGPRQEEFT VLRAVLANPL TTDEIMEAIL AEQCEIARTP EIQALLRQIE RRCAGGERDE PLQLQDYPGE LDELDES //