ID B9M3A1_GEODF Unreviewed; 556 AA.
AC B9M3A1;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Pyridoxal-5'-phosphate-dependent decarboxylase {ECO:0000313|EMBL:ACM19511.1};
GN OrderedLocusNames=Geob_1151 {ECO:0000313|EMBL:ACM19511.1};
OS Geotalea daltonii (strain DSM 22248 / JCM 15807 / FRC-32) (Geobacter
OS daltonii).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geotalea.
OX NCBI_TaxID=316067 {ECO:0000313|EMBL:ACM19511.1, ECO:0000313|Proteomes:UP000007721};
RN [1] {ECO:0000313|EMBL:ACM19511.1, ECO:0000313|Proteomes:UP000007721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22248 / JCM 15807 / FRC-32
RC {ECO:0000313|Proteomes:UP000007721};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Kostka J., Richardson P.;
RT "Complete sequence of Geobacter sp. FRC-32.";
RL Submitted (JAN-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}.
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DR EMBL; CP001390; ACM19511.1; -; Genomic_DNA.
DR RefSeq; WP_012646240.1; NC_011979.1.
DR AlphaFoldDB; B9M3A1; -.
DR STRING; 316067.Geob_1151; -.
DR KEGG; geo:Geob_1151; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_011856_0_4_7; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000007721; 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:UP000007721}.
FT MOD_RES 338
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 556 AA; 60908 MW; 0238BBFE25959B0D CRC64;
MLKNREAARA NLENLYRIFT VPEAPDSTLG AIDQAIAADV TGFLQTHIVA IERDLEAIEA
DFASAIIPEE PTYVSEYTEF VKENLVAQSV HTAAPGFVGH MTSAIPYFML PLARLMTALN
QNLVKVETSK AFTPMERQVL AMLHHLVYRR DADFYPAWIH NSQHALGAFC SGGTIANVTA
LWVARNRLFA PSADFGGLAQ EGLGRALQHR GAEGIAVLVS ERGHYSFGKA ADLLGLGRDN
LIKVQTDAHN RVDLKLLREE VRRLQDRNIL PLALVGIAGT TETGNVDPLE ALADLAGELG
CHFHVDAAWG GPTLFSDRFR SLLSGIERAD SVTIDAHKQL YVPMGAGMVV FKDPTALSAI
EHHANYILRH GSKDLGSHTL EGSRPGMAML VHAGLSIIGR KGYELLMDMG IERARTFAAM
IRQYPDFELT SEPELNILTY RYCPLNVQKA LAAAPAEQRA GINALLDQVC QLLQKHQREA
GKTFVSRTRL RVARHDEELT VLRVVLANPL TTDEILAAVL AEQCEIVQQP EIQGLLQQVE
EICTGLTAKA ADQSPN
//
