ID Q39V49_GEOMG Unreviewed; 550 AA.
AC Q39V49;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 24-JAN-2024, entry version 98.
DE SubName: Full=Pyridoxal-5'-phosphate-dependent decarboxylase {ECO:0000313|EMBL:ABB31875.1};
GN OrderedLocusNames=Gmet_1644 {ECO:0000313|EMBL:ABB31875.1};
OS Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=269799 {ECO:0000313|EMBL:ABB31875.1, ECO:0000313|Proteomes:UP000007073};
RN [1] {ECO:0000313|EMBL:ABB31875.1, ECO:0000313|Proteomes:UP000007073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC {ECO:0000313|Proteomes:UP000007073};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Geobacter metallireducens GS-15.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABB31875.1, ECO:0000313|Proteomes:UP000007073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC {ECO:0000313|Proteomes:UP000007073};
RX PubMed=19473543; DOI=10.1186/1471-2180-9-109;
RA Aklujkar M., Krushkal J., DiBartolo G., Lapidus A., Land M.L., Lovley D.R.;
RT "The genome sequence of Geobacter metallireducens: features of metabolism,
RT physiology and regulation common and dissimilar to Geobacter
RT sulfurreducens.";
RL BMC Microbiol. 9:109-109(2009).
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; CP000148; ABB31875.1; -; Genomic_DNA.
DR RefSeq; WP_004511420.1; NC_007517.1.
DR AlphaFoldDB; Q39V49; -.
DR STRING; 269799.Gmet_1644; -.
DR DNASU; 3740413; -.
DR KEGG; gme:Gmet_1644; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_011856_0_4_7; -.
DR OMA; RHATYHA; -.
DR Proteomes; UP000007073; 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:UP000007073}.
FT MOD_RES 338
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 550 AA; 60722 MW; 3A6F81B10475A03F CRC64;
MPKNRDAARA SLENLYRIFT VPEAPDSTLG AIDQAIAGDV AGFLQTHIVA IERPLEEIEA
DFSSFSIPEE PTYVSEYTEF VKENLVAHSV HTASPAFVGH MTSALPYFML PLARLMTALN
QNVVKVETSK AFTPMERQVL AMLHHLVYGR NDDFYPQWIH NSQHALGAFC SGGTLANVTA
LWVARNRLFA PDGEFRGIAQ EGLARALKHR GADGIAVLVS ERGHYSLGKA ADLLGIGRDD
LIKIKTDANN RIDLKALREE CRRLQDRNTL PLALVGIAGT TETGNVDPLE AMADLAQELG
CHFHVDAAWG GPTLFSDRHR HLLRGIERAD SVTIDGHKQL YVPMGAGMVV FKDPTALSAI
EHHANYILRH GSKDLGSHTL EGSRPGKAML VHAGFSIIGR KGYELLIDMG IERARTFADM
IQRHPDFELI SEPELNILTY RYCPPAIQQA LTDATAQQRA AINGLLDQVC QLLQKYQREA
GKTFVSRTRL HVARHDMELT VLRVVLANPL TTDEILEAVL AEQCEIVRLP EIQALLRQAE
ELCPGLAKAV
//