ID   B3E5L1_TRIL1            Unreviewed;       538 AA.
AC   B3E5L1;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ACD94682.1};
GN   OrderedLocusNames=Glov_0959 {ECO:0000313|EMBL:ACD94682.1};
OS   Trichlorobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ) (Geobacter
OS   lovleyi).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Trichlorobacter.
OX   NCBI_TaxID=398767 {ECO:0000313|EMBL:ACD94682.1, ECO:0000313|Proteomes:UP000002420};
RN   [1] {ECO:0000313|EMBL:ACD94682.1, ECO:0000313|Proteomes:UP000002420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1151 / DSM 17278 / SZ
RC   {ECO:0000313|Proteomes:UP000002420};
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., Chertkov O., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Sung Y., Fletcher K.E.,
RA   Ritalahti K.M., Loeffler F.E., Richardson P.;
RT   "Complete sequence of chromosome of Geobacter lovleyi SZ.";
RL   Submitted (MAY-2008) 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; CP001089; ACD94682.1; -; Genomic_DNA.
DR   RefSeq; WP_012469032.1; NC_010814.1.
DR   AlphaFoldDB; B3E5L1; -.
DR   STRING; 398767.Glov_0959; -.
DR   KEGG; glo:Glov_0959; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_011856_0_4_7; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000002420; 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:UP000002420}.
FT   MOD_RES         335
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   538 AA;  59494 MW;  B51ACF4BF660F4A0 CRC64;
     MPTKARANLE TLYRIFTVPE APDSTLGAVD QAITADVAGF LQNHIVAMER PLEEIEASFS
     SVTIPEEPTY VSDYTEFVKE NLVAQSVHTA SPGFIGHMTS ALPYFMLPLT RLMTALNQNT
     VKVETSKAFT PLERQVLAML HHLIYRCPDE FYPSWIHNSQ AALGAFCSGG TIANTTALWV
     ARNRFFAPDG AFRGIAQEGL ARALKHRGVD GIAVLVSERG HYSLGKAADL LGVGRDHLVK
     VKTAEDNRID LKALRQECQR LQDQNIRPLA LVGIGGTTET GNIDPLEAMA DLARELDCHF
     HVDAAWGGPT LFSDRHRHLL AGIERADSVT IDAHKQLYVP MGAGMVLFRD PTAVSAIEHH
     AAYILRHGSK DLGSHTLEGS RPGKALLVHA GLSIMGRKGY ELLIDLGIER ARTFAGMIRQ
     HPDFELTSEP ELNILTYRYC PAAIQHLLAT APQAEQARIN GLLDQVCQLL QKHQRESGKT
     FVSRTRLRMS RYGEEITVLR SVLANPLTTD EILTSVLSEQ CEIVRQPEIQ ALLQQVWR
//