ID A0A0M1J9G2_9GAMM Unreviewed; 451 AA.
AC A0A0M1J9G2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:KOR29936.1};
GN ORFNames=TI03_00950 {ECO:0000313|EMBL:KOR29936.1};
OS Achromatium sp. WMS1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Achromatium.
OX NCBI_TaxID=1604834 {ECO:0000313|EMBL:KOR29936.1, ECO:0000313|Proteomes:UP000036736};
RN [1] {ECO:0000313|EMBL:KOR29936.1, ECO:0000313|Proteomes:UP000036736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMS1 {ECO:0000313|EMBL:KOR29936.1};
RX PubMed=26322031; DOI=10.3389/fmicb.2015.00822;
RA Mansor M., Hamilton T.L., Fantle M.S., Macalady J.L.;
RT "Metabolic diversity and ecological niches of Achromatium populations
RT revealed with single-cell genomic sequencing.";
RL Front. Microbiol. 6:822-822(2015).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOR29936.1}.
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DR EMBL; JXSM01000022; KOR29936.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M1J9G2; -.
DR PATRIC; fig|1604834.3.peg.463; -.
DR Proteomes; UP000036736; Unassembled WGS sequence.
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; 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 PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 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:UP000036736}.
FT MOD_RES 286
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 451 AA; 48824 MW; 4D229CABFEAB6496 CRC64;
MNEALFMEIA KRAWYYQEGI LSRSVVPSAA AMDKLQELKD KPLPENPTSA TEVLDMLDRY
GSPATIASTG GRYFGLVVGS TLPAALAANW LVTTWDQNAA ARIMAPGTVA IETVAARWIL
ELLSLPAQSG VGFVTGSTMA HFVCLAAARN ALLTKMGWDV ENDGLFGAPS FRVVVSQDVH
ISVIKVLGML GLGRNRIERV PVDAEGRMLT SQLPALDDKT VVCIQAGNVH TGNFDPATEI
CARAQDAGAW VHVDGAFGLW AAASPRYAHL VAGVAKADSW GVDAHKWLNV PYDCGIAICR
DPIPMQSALA VRSEYLVFDP QGEPEDFTPE MSRRARGIDV WAAIQSLGRK GMANLIELSC
EHAQTFKTRL TQAGFEVLNE VVINQVLVAF GTDEHTKHVV NTLQQDGTTW CGDTIWQGRV
VMRISISSWC TSSEDVNRSI DAIIKIATAT K
//
