ID A0A1W9HAS3_9PROT Unreviewed; 452 AA.
AC A0A1W9HAS3;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:OQW44404.1};
GN ORFNames=A4S16_03715 {ECO:0000313|EMBL:OQW44404.1};
OS Proteobacteria bacterium SG_bin6.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1827383 {ECO:0000313|EMBL:OQW44404.1, ECO:0000313|Proteomes:UP000192863};
RN [1] {ECO:0000313|EMBL:OQW44404.1, ECO:0000313|Proteomes:UP000192863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG_bin6 {ECO:0000313|EMBL:OQW44404.1};
RX PubMed=28390307; DOI=10.1016/j.watres.2017.03.042;
RA Wang Y., Ma L., Mao Y., Jiang X., Xia Y., Yu K., Li B., Zhang T.;
RT "Comammox in drinking water systems.";
RL Water Res. 116:332-341(2017).
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:OQW44404.1}.
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DR EMBL; LWDJ01000044; OQW44404.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9HAS3; -.
DR Proteomes; UP000192863; 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}.
FT MOD_RES 286
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 452 AA; 47457 MW; A54FFDE3FC2E15D2 CRC64;
MTELDLLADA DARARNYVAT SSARRAYPDP EALAALSGFD EPLPVQGAAP EETLAMLDRL
GSPATVASNG PRYFGFVKGA SLPVAAAAER LVLAWDQSAA SAVGAPGPAA IERVAGRWIT
EILDLPRESA VGFGTSASAC TIGCLTAARR TLLGRLGWNF DAQGLDGAPP LRVVISETAH
ITVKKALRLL GFGLERVILA PVDGQGRVDP ARLPPLDDRT ILCLQAGEVN TGSFDPFAAI
LPCAREAGAW VHVDGAFGLW ARAAAASRPL TEGIALADSW TTDGHKWLNT PYDGAMSICR
DAGALAAAMN SDAAYATSEP DAQKNLTLEF SRRARGVAIW AALRSLGREG VAALVDRHRA
QARRLGDGLA AAGFEVLNDV VLNQVLIRAG SSEQTEQVRQ AAAASGEIWF GPTIWQGAPA
ARLSVCSWRT TDADIDRAIA LLARLLRAGT AR
//
