ID A0A0J9E7U3_9RHOB Unreviewed; 449 AA.
AC A0A0J9E7U3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000313|EMBL:KMW58801.1};
DE EC=4.1.1.28 {ECO:0000313|EMBL:KMW58801.1};
GN ORFNames=AIOL_003781 {ECO:0000313|EMBL:KMW58801.1};
OS Candidatus Rhodobacter lobularis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1675527 {ECO:0000313|EMBL:KMW58801.1, ECO:0000313|Proteomes:UP000037178};
RN [1] {ECO:0000313|EMBL:KMW58801.1, ECO:0000313|Proteomes:UP000037178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGS {ECO:0000313|EMBL:KMW58801.1};
RA Jourda C., Santini S., Claverie J.-M.;
RT "Draft genome sequence of an Alphaproteobacteria species associated to the
RT Mediterranean sponge Oscarella lobularis.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KMW58801.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFTY01000002; KMW58801.1; -; Genomic_DNA.
DR RefSeq; WP_053101309.1; NZ_LFTY01000002.1.
DR AlphaFoldDB; A0A0J9E7U3; -.
DR STRING; 1675527.AIOL_003781; -.
DR PATRIC; fig|1675527.3.peg.3961; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000037178; Unassembled WGS sequence.
DR GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IEA:UniProtKB-EC.
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:UP000037178}.
FT MOD_RES 286
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 449 AA; 47933 MW; F357B38DFC560087 CRC64;
MTDRPKTPRP FPFDAAQTTR MLDWARARIE DGPDPKAGAR DFATLEPVLG GSVTENGIGA
EAAFRLFTDA IVPTTRPYDH PASLSFVAAA PSTASLSFDA VLGAAEIFAG NWDGGAGAVH
AENQALAWLA GLAGWDGKAG GVFVAGGTLG NLSALHAARN WAAAQRERPE RWAILASVEA
HSSIKAVADV MDVDLILVET DTNGRMSAEA AKQALTGREC AIVANAGATN CGSVDDILGL
ADLAEEQGLW LHLDGAYGLA AIADPEARAI FEGIERAHSF IVDPHKWLFA PYDSCALVYR
DARWGAAAHG QRAAYLDAVD QAAWNPSDYA LHLTRRARGL PLWFSLATHG SRAYGEAIAT
TLRIARDIAE GIDAMPGLEL TLGPQLTVIL FRPHAMSDAE MEVWAETHRR SGALLCLPTT
WRGRKVFRLC IVNPTTDPKE ILAVLETLT
//
