ID A0A0J9GTR4_9RHOB Unreviewed; 481 AA.
AC A0A0J9GTR4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000313|EMBL:KMW56913.1};
DE EC=4.1.1.28 {ECO:0000313|EMBL:KMW56913.1};
GN ORFNames=AIOL_001870 {ECO:0000313|EMBL:KMW56913.1};
OS Candidatus Rhodobacter lobularis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1675527 {ECO:0000313|EMBL:KMW56913.1, ECO:0000313|Proteomes:UP000037178};
RN [1] {ECO:0000313|EMBL:KMW56913.1, ECO:0000313|Proteomes:UP000037178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGS {ECO:0000313|EMBL:KMW56913.1};
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|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533, 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:KMW56913.1}.
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DR EMBL; LFTY01000002; KMW56913.1; -; Genomic_DNA.
DR RefSeq; WP_053101225.1; NZ_LFTY01000002.1.
DR AlphaFoldDB; A0A0J9GTR4; -.
DR STRING; 1675527.AIOL_001870; -.
DR PATRIC; fig|1675527.3.peg.1967; -.
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:0006520; P:amino 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; IPR010977; Aromatic_deC.
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 PRINTS; PR00800; YHDCRBOXLASE.
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 300
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 481 AA; 51920 MW; 97582E7CC114AA5F CRC64;
MAAPAVRQDH IKVSKQLPLE RAAAYGQTFR CQPRPLHPTA TTQQLRDQFC KPLPEMPTPG
EAVIDQLIAA AEPGLVGNTD PNFYAWVMGG SDPVGVAADW LTSIWGQNAA IFQTSPAAAI
AEEAVSEWLL DLLDLPRSCS VGFVTGATMA GFVALAAART TVLARQGHDF EQNGLQSAPL
IQIYISDDSH ASNLAALRHL GFGEANLVRI PSDADGLMST EDLKMAMVQT VGPKIIIATA
GHINSGGFEN FELIADLAQE HNAWLHVDGA FGLWARVLPE MAHLTRGLER ADSWSVDGHK
WLQIPYDSGF AIVKDAQAHK RAMDISAGYL NQADEDGRNP TEFNPELSRR ARGFAAWAIM
RSLGKSGIRD LVAEHCESAR GLAEQIDAIP GVYVIGSVTL NQIILAVSHE FADPCAMTKS
LAGILNSDHG VFVRTAEWKG RTVLRFSLIT KGTGASQTQF LSKAIRSSLK QVLENPVFAK
N
//
