ID A0A0K0XS35_9GAMM Unreviewed; 478 AA.
AC A0A0K0XS35;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000313|EMBL:AKS40432.1};
DE SubName: Full=Glutamate/tyrosine decarboxylase-like PLP-dependent enzyme {ECO:0000313|EMBL:MBB6088246.1};
GN ORFNames=HNQ63_002727 {ECO:0000313|EMBL:MBB6088246.1}, WM2015_41
GN {ECO:0000313|EMBL:AKS40432.1};
OS Wenzhouxiangella marina.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Wenzhouxiangellaceae; Wenzhouxiangella.
OX NCBI_TaxID=1579979 {ECO:0000313|EMBL:AKS40432.1, ECO:0000313|Proteomes:UP000066624};
RN [1] {ECO:0000313|EMBL:AKS40432.1, ECO:0000313|Proteomes:UP000066624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42284 {ECO:0000313|EMBL:AKS40432.1,
RC ECO:0000313|Proteomes:UP000066624};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB6088246.1, ECO:0000313|Proteomes:UP000581413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 103414 {ECO:0000313|EMBL:MBB6088246.1,
RC ECO:0000313|Proteomes:UP000581413};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) 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}.
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DR EMBL; CP012154; AKS40432.1; -; Genomic_DNA.
DR EMBL; JACHIC010000004; MBB6088246.1; -; Genomic_DNA.
DR RefSeq; WP_049724150.1; NZ_JACHIC010000004.1.
DR AlphaFoldDB; A0A0K0XS35; -.
DR STRING; 1579979.WM2015_41; -.
DR KEGG; wma:WM2015_41; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000066624; Chromosome.
DR Proteomes; UP000581413; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
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; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR PANTHER; PTHR11999:SF177; MIP05841P; 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:UP000066624}.
FT MOD_RES 308
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 478 AA; 52051 MW; 8898F474C3F46E05 CRC64;
MVSDELIGRL GELEAQARQL DPRPDQRRRD GQQALAHAEA FLEALDDAPA YVHRDGRAAG
LLEQPIAEQG IGLERALGLL DAHVDHEGIT TASGRFGGYI PGGGLFHSAL GDFLAAITNR
YSGVFFASPG AVRLENQLVR WMAELVGLPE GSAGALSSGG SIANLSAIVA ARDAHGIEGE
RIEKAVIYLT EHTHHCVDKA LHLAGLGRIV QRRIAVDGNH RLRAEALCEQ IERDRAEGLE
PWMVLASAGT TNTGSVDPLE AIASIAGEQG LWFHVDAAYG GFFLLTEAGR QRMRGIERAD
SVVMDPHKTL FLPYGCGVVL VRDGERLRAS HSGQADYLQD TMIAMDEASP ADLSPELTRH
FRGLRLWLPL QVLGLAPFRA ALEEKLLLAR YFRQRMIEGG RFEVGPEPDL SVVTFRLPEG
DAANQALMNA LLDDGRVFLS STRLDGRYTL RLAAVCHRTH RRDVDEMVDV LHRLAAGS
//