ID A0A0S7BXE6_9BACT Unreviewed; 480 AA.
AC A0A0S7BXE6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glutamate/tyrosine decarboxylase {ECO:0000313|EMBL:GAP42462.1};
GN ORFNames=TBC1_11591 {ECO:0000313|EMBL:GAP42462.1};
OS Lentimicrobium saccharophilum.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Lentimicrobiaceae;
OC Lentimicrobium.
OX NCBI_TaxID=1678841 {ECO:0000313|EMBL:GAP42462.1};
RN [1] {ECO:0000313|EMBL:GAP42462.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBC1 {ECO:0000313|EMBL:GAP42462.1};
RA Tourlousse D.M., Matsuura N., Sun L., Toyonaga M., Kuroda K., Ohashi A.,
RA Cruz R., Yamaguchi T., Sekiguchi Y.;
RT "Draft Genome Sequence of Bacteroidales Strain TBC1, a Novel Isolate from a
RT Methanogenic Wastewater Treatment System.";
RL Genome Announc. 3:e01168-15(2015).
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; DF968182; GAP42462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7BXE6; -.
DR STRING; 1678841.TBC1_11591; -.
DR PATRIC; fig|1678841.3.peg.671; -.
DR Proteomes; UP000053091; 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 CDD; cd06450; DOPA_deC_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 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 InterPro; IPR021115; Pyridoxal-P_BS.
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.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 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:UP000053091}.
FT MOD_RES 298
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 480 AA; 53902 MW; 504BA81010D9DDFF CRC64;
MLEVMDSKEF RKQAHVLADR MADYFEEISD YPVKSQVKPG EILSALPLSA PVNGESFETI
MSDFERIIMP GITHWQSPSF FAFFPANSSY PSVLAEMLTA ALGQQGMIWE TSPAATELEQ
RVMEWLRELC GLPASWTGVI QDTASASTLT ALLSAREKTT GFRTNLEGFT GMGKLRVYCS
SETHSSIEKA VKIAGFGKNN LVKVAVDENF ALISAQLEMA IKEDLKKGYT PCAAVASIGT
TGSTAVDPVD EIGKICERYK IWLHVDAAFG GTAFLLPEMR HFAAGLEYAD SYVFNPHKWM
FTNFDASAYF VRDPELLIRT FEILPEYLKT RTRGLVNDYR DWGVALGRRF RALKLWFVIR
SFGAEGLREK IRLHNSLAGW LKDRVSEHPD FELMAPVDFS LVCFRYKPKV LSAGEDLDRI
NASLLSELNG SGKLYLSHTR LNGRFVLRMV TAQTTITRDH VLRAWDLIQQ TALKLSLKIE
//
