ID   A0A1H7R2P7_9RHOB        Unreviewed;       468 AA.
AC   A0A1H7R2P7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Glutamate or tyrosine decarboxylase {ECO:0000313|EMBL:SEL54369.1};
GN   ORFNames=SAMN04488526_2911 {ECO:0000313|EMBL:SEL54369.1};
OS   Jannaschia helgolandensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia.
OX   NCBI_TaxID=188906 {ECO:0000313|EMBL:SEL54369.1, ECO:0000313|Proteomes:UP000199283};
RN   [1] {ECO:0000313|EMBL:SEL54369.1, ECO:0000313|Proteomes:UP000199283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14858 {ECO:0000313|EMBL:SEL54369.1,
RC   ECO:0000313|Proteomes:UP000199283};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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|RuleBase:RU000382}.
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; FNZQ01000006; SEL54369.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7R2P7; -.
DR   STRING; 188906.SAMN04488526_2911; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000199283; 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:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.170; -; 1.
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   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   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:UP000199283}.
FT   MOD_RES         298
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   468 AA;  49519 MW;  13438D610F27E516 CRC64;
     MTGTSEGHRL DPTDWSAFEA DLHRVASACV ARLRAARELP WQAPPEDMAA RVAITGRGMP
     TTDLFDRIAT DIMPHATGNT HPRFWGWVHG TGTATGVAAE MVAATMNANM GGRDQGGAEV
     ERAVIKWLHD IAGWQDGSGL MTSGTSQATI LALSCARMRA FPSVRADGLA ALPEMRVYIA
     AGGHSCVKKA LEVMGHGAAA IVQVPAPMGR MDVDALRAAI AADRTAGRHP LAVVGTVGSV
     NLGTYDDLNA LADVARDEEM WLHCDAAFGF WTRLADAPWR DLSKGIERAD SVAMDFHKWM
     AVPYSAGAVL IRDETLHLAT FRERPEYLAA GADGLAGGDW WATDYGLELS RSFSALKVWA
     TVEGLGMDAL GAQITDNCRQ AAHMGDLAQA SDVLDLAAPV VSNLCVIRPL QGEASALAAQ
     LQLSGEAVFS TTIVDGTSCL RAAIVNHRTT TVDVEAAVRA LESAARAA
//