ID   A0A142EJR7_9BACT        Unreviewed;       485 AA.
AC   A0A142EJR7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Amino acid decarboxylase {ECO:0000313|EMBL:AMQ55372.1};
GN   ORFNames=AO498_03115 {ECO:0000313|EMBL:AMQ55372.1};
OS   Algoriphagus sanaruensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Algoriphagus.
OX   NCBI_TaxID=1727163 {ECO:0000313|EMBL:AMQ55372.1, ECO:0000313|Proteomes:UP000073816};
RN   [1] {ECO:0000313|Proteomes:UP000073816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M8-2 {ECO:0000313|Proteomes:UP000073816};
RA   Shintani M.;
RT   "Complete sequence of Algoriphagus sp. M8-2.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AMQ55372.1, ECO:0000313|Proteomes:UP000073816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M8-2 {ECO:0000313|EMBL:AMQ55372.1,
RC   ECO:0000313|Proteomes:UP000073816};
RX   PubMed=27174266;
RA   Muraguchi Y., Kushimoto K., Ohtsubo Y., Suzuki T., Dohra H., Kimbara K.,
RA   Shintani M.;
RT   "Complete Genome Sequence of Algoriphagus sp. Strain M8-2, Isolated from a
RT   Brackish Lake.";
RL   Genome Announc. 4:0-0(2016).
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}.
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DR   EMBL; CP012836; AMQ55372.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A142EJR7; -.
DR   STRING; 1727163.AO498_03115; -.
DR   KEGG; alm:AO498_03115; -.
DR   PATRIC; fig|1727163.4.peg.645; -.
DR   Proteomes; UP000073816; Chromosome.
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; 3.90.1150.170; -; 2.
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   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:UP000073816}.
FT   MOD_RES         303
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   485 AA;  54427 MW;  3E1D35A7A558E44D CRC64;
     MNKPQDLTLD PENWDQMRAL GHQMIDDLFD YWQSIREQKI WRPIPEEVKD FLNLPIPENA
     QPAEEVYADF KNYVFPYNKG NVHPRFFAWI QGTGTPMGVL ADLLASGMNP NTTIGEHSAM
     YVDRQVVNWC KQLMNFPAEA SGILVSGGSM ANITALTVAR NSFGEEKIRQ RGLKAASAQL
     VLYCSVETHS CIQKAAEIIG LGSEAVRKIG VDDQFQMDVL ELESQIQDDL NQGLLPFCVV
     GTSGTVNTGA IDPLEELLAI SKKYGLWFHI DGAYGALAKL DPAYSSRLKA IESADSLAFD
     LHKWLYVPYE VGCTLIRDAD KHREAFAITP NYLLQESRGL SGGLDSINNY GFELSRGFKA
     LKIWMSLKEH GREKYANMIA QNNQQAAYLA SLVEGHPDLE LMAPVSMSIT CFRMIKPDLD
     ESQLKELNRE ILLRLQEEGI ASPSSTILNG KYTLRIANVN QRTRMEDMDI LVREVVRIGK
     EIHSF
//