ID   A0A0N8KFB5_9BACT        Unreviewed;       419 AA.
AC   A0A0N8KFB5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Tyrosine decarboxylase {ECO:0000313|EMBL:KPQ13674.1};
GN   ORFNames=HLUCCX10_12410 {ECO:0000313|EMBL:KPQ13674.1};
OS   Algoriphagus marincola HL-49.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Algoriphagus.
OX   NCBI_TaxID=1305737 {ECO:0000313|EMBL:KPQ13674.1, ECO:0000313|Proteomes:UP000050421};
RN   [1] {ECO:0000313|EMBL:KPQ13674.1, ECO:0000313|Proteomes:UP000050421}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-49 {ECO:0000313|EMBL:KPQ13674.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         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:KPQ13674.1}.
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DR   EMBL; LJXT01000083; KPQ13674.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N8KFB5; -.
DR   STRING; 1305737.GCA_000526355_01631; -.
DR   PATRIC; fig|1305737.6.peg.3119; -.
DR   eggNOG; COG0076; Bacteria.
DR   Proteomes; UP000050421; Unassembled WGS sequence.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.10; 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   PANTHER; PTHR46101; -; 1.
DR   PANTHER; PTHR46101:SF18; HISTIDINE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
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}.
FT   MOD_RES         267
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   419 AA;  47686 MW;  CFAD5A174DD4EA54 CRC64;
     MMIEMKYWKK LNAEQRLNRV QQALKDNVDF SKDANLGYPA SRLDEKVFTN ESLFLREMPV
     LSTYIANPNH IGCHTFGTSE FAFKGTQDIE REVLNMMAVD LFKIEEDQFD GYISPGGTEA
     NAQAIWIYRN EFMKKFGAKV DEIVILASED THYSIPKSAN LLMLDWEKVP VDTETRDVTP
     EAVRGSIKAA LGKGKKYFIV VANMGTTMFG SVDDPTVFTD ALKEYQLPFR LHIDGAYGGF
     VYPFGDFENQ INFTNPDITS ITIDAHKMLQ APYGTGIFVC RKGLIENVLT SEAKYVEGMD
     LTLCGSRSGA NAVAVWVILT TYGPHKWYEK ISVIKMRTNW LCKQLDQLGV TYFREPEMNI
     VTIRSECVPE ELAHKYNLVP QTHDESNQWY KIVLMDHVEI EHLKDFIQDM VSCGHPNPS
//