ID   DCHS_SOLLC              Reviewed;         413 AA.
AC   P54772;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Histidine decarboxylase;
DE            Short=HDC;
DE            EC=4.1.1.22;
DE   AltName: Full=TOM92;
GN   Name=HDC;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Ailsa Craig;
RX   PubMed=8219096; DOI=10.1007/bf00019310;
RA   Picton S., Gray J.E., Payton S., Barton S.L., Lowe A., Grierson D.;
RT   "A histidine decarboxylase-like mRNA is involved in tomato fruit
RT   ripening.";
RL   Plant Mol. Biol. 23:627-631(1993).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-histidine = CO2 + histamine; Xref=Rhea:RHEA:20840,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57595,
CC         ChEBI:CHEBI:58432; EC=4.1.1.22;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- TISSUE SPECIFICITY: Ripe fruits; not detected in leaves and unripe
CC       fruit.
CC   -!- DEVELOPMENTAL STAGE: Accumulates during early fruit ripening and then
CC       declines.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; X71900; CAA50719.1; -; mRNA.
DR   PIR; S39554; S39554.
DR   RefSeq; NP_001234136.2; NM_001247207.2.
DR   AlphaFoldDB; P54772; -.
DR   SMR; P54772; -.
DR   STRING; 4081.Solyc08g066250.2.1; -.
DR   PRIDE; P54772; -.
DR   GeneID; 544085; -.
DR   KEGG; sly:544085; -.
DR   eggNOG; KOG0629; Eukaryota.
DR   InParanoid; P54772; -.
DR   OrthoDB; 810772at2759; -.
DR   BRENDA; 4.1.1.22; 3101.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; P54772; baseline.
DR   GO; GO:0004398; F:histidine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   2: Evidence at transcript level;
KW   Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..413
FT                   /note="Histidine decarboxylase"
FT                   /id="PRO_0000146954"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         242
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   413 AA;  47629 MW;  5361F40D8D9A99D3 CRC64;
     MESDIKNETS FQELDMILTQ YLETLSERKK YHIGYPINMC YEHHATLAPL LQFHLNNCGD
     PFTQHPTDFH SKDFEVAVLD WFAQLWEIEK DEYWGYITSG GTEGNLHGFW LGRRELLPNG
     YLYASKDSHY SIFKAARMYR MELQTINTLV NGEIDYEDLQ SKLLVNKNKP AIININIGTT
     FKGAIDDLDF VIQTLENCGY SNDNYYIHCD RALCGLILPF IKHAKKITFK KPIGSISISG
     HKFLGCPMSC GVQITRRSYV STLSKIEYIN SADATISGSR NGFTPIFLWY CLSKKGHARL
     QQDSITCIEN ARYLKDRLLE AGISVMLNDF SITVVFERPC DHKFIRRWNL CCLRGMAHVV
     IMPGITRETI DSFFKDLMQE RNYKWYQDVK ALPPCLADDL ALNCMCSNKK MHN