ID   DCHS_RAOOR              Reviewed;         228 AA.
AC   Q8L0Z4;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Histidine decarboxylase;
DE            Short=HDC;
DE            EC=4.1.1.22;
DE   Flags: Fragment;
GN   Name=hdc;
OS   Raoultella ornithinolytica (Klebsiella ornithinolytica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Raoultella.
OX   NCBI_TaxID=54291;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=19-2;
RX   PubMed=12089029; DOI=10.1128/aem.68.7.3462-3466.2002;
RA   Kanki M., Yoda T., Tsukamoto T., Shibata T.;
RT   "Klebsiella pneumoniae produces no histamine: Raoultella planticola and
RT   Raoultella ornithinolytica strains are histamine producers.";
RL   Appl. Environ. Microbiol. 68:3462-3466(2002).
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         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- MISCELLANEOUS: This histamine-producing bacteria (HPB) causes histamine
CC       fish poisoning.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; AB075222; BAB97311.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8L0Z4; -.
DR   SMR; Q8L0Z4; -.
DR   STRING; 1286170.RORB6_18940; -.
DR   eggNOG; COG0076; Bacteria.
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   Gene3D; 3.40.640.10; -; 1.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyridoxal phosphate.
FT   CHAIN           <1..>228
FT                   /note="Histidine decarboxylase"
FT                   /id="PRO_0000146956"
FT   BINDING         30
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         143
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         228
SQ   SEQUENCE   228 AA;  25560 MW;  B03AF6CAD1ED556E CRC64;
     NGGTEGNMFG CYLGREIFPN GTLYYSKDTH YSVAKIVKLL RIKSTLVESQ PNGEMDYADL
     IKKIKRDNEK HPIIFANIGT TVRGAIDNIA IIQQSISELG IERKDYYLHA DAALSGMILP
     FVDNPQPFNF ADGIDSIGVS GHKMIGSPIP CGIVVAKKKN VDRISVEIDY ISAHDKTISG
     SRNGHTPLMM WEAIRSHSWE EWRRRIERSL NMAQYAVDRF QSAGIDAW