ID   DCHS_RAOPL              Reviewed;         378 AA.
AC   P28578; Q8KHD1; Q8KHF6;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Histidine decarboxylase;
DE            Short=HDC;
DE            EC=4.1.1.22;
GN   Name=hdc;
OS   Raoultella planticola (Klebsiella planticola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Raoultella.
OX   NCBI_TaxID=575;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43176 / T-2;
RX   PubMed=2033044; DOI=10.1016/s0021-9258(18)92838-3;
RA   Kamath A.V., Vaaler G.L., Snell E.E.;
RT   "Pyridoxal phosphate-dependent histidine decarboxylases. Cloning,
RT   sequencing, and expression of genes from Klebsiella planticola and
RT   Enterobacter aerogenes and properties of the overexpressed enzymes.";
RL   J. Biol. Chem. 266:9432-9437(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 91-318.
RC   STRAIN=19-3, 27-1, 28-1, 42-1, S8, and Y1-1;
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   -!- 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; M62746; AAA25071.1; -; Genomic_DNA.
DR   EMBL; AB075216; BAB97305.1; -; Genomic_DNA.
DR   EMBL; AB075217; BAB97306.1; -; Genomic_DNA.
DR   EMBL; AB075218; BAB97307.1; -; Genomic_DNA.
DR   EMBL; AB075219; BAB97308.1; -; Genomic_DNA.
DR   EMBL; AB075220; BAB97309.1; -; Genomic_DNA.
DR   EMBL; AB075221; BAB97310.1; -; Genomic_DNA.
DR   PIR; B40004; B40004.
DR   AlphaFoldDB; P28578; -.
DR   SMR; P28578; -.
DR   BRENDA; 4.1.1.22; 2813.
DR   GO; GO:0004398; F:histidine decarboxylase activity; IEA:UniProtKB-UniRule.
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   HAMAP; MF_00609; Pyridoxal_decarbox; 1.
DR   InterPro; IPR023523; Hist_deCOase_bac.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..378
FT                   /note="Histidine decarboxylase"
FT                   /id="PRO_0000146957"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         233
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   VARIANT         148
FT                   /note="A -> T (in strain: 28-1 and 42-1)"
FT   VARIANT         184
FT                   /note="Q -> E (in strain: 28-1 and 42-1)"
FT   CONFLICT        156
FT                   /note="R -> A (in Ref. 1; AAA25071)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   378 AA;  42898 MW;  AB2058BB5552EB63 CRC64;
     MTLSISDQNK LDSFWSYCVK NQYFNIGYPE SADFDYTILE RFMRFSINNC GDWGEYCNYL
     LNSFDFEKEV MEYFAQLFKI PFEESWGYVT NGGTEGNMFG CYLGREIFPN GTLYYSKDTH
     YSVAKIVKLL RIKSTLVESQ PNGEMDYADL IKKIKRDNEK HPIIFANIGT TVRGAIDNIA
     IIQQSISELG IERKDYYLHA DAALSGMILP FVDNPQPFNF ADGIDSIGVS GHKMIGSPIP
     CGIVVAKKKN VDRISVEIDY ISAHDKTISG SRNGHTPLMM WEAIRSHSWE EWRRRIERSL
     NMAQYAVDRF QSAGIDAWRN KNSITVVFPC PSEAVWKKHC LATSGDIAHL IATAHHLDSS
     KIDALIDDVI ADLKKQAA