ID   DCHS_KLEPL     STANDARD;      PRT;   377 AA.
AC   P28578; Q8KHD1; Q8KHF6;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2002, sequence version 3.
DT   07-FEB-2006, entry version 40.
DE   Histidine decarboxylase (EC 4.1.1.22) (HDC).
GN   Name=hdc;
OS   Klebsiella planticola (Raoultella planticola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Raoultella.
OX   NCBI_TaxID=575;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43176;
RX   MEDLINE=91236707; PubMed=2033044;
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 90-317.
RC   STRAIN=19-3, 27-1, 28-1, 42-1, S8, and Y1-1;
RX   MEDLINE=22083483; PubMed=12089029;
RX   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
RT   and Raoultella ornithinolytica strains are histamine producers.";
RL   Appl. Environ. Microbiol. 68:3462-3466(2002).
CC   -!- CATALYTIC ACTIVITY: L-histidine = histamine + CO(2).
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- MISCELLANEOUS: This histamine-producing bacteria (HPB) causes
CC       histamine fish poisoning.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
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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   HAMAP; MF_00609; -; 1.
DR   InterPro; IPR002129; Pyridoxal_deC.
DR   PANTHER; PTHR11999; Pyridoxal_deC; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
KW   Decarboxylase; Lyase; Pyridoxal phosphate.
FT   INIT_MET      0      0       By similarity.
FT   CHAIN         1    377       Histidine decarboxylase.
FT                                /FTId=PRO_0000146957.
FT   BINDING     232    232       Pyridoxal phosphate (covalent)
FT                                (Potential).
FT   VARIANT     147    147       A -> T (in strain: 28-1 and 42-1).
FT   VARIANT     183    183       Q -> E (in strain: 28-1 and 42-1).
FT   CONFLICT    155    155       R -> A (in Ref. 1).
SQ   SEQUENCE   377 AA;  42767 MW;  131A20A0A540D25A CRC64;
     TLSISDQNKL DSFWSYCVKN QYFNIGYPES ADFDYTILER FMRFSINNCG DWGEYCNYLL
     NSFDFEKEVM EYFAQLFKIP FEESWGYVTN GGTEGNMFGC YLGREIFPNG TLYYSKDTHY
     SVAKIVKLLR IKSTLVESQP NGEMDYADLI KKIKRDNEKH PIIFANIGTT VRGAIDNIAI
     IQQSISELGI ERKDYYLHAD AALSGMILPF VDNPQPFNFA DGIDSIGVSG HKMIGSPIPC
     GIVVAKKKNV DRISVEIDYI SAHDKTISGS RNGHTPLMMW EAIRSHSWEE WRRRIERSLN
     MAQYAVDRFQ SAGIDAWRNK NSITVVFPCP SEAVWKKHCL ATSGDIAHLI ATAHHLDSSK
     IDALIDDVIA DLKKQAA
//