ID   DCHS_KLEPL     STANDARD;      PRT;   377 AA.
AC   P28578; Q8KHD1; Q8KHF6;
DT   01-DEC-1992 (Rel. 24, Created)
DT   28-FEB-2003 (Rel. 41, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
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.
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 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.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; M62746; AAA25071.1; -.
DR   EMBL; AB075216; BAB97305.1; -.
DR   EMBL; AB075217; BAB97306.1; -.
DR   EMBL; AB075218; BAB97307.1; -.
DR   EMBL; AB075219; BAB97308.1; -.
DR   EMBL; AB075220; BAB97309.1; -.
DR   EMBL; AB075221; BAB97310.1; -.
DR   PIR; B40004; B40004.
DR   HAMAP; MF_00609; -; 1.
DR   InterPro; IPR002129; Pyridoxal_deC.
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   BINDING     232    232       Pyridoxal phosphate (covalent)
FT                                (Potential).
FT   VARIANT     147    147       A -> T (in strain 28-1 and strain 42-1).
FT   VARIANT     183    183       Q -> E (in strain 28-1 and strain 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
//