ID   DCHS_KLEAE              Reviewed;         378 AA.
AC   P28577;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Histidine decarboxylase;
DE            Short=HDC;
DE            EC=4.1.1.22;
GN   Name=hdc;
OS   Klebsiella aerogenes (Enterobacter aerogenes).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=548;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
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   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; M62745; AAA24802.1; -; Genomic_DNA.
DR   PIR; A40004; A40004.
DR   RefSeq; WP_015369839.1; NZ_WPHE01000003.1.
DR   AlphaFoldDB; P28577; -.
DR   SMR; P28577; -.
DR   STRING; 548.EAG7_04977; -.
DR   GeneID; 66602288; -.
DR   OMA; EIDCEDF; -.
DR   OrthoDB; 1478871at2; -.
DR   BioCyc; MetaCyc:MON-14638; -.
DR   BRENDA; 4.1.1.22; 152.
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_0000146955"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         233
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   378 AA;  42434 MW;  F4404B2F5CB5EF97 CRC64;
     MSLSIADQNK LDAFWSYCVK NRYFNIGYPE SADFDYTMLE RFLRFSINNC GDWGEYCNYL
     LNSFDFEKEV MEYFSGIFKI PFAESWGYVT NGGTESNMFG CYLGRELFPE GTLYYSKDTH
     YSVAKIVKLL RIKSQLVESQ PDGEMDYDDL INKIRTSGER HPIIFANIGT TVRGAVDNIA
     EIQKRIAALG IPREDYYLHA DAALSGMILP FVEDPQPFTF ADGIDSIGVS GHKMIGSPIP
     CGIVVAKKAN VDRISVEIDY ISAHDKTISG SRNGHTPLMM WAAVRSHTDA EWHRRIGHSL
     NMAKYAVDRF KAAGIDALCH KNSITVVFPK PSEWVWKKHC LATSGNVAHL ITTAHHLDSS
     RIDALIDDVI ADLAQRAA