ID   DCHS_PSEFL              Reviewed;         405 AA.
AC   P95477;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Histidine decarboxylase {ECO:0000255|HAMAP-Rule:MF_00609};
DE            Short=HDC {ECO:0000255|HAMAP-Rule:MF_00609};
DE            EC=4.1.1.22 {ECO:0000255|HAMAP-Rule:MF_00609};
GN   Name=hdc {ECO:0000255|HAMAP-Rule:MF_00609}; Synonyms=pmsA;
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WCS374;
RX   PubMed=11222588; DOI=10.1128/jb.183.6.1909-1920.2001;
RA   Mercado-Blanco J., van der Drift K.M.G.M., Olsson P.E., Thomas-Oates J.E.,
RA   Van Loon L.C., Bakker P.A.H.M.;
RT   "Analysis of the pmsCEAB gene cluster involved in biosynthesis of salicylic
RT   acid and the siderophore pseudomonine in the biocontrol strain Pseudomonas
RT   fluorescens WCS374.";
RL   J. Bacteriol. 183:1909-1920(2001).
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00609};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00609};
CC   -!- PATHWAY: Siderophore biosynthesis; pseudomonine biosynthesis.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00609}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00609}.
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DR   EMBL; Y09356; CAA70530.1; -; Genomic_DNA.
DR   AlphaFoldDB; P95477; -.
DR   SMR; P95477; -.
DR   BRENDA; 4.1.1.22; 5121.
DR   UniPathway; UPA00024; -.
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   CHAIN           1..405
FT                   /note="Histidine decarboxylase"
FT                   /id="PRO_0000146959"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00609"
FT   MOD_RES         234
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00609"
SQ   SEQUENCE   405 AA;  45727 MW;  801C199C559731D9 CRC64;
     MTLSPADQSK LEGFWQHCVT HQYFNIGYPE SADFDYSQLH RFLQFSINNL LGTGNEYSNY
     LLNSFDFEKD VMTYFAELFN IALEDSWGYV TNGGTEGNMF GCYLGRELFP DGTLYYSKDT
     HYSVAKIVKL LRIKCRAVES LPNGEIDYDD LMAKITADQE RHPIIFANIG TTMRGALDNI
     VTIQQRLQQA GIARHDYYLH ADAALSGMIL PFVDHPQPFS FADGIDSICV SGHKMIGSPI
     PCGIVVAKRN NVARISVEVD YIRAHDKTIS GSRNGHTPLM MWAALRSYSW AEWRHRIKHS
     LDTAQYAVDR FQASGIDAWR NENSITVVFP CPSERIATKY CLATSGNSAH LITTPHHHDC
     SMIDALIDEV VAEAQLNTLR SKRAFTEQTV VERLPAASFN LRTHY