ID   DCHS_MORMO              Reviewed;         378 AA.
AC   P05034;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Histidine decarboxylase;
DE            Short=HDC;
DE            EC=4.1.1.22;
GN   Name=hdc;
OS   Morganella morganii (Proteus morganii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Morganella.
OX   NCBI_TaxID=582;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AM-15C;
RX   PubMed=3015950; DOI=10.1016/s0021-9258(18)67340-5;
RA   Vaaler G.L., Brasch M.A., Snell E.E.;
RT   "Pyridoxal 5'-phosphate-dependent histidine decarboxylase. Nucleotide
RT   sequence of the hdc gene and the corresponding amino acid sequence.";
RL   J. Biol. Chem. 261:11010-11014(1986).
RN   [2]
RP   PROTEIN SEQUENCE OF 233-247 AND 322-334, CATALYTIC ACTIVITY, COFACTOR, AND
RP   PUTATIVE ACTIVE SITE.
RX   PubMed=3733745; DOI=10.1016/s0021-9258(18)67339-9;
RA   Hayashi H., Tanase S., Snell E.E.;
RT   "Pyridoxal 5'-phosphate-dependent histidine decarboxylase. Inactivation by
RT   alpha-fluoromethylhistidine and comparative sequences at the inhibitor- and
RT   coenzyme-binding sites.";
RL   J. Biol. Chem. 261:11003-11009(1986).
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         Evidence={ECO:0000269|PubMed:3733745};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:3733745};
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; J02577; AAA25321.1; -; Genomic_DNA.
DR   PIR; A25013; A25013.
DR   RefSeq; WP_072869018.1; NZ_FRBZ01000002.1.
DR   AlphaFoldDB; P05034; -.
DR   SMR; P05034; -.
DR   BRENDA; 4.1.1.22; 3426.
DR   SABIO-RK; P05034; -.
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   1: Evidence at protein level;
KW   Decarboxylase; Direct protein sequencing; Lyase; Pyridoxal phosphate.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..378
FT                   /note="Histidine decarboxylase"
FT                   /id="PRO_0000146958"
FT   ACT_SITE        323
FT                   /evidence="ECO:0000255"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         233
FT                   /note="N6-(pyridoxal phosphate)lysine"
SQ   SEQUENCE   378 AA;  42875 MW;  809721A1AF399C18 CRC64;
     MTLSINDQNK LDAFWAYCVK NQYFNIGYPE SADFDYTNLE RFLRFSINNC GDWGEYCNYL
     LNSFDFEKEV MEYFADLFKI PFEQSWGYVT NGGTEGNMFG CYLGREIFPD GTLYYSKDTH
     YSVAKIVKLL RIKSQVVESQ PNGEIDYDDL MKKIADDKEA HPIIFANIGT TVRGAIDDIA
     EIQKRLKAAG IKREDYYLHA DAALSGMILP FVDDAQPFTF ADGIDSIGVS GHKMIGSPIP
     CGIVVAKKEN VDRISVEIDY ISAHDKTITG SRNGHTPLML WEAIRSHSTE EWKRRITRSL
     DMAQYAVDRM QKAGINAWRN KNSITVVFPC PSERVWREHC LATSGDVAHL ITTAHHLDTV
     QIDKLIDDVI ADFNLHAA