ID   DCHS_CLOP1              Reviewed;         320 AA.
AC   Q0TU55; P04194;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Histidine decarboxylase proenzyme;
DE            EC=4.1.1.22;
DE   AltName: Full=Pi chain;
DE   Contains:
DE     RecName: Full=Histidine decarboxylase beta chain;
DE   Contains:
DE     RecName: Full=Histidine decarboxylase alpha chain;
DE   Flags: Precursor;
GN   Name=hdc; OrderedLocusNames=CPF_0378;
OS   Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS   6125 / NCTC 8237 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2108713; DOI=10.1021/bi00453a016;
RA   van Poelje P.D., Snell E.E.;
RT   "Cloning, sequencing, expression, and site-directed mutagenesis of the gene
RT   from Clostridium perfringens encoding pyruvoyl-dependent histidine
RT   decarboxylase.";
RL   Biochemistry 29:132-139(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC   Type A;
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA   Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA   Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA   Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA   Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA   Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT   Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
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=pyruvate; Xref=ChEBI:CHEBI:15361;
CC       Note=Binds 1 pyruvoyl group covalently per subunit.;
CC   -!- SUBUNIT: The proenzyme is a hexamer of identical pi chains; each pi
CC       chain monomer is cleaved to form a small (or beta) chain and a large
CC       (or alpha) chain by non-hydrolytic self-catalysis.
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DR   EMBL; J02880; AAA83526.1; -; Genomic_DNA.
DR   EMBL; CP000246; ABG84693.1; -; Genomic_DNA.
DR   PIR; A33770; DCCLHP.
DR   RefSeq; WP_003450230.1; NC_008261.1.
DR   AlphaFoldDB; Q0TU55; -.
DR   SMR; Q0TU55; -.
DR   MEROPS; X39.001; -.
DR   PRIDE; Q0TU55; -.
DR   EnsemblBacteria; ABG84693; ABG84693; CPF_0378.
DR   GeneID; 29572497; -.
DR   KEGG; cpf:CPF_0378; -.
DR   eggNOG; ENOG502Z80V; Bacteria.
DR   HOGENOM; CLU_942196_0_0_9; -.
DR   OMA; ALTCAPY; -.
DR   OrthoDB; 1546986at2; -.
DR   SABIO-RK; Q0TU55; -.
DR   Proteomes; UP000001823; Chromosome.
DR   GO; GO:0004398; F:histidine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006547; P:histidine metabolic process; IEA:InterPro.
DR   Gene3D; 3.50.20.10; -; 1.
DR   Gene3D; 4.10.510.10; -; 1.
DR   InterPro; IPR003427; His_de-COase_proenz.
DR   InterPro; IPR016106; Pyr-dep_his-deCO2ase_N.
DR   InterPro; IPR016104; Pyr-dep_his/arg-deCO2ase.
DR   InterPro; IPR016105; Pyr-dep_his/arg-deCO2ase_sand.
DR   Pfam; PF02329; HDC; 1.
DR   PIRSF; PIRSF001341; His_decarboxylas; 1.
DR   SFLD; SFLDF00466; Pyruvoyl-dependent_histidine_d; 1.
DR   SUPFAM; SSF56271; SSF56271; 1.
DR   TIGRFAMs; TIGR00541; hisDCase_pyru; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyruvate; Zymogen.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   PROPEP          2..11
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000273586"
FT   CHAIN           12..97
FT                   /note="Histidine decarboxylase beta chain"
FT                   /id="PRO_0000273587"
FT   CHAIN           98..320
FT                   /note="Histidine decarboxylase alpha chain"
FT                   /id="PRO_0000273588"
FT   ACT_SITE        215
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   SITE            97..98
FT                   /note="Cleavage (non-hydrolytic)"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         98
FT                   /note="Pyruvic acid (Ser)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   320 AA;  35524 MW;  64B2666FFC15133D CRC64;
     MNKNLEANRN RTLSEGIHKN IKVRAPKIDK TAISPYDRYC DGYGMPGAYG NGYVSVLKVS
     VGTVKKTDDI LLDGIVSYDR AEINDAYVGQ INMLTASSFC GVAGQVWGHD LATHDSIAND
     EIKPLYELKQ FDGTPLKVYD AKPLLEAGIE LFGTEKNRRF TTAPGAHVIC ANKSATAYRP
     KENRPLKEGE AYGVWSFIAL SLSNDRDHCA DLFIEDAGLW TKNDNPEDLK KFLEDHRKAV
     TWSVVECGRD SHVVFERTYI GFAYVIMKPG EIGNALTCAP YVTLARDAVP SEGFPSLNRI
     SLSQWLDDMN FDSLVNPSKK