ID   DCHS_CLOPE              Reviewed;         320 AA.
AC   P0C2E5; P04194;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=CPE0390;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
RN   [2]
RP   PROTEIN SEQUENCE OF 12-130, AND PYRUVATE FORMATION AT SER-98.
RX   PubMed=2857718; DOI=10.1016/s0021-9258(18)89433-9;
RA   Huynh Q.K., Snell E.E.;
RT   "Pyruvoyl-dependent histidine decarboxylases. Preparation and amino acid
RT   sequences of the beta chains of histidine decarboxylase from Clostridium
RT   perfringens and Lactobacillus buchneri.";
RL   J. Biol. Chem. 260:2798-2803(1985).
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; BA000016; BAB80096.1; -; Genomic_DNA.
DR   PIR; A33770; DCCLHP.
DR   RefSeq; WP_011009781.1; NC_003366.1.
DR   AlphaFoldDB; P0C2E5; -.
DR   SMR; P0C2E5; -.
DR   EnsemblBacteria; BAB80096; BAB80096; BAB80096.
DR   KEGG; cpe:CPE0390; -.
DR   HOGENOM; CLU_942196_0_0_9; -.
DR   OMA; ALTCAPY; -.
DR   Proteomes; UP000000818; 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   1: Evidence at protein level;
KW   Decarboxylase; Direct protein sequencing; Lyase; Pyruvate;
KW   Reference proteome; Zymogen.
FT   INIT_MET        1
FT                   /note="Removed"
FT   PROPEP          2..11
FT                   /evidence="ECO:0000269|PubMed:2857718"
FT                   /id="PRO_0000029950"
FT   CHAIN           12..97
FT                   /note="Histidine decarboxylase beta chain"
FT                   /id="PRO_0000029951"
FT   CHAIN           98..320
FT                   /note="Histidine decarboxylase alpha chain"
FT                   /id="PRO_0000029952"
FT   ACT_SITE        215
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   SITE            97..98
FT                   /note="Cleavage (non-hydrolytic)"
FT   MOD_RES         98
FT                   /note="Pyruvic acid (Ser)"
FT                   /evidence="ECO:0000269|PubMed:2857718"
FT   CONFLICT        51
FT                   /note="N -> D (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        109
FT                   /note="H -> V (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        114
FT                   /note="H -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        119
FT                   /note="K -> N (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        123
FT                   /note="K -> F (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        129
FT                   /note="K -> M (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   320 AA;  35538 MW;  6206358C1D1140DC CRC64;
     MNKNLEANRN RTLSEGIHKN IKVRAPKIDK TAISPYDRYC DGYGMPGAYG NGYVSVLKVS
     VGTVKKTDDI LLDGIVSYDR AEINDAYVGQ INMLTASSFC GVAGQVWGHD LATHDSIAKD
     EIKPLYELKQ FDGTPLKVYD AKPLLEAGIE LFGTEKNRRF TTAPGAHVIC ANKSATAYRP
     KENRPLKEGE AYGVWSFIAL SLSNDRDHCA DLFIEDAGLW TKNDNPEDLK KFLEDHRKAV
     TWSVVECGRD SHVVFERTYI GFAYVIMKPG EIGNALTCAP YVTLARDAVP SEGFPSLNRI
     SLSQWLDDMN FDSLVNPSKK