ID DCHS_LACS3 Reviewed; 311 AA. AC P00862; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 02-SEP-2026, entry version 136. 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; GN Name=hdcA; OS Lactobacillus sp. (strain 30a). OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1593; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3021766; DOI=10.1016/s0021-9258(18)66851-6; RA Vanderslice P., Copeland W.C., Robertus J.D.; RT "Cloning and nucleotide sequence of wild type and a mutant histidine RT decarboxylase from Lactobacillus 30a."; RL J. Biol. Chem. 261:15186-15191(1986). RN [2] RP PROTEIN SEQUENCE OF 2-82. RX PubMed=6752140; DOI=10.1016/s0021-9258(18)33579-8; RA Vaaler G.L., Recsei P.A., Fox J.L., Snell E.E.; RT "Histidine decarboxylase of Lactobacillus 30a. Comparative sequences of the RT beta chain from wild type and mutant enzymes."; RL J. Biol. Chem. 257:12770-12774(1982). RN [3] RP PROTEIN SEQUENCE OF 83-308, AND PYRUVATE FORMATION AT SER-83. RX PubMed=6698997; DOI=10.1016/s0021-9258(17)43222-4; RA Huynh Q.K., Recsei P.A., Vaaler G.L., Snell E.E.; RT "Histidine decarboxylase of Lactobacillus 30a. Sequences of the overlapping RT peptides, the complete alpha chain, and prohistidine decarboxylase."; RL J. Biol. Chem. 259:2833-2839(1984). RN [4] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). RX PubMed=4009714; DOI=10.1016/0022-2836(85)90204-9; RA Parks E.H., Ernst S.R., Hamlin R., Xuong N.G., Hackert M.L.; RT "Structure determination of histidine decarboxylase from Lactobacillus 30a RT at 3.0-A resolution."; RL J. Mol. Biol. 182:455-465(1985). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, AND RP SUBSTRATE BINDING AT ASP-64 AND SER-82. RX PubMed=2745463; DOI=10.1016/s0021-9258(18)63917-1; RA Gallagher T., Snell E.E., Hackert M.L.; RT "Pyruvoyl-dependent histidine decarboxylase. Active site structure and RT mechanistic analysis."; RL J. Biol. Chem. 264:12737-12743(1989). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=8464063; DOI=10.1006/jmbi.1993.1168; RA Gallagher T., Rozwarski D.A., Ernst S.R., Hackert M.L.; RT "Refined structure of the pyruvoyl-dependent histidine decarboxylase from RT Lactobacillus 30a."; RL J. Mol. Biol. 230:516-528(1993). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). RX PubMed=11243783; DOI=10.1006/jmbi.2000.4430; RA Schelp E., Worley S., Monzingo A.F., Ernst S., Robertus J.D.; RT "pH-induced structural changes regulate histidine decarboxylase activity in RT Lactobacillus 30a."; RL J. Mol. Biol. 306:727-732(2001). CC -!- CATALYTIC ACTIVITY: CC Reaction=L-histidine + H(+) = histamine + CO2; 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. CC {ECO:0000269|PubMed:2745463}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J02613; AAB59151.1; -; Genomic_DNA. DR PIR; A25932; DCLBHP. DR PDB; 1HQ6; X-ray; 2.70 A; A/C=2-82, B/D=83-311. DR PDB; 1IBT; X-ray; 2.60 A; A/C/E=2-82, B/D/F=83-311. DR PDB; 1IBU; X-ray; 3.10 A; A/C/E=2-82, B/D/F=83-311. DR PDB; 1IBV; X-ray; 2.50 A; A/C/E=2-82, B/D/F=84-311. DR PDB; 1IBW; X-ray; 3.20 A; A/C/E=2-82, B/D/F=84-311. DR PDB; 1PYA; X-ray; 2.50 A; A/C/E=2-82, B/D/F=84-311. DR AlphaFoldDB; P00862; -. DR SMR; P00862; -. DR MEROPS; X39.001; -. DR BioCyc; MetaCyc:MONOMER-14628; -. DR BRENDA; 4.1.1.22; 2897. DR SABIO-RK; P00862; -. DR EvolutionaryTrace; P00862; -. DR GO; GO:0004398; F:histidine decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro. DR Gene3D; 4.10.510.10; Pyruvoyl-Dependent Histidine Decarboxylas, subunit A; 1. DR Gene3D; 3.50.20.10; Pyruvoyl-Dependent Histidine Decarboxylase, subunit B; 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 NCBIfam; TIGR00541; hisDCase_pyru; 1. DR Pfam; PF02329; HDC; 1. DR PIRSF; PIRSF001341; His_decarboxylas; 1. DR SFLD; SFLDS00055; Pyruvoyl-Dependent_Histidine/A; 1. DR SFLD; SFLDF00466; Pyruvoyl-dependent_histidine_d; 1. DR SFLD; SFLDG01171; Pyruvoyl-dependent_histidine_d; 1. DR SUPFAM; SSF56271; Pyruvoyl-dependent histidine and arginine decarboxylases; 1. DR PDBsum; 1HQ6; -. DR PDBsum; 1IBT; -. DR PDBsum; 1IBU; -. DR PDBsum; 1IBV; -. DR PDBsum; 1IBW; -. DR PDBsum; 1PYA; -. PE 1: Evidence at protein level; KW 3D-structure; Decarboxylase; Direct protein sequencing; Lyase; Pyruvate; KW Zymogen. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:6752140" FT CHAIN 2..82 FT /note="Histidine decarboxylase beta chain" FT /id="PRO_0000029953" FT CHAIN 83..311 FT /note="Histidine decarboxylase alpha chain" FT /id="PRO_0000029954" FT ACT_SITE 198 FT /note="Proton donor" FT BINDING 64 FT /ligand="substrate" FT BINDING 82 FT /ligand="substrate" FT SITE 82..83 FT /note="Cleavage (non-hydrolytic)" FT MOD_RES 83 FT /note="Pyruvic acid (Ser)" FT /evidence="ECO:0000269|PubMed:6698997" FT CONFLICT 207 FT /note="N -> D (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 266 FT /note="L -> I (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 271 FT /note="I -> L (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 285..287 FT /note="Missing (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 3..9 FT /evidence="ECO:0007829|PDB:1IBV" FT TURN 10..12 FT /evidence="ECO:0007829|PDB:1IBV" FT STRAND 17..19 FT /evidence="ECO:0007829|PDB:1IBU" FT STRAND 21..23 FT /evidence="ECO:0007829|PDB:1IBV" FT STRAND 25..27 FT /evidence="ECO:0007829|PDB:1IBV" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:1IBV" FT STRAND 38..40 FT /evidence="ECO:0007829|PDB:1IBV" FT STRAND 43..50 FT /evidence="ECO:0007829|PDB:1IBV" FT HELIX 55..65 FT /evidence="ECO:0007829|PDB:1IBV" FT TURN 66..68 FT /evidence="ECO:0007829|PDB:1IBV" FT STRAND 69..71 FT /evidence="ECO:0007829|PDB:1IBV" FT STRAND 77..81 FT /evidence="ECO:0007829|PDB:1IBV" FT STRAND 89..92 FT /evidence="ECO:0007829|PDB:1IBV" FT TURN 93..95 FT /evidence="ECO:0007829|PDB:1IBV" FT STRAND 96..98 FT /evidence="ECO:0007829|PDB:1PYA" FT HELIX 100..104 FT /evidence="ECO:0007829|PDB:1IBV" FT HELIX 105..107 FT /evidence="ECO:0007829|PDB:1PYA" FT STRAND 108..112 FT /evidence="ECO:0007829|PDB:1IBV" FT STRAND 118..123 FT /evidence="ECO:0007829|PDB:1IBV" FT HELIX 125..135 FT /evidence="ECO:0007829|PDB:1IBV" FT STRAND 138..141 FT /evidence="ECO:0007829|PDB:1IBV" FT STRAND 150..162 FT /evidence="ECO:0007829|PDB:1IBV" FT TURN 170..172 FT /evidence="ECO:0007829|PDB:1IBV" FT STRAND 175..187 FT /evidence="ECO:0007829|PDB:1IBV" FT TURN 189..191 FT /evidence="ECO:0007829|PDB:1IBV" FT STRAND 194..203 FT /evidence="ECO:0007829|PDB:1IBV" FT HELIX 208..233 FT /evidence="ECO:0007829|PDB:1IBV" FT STRAND 237..248 FT /evidence="ECO:0007829|PDB:1IBV" FT STRAND 253..267 FT /evidence="ECO:0007829|PDB:1IBV" FT HELIX 268..270 FT /evidence="ECO:0007829|PDB:1IBV" FT HELIX 279..288 FT /evidence="ECO:0007829|PDB:1IBV" FT HELIX 291..298 FT /evidence="ECO:0007829|PDB:1IBV" FT HELIX 300..302 FT /evidence="ECO:0007829|PDB:1IBV" FT TURN 305..307 FT /evidence="ECO:0007829|PDB:1IBV" SQ SEQUENCE 311 AA; 34233 MW; D489583546578A0E CRC64; MSELDAKLNK LGVDRIAISP YKQWTRGYME PGNIGNGYVT GLKVDAGVRD KSDDDVLDGI VSYDRAETKN AYIGQINMTT ASSFTGVQGR VIGYDILRSP EVDKAKPLFT ETQWDGSELP IYDAKPLQDA LVEYFGTEQD RRHYPAPGSF IVCANKGVTA ERPKNDADMK PGQGYGVWSA IAISFAKDPT KDSSMFVEDA GVWETPNEDE LLEYLEGRRK AMAKSIAECG QDAHASFESS WIGFAYTMME PGQIGNAITV APYVSLPIDS IPGGSILTPD KDMEIMENLT MPEWLEKMGY KSLSANNALK Y //