DCHS_LACS3
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 03-AUG-2022, entry version 123.
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; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus; unclassified 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=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.
CC {ECO:0000269|PubMed:2745463}.
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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 PDBsum; 1HQ6; -.
DR PDBsum; 1IBT; -.
DR PDBsum; 1IBU; -.
DR PDBsum; 1IBV; -.
DR PDBsum; 1IBW; -.
DR PDBsum; 1PYA; -.
DR AlphaFoldDB; P00862; -.
DR SMR; P00862; -.
DR MEROPS; X39.001; -.
DR BioCyc; MetaCyc:MON-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: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 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..91
FT /evidence="ECO:0007829|PDB:1IBV"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:1IBV"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1IBV"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:1IBV"
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 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
