MCAT_LACPN
ID MCAT_LACPN Reviewed; 266 AA.
AC P60355;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Manganese catalase;
DE EC=1.11.1.6;
DE AltName: Full=Pseudocatalase;
OS Lactiplantibacillus plantarum (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=1590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-32 AND 67-86.
RC STRAIN=ATCC 14431 / CECT 221 / LMD 73.4 / T-1043-5;
RX PubMed=8939876; DOI=10.1074/jbc.271.47.29521;
RA Igarashi T., Kono Y., Tanaka K.;
RT "Molecular cloning of manganese catalase from Lactobacillus plantarum.";
RL J. Biol. Chem. 271:29521-29524(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS), AND SUBUNIT.
RX PubMed=11587647; DOI=10.1016/s0969-2126(01)00628-1;
RA Barynin V.V., Whittaker M.M., Antonyuk S.V., Lamzin V.S., Harrison P.M.,
RA Artymiuk P.J., Whittaker J.W.;
RT "Crystal structure of manganese catalase from Lactobacillus plantarum.";
RL Structure 9:725-738(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS), AND MUTAGENESIS OF TYR-42.
RX PubMed=12631270; DOI=10.1046/j.1432-1033.2003.03459.x;
RA Whittaker M.M., Barynin V.V., Igarashi T., Whittaker J.W.;
RT "Outer sphere mutagenesis of Lactobacillus plantarum manganese catalase
RT disrupts the cluster core. Mechanistic implications.";
RL Eur. J. Biochem. 270:1102-1116(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 1 Ca(2+) ion per subunit.;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=Binds 2 manganese ions per subunit.;
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:11587647}.
CC -!- SIMILARITY: Belongs to the manganese catalase family. {ECO:0000305}.
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; D87070; BAA13239.1; -; Genomic_DNA.
DR PDB; 1JKU; X-ray; 1.84 A; A/B/C/D/E/F=1-266.
DR PDB; 1JKV; X-ray; 1.39 A; A/B/C/D/E/F=1-266.
DR PDB; 1O9I; X-ray; 1.33 A; A/B/C/D/E/F=1-266.
DR PDBsum; 1JKU; -.
DR PDBsum; 1JKV; -.
DR PDBsum; 1O9I; -.
DR AlphaFoldDB; P60355; -.
DR SMR; P60355; -.
DR DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid.
DR PeroxiBase; 3978; LplMnCat01.
DR EvolutionaryTrace; P60355; -.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01051; Mn_catalase; 1.
DR Gene3D; 1.20.1260.10; -; 1.
DR Gene3D; 3.30.1530.10; -; 1.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR007760; Mn_catalase.
DR InterPro; IPR027407; Mn_catalase_C.
DR InterPro; IPR039377; Mn_catalase_dom.
DR Pfam; PF05067; Mn_catalase; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Manganese; Metal-binding;
KW Oxidoreductase; Peroxidase.
FT CHAIN 1..266
FT /note="Manganese catalase"
FT /id="PRO_0000096155"
FT REGION 243..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 35
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 66
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT BINDING 66
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT BINDING 69
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT BINDING 148
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT BINDING 181
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 220
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT MUTAGEN 42
FT /note="Y->F: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12631270"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:1O9I"
FT HELIX 19..30
FT /evidence="ECO:0007829|PDB:1O9I"
FT HELIX 35..48
FT /evidence="ECO:0007829|PDB:1O9I"
FT HELIX 53..80
FT /evidence="ECO:0007829|PDB:1O9I"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1O9I"
FT HELIX 88..93
FT /evidence="ECO:0007829|PDB:1O9I"
FT HELIX 97..103
FT /evidence="ECO:0007829|PDB:1O9I"
FT HELIX 106..110
FT /evidence="ECO:0007829|PDB:1O9I"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1JKU"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1O9I"
FT HELIX 137..159
FT /evidence="ECO:0007829|PDB:1O9I"
FT HELIX 165..196
FT /evidence="ECO:0007829|PDB:1O9I"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:1O9I"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:1O9I"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:1O9I"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1O9I"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:1O9I"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:1O9I"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:1O9I"
SQ SEQUENCE 266 AA; 29743 MW; 2943A15DD7A60CB1 CRC64;
MFKHTRKLQY NAKPDRSDPI MARRLQESLG GQWGETTGMM SYLSQGWAST GAEKYKDLLL
DTGTEEMAHV EMISTMIGYL LEDAPFGPED LKRDPSLATT MAGMDPEHSL VHGLNASLNN
PNGAAWNAGY VTSSGNLVAD MRFNVVRESE ARLQVSRLYS MTEDEGVRDM LKFLLARETQ
HQLQFMKAQE ELEEKYGIIV PGDMKEIEHS EFSHVLMNFS DGDGSKAFEG QVAKDGEKFT
YQENPEAMGG IPHIKPGDPR LHNHQG
