SODM_VIRHA
ID SODM_VIRHA Reviewed; 202 AA.
AC Q7SIC3;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Superoxide dismutase [Mn];
DE EC=1.15.1.1;
DE Flags: Fragment;
GN Name=sodA;
OS Virgibacillus halodenitrificans (Bacillus halodenitrificans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=1482;
RN [1]
RP CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=ATCC 49067;
RX PubMed=12713952; DOI=10.1016/s1047-8477(03)00014-5;
RA Chen C.J., Liu M.Y., Chang T., Chang W.C., Wang B.C., Le Gall J.;
RT "Crystal structure of a nucleoside diphosphate kinase from Bacillus
RT halodenitrificans: coexpression of its activity with a Mn-superoxide
RT dismutase.";
RL J. Struct. Biol. 142:247-255(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH MANGANESE ION,
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,
RP COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 49067;
RX PubMed=12457847; DOI=10.1016/s1047-8477(02)00531-2;
RA Liao J., Liu M.Y., Chang T., Li M., Le Gall J., Gui L.L., Zhang J.P.,
RA Jiang T., Liang D.C., Chang W.R.;
RT "Three-dimensional structure of manganese superoxide dismutase from
RT Bacillus halodenitrificans, a component of the so-called 'green protein'.";
RL J. Struct. Biol. 139:171-180(2002).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
CC Active only in homodimeric state. {ECO:0000269|PubMed:12457847}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:18421; EC=1.15.1.1;
CC Evidence={ECO:0000269|PubMed:12713952};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12457847};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:12457847};
CC -!- SUBUNIT: Homodimer; under aerobic conditions. Under anaerobic
CC conditions it is a component of the so-called 'green protein' complex
CC (GPC), which consists of at least two components, SodA and a nucleoside
CC diphosphate kinase (NDK). {ECO:0000269|PubMed:12457847,
CC ECO:0000269|PubMed:12713952}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12457847}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR PDB; 1JR9; X-ray; 2.80 A; A=1-202.
DR PDBsum; 1JR9; -.
DR AlphaFoldDB; Q7SIC3; -.
DR SMR; Q7SIC3; -.
DR STRING; 1482.BME96_08715; -.
DR eggNOG; COG0605; Bacteria.
DR EvolutionaryTrace; Q7SIC3; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.287.990; -; 1.
DR Gene3D; 3.55.40.20; -; 1.
DR InterPro; IPR001189; Mn/Fe_SOD.
DR InterPro; IPR019833; Mn/Fe_SOD_BS.
DR InterPro; IPR019832; Mn/Fe_SOD_C.
DR InterPro; IPR019831; Mn/Fe_SOD_N.
DR InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR InterPro; IPR036314; SOD_C_sf.
DR Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PIRSF; PIRSF000349; SODismutase; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF46609; SSF46609; 1.
DR SUPFAM; SSF54719; SSF54719; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Manganese; Metal-binding; Oxidoreductase;
KW Phosphoprotein.
FT CHAIN <1..202
FT /note="Superoxide dismutase [Mn]"
FT /id="PRO_0000398825"
FT BINDING 27
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 164
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 168
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT MOD_RES 34
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 70
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT TURN 14..18
FT /evidence="ECO:0007829|PDB:1JR9"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:1JR9"
FT HELIX 31..40
FT /evidence="ECO:0007829|PDB:1JR9"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:1JR9"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:1JR9"
FT HELIX 66..87
FT /evidence="ECO:0007829|PDB:1JR9"
FT HELIX 100..109
FT /evidence="ECO:0007829|PDB:1JR9"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:1JR9"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:1JR9"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:1JR9"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:1JR9"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:1JR9"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:1JR9"
FT TURN 170..176
FT /evidence="ECO:0007829|PDB:1JR9"
FT HELIX 178..188
FT /evidence="ECO:0007829|PDB:1JR9"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:1JR9"
SQ SEQUENCE 202 AA; 22661 MW; 9B23942D598E667C CRC64;
AKFELPELPY AYDALEPTID KETMNIHHTK HHNTYVTKLN GALEGHEDLK NKSLNDLISN
LDAVPENIRT AVRNNGGGHA NHSLFWKLMS PNGGGKPTGE VADKINDKYG SFEKFQEEFA
AAAAGRFGSG WAWLVVNNGE IEIMSTPIQD NPLMEGKKPI LGLDVWEHAY YLKYQNKRPD
YISAFWNVVN WDEVAAQYSQ AA
