SODC_BOMMO
ID SODC_BOMMO Reviewed; 154 AA.
AC P82205; Q6SA03;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1;
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1] {ECO:0000312|EMBL:AAR97568.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Kl20 {ECO:0000312|EMBL:AAR97568.1};
RA Hong S.M., Kang S.W., Kim N.S., Lee J.S., Nho S.K.;
RT "Cu/Zn superoxide dismutase in Bombyx mori.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-31.
RC STRAIN=Xinhang X Keming {ECO:0000269|PubMed:11280994};
RC TISSUE=Body wall {ECO:0000269|PubMed:11280994}, and
RC Fat body {ECO:0000269|PubMed:11280994};
RX PubMed=11280994;
RA Zhong B.-X.;
RT "Protein database for several tissues derived from five instar of
RT silkworm.";
RL Yi Chuan Xue Bao 28:217-224(2001).
RN [3] {ECO:0007744|PDB:3L9E, ECO:0007744|PDB:3L9Y}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC
RP IONS, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=20310068; DOI=10.1002/prot.22709;
RA Zhang N.N., He Y.X., Li W.F., Teng Y.B., Yu J., Chen Y., Zhou C.Z.;
RT "Crystal structures of holo and Cu-deficient Cu/Zn-SOD from the silkworm
RT Bombyx mori and the implications in amyotrophic lateral sclerosis.";
RL Proteins 78:1999-2004(2010).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
CC {ECO:0000250|UniProtKB:P00441}.
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:0000250|UniProtKB:P00441};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000305|PubMed:20310068};
CC Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:20310068};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000305|PubMed:20310068};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:20310068};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20310068}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00441}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AY461705; AAR97568.1; -; mRNA.
DR RefSeq; NP_001037084.1; NM_001043619.1.
DR PDB; 3L9E; X-ray; 2.05 A; A/B/C/D=1-154.
DR PDB; 3L9Y; X-ray; 1.80 A; A/B=1-154.
DR PDBsum; 3L9E; -.
DR PDBsum; 3L9Y; -.
DR AlphaFoldDB; P82205; -.
DR SMR; P82205; -.
DR STRING; 7091.BGIBMGA001307-TA; -.
DR EnsemblMetazoa; BGIBMGA001307-RA; BGIBMGA001307-TA; BGIBMGA001307.
DR GeneID; 692639; -.
DR KEGG; bmor:692639; -.
DR CTD; 692639; -.
DR eggNOG; KOG0441; Eukaryota.
DR HOGENOM; CLU_056632_4_1_1; -.
DR InParanoid; P82205; -.
DR OMA; AQRGFHI; -.
DR OrthoDB; 1574423at2759; -.
DR EvolutionaryTrace; P82205; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IPI:UniProtKB.
DR CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR Gene3D; 2.60.40.200; -; 1.
DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR InterPro; IPR018152; SOD_Cu/Zn_BS.
DR InterPro; IPR001424; SOD_Cu_Zn_dom.
DR PANTHER; PTHR10003; PTHR10003; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR PRINTS; PR00068; CUZNDISMTASE.
DR SUPFAM; SSF49329; SSF49329; 1.
DR PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Copper; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11280994"
FT CHAIN 2..154
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000164080"
FT BINDING 45
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:20310068,
FT ECO:0007744|PDB:3L9Y"
FT BINDING 47
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:20310068,
FT ECO:0007744|PDB:3L9Y"
FT BINDING 62
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:20310068,
FT ECO:0007744|PDB:3L9Y"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:20310068,
FT ECO:0007744|PDB:3L9E, ECO:0007744|PDB:3L9Y"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:20310068,
FT ECO:0007744|PDB:3L9E, ECO:0007744|PDB:3L9Y"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:20310068,
FT ECO:0007744|PDB:3L9E, ECO:0007744|PDB:3L9Y"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:20310068,
FT ECO:0007744|PDB:3L9E, ECO:0007744|PDB:3L9Y"
FT BINDING 120
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:20310068,
FT ECO:0007744|PDB:3L9Y"
FT DISULFID 56..146
FT /evidence="ECO:0000269|PubMed:20310068,
FT ECO:0007744|PDB:3L9E, ECO:0007744|PDB:3L9Y"
FT STRAND 3..23
FT /evidence="ECO:0007829|PDB:3L9Y"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:3L9Y"
FT STRAND 39..48
FT /evidence="ECO:0007829|PDB:3L9Y"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:3L9Y"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:3L9Y"
FT STRAND 93..103
FT /evidence="ECO:0007829|PDB:3L9Y"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:3L9Y"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:3L9Y"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:3L9Y"
FT TURN 132..136
FT /evidence="ECO:0007829|PDB:3L9Y"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:3L9Y"
SQ SEQUENCE 154 AA; 15842 MW; 174BF407D1820775 CRC64;
MPAKAVCVLR GDVSGTVFFD QQDEKSPVVV SGEVQGLTKG KHGFHVHEFG DNTNGCTSAG
AHFNPEKQDH GGPSSAVRHV GDLGNIEAIE DSGVTKVSIQ DSQISLHGPN SIIGRTLVVH
ADPDDLGLGG HELSKTTGNA GGRIACGVIG LAKI
