SODC_BRUAB
ID SODC_BRUAB Reviewed; 173 AA.
AC P15453; Q578I8;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=sodC; OrderedLocusNames=BruAb2_0527;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
RN [2]
RP PROTEIN SEQUENCE OF 20-173.
RX PubMed=2105741; DOI=10.1021/bi00454a010;
RA Beck B.L., Tabatabai L.B., Mayfield J.E.;
RT "A protein isolated from Brucella abortus is a Cu-Zn superoxide
RT dismutase.";
RL Biochemistry 29:372-376(1990).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
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 -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AE017224; AAX75946.1; -; Genomic_DNA.
DR PIR; A33893; A33893.
DR RefSeq; WP_002972093.1; NC_006933.1.
DR PDB; 4L05; X-ray; 1.10 A; A=20-173.
DR PDBsum; 4L05; -.
DR AlphaFoldDB; P15453; -.
DR SMR; P15453; -.
DR EnsemblBacteria; AAX75946; AAX75946; BruAb2_0527.
DR GeneID; 45126038; -.
DR GeneID; 55592359; -.
DR KEGG; bmb:BruAb2_0527; -.
DR HOGENOM; CLU_056632_7_1_5; -.
DR OMA; AQRGFHI; -.
DR EvolutionaryTrace; P15453; -.
DR PRO; PR:P15453; -.
DR Proteomes; UP000000540; Chromosome II.
DR GO; GO:0042597; C:periplasmic space; 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 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 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; Direct protein sequencing;
KW Disulfide bond; Metal-binding; Oxidoreductase; Periplasm; Signal; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:2105741"
FT CHAIN 20..173
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000032820"
FT BINDING 67
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 74..169
FT /evidence="ECO:0000250"
FT STRAND 21..30
FT /evidence="ECO:0007829|PDB:4L05"
FT STRAND 33..44
FT /evidence="ECO:0007829|PDB:4L05"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:4L05"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:4L05"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:4L05"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:4L05"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:4L05"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:4L05"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:4L05"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:4L05"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:4L05"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:4L05"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:4L05"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:4L05"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:4L05"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:4L05"
SQ SEQUENCE 173 AA; 18131 MW; BA78F7E0FB62C69A CRC64;
MKSLFIASTM VLMAFPAFAE STTVKMYEAL PTGPGKEVGT VVISEAPGGL HFKVNMEKLT
PGYHGFHVHE NPSCAPGEKD GKIVPALAAG GHYDPGNTHH HLGPEGDGHM GDLPRLSANA
DGKVSETVVA PHLKKLAEIK QRSLMVHVGG DNYSDKPEPL GGGGARFACG VIE
