ID A1B2I8_PARDP Unreviewed; 165 AA.
AC A1B2I8;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 03-MAY-2023, entry version 105.
DE SubName: Full=Superoxide dismutase, copper/zinc binding protein {ECO:0000313|EMBL:ABL69732.1};
GN OrderedLocusNames=Pden_1634 {ECO:0000313|EMBL:ABL69732.1};
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL69732.1, ECO:0000313|Proteomes:UP000000361};
RN [1] {ECO:0000313|Proteomes:UP000000361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000256|ARBA:ARBA00010457}.
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DR EMBL; CP000489; ABL69732.1; -; Genomic_DNA.
DR RefSeq; WP_011747931.1; NC_008686.1.
DR AlphaFoldDB; A1B2I8; -.
DR STRING; 318586.Pden_1634; -.
DR EnsemblBacteria; ABL69732; ABL69732; Pden_1634.
DR GeneID; 75501116; -.
DR KEGG; pde:Pden_1634; -.
DR eggNOG; COG2032; Bacteria.
DR HOGENOM; CLU_056632_8_1_5; -.
DR OMA; KWVAFHV; -.
DR OrthoDB; 5431326at2; -.
DR Proteomes; UP000000361; Chromosome 1.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
DR CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 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:SF71; SUPEROXIDE DISMUTASE [CU-ZN]; 1.
DR PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR PRINTS; PR00068; CUZNDISMTASE.
DR SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR PROSITE; PS00087; SOD_CU_ZN_1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..165
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002632256"
FT DOMAIN 35..164
FT /note="Superoxide dismutase copper/zinc binding"
FT /evidence="ECO:0000259|Pfam:PF00080"
FT REGION 72..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 165 AA; 16864 MW; E150D14427C6D063 CRC64;
MRNHLVALGF ALLPISAHAQ DAKATFLDQE GQEAGSAALT ATPSGVLIEV EATGLPASNW
VAFHIHETGS CDHGTGHESA GGHFNPSGAP HGVLSEGGPH AGDMPNIWVD AEGTARAQVF
NPMVTLADGD NGIKGRALMI HAGPDDYQTQ PTGAAGDRLA CAVIE
//