ID B4WB81_9CAUL Unreviewed; 191 AA.
AC B4WB81;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Copper/zinc superoxide dismutase {ECO:0000313|EMBL:EDX79782.1};
GN ORFNames=BBAL3_939 {ECO:0000313|EMBL:EDX79782.1};
OS Brevundimonas sp. BAL3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=391600 {ECO:0000313|EMBL:EDX79782.1, ECO:0000313|Proteomes:UP000003957};
RN [1] {ECO:0000313|EMBL:EDX79782.1, ECO:0000313|Proteomes:UP000003957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL3 {ECO:0000313|EMBL:EDX79782.1,
RC ECO:0000313|Proteomes:UP000003957};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000256|ARBA:ARBA00010457}.
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; DS989898; EDX79782.1; -; Genomic_DNA.
DR RefSeq; WP_008260309.1; NZ_DS989898.1.
DR AlphaFoldDB; B4WB81; -.
DR STRING; 391600.BBAL3_939; -.
DR eggNOG; COG2032; Bacteria.
DR HOGENOM; CLU_056632_8_1_5; -.
DR OrthoDB; 5431326at2; -.
DR Proteomes; UP000003957; Unassembled WGS sequence.
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; IPR001424; SOD_Cu_Zn_dom.
DR PANTHER; PTHR10003:SF71; SUPEROXIDE DISMUTASE; 1.
DR PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..191
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002825660"
FT DOMAIN 55..187
FT /note="Superoxide dismutase copper/zinc binding"
FT /evidence="ECO:0000259|Pfam:PF00080"
SQ SEQUENCE 191 AA; 19070 MW; 188ACCCB35E7EDF7 CRC64;
MRFTPLAAAL ALAAPLALAG ACASTADAAQ MQAERAPVGA TGQAVLINAQ GANIGRVDLR
QGPTGLVIKV EASGLTPGWH GIHIHATGQC AAPFTSSGAH INHGEPKAPH GLLNAAGPDD
GDLPNVYAGA DGKVNAELFT TRARISSEGP GQWLWDADGS AIIIHANPDD HSSQPIGGAG
DRVACAALSA S
//
