GenomeNet

Database: UniProt
Entry: E1VGY7_9GAMM
LinkDB: E1VGY7_9GAMM
Original site: E1VGY7_9GAMM 
ID   E1VGY7_9GAMM            Unreviewed;       170 AA.
AC   E1VGY7;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Predicted Cu/Zn superoxide dismutase {ECO:0000313|EMBL:CBL44079.1};
GN   Name=sodC {ECO:0000313|EMBL:CBL44079.1};
GN   ORFNames=HDN1F_04960 {ECO:0000313|EMBL:CBL44079.1};
OS   gamma proteobacterium HdN1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=83406 {ECO:0000313|EMBL:CBL44079.1, ECO:0000313|Proteomes:UP000002677};
RN   [1] {ECO:0000313|EMBL:CBL44079.1, ECO:0000313|Proteomes:UP000002677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HdN1 {ECO:0000313|Proteomes:UP000002677};
RA   Widdel F., Rabus R., Grundmann O., Werner I., Schreiber F., Ehrenreich P.,
RA   Behrends A., Wilkes H., Kube M., Reinhardt R., Zedelius J.;
RT   "Alkane degradation by a new type of denitrifying bacterium with possible
RT   involvement of the electron acceptor in substrate activation.";
RL   Environ. Microbiol. 0:0-0(2010).
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|ARBA:ARBA00001935};
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; FP929140; CBL44079.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1VGY7; -.
DR   STRING; 83406.HDN1F_04960; -.
DR   KEGG; gpb:HDN1F_04960; -.
DR   eggNOG; COG2032; Bacteria.
DR   HOGENOM; CLU_056632_7_1_6; -.
DR   OrthoDB; 5431326at2; -.
DR   Proteomes; UP000002677; Chromosome.
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; 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; PS00087; SOD_CU_ZN_1; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002677};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..170
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003152934"
FT   DOMAIN          37..169
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   170 AA;  17124 MW;  AEF51DE1DDA56E20 CRC64;
     MNKTIIFASI LISSSAFASA DVTMNTVNEK GVGASIGTVA LSDSKFGLVL TPKLHGLPPG
     LHGFHVHQNP SCAAQEKDGV MTPALAAGGH LDPSASNKHG EPWGDGHLGD LPPIYVDASG
     NASQPVLAPR LKAADLVGHS LMIHAGGDNH ADHPAPLGGG AGRIACGVVK
//
DBGET integrated database retrieval system