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Database: UniProt
Entry: H0HM15_9RHIZ
LinkDB: H0HM15_9RHIZ
Original site: H0HM15_9RHIZ 
ID   H0HM15_9RHIZ            Unreviewed;       171 AA.
AC   H0HM15;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   16-JAN-2019, entry version 28.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=MAXJ12_05893 {ECO:0000313|EMBL:EHK58207.1};
OS   Mesorhizobium alhagi CCNWXJ12-2.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=1107882 {ECO:0000313|EMBL:EHK58207.1, ECO:0000313|Proteomes:UP000003250};
RN   [1] {ECO:0000313|EMBL:EHK58207.1, ECO:0000313|Proteomes:UP000003250}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCNWXJ12-2 {ECO:0000313|EMBL:EHK58207.1,
RC   ECO:0000313|Proteomes:UP000003250};
RX   PubMed=22328758; DOI=10.1128/JB.06635-11;
RA   Zhou M., Chen W., Chen H., Wei G.;
RT   "Draft Genome Sequence of Mesorhizobium alhagi CCNWXJ12-2T, a Novel
RT   Salt-Resistant Species Isolated from the Desert of Northwestern
RT   China.";
RL   J. Bacteriol. 194:1261-1262(2012).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000393}.
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:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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DR   EMBL; AHAM01000038; EHK58207.1; -; Genomic_DNA.
DR   EnsemblBacteria; EHK58207; EHK58207; MAXJ12_05893.
DR   PATRIC; fig|1107882.3.peg.1165; -.
DR   Proteomes; UP000003250; Unassembled WGS sequence.
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; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000003250};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003250};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    171       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003534017.
FT   DOMAIN       37    170       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   171 AA;  17571 MW;  E4BC50357C1DA6D8 CRC64;
     MDMKRAIITA TAILALTAVS GAQEPPSATA NFVNAAGEEN GTAKLTGTEG GVLIEIEVTG
     LPASQWVGFH VHETGTCDPA TGHESAGGHF NPTDAKHGYN VDGGPHAGDM PNQYVGADGT
     LRAQVFNGSV RLDEGDTNIR GKALMIHGGQ DDYESQPSGD AGDRQACAVI E
//
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