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Database: UniProt
Entry: C9PMK0_9PAST
LinkDB: C9PMK0_9PAST
Original site: C9PMK0_9PAST 
ID   C9PMK0_9PAST            Unreviewed;       195 AA.
AC   C9PMK0;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   10-APR-2019, entry version 40.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=sodC {ECO:0000313|EMBL:EEX51420.1};
GN   ORFNames=HMPREF0621_0224 {ECO:0000313|EMBL:EEX51420.1};
OS   Pasteurella dagmatis ATCC 43325.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=667128 {ECO:0000313|EMBL:EEX51420.1, ECO:0000313|Proteomes:UP000005519};
RN   [1] {ECO:0000313|EMBL:EEX51420.1, ECO:0000313|Proteomes:UP000005519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43325 {ECO:0000313|EMBL:EEX51420.1,
RC   ECO:0000313|Proteomes:UP000005519};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z.,
RA   Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L.,
RA   Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D.,
RA   Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R.,
RA   San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S.,
RA   Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K.,
RA   Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EEX51420.1}.
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DR   EMBL; ACZR01000001; EEX51420.1; -; Genomic_DNA.
DR   RefSeq; WP_005765223.1; NZ_GG704815.1.
DR   ProteinModelPortal; C9PMK0; -.
DR   EnsemblBacteria; EEX51420; EEX51420; HMPREF0621_0224.
DR   eggNOG; ENOG4108Z7T; Bacteria.
DR   eggNOG; COG2032; LUCA.
DR   BioCyc; GCF_000163475-HMP:HMPREF0621_RS00975-MONOMER; -.
DR   Proteomes; UP000005519; 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; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005519};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393,
KW   ECO:0000313|EMBL:EEX51420.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005519};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25    195       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002998557.
FT   DOMAIN       56    194       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   195 AA;  20453 MW;  AAE9F05A1B543515 CRC64;
     MKKTLLAALL SCGIGMGMSM SAIAHSHEGH DHKHAHSHAG EKIEVKVELL DPVKGNQDAG
     KVIITESPYG LVFTPELKGL ATGLHGFHIH QNPSCDAKEK DGKLVAGLAA GGHWDPKKAG
     KHGYPWSDEA HLGDLPALTV NADGTSTNPV LAPRLKHLDD VKGRSLMIHE GGDNHSDHPA
     PLGGGGPRMA CGVIK
//
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