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Database: UniProt/TrEMBL
Entry: B8F4Z8_HAEPS
LinkDB: B8F4Z8_HAEPS
Original site: B8F4Z8_HAEPS 
ID   B8F4Z8_HAEPS            Unreviewed;       180 AA.
AC   B8F4Z8;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   25-OCT-2017, entry version 56.
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:ACL32400.1};
GN   OrderedLocusNames=HAPS_0756 {ECO:0000313|EMBL:ACL32400.1};
OS   Haemophilus parasuis serovar 5 (strain SH0165).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=557723 {ECO:0000313|EMBL:ACL32400.1, ECO:0000313|Proteomes:UP000006743};
RN   [1] {ECO:0000313|EMBL:ACL32400.1, ECO:0000313|Proteomes:UP000006743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH0165 {ECO:0000313|EMBL:ACL32400.1,
RC   ECO:0000313|Proteomes:UP000006743};
RX   PubMed=19074396; DOI=10.1128/JB.01682-08;
RA   Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R.,
RA   Jin M., Jin Q., Chen H.;
RT   "Complete genome sequence of Haemophilus parasuis SH0165.";
RL   J. Bacteriol. 191:1359-1360(2009).
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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; CP001321; ACL32400.1; -; Genomic_DNA.
DR   RefSeq; WP_005710764.1; NC_011852.1.
DR   ProteinModelPortal; B8F4Z8; -.
DR   STRING; 557723.HAPS_0756; -.
DR   EnsemblBacteria; ACL32400; ACL32400; HAPS_0756.
DR   GeneID; 7278271; -.
DR   KEGG; hap:HAPS_0756; -.
DR   eggNOG; ENOG4108Z7T; Bacteria.
DR   eggNOG; COG2032; LUCA.
DR   HOGENOM; HOG000263449; -.
DR   KO; K04565; -.
DR   OMA; HKGDIGN; -.
DR   Proteomes; UP000006743; Chromosome.
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:UP000006743};
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:UP000006743};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    180       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002868750.
FT   DOMAIN       40    179       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   180 AA;  19004 MW;  9EAD6500EB43031F CRC64;
     MKKTVLTLAL TALFGFSTSA IANSATQIEV KVQQLDLQNG NKDVGTVTIT ESPYGLVFTP
     NLKGLSHGLH GFHIHEKPSC EPKEKDGKLV AGLGAGGHWD PKETKKHGYP WSDEAHLGDL
     PALAVDHEGN ATNPVLAPRL KKLEEVKGRS LMIHAGGDNH SDHPAPLGGG GARMACGVIN
//
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