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Database: UniProt
Entry: A1VXQ2
LinkDB: A1VXQ2
Original site: A1VXQ2 
ID   SODF_CAMJJ              Reviewed;         220 AA.
AC   A1VXQ2; P53640;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   05-DEC-2018, entry version 65.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sodB; OrderedLocusNames=CJJ81176_0205;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8005660;
RA   Pesci E.C., Cottle D.L., Pickett C.L.;
RT   "Genetic, enzymatic, and pathogenic studies of the iron superoxide
RT   dismutase of Campylobacter jejuni.";
RL   Infect. Immun. 62:2687-2694(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems.
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   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; U08132; AAA53139.1; -; Genomic_DNA.
DR   EMBL; CP000538; EAQ73242.1; -; Genomic_DNA.
DR   PIR; H81434; H81434.
DR   RefSeq; WP_002851662.1; NC_008787.1.
DR   ProteinModelPortal; A1VXQ2; -.
DR   SMR; A1VXQ2; -.
DR   STRING; 354242.Cjejjejuni_010100000960; -.
DR   EnsemblBacteria; EAQ73242; EAQ73242; CJJ81176_0205.
DR   KEGG; cjj:CJJ81176_0205; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013584; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   Proteomes; UP000000646; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 1.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019833; Mn/Fe_SOD_BS.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN         1    220       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000285826.
FT   METAL        26     26       Iron. {ECO:0000250}.
FT   METAL        73     73       Iron. {ECO:0000250}.
FT   METAL       164    164       Iron. {ECO:0000250}.
FT   METAL       168    168       Iron. {ECO:0000250}.
SQ   SEQUENCE   220 AA;  24813 MW;  1E0BE7150960D017 CRC64;
     MFELRKLPYD TNAFGDFLSA ETFSYHHGKH HNTYVTNLNN LIKDTEFAGK DLVSIIKTSN
     GGVFNNAAQV YNHDFYFDCI KPSTGCGCGG SCQSIDANLQ AALEKEFGSL ENFKAEFIKG
     ATGVFGSGWF WLVYNTKNQK LEFVGTSNAA TPITEDKVPL LVVDVWEHAY YVDHRNARPA
     YLEKFYAHIN WEFVAKAYEW ALKEGMGSVS FYANELHPVK
//
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