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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7

DescriptionRecName: Full=Superoxide dismutase [Fe]; EC=1.15.1.1;
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MyHits synonymsSODF_RHOCA , O30970 , 5614DAD17AD0238A
match map segment
ipat:SOD_MN ipfam:Sod_Fe_N ipfam:Sod_Fe_C  
Legends: 1, ipat:SOD_MN [T].
ID   SODF_RHOCA              Reviewed;         200 AA.
AC   O30970;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   02-NOV-2016, entry version 58.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sodB; Synonyms=sod;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=DSM 938 / 37b4;
RX   PubMed=9765573;
RA   Cortez N., Carrillo N., Pasternak C., Balzer A., Klug G.;
RT   "Molecular cloning and expression analysis of the Rhodobacter
RT   capsulatus sodB gene, encoding an iron superoxide dismutase.";
RL   J. Bacteriol. 180:5413-5420(1998).
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
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; AF022931; AAC64207.1; -; Genomic_DNA.
DR   ProteinModelPortal; O30970; -.
DR   STRING; 272942.RCAP_rcc02311; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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   PANTHER; PTHR11404; PTHR11404; 1.
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   1: Evidence at protein level;
KW   Iron; Metal-binding; Oxidoreductase.
FT   CHAIN         1    200       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000160000.
FT   METAL        28     28       Iron. {ECO:0000250}.
FT   METAL        82     82       Iron. {ECO:0000250}.
FT   METAL       165    165       Iron. {ECO:0000250}.
FT   METAL       169    169       Iron. {ECO:0000250}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       165    172       ipat:SOD_MN [T]
FT   MYHIT         3     89       ipfam:Sod_Fe_N [T]
FT   MYHIT        99    199       ipfam:Sod_Fe_C [T]
SQ   SEQUENCE   200 AA;  22122 MW;  5614DAD17AD0238A CRC64;
     MAFELPALPY AHDALASLGM SKETLEYHHD LHHKAYVDNG NKLIAGTEWE GKSVEEIVKG
     TYCAGAVAQS GIFNNASQHW NHAQFWEMMG PGEDKKMPGA LEKALVESFG SVAKFKEDFA
     AAGAGQFGSG WAWLVKDSDG ALKITKTENG VNPLCFGQTA LLGCDVWEHS YYIDFRNKRP
     AYLTNFLDKL VNWENVASRM
//