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 03-MAY-2023, entry version 75.
DE RecName: Full=Superoxide dismutase [Fe];
DE EC=1.15.1.1;
GN Name=sodB; Synonyms=sod;
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=DSM 938 / 37b4;
RX PubMed=9765573; DOI=10.1128/jb.180.20.5413-5420.1998;
RA Cortez N., Carrillo N., Pasternak C., Balzer A., Klug G.;
RT "Molecular cloning and expression analysis of the Rhodobacter capsulatus
RT 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 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 family.
CC {ECO:0000305}.
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DR EMBL; AF022931; AAC64207.1; -; Genomic_DNA.
DR RefSeq; WP_074556057.1; NZ_FNAY01000032.1.
DR PDB; 7AZQ; X-ray; 2.00 A; A/E=2-200.
DR PDB; 7AZR; X-ray; 2.10 A; A/E=2-200.
DR PDBsum; 7AZQ; -.
DR PDBsum; 7AZR; -.
DR AlphaFoldDB; O30970; -.
DR SMR; O30970; -.
DR OrthoDB; 9803125at2; -.
DR BRENDA; 1.15.1.1; 5381.
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; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 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 PANTHER; PTHR42769; SUPEROXIDE DISMUTASE; 1.
DR PANTHER; PTHR42769:SF3; SUPEROXIDE DISMUTASE [FE] 2, CHLOROPLASTIC; 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; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..200
FT /note="Superoxide dismutase [Fe]"
FT /id="PRO_0000160000"
FT BINDING 28
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT TURN 12..15
FT /evidence="ECO:0007829|PDB:7AZQ"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:7AZQ"
FT HELIX 22..30
FT /evidence="ECO:0007829|PDB:7AZQ"
FT HELIX 32..44
FT /evidence="ECO:0007829|PDB:7AZQ"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:7AZQ"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:7AZQ"
FT HELIX 71..88
FT /evidence="ECO:0007829|PDB:7AZQ"
FT HELIX 99..109
FT /evidence="ECO:0007829|PDB:7AZQ"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:7AZQ"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:7AZQ"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:7AZQ"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:7AZQ"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:7AZQ"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:7AZQ"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:7AZQ"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:7AZQ"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:7AZQ"
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
//
