ID A5FGP6_FLAJ1 Unreviewed; 260 AA.
AC A5FGP6;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Superoxide dismutase {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
DE EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
GN OrderedLocusNames=Fjoh_2595 {ECO:0000313|EMBL:ABQ05622.1};
OS Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=376686 {ECO:0000313|EMBL:ABQ05622.1, ECO:0000313|Proteomes:UP000006694};
RN [1] {ECO:0000313|EMBL:ABQ05622.1, ECO:0000313|Proteomes:UP000006694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 /
RC UW101 {ECO:0000313|Proteomes:UP000006694};
RX PubMed=19717629; DOI=10.1128/AEM.01495-09;
RA McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA Cheng Y.Q., Stein J.L.;
RT "Novel features of the polysaccharide-digesting gliding bacterium
RT Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL Appl. Environ. Microbiol. 75:6864-6875(2009).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
CC {ECO:0000256|RuleBase:RU000414}.
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:RU000414};
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}.
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DR EMBL; CP000685; ABQ05622.1; -; Genomic_DNA.
DR RefSeq; WP_012024661.1; NZ_MUGZ01000009.1.
DR AlphaFoldDB; A5FGP6; -.
DR STRING; 376686.Fjoh_2595; -.
DR KEGG; fjo:Fjoh_2595; -.
DR eggNOG; COG0605; Bacteria.
DR HOGENOM; CLU_031625_0_1_10; -.
DR OrthoDB; 9803125at2; -.
DR Proteomes; UP000006694; 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; 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; PTHR43595; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43595:SF2; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
DR Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000414};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000414}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..260
FT /note="Superoxide dismutase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030164433"
FT DOMAIN 55..137
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 145..248
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
SQ SEQUENCE 260 AA; 29870 MW; 5DAE11F915DAC2D1 CRC64;
MKKIIVLFSI LPSFILLFSC NDNNKLTEVV EVPLPTKEEK IVIGSPNDVK ADPGSFELTK
LPFAYDGLSP ALRSLTMETH YSKHYLSYTN NFNKAIVSTE FENMPIEDIL KKLDLNNAKL
RQNAGGYYNH TLYFNILTPK EQTPKDTLSG SINKEFGSFN NLTTQFKGQA EKQFGSGWVW
LVVDRYGKLQ ITTTEDQDNP LMKNALIPGT PILGIDLWEH AYYLDYQNRK GSYIDAFYEH
INWEKVNEYY IEALKKVKKV
//
