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Database: UniProt
Entry: F0NXD3_WEEVC
LinkDB: F0NXD3_WEEVC
Original site: F0NXD3_WEEVC 
ID   F0NXD3_WEEVC            Unreviewed;       198 AA.
AC   F0NXD3;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 58.
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=Weevi_0183 {ECO:0000313|EMBL:ADX66907.1};
OS   Weeksella virosa (strain ATCC 43766 / DSM 16922 / JCM 21250 / CCUG 30538 /
OS   CDC 9751 / IAM 14551 / NBRC 16016 / NCTC 11634 / CL345/78).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Weeksella.
OX   NCBI_TaxID=865938 {ECO:0000313|EMBL:ADX66907.1, ECO:0000313|Proteomes:UP000008641};
RN   [1] {ECO:0000313|EMBL:ADX66907.1, ECO:0000313|Proteomes:UP000008641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43766 / DSM 16922 / JCM 21250 / NBRC 16016 / NCTC 11634 /
RC   CL345/78 {ECO:0000313|Proteomes:UP000008641};
RX   PubMed=21475590;
RA   Lang E., Teshima H., Lucas S., Lapidus A., Hammon N., Deshpande S.,
RA   Nolan M., Cheng J.F., Pitluck S., Liolios K., Pagani I., Mikhailova N.,
RA   Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Brambilla E.M., Kopitz M., Rohde M., Goker M., Tindall B.J., Detter J.C.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Weeksella virosa type strain (9751).";
RL   Stand. Genomic Sci. 4:81-90(2011).
RN   [2] {ECO:0000313|Proteomes:UP000008641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43766 / DSM 16922 / JCM 21250 / NBRC 16016 / NCTC 11634 /
RC   CL345/78 {ECO:0000313|Proteomes:UP000008641};
RX   DOI=10.4056/sigs.1603927;
RA   Lang E., Teshima H., Lucas S., Lapidus A., Hammon N., Deshpande S.,
RA   Nolan M., Cheng J., Pitluck S., Liolios K., Pagani I., Mikhailova N.,
RA   Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Brambilla E.,
RA   Kopitz M., Rohde M., Goker M., Tindall B., Detter J., Woyke T., Bristow J.,
RA   Eisen J., Markowitz V., Hugenholtz P., Klenk H., Kyrpides N.;
RT   "Complete genome sequence of Weeksella virosa type strain (9751T).";
RL   Stand. Genomic Sci. 4:81-90(2011).
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; CP002455; ADX66907.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0NXD3; -.
DR   STRING; 865938.Weevi_0183; -.
DR   KEGG; wvi:Weevi_0183; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_0_0_10; -.
DR   OMA; REMYVET; -.
DR   OrthoDB; 9803125at2; -.
DR   Proteomes; UP000008641; 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; 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   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000349-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008641}.
FT   DOMAIN          6..88
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          95..196
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   BINDING         29
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         80
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         163
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         167
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ   SEQUENCE   198 AA;  22698 MW;  C1D845BF5BB912AD CRC64;
     MKITQTLPEL PYDTNALNPI ITEETFDYHY GKHHAAYVNN LAGLVKNTPL ETATVEEIIQ
     KGFAENNAGL FNNAAQHWNH SFFWHCLSPN GGKAPQGRIA ELINRDFGSF EEFQNKFSET
     AIKLFGAGWA WLAQNDQGLL EIVPMKDAHT PLTENKTPIL TLDVWEHAYY IDYRNARPKF
     VEGFWEIVNW DFANKNLK
//
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