ID   F4L274_HALH1            Unreviewed;       241 AA.
AC   F4L274;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
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=Halhy_3829 {ECO:0000313|EMBL:AEE51681.1};
OS   Haliscomenobacter hydrossis (strain ATCC 27775 / DSM 1100 / LMG 10767 / O).
OC   Bacteria; Bacteroidota; Saprospiria; Saprospirales; Haliscomenobacteraceae;
OC   Haliscomenobacter.
OX   NCBI_TaxID=760192 {ECO:0000313|EMBL:AEE51681.1, ECO:0000313|Proteomes:UP000008461};
RN   [1] {ECO:0000313|EMBL:AEE51681.1, ECO:0000313|Proteomes:UP000008461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27775 / DSM 1100 / LMG 10767 / O
RC   {ECO:0000313|Proteomes:UP000008461};
RX   PubMed=21886862; DOI=10.4056/sigs.1964579;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Daligault H., Lapidus A., Zeytun A., Nolan M., Lucas S., Del Rio T.G.,
RA   Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Pagani I., Ivanova N., Huntemann M., Mavromatis K., Mikhailova N., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Rohde M.,
RA   Verbarg S., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of Haliscomenobacter hydrossis type strain (O).";
RL   Stand. Genomic Sci. 4:352-360(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 1100;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Pagani I.,
RA   Daligault H., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Verbarg S., Frueling A.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "Complete sequence of chromosome of Haliscomenobacter hydrossis DSM 1100.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002691; AEE51681.1; -; Genomic_DNA.
DR   RefSeq; WP_013766220.1; NC_015510.1.
DR   AlphaFoldDB; F4L274; -.
DR   STRING; 760192.Halhy_3829; -.
DR   GeneID; 78193602; -.
DR   KEGG; hhy:Halhy_3829; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_2_2_10; -.
DR   OrthoDB; 9803125at2; -.
DR   Proteomes; UP000008461; 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; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR   PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 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:UP000008461}.
FT   DOMAIN          44..123
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          130..232
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   BINDING         68
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         116
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         199
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         203
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ   SEQUENCE   241 AA;  27702 MW;  BA283051907C9D37 CRC64;
     MDRSTFLKNT AILGTASLLP NNSVFANNVT ENGIDKLVDA DGNFALQALP YKETFLEPYM
     DEETVHLHYM FHHGGAVKGA NKDLQMIRKA LDENSVETVD YWTKKLSYHL SSHILHTIFW
     TNLTNKKTEP AGELLKKIER DFGSYDKLKL LISKTSKDVD GNGWGILGYQ PYTDKLTVLQ
     CENHEKLTQW GVIPLLVIDV WEHSYYLKYR NKRADFVDNL FGILNWDNVA QRFDTGLKLL
     K
//