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Database: UniProt/TrEMBL
Entry: E4NT27_HALBP
LinkDB: E4NT27_HALBP
Original site: E4NT27_HALBP 
ID   E4NT27_HALBP            Unreviewed;       199 AA.
AC   E4NT27;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 71.
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=Hbor_14400 {ECO:0000313|EMBL:ADQ67020.1};
GN   ORFNames=C499_04651 {ECO:0000313|EMBL:ELY29811.1};
OS   Halogeometricum borinquense (strain ATCC 700274 / DSM 11551 / JCM 10706 /
OS   KCTC 4070 / PR3).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Halogeometricum.
OX   NCBI_TaxID=469382 {ECO:0000313|EMBL:ADQ67020.1, ECO:0000313|Proteomes:UP000006663};
RN   [1] {ECO:0000313|EMBL:ADQ67020.1, ECO:0000313|Proteomes:UP000006663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700274 / DSM 11551 / JCM 10706 / KCTC 4070 / PR3
RC   {ECO:0000313|Proteomes:UP000006663}, and PR 3
RC   {ECO:0000313|EMBL:ADQ67020.1};
RX   PubMed=21304651; DOI=10.4056/sigs.23264;
RA   Malfatti S., Tindall B.J., Schneider S., Fahnrich R., Lapidus A.,
RA   Labuttii K., Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S.,
RA   Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Anderson I.,
RA   Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA   D'haeseleer P., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Chain P.;
RT   "Complete genome sequence of Halogeometricum borinquense type strain
RT   (PR3).";
RL   Stand. Genomic Sci. 1:150-159(2009).
RN   [2] {ECO:0000313|EMBL:ELY29811.1, ECO:0000313|Proteomes:UP000011585}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11551 {ECO:0000313|EMBL:ELY29811.1,
RC   ECO:0000313|Proteomes:UP000011585};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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; CP001690; ADQ67020.1; -; Genomic_DNA.
DR   EMBL; AOHT01000013; ELY29811.1; -; Genomic_DNA.
DR   RefSeq; WP_006054250.1; NZ_AOHT01000013.1.
DR   AlphaFoldDB; E4NT27; -.
DR   SMR; E4NT27; -.
DR   STRING; 469382.Hbor_14400; -.
DR   GeneID; 9993259; -.
DR   KEGG; hbo:Hbor_14400; -.
DR   PATRIC; fig|469382.19.peg.912; -.
DR   eggNOG; arCOG04147; Archaea.
DR   HOGENOM; CLU_031625_2_0_2; -.
DR   OMA; YLHSIFW; -.
DR   OrthoDB; 32917at2157; -.
DR   Proteomes; UP000006663; Chromosome.
DR   Proteomes; UP000011585; Unassembled WGS sequence.
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   NCBIfam; NF041312; Superox_dis_Halo; 1.
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:UP000006663}.
FT   DOMAIN          2..83
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          90..187
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   BINDING         27
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         75
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         157
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         161
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ   SEQUENCE   199 AA;  22493 MW;  1BFCE48D64AE544F CRC64;
     MSYELDPLPY EYDALEPHIS EQVLTWHHDT HHQGYVNGWN SAEETLESNR EEGDFGSSPG
     AIRNVTHNGC GHILHDLFWN SMSPEGGSEP TGSLADRIEE DFGSYEAWKG EFEAAAGNAG
     GWALLVYDSF SNQLRNVVVD KHDQGALWGS HPILALDVWE HSYYHDYGPA RGDFIDAFFE
     VVDWEEPSAR YEQAVELFE
//
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