ID V4HNI7_9EURY Unreviewed; 200 AA.
AC V4HNI7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 16-JAN-2019, entry version 24.
DE RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN ORFNames=K933_03660 {ECO:0000313|EMBL:ESP89489.1}, K933_16177
GN {ECO:0000313|EMBL:ESP87071.1};
OS Candidatus Halobonum tyrrellensis G22.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
OC Haloferacales; Halorubraceae; Candidatus Halobonum.
OX NCBI_TaxID=1324957 {ECO:0000313|EMBL:ESP89489.1, ECO:0000313|Proteomes:UP000017840};
RN [1] {ECO:0000313|EMBL:ESP89489.1, ECO:0000313|Proteomes:UP000017840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G22 {ECO:0000313|EMBL:ESP89489.1,
RC ECO:0000313|Proteomes:UP000017840};
RX PubMed=24336364;
RA Ugalde J.A., Narasingarao P., Kuo S., Podell S., Allen E.E.;
RT "Draft Genome Sequence of 'Candidatus Halobonum tyrrellensis' Strain
RT G22, Isolated from the Hypersaline Waters of Lake Tyrrell,
RT Australia.";
RL Genome Announc. 1:e01001-13(2013).
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
CC family. {ECO:0000256|RuleBase:RU000414}.
CC -!- CAUTION: The sequence shown here is derived from an
CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC preliminary data. {ECO:0000313|EMBL:ESP89489.1}.
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DR EMBL; ASGZ01000064; ESP87071.1; -; Genomic_DNA.
DR EMBL; ASGZ01000009; ESP89489.1; -; Genomic_DNA.
DR RefSeq; WP_023393323.1; NZ_ASGZ01000064.1.
DR EnsemblBacteria; ESP87071; ESP87071; K933_16177.
DR EnsemblBacteria; ESP89489; ESP89489; K933_03660.
DR PATRIC; fig|1324957.4.peg.3285; -.
DR OrthoDB; 74803at2157; -.
DR Proteomes; UP000017840; 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; -; 1.
DR Gene3D; 2.40.500.20; -; 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 Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PIRSF; PIRSF000349; SODismutase; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF46609; SSF46609; 1.
DR SUPFAM; SSF54719; SSF54719; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 3: Inferred from homology;
KW Complete proteome {ECO:0000313|Proteomes:UP000017840};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW ECO:0000256|RuleBase:RU000414};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW Reference proteome {ECO:0000313|Proteomes:UP000017840}.
FT DOMAIN 3 84 Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT DOMAIN 91 189 Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT METAL 28 28 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 76 76 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 158 158 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 162 162 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ SEQUENCE 200 AA; 22789 MW; 455E4666CB4665EA CRC64;
MSEYELPPLP YDYDALEPHI SEQVLTWHHD THHQGYVNGW NSAEETLEQN REEGEFGSSG
SALRNVTHNG SGHMLHTLFW QSMSPEGGDE PSGELADRIE EDFGSYDAWK GEFEAAAKNA
SGWALLVYDS FSNELHNVVV DKHDQGALWG SHPVLALDVW EHSYYYDYGP ARGDFIDAFF
EVVDWTEPAE RYEQATQLFE
//
