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Database: UniProt
Entry: C7NYW1_HALMD
LinkDB: C7NYW1_HALMD
Original site: C7NYW1_HALMD 
ID   C7NYW1_HALMD            Unreviewed;       203 AA.
AC   C7NYW1;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   16-JAN-2019, entry version 55.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=Hmuk_2542 {ECO:0000313|EMBL:ACV48650.1};
OS   Halomicrobium mukohataei (strain ATCC 700874 / DSM 12286 / JCM 9738 /
OS   NCIMB 13541) (Haloarcula mukohataei).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
OC   Halobacteriales; Haloarculaceae; Halomicrobium.
OX   NCBI_TaxID=485914 {ECO:0000313|EMBL:ACV48650.1, ECO:0000313|Proteomes:UP000001746};
RN   [1] {ECO:0000313|EMBL:ACV48650.1, ECO:0000313|Proteomes:UP000001746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB 13541
RC   {ECO:0000313|Proteomes:UP000001746};
RX   PubMed=21304667; DOI=10.4056/sigs.42644;
RA   Tindall B.J., Schneider S., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F.,
RA   Saunders E., Bruce D., Goodwin L., Pitluck S., Mikhailova N., Pati A.,
RA   Ivanova N., Mavrommatis K., Chen A., Palaniappan K., Chain P.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Han C.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Klenk H.P., Kyrpides N.C., Detter J.C.;
RT   "Complete genome sequence of Halomicrobium mukohataei type strain
RT   (arg-2).";
RL   Stand. Genomic Sci. 1:270-277(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
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; CP001688; ACV48650.1; -; Genomic_DNA.
DR   RefSeq; WP_015763492.1; NC_013202.1.
DR   ProteinModelPortal; C7NYW1; -.
DR   SMR; C7NYW1; -.
DR   STRING; 485914.Hmuk_2542; -.
DR   EnsemblBacteria; ACV48650; ACV48650; Hmuk_2542.
DR   GeneID; 8412086; -.
DR   KEGG; hmu:Hmuk_2542; -.
DR   eggNOG; arCOG04147; Archaea.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; YEGWKGE; -.
DR   OrthoDB; 74803at2157; -.
DR   BioCyc; HMUK485914:GCKD-2547-MONOMER; -.
DR   Proteomes; UP000001746; 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; -; 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:UP000001746};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:ACV48650.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001746}.
FT   DOMAIN        8     87       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       94    193       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        31     31       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        79     79       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       165    165       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   203 AA;  22486 MW;  DB35183CF33E781A CRC64;
     MSEHSDPELP PLPYDYDALE PHISEQVLTW HHDTHHQGYV NGLAAAEETL AENRESGEFG
     SSAGALGNVT HNGSGHYLHT LFWDNMSPNG GGEPSGELRD RIEADFGSYE GWKGEFEAAA
     SAAGGWALLV YDPVAKQLRN VTVDKHDQGA LWGSHPIMAL DVWEHSYYYD YGPDRGSFVD
     AFFEVVDWDE VASQYETAVG HFE
//
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