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Database: UniProt
Entry: H1XSM6_9BACT
LinkDB: H1XSM6_9BACT
Original site: H1XSM6_9BACT 
ID   H1XSM6_9BACT            Unreviewed;       240 AA.
AC   H1XSM6;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   16-JAN-2019, entry version 32.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=Cabys_1835 {ECO:0000313|EMBL:APF18584.1}, Calab_2967
GN   {ECO:0000313|EMBL:EHO42574.1};
OS   Caldithrix abyssi DSM 13497.
OC   Bacteria; Calditrichaeota; Calditrichae; Calditrichales;
OC   Calditrichaceae; Caldithrix.
OX   NCBI_TaxID=880073 {ECO:0000313|EMBL:EHO42574.1, ECO:0000313|Proteomes:UP000004671};
RN   [1] {ECO:0000313|EMBL:EHO42574.1, ECO:0000313|Proteomes:UP000004671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13497 {ECO:0000313|EMBL:EHO42574.1,
RC   ECO:0000313|Proteomes:UP000004671};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N.,
RA   Chertkov O., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The permanent draft genome of Caldithrix abyssi DSM 13497.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:APF18584.1, ECO:0000313|Proteomes:UP000183868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LF13 {ECO:0000313|EMBL:APF18584.1,
RC   ECO:0000313|Proteomes:UP000183868};
RA   Kublanov I., Sigalova O., Gavrilov S., Lebedinsky A., Ivanova N.,
RA   Daum C., Reddy T., Klenk H.P., Goker M., Reva O., Miroshnichenko M.,
RA   Kyprides N., Woyke T., Gelfand M.;
RT   "Genomic analysis of Caldithrix abyssi and proposal of a novel
RT   bacterial phylum Caldithrichaeota.";
RL   Submitted (NOV-2016) 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
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; CP018099; APF18584.1; -; Genomic_DNA.
DR   EMBL; CM001402; EHO42574.1; -; Genomic_DNA.
DR   RefSeq; WP_006929931.1; NZ_CP018099.1.
DR   ProteinModelPortal; H1XSM6; -.
DR   EnsemblBacteria; EHO42574; EHO42574; Calab_2967.
DR   KEGG; caby:Cabys_1835; -.
DR   KO; K04564; -.
DR   OrthoDB; 1440645at2; -.
DR   BioCyc; CABY880073:G10QG-2956-MONOMER; -.
DR   Proteomes; UP000004671; Chromosome.
DR   Proteomes; UP000183868; 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   InterPro; IPR006311; TAT_signal.
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.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000004671,
KW   ECO:0000313|Proteomes:UP000183868};
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:UP000004671};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     26       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        27    240       Superoxide dismutase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5009695290.
FT   DOMAIN       41    122       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      132    233       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        66     66       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       114    114       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       201    201       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       205    205       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   240 AA;  27035 MW;  73C781E9C3A64459 CRC64;
     MSNRRNFLKA SGLVMAGGIL APHIMAANAE QSADLSGQLT EHKLPPLPYA YDALEPYINR
     RIMELHHSKH HAGYVKGLNK AEKELARARA TGDFGLIQYW SRKAAFNGGG HFLHSMFWKV
     MAPAGKGGGG KPKGELLKMI ERDFGSFEAF KAQFSAAAKA VEGSGWGLLH YRPQDDRLIV
     LQAENQQKLS PWGSTPVMGI DVWEHAYYLQ YENKRAAYIE AWWNIVNWEQ VWKNILALRK
//
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