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
//
