ID A9AXW8_HERA2 Unreviewed; 255 AA.
AC A9AXW8;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 87.
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=Haur_2294 {ECO:0000313|EMBL:ABX04934.1};
OS Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC Bacteria; Chloroflexota; Chloroflexia; Herpetosiphonales;
OC Herpetosiphonaceae; Herpetosiphon.
OX NCBI_TaxID=316274 {ECO:0000313|EMBL:ABX04934.1, ECO:0000313|Proteomes:UP000000787};
RN [1] {ECO:0000313|Proteomes:UP000000787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23779 / DSM 785 / 114-95
RC {ECO:0000313|Proteomes:UP000000787};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABX04934.1, ECO:0000313|Proteomes:UP000000787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23779 / DSM 785 / 114-95
RC {ECO:0000313|Proteomes:UP000000787};
RX PubMed=22675585; DOI=10.4056/sigs.2194987;
RA Kiss H., Nett M., Domin N., Martin K., Maresca J.A., Copeland A.,
RA Lapidus A., Lucas S., Berry K.W., Glavina Del Rio T., Dalin E., Tice H.,
RA Pitluck S., Richardson P., Bruce D., Goodwin L., Han C., Detter J.C.,
RA Schmutz J., Brettin T., Land M., Hauser L., Kyrpides N.C., Ivanova N.,
RA Goker M., Woyke T., Klenk H.P., Bryant D.A.;
RT "Complete genome sequence of the filamentous gliding predatory bacterium
RT Herpetosiphon aurantiacus type strain (114-95(T)).";
RL Stand. Genomic Sci. 5:356-370(2011).
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; CP000875; ABX04934.1; -; Genomic_DNA.
DR AlphaFoldDB; A9AXW8; -.
DR STRING; 316274.Haur_2294; -.
DR KEGG; hau:Haur_2294; -.
DR eggNOG; COG0605; Bacteria.
DR HOGENOM; CLU_031625_0_1_0; -.
DR InParanoid; A9AXW8; -.
DR BioCyc; HAUR316274:GHYA-2322-MONOMER; -.
DR Proteomes; UP000000787; 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; 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 InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43595; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43595:SF2; 37S RIBOSOMAL PROTEIN S26, 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.
DR PROSITE; PS51318; TAT; 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}.
FT DOMAIN 52..140
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 149..247
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT BINDING 77
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 132
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 215
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 219
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ SEQUENCE 255 AA; 27779 MW; 2131196E5E2234C7 CRC64;
MSERFNLSRR GFLGAVGLGS LAAIWGSKGA SAKKYGGVGK TFDQATVPTN GKFTLPALPY
DYGDLEPHLD AETMYIHHQK HHQALVTNLN AALADYPKLQ SMNVAELLHG LSSLPSAIQT
AVRNNAGGHA NHAIWWATLS PKGGGNAGGA LAAAINAKYG SFNSFKTTFN DIAARRFGSG
WGWLSTDSKG TLYLASYPNQ DSPYMEGLTP LLGVDVWEHA YYLKFRQKRA EFLSAWWNVI
NWGEVGRRYD LAIAK
//
