ID   F8KZR5_PARAV            Unreviewed;       178 AA.
AC   F8KZR5;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=sOD {ECO:0000313|EMBL:CCB86420.1};
GN   OrderedLocusNames=PUV_14700 {ECO:0000313|EMBL:CCB86420.1};
OS   Parachlamydia acanthamoebae (strain UV7).
OC   Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC   Parachlamydia.
OX   NCBI_TaxID=765952 {ECO:0000313|EMBL:CCB86420.1, ECO:0000313|Proteomes:UP000000495};
RN   [1] {ECO:0000313|EMBL:CCB86420.1, ECO:0000313|Proteomes:UP000000495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UV7 {ECO:0000313|Proteomes:UP000000495};
RX   PubMed=21690563; DOI=10.1093/molbev/msr161;
RA   Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., Brunham R.C.,
RA   Read T.D., Bavoil P.M., Sachse K., Kahane S., Friedman M.G., Rattei T.,
RA   Myers G.S., Horn M.;
RT   "Unity in variety--the pan-genome of the Chlamydiae.";
RL   Mol. Biol. Evol. 28:3253-3270(2011).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000393}.
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:RU000393};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00010457, ECO:0000256|RuleBase:RU000393}.
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DR   EMBL; FR872580; CCB86420.1; -; Genomic_DNA.
DR   RefSeq; WP_013924963.1; NC_015702.1.
DR   AlphaFoldDB; F8KZR5; -.
DR   STRING; 765952.PUV_14700; -.
DR   KEGG; puv:PUV_14700; -.
DR   eggNOG; COG2032; Bacteria.
DR   HOGENOM; CLU_056632_4_1_0; -.
DR   OrthoDB; 9792957at2; -.
DR   Proteomes; UP000000495; Chromosome.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003:SF71; SUPEROXIDE DISMUTASE; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393,
KW   ECO:0000313|EMBL:CCB86420.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000495};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..178
FT                   /note="Superoxide dismutase [Cu-Zn]"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003379138"
FT   DOMAIN          47..173
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   178 AA;  19227 MW;  224BE93048D46717 CRC64;
     MRKLLAYGLC LFLLTSCNSS EQKAEDPHHI KKANAVVNPT EGYKTWGNIT FTETKEGVQI
     VANVQGLPAG KHGFHIHEFG DCSAPDASSA GAHYDPTHHK HGGPDDLDRH VGDLGNLEAN
     ENGHALYERL DKTITLNGPN SIVGKSIVIH EDEDDFKSQP AGNSGKRVAC GLILPLEE
//