ID   Q13FS4_PARXL            Unreviewed;       302 AA.
AC   Q13FS4;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=Superoxide dismutase {ECO:0000313|EMBL:ABE37065.1};
GN   ORFNames=Bxe_C1205 {ECO:0000313|EMBL:ABE37065.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE37065.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE37065.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE37065.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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DR   EMBL; CP000272; ABE37065.1; -; Genomic_DNA.
DR   RefSeq; WP_005797796.1; NZ_CP008761.1.
DR   AlphaFoldDB; Q13FS4; -.
DR   STRING; 266265.Bxe_C1205; -.
DR   KEGG; bxb:DR64_8601; -.
DR   KEGG; bxe:Bxe_C1205; -.
DR   eggNOG; COG0605; Bacteria.
DR   eggNOG; COG0607; Bacteria.
DR   OrthoDB; 9811849at2; -.
DR   Proteomes; UP000001817; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:InterPro.
DR   GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:InterPro.
DR   CDD; cd01444; GlpE_ST; 1.
DR   Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   InterPro; IPR023695; Thiosulf_sulfurTrfase.
DR   PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR   PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   SMART; SM00450; RHOD; 1.
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   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   4: Predicted;
FT   DOMAIN          210..300
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   302 AA;  32861 MW;  B445FC6713C42BC3 CRC64;
     MDLQLRPLTI NLAALNGLSE KLILSHHANN YTGAVKRLDA IRQQLAHLDW PTAPVFMING
     LKREELIAAN SAWLHELYFD TLGGDGALPD SGLAVALARD FGSVDRWRTE FSALAKAMGG
     GSGWALLSWS TREARLINHW AADHTNLLAG ATPLLALDMY EHAYHMDFGA KAAAYVDAFM
     QNIRWNAVMQ RYAAAVEADA LPWSAAPEEV GGDLQLIDVR RTAGYAQAPD RIAGAIRRDP
     VQLANWSREI DTSKPVLVYC VHGHEVSQSV ALALRAHGLD ARFVAGGIEA CRAAGVTFEA
     KE
//