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Database: UniProt
Entry: T0H039_9SPHN
LinkDB: T0H039_9SPHN
Original site: T0H039_9SPHN 
ID   T0H039_9SPHN            Unreviewed;       181 AA.
AC   T0H039;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Superoxide dismutase {ECO:0000313|EMBL:EQB06327.1};
GN   ORFNames=L485_01500 {ECO:0000313|EMBL:EQB06327.1};
OS   Sphingobium baderi LL03.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1114964 {ECO:0000313|EMBL:EQB06327.1, ECO:0000313|Proteomes:UP000015524};
RN   [1] {ECO:0000313|EMBL:EQB06327.1, ECO:0000313|Proteomes:UP000015524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LL03 {ECO:0000313|EMBL:EQB06327.1,
RC   ECO:0000313|Proteomes:UP000015524};
RX   PubMed=24051322;
RA   Kaur J., Verma H., Tripathi C., Khurana J.P., Lal R.;
RT   "Draft Genome Sequence of a Hexachlorocyclohexane-Degrading Bacterium,
RT   Sphingobium baderi Strain LL03T.";
RL   Genome Announc. 1:e00751-13(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00010457}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EQB06327.1}.
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DR   EMBL; ATIB01000017; EQB06327.1; -; Genomic_DNA.
DR   RefSeq; WP_021243322.1; NZ_KQ130471.1.
DR   AlphaFoldDB; T0H039; -.
DR   PATRIC; fig|1114964.3.peg.278; -.
DR   eggNOG; COG2032; Bacteria.
DR   OrthoDB; 5431326at2; -.
DR   Proteomes; UP000015524; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
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; 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   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015524};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..181
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009975902"
FT   DOMAIN          47..177
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   181 AA;  18174 MW;  5EC60E9B8C270D16 CRC64;
     MKFVSMAWAL PLFTTVAACA TVPEESASAG EAPVAYAKLL AGDGTARGEA KVTQAADGLH
     VLVRAEGLTP GLHAVHVHTT GTCTPPDFVS AGGHWNPTDR QHGKDNPHGM HMGDMPNMLA
     GSDGTGEMEY VIPGGLVSSG AMPLLDADGA AIVIHAQADD NKTDPAGNAG GRAACGVLAA
     G
//
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