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Database: UniProt/TrEMBL
Entry: A0A0G3XBX6_9SPHN
LinkDB: A0A0G3XBX6_9SPHN
Original site: A0A0G3XBX6_9SPHN 
ID   A0A0G3XBX6_9SPHN        Unreviewed;       176 AA.
AC   A0A0G3XBX6;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Putative superoxide dismutase (Cu/Zn) {ECO:0000313|EMBL:AKM08131.1};
DE   Flags: Precursor;
GN   ORFNames=AM2010_2069 {ECO:0000313|EMBL:AKM08131.1};
OS   Pelagerythrobacter marensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Pelagerythrobacter.
OX   NCBI_TaxID=543877 {ECO:0000313|EMBL:AKM08131.1, ECO:0000313|Proteomes:UP000037643};
RN   [1] {ECO:0000313|EMBL:AKM08131.1, ECO:0000313|Proteomes:UP000037643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 22370 {ECO:0000313|EMBL:AKM08131.1,
RC   ECO:0000313|Proteomes:UP000037643};
RA   Kim K.M.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP011805; AKM08131.1; -; Genomic_DNA.
DR   RefSeq; WP_047807010.1; NZ_LMVG01000004.1.
DR   AlphaFoldDB; A0A0G3XBX6; -.
DR   STRING; 543877.AM2010_2069; -.
DR   KEGG; amx:AM2010_2069; -.
DR   PATRIC; fig|543877.4.peg.2103; -.
DR   OrthoDB; 5431326at2; -.
DR   Proteomes; UP000037643; Chromosome.
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:UP000037643};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..176
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002562408"
FT   DOMAIN          44..172
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
FT   REGION          86..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   176 AA;  17582 MW;  20E0B33114ED3398 CRC64;
     MTRLPVLAAA VASISLAGCA STPAPTAETL GTAQLSLANG APAGTAEIVA AGDHVSMHVT
     VSGIDAGPHG FHLHTTGACR APDFKSAGGH LNPTDNEHGA ENPDGSHFGD LPNLQVGSNR
     TASASFDLGH GRARAMEWLF DADGTAVVIH AGADDYRSDP AGNAGARIAC GVLEQG
//
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