ID   A0A0P7X6Z1_9GAMM        Unreviewed;       184 AA.
AC   A0A0P7X6Z1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Cu-Zn family superoxide dismutase Sod1 {ECO:0000313|EMBL:KPQ01989.1};
GN   Name=sod1 {ECO:0000313|EMBL:KPQ01989.1};
GN   ORFNames=HLUCCO02_04835 {ECO:0000313|EMBL:KPQ01989.1};
OS   Idiomarinaceae bacterium HL-53.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae.
OX   NCBI_TaxID=1298881 {ECO:0000313|EMBL:KPQ01989.1, ECO:0000313|Proteomes:UP000053932};
RN   [1] {ECO:0000313|EMBL:KPQ01989.1, ECO:0000313|Proteomes:UP000053932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-53 {ECO:0000313|EMBL:KPQ01989.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|ARBA:ARBA00001935};
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:KPQ01989.1}.
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DR   EMBL; LIHO01000012; KPQ01989.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7X6Z1; -.
DR   STRING; 1298881.Ga0003345_0822; -.
DR   OrthoDB; 5431326at2; -.
DR   Proteomes; UP000053932; 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; 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.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..184
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010259559"
FT   DOMAIN          50..178
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   184 AA;  19109 MW;  CEBB577B4EB2A1DB CRC64;
     MKIKVLTSAV LLSALTACGG AHNMDSDVTY EGPEKAIAYL HPTDGNEGMQ GYVVFQRADD
     GMDIMAHIEG LPGGSEHGFH VHEYGDCSAA DGTSAGGHFN PAQMPHGGPA YDERHVGDLG
     NVRADENGMA HHEAIDPHLT MSGENSILGR AVVVHAQQDD MSSQPTGNAG ARLLCGVIGV
     ANPG
//