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Database: UniProt
Entry: A0A419W6M5_9BACT
LinkDB: A0A419W6M5_9BACT
Original site: A0A419W6M5_9BACT 
ID   A0A419W6M5_9BACT        Unreviewed;       199 AA.
AC   A0A419W6M5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Cu-Zn family superoxide dismutase {ECO:0000313|EMBL:RKD91080.1};
GN   ORFNames=BC643_1429 {ECO:0000313|EMBL:RKD91080.1};
OS   Mangrovibacterium diazotrophicum.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC   Mangrovibacterium.
OX   NCBI_TaxID=1261403 {ECO:0000313|EMBL:RKD91080.1, ECO:0000313|Proteomes:UP000283387};
RN   [1] {ECO:0000313|EMBL:RKD91080.1, ECO:0000313|Proteomes:UP000283387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27148 {ECO:0000313|EMBL:RKD91080.1,
RC   ECO:0000313|Proteomes:UP000283387};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (SEP-2018) 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:RKD91080.1}.
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DR   EMBL; RAPN01000001; RKD91080.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A419W6M5; -.
DR   Proteomes; UP000283387; 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   Reference proteome {ECO:0000313|Proteomes:UP000283387};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..199
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019255532"
FT   DOMAIN          66..194
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   199 AA;  20670 MW;  6069B4BAD81D2A89 CRC64;
     MNNRRLVKLS FWGTMLLLVA QACTSGTKPA DHDHDMVMHD KVMPAPADNG VEKAICVLQP
     TEGNTVSGTV TFTKTDGGVV VKAEVSGLTP GKHGFHIHQF GDLTAPDGTS AGGHFNPEGH
     DHGAPTGEMR HVGDLGNLEA NAEGVAIYEV TYPSMTFAGP ESILGRGIIV HADEDDLVSQ
     PTGAAGARVA IGVIGVAKQ
//
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