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Database: UniProt/TrEMBL
Entry: A0A127H1M5_9GAMM
LinkDB: A0A127H1M5_9GAMM
Original site: A0A127H1M5_9GAMM 
ID   A0A127H1M5_9GAMM        Unreviewed;       209 AA.
AC   A0A127H1M5;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   07-JUN-2017, entry version 7.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=AK825_12675 {ECO:0000313|EMBL:AMN68436.1};
OS   Psychrobacter sp. P11G5.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Psychrobacter.
OX   NCBI_TaxID=1699624 {ECO:0000313|EMBL:AMN68436.1};
RN   [1] {ECO:0000313|EMBL:AMN68436.1, ECO:0000313|Proteomes:UP000073122}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P11G5 {ECO:0000313|EMBL:AMN68436.1,
RC   ECO:0000313|Proteomes:UP000073122};
RX   PubMed=26879123; DOI=10.1186/s12864-016-2445-4;
RA   Moghadam M.S., Albersmeier A., Winkler A., Cimmino L., Rise K.,
RA   Hohmann-Marriott M.F., Kalinowski J., Ruckert C., Wentzel A., Lale R.;
RT   "Isolation and genome sequencing of four Arctic marine Psychrobacter
RT   strains exhibiting multicopper oxidase activity.";
RL   BMC Genomics 17:117-117(2016).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; CP012533; AMN68436.1; -; Genomic_DNA.
DR   RefSeq; WP_068038098.1; NZ_CP012533.1.
DR   EnsemblBacteria; AMN68436; AMN68436; AK825_12675.
DR   KEGG; psyg:AK825_12675; -.
DR   PATRIC; fig|1699624.3.peg.2621; -.
DR   KO; K04564; -.
DR   Proteomes; UP000073122; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019833; Mn/Fe_SOD_BS.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000073122};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        5     87       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       96    198       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        80     80       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       165    165       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       169    169       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   209 AA;  23535 MW;  230B93F9682D132E CRC64;
     MSKITLPDLP YAKDALEPHI SAETLEYHHD KHHAAYVNKL NDLLPGSGLE DKTLPEIIEA
     TSKDDSKQGM FNQAAQVWNH TFYWNCMTPD NGGGEPTGDL KAKIEEDFGS YDKFREEFKN
     AALTQFGSGW AWLVADKEGG KLSIAKTANA DTPLAHGQVA VLTCDVWEHA YYIDYRNRRP
     DYVDTFLDKL VNWDYANAKY KGQDAGVEE
//
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