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Database: UniProt/TrEMBL
Entry: A0A0H4W3H4_9BORD
LinkDB: A0A0H4W3H4_9BORD
Original site: A0A0H4W3H4_9BORD 
ID   A0A0H4W3H4_9BORD        Unreviewed;       203 AA.
AC   A0A0H4W3H4;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   22-NOV-2017, entry version 17.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodB_1 {ECO:0000313|EMBL:AKQ55349.1};
GN   ORFNames=ACR54_02032 {ECO:0000313|EMBL:AKQ55349.1};
OS   Bordetella hinzii.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=103855 {ECO:0000313|EMBL:AKQ55349.1, ECO:0000313|Proteomes:UP000036382};
RN   [1] {ECO:0000313|Proteomes:UP000036382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F582 {ECO:0000313|Proteomes:UP000036382};
RA   Weigand M.R., Changayil S., Kulasekarapandian Y., Batra D.,
RA   Williams M.M., Tondella M.L.;
RT   "Complete Genome Sequences of Two Bordetella hinzii Isolated from
RT   Humans.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; CP012076; AKQ55349.1; -; Genomic_DNA.
DR   RefSeq; WP_029580616.1; NZ_LT906461.1.
DR   EnsemblBacteria; AKQ55349; AKQ55349; ACR54_02032.
DR   GeneID; 29513416; -.
DR   KEGG; bhz:ACR54_02032; -.
DR   PATRIC; fig|103855.14.peg.1960; -.
DR   KO; K04564; -.
DR   Proteomes; UP000036382; 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   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
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:UP000036382};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AKQ55349.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036382}.
FT   DOMAIN        2     89       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       96    197       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        81     81       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       168    168       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   203 AA;  22942 MW;  83344F022C7F255B CRC64;
     MAYTLPPLPY AYDALEPHID AQTMEIHYTR HHQTYINNLN AALQSRGLSF PPVETLLADI
     DRLPQDIRAA VRNNGGGHAN HSLFWDIMSP RGGGRPQGRL AASIDAELGG LDRFKEQFTQ
     AALTRFGSGW AWLCVTPRKT LLVQSSANQD SPLMEGHTPI LGLDVWEHAY YLKYQNRRPD
     YIAAFYEVIH WPEVARRYEA ALA
//
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