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Database: UniProt
Entry: P43725
LinkDB: P43725
Original site: P43725 
ID   SODM_HAEIN              Reviewed;         215 AA.
AC   P43725;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   05-DEC-2018, entry version 119.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sodA; OrderedLocusNames=HI_1088;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Eagan / Serotype B;
RX   PubMed=7934846; DOI=10.1111/j.1365-2958.1993.tb00954.x;
RA   Kroll J.S., Langford P.R., Saah J.R., Loynds B.M.;
RT   "Molecular and genetic characterization of superoxide dismutase in
RT   Haemophilus influenzae type b.";
RL   Mol. Microbiol. 10:839-848(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M.,
RA   Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA   Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA   Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA   Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA   Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-6.
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=10675023;
RX   DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4;
RA   Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B.,
RA   Gray C., Fountoulakis M.;
RT   "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL   Electrophoresis 21:411-429(2000).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; X73832; CAA52054.1; -; Genomic_DNA.
DR   EMBL; L42023; AAC22745.1; -; Genomic_DNA.
DR   PIR; C64182; C64182.
DR   PIR; S39871; S39871.
DR   RefSeq; NP_439245.1; NC_000907.1.
DR   RefSeq; WP_005693413.1; NC_000907.1.
DR   ProteinModelPortal; P43725; -.
DR   SMR; P43725; -.
DR   STRING; 71421.HI1088; -.
DR   EnsemblBacteria; AAC22745; AAC22745; HI_1088.
DR   GeneID; 950093; -.
DR   KEGG; hin:HI1088; -.
DR   PATRIC; fig|71421.8.peg.1133; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; YEGWKGE; -.
DR   PhylomeDB; P43725; -.
DR   BioCyc; HINF71421:G1GJ1-1123-MONOMER; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 1.
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   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Manganese;
KW   Metal-binding; Oxidoreductase; Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:10675023}.
FT   CHAIN         2    215       Superoxide dismutase [Mn].
FT                                /FTId=PRO_0000160038.
FT   METAL        27     27       Manganese. {ECO:0000250}.
FT   METAL        83     83       Manganese. {ECO:0000250}.
FT   METAL       170    170       Manganese. {ECO:0000250}.
FT   METAL       174    174       Manganese. {ECO:0000250}.
FT   CONFLICT    208    215       TAHSNCAK -> STL (in Ref. 1).
FT                                {ECO:0000305}.
SQ   SEQUENCE   215 AA;  24110 MW;  80FAC9F1C0D59D25 CRC64;
     MSYTLPELGY AYNALEPHFD AQTMEIHHSK HHQAYVNNAN AALEGLPAEL VEMYPGHLIS
     NLDKIPAEKR GALRNNAGGH TNHSLFWKSL KKGTTLQGAL KDAIERDFGS VDAFKAEFEK
     AAATRFGSGW AWLVLTAEGK LAVVSTANQD NPLMGKEVAG CEGFPLLGLD VWEHAYYLKF
     QNRRPDYIKE FWNVVNWDFV AERFEQKTAH SNCAK
//
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