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Protein

Superoxide dismutase [Mn] 1

Gene

sodA1

Organism
Bacillus anthracis
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Mn2+By similarityNote: Binds 1 Mn2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi28 – 281ManganeseBy similarity
Metal bindingi83 – 831ManganeseBy similarity
Metal bindingi165 – 1651ManganeseBy similarity
Metal bindingi169 – 1691ManganeseBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciANTHRA:SODA-1-MONOMER.
BANT260799:GJAJ-4233-MONOMER.
BANT261594:GJ7F-4375-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Mn] 1 (EC:1.15.1.1)
Gene namesi
Name:sodA1
Synonyms:sodA-1
Ordered Locus Names:BA_4499, GBAA_4499, BAS4177
OrganismiBacillus anthracis
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000000594 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 203203Superoxide dismutase [Mn] 1PRO_0000160012Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi198094.BA_4499.

Structurei

Secondary structure

1
203
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni13 – 197Combined sources
Helixi22 – 309Combined sources
Helixi32 – 4413Combined sources
Helixi48 – 514Combined sources
Helixi55 – 606Combined sources
Helixi62 – 643Combined sources
Helixi67 – 8822Combined sources
Helixi100 – 11011Combined sources
Helixi113 – 12614Combined sources
Beta strandi129 – 13810Combined sources
Beta strandi141 – 1488Combined sources
Helixi153 – 1564Combined sources
Beta strandi159 – 1657Combined sources
Helixi168 – 1703Combined sources
Helixi172 – 1754Combined sources
Helixi179 – 1868Combined sources
Turni187 – 1893Combined sources
Helixi192 – 20110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XUQX-ray1.80A/B1-203[»]
ProteinModelPortaliQ81LW0.
SMRiQ81LW0. Positions 3-202.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ81LW0.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0605.
HOGENOMiHOG000013583.
KOiK04564.
OMAiFWEVIAP.
OrthoDBiEOG63NMNT.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000349. SODismutase. 1 hit.
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q81LW0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKHELPNLP YAYDALEPHF DKETMNIHHT KHHNTYITNL NAALEGHAEL
60 70 80 90 100
ADKSVEELVA NLNEVPEAIR TAVRNNGGGH ANHTFFWTIL SPNGGGQPVG
110 120 130 140 150
ELATAIEAKF GSFDAFKEEF AKAGATRFGS GWAWLVVNNG ELEVTSTPNQ
160 170 180 190 200
DSPLTEGKTP VIGLDVWEHA YYLNYQNRRP DYIGAFWNVV DWNAAEKRYQ

EAK
Length:203
Mass (Da):22,664
Last modified:June 1, 2003 - v1
Checksum:i61B0B7D44A090D97
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP28210.1.
AE017334 Genomic DNA. Translation: AAT33618.1.
AE017225 Genomic DNA. Translation: AAT56477.1.
RefSeqiNP_846724.1. NC_003997.3.
WP_001052031.1. NZ_KN050651.1.
YP_021143.1. NC_007530.2.
YP_030426.1. NC_005945.1.

Genome annotation databases

EnsemblBacteriaiAAP28210; AAP28210; BA_4499.
AAT33618; AAT33618; GBAA_4499.
AAT56477; AAT56477; BAS4177.
GeneIDi1088022.
23126014.
2851955.
KEGGiban:BA_4499.
bar:GBAA_4499.
bat:BAS4177.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP28210.1.
AE017334 Genomic DNA. Translation: AAT33618.1.
AE017225 Genomic DNA. Translation: AAT56477.1.
RefSeqiNP_846724.1. NC_003997.3.
WP_001052031.1. NZ_KN050651.1.
YP_021143.1. NC_007530.2.
YP_030426.1. NC_005945.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XUQX-ray1.80A/B1-203[»]
ProteinModelPortaliQ81LW0.
SMRiQ81LW0. Positions 3-202.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198094.BA_4499.

Protocols and materials databases

DNASUi1088022.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP28210; AAP28210; BA_4499.
AAT33618; AAT33618; GBAA_4499.
AAT56477; AAT56477; BAS4177.
GeneIDi1088022.
23126014.
2851955.
KEGGiban:BA_4499.
bar:GBAA_4499.
bat:BAS4177.

Phylogenomic databases

eggNOGiCOG0605.
HOGENOMiHOG000013583.
KOiK04564.
OMAiFWEVIAP.
OrthoDBiEOG63NMNT.

Enzyme and pathway databases

BioCyciANTHRA:SODA-1-MONOMER.
BANT260799:GJAJ-4233-MONOMER.
BANT261594:GJ7F-4375-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ81LW0.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000349. SODismutase. 1 hit.
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
    Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J.
    , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
    Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames / isolate Porton.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames ancestor.
  3. "Complete genome sequence of Bacillus anthracis Sterne."
    Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sterne.

Entry informationi

Entry nameiSODM1_BACAN
AccessioniPrimary (citable) accession number: Q81LW0
Secondary accession number(s): Q6HTB2, Q6KMK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: June 1, 2003
Last modified: June 24, 2015
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.