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Protein
Submitted name:

Chlorite dismutase

Gene

cld

Organism
Nitrospira defluvii
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi186 – 1861Iron (heme axial ligand); via tele nitrogenCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseImported

Keywords - Ligandi

HemeCombined sources, Iron, Metal-binding

Enzyme and pathway databases

BioCyciNDEF330214:GI4U-1369-MONOMER.
BRENDAi1.13.11.49. 9833.

Names & Taxonomyi

Protein namesi
Submitted name:
Chlorite dismutaseImported (EC:1.13.11.49Imported)
Gene namesi
Name:cldImported
Synonyms:cld1Imported
ORF Names:NIDE1387Imported
OrganismiNitrospira defluviiImported
Taxonomic identifieri330214 [NCBI]
Taxonomic lineageiBacteriaNitrospiraeNitrospiralesNitrospiraceaeNitrospira
Proteomesi
  • UP000001660 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Chaini27 – 264238Sequence analysisPRO_5007640445Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi330214.NIDE1387.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NN1X-ray1.85A/B/C/D/E27-264[»]
3NN2X-ray1.94A/B/C/D/E27-264[»]
3NN3X-ray2.60A/B/C/D/E27-264[»]
3NN4X-ray2.70A/B/C/D/E27-264[»]
4M05X-ray2.28A/B/C/D/E27-264[»]
4M06X-ray2.60A/B/C/D/E27-264[»]
4M07X-ray2.50A/B/C/D/E27-264[»]
4M08X-ray2.80A/B/C/D/E27-264[»]
4M09X-ray2.45A/B/C/D/E27-264[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

SignalSequence analysis

Phylogenomic databases

eggNOGiENOG4108VMV. Bacteria.
ENOG4111JF8. LUCA.
HOGENOMiHOG000068200.
KOiK09162.

Family and domain databases

InterProiIPR011008. Dimeric_a/b-barrel.
IPR010644. Put_peroxidase/dismutase.
[Graphical view]
PfamiPF06778. Chlor_dismutase. 1 hit.
[Graphical view]
SUPFAMiSSF54909. SSF54909. 1 hit.

Sequencei

Sequence statusi: Complete.

B3U4H7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNFRSAGRIA VLAGLLVLVA VWPAPAADRE KLLTESGVYG TFATFQMDHD
60 70 80 90 100
WWDLPGESRV ISVAEVKGLV EQWSGKILVE SYLLRGLSDH ADLMFRVHAR
110 120 130 140 150
TLSDTQQFLS AFMGTRLGRH LTSGGLLHGV SKKPTYVAGF PESMKTELQV
160 170 180 190 200
NGESGSRPYA IVIPIKKDAE WWALDQEART ALMQEHTQAA LPYLKTVKRK
210 220 230 240 250
LYHSTGLDDV DFITYFETER LEDFHNLVRA LQQVKEFRHN RRFGHPTLLG
260
TMSPLDEILE KFAQ
Length:264
Mass (Da):29,857
Last modified:September 2, 2008 - v1
Checksum:iDE679F294DF38032
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU559167 Genomic DNA. Translation: ACE75544.1.
FP929003 Genomic DNA. Translation: CBK41137.1.
RefSeqiWP_013247962.1. NC_014355.1.

Genome annotation databases

EnsemblBacteriaiCBK41137; CBK41137; NIDE1387.
KEGGinde:NIDE1387.
PATRICi42241857. VBICanNit28252_1323.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU559167 Genomic DNA. Translation: ACE75544.1.
FP929003 Genomic DNA. Translation: CBK41137.1.
RefSeqiWP_013247962.1. NC_014355.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NN1X-ray1.85A/B/C/D/E27-264[»]
3NN2X-ray1.94A/B/C/D/E27-264[»]
3NN3X-ray2.60A/B/C/D/E27-264[»]
3NN4X-ray2.70A/B/C/D/E27-264[»]
4M05X-ray2.28A/B/C/D/E27-264[»]
4M06X-ray2.60A/B/C/D/E27-264[»]
4M07X-ray2.50A/B/C/D/E27-264[»]
4M08X-ray2.80A/B/C/D/E27-264[»]
4M09X-ray2.45A/B/C/D/E27-264[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi330214.NIDE1387.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCBK41137; CBK41137; NIDE1387.
KEGGinde:NIDE1387.
PATRICi42241857. VBICanNit28252_1323.

Phylogenomic databases

eggNOGiENOG4108VMV. Bacteria.
ENOG4111JF8. LUCA.
HOGENOMiHOG000068200.
KOiK09162.

Enzyme and pathway databases

BioCyciNDEF330214:GI4U-1369-MONOMER.
BRENDAi1.13.11.49. 9833.

Family and domain databases

InterProiIPR011008. Dimeric_a/b-barrel.
IPR010644. Put_peroxidase/dismutase.
[Graphical view]
PfamiPF06778. Chlor_dismutase. 1 hit.
[Graphical view]
SUPFAMiSSF54909. SSF54909. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Environmental genomics reveals a functional chlorite dismutase in the nitrite-oxidizing bacterium 'Candidatus Nitrospira defluvii'."
    Maixner F., Wagner M., Lucker S., Pelletier E., Schmitz-Esser S., Hace K., Spieck E., Konrat R., Le Paslier D., Daims H.
    Environ. Microbiol. 10:3043-3056(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Structural and functional characterisation of the chlorite dismutase from the nitrite-oxidizing bacterium "Candidatus Nitrospira defluvii": identification of a catalytically important amino acid residue."
    Kostan J., Sjoblom B., Maixner F., Mlynek G., Furtmuller P.G., Obinger C., Wagner M., Daims H., Djinovic-Carugo K.
    J. Struct. Biol. 172:331-342(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 27-264 IN COMPLEX WITH HEME.
  3. "A Nitrospira metagenome illuminates the physiology and evolution of globally important nitrite-oxidizing bacteria."
    Lucker S., Wagner M., Maixner F., Pelletier E., Koch H., Vacherie B., Rattei T., Sinninghe Damste J., Spieck E., Le Paslier D., Daims H.
    Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2010)
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Itskovich V.B.
    Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  5. "Manipulating conserved heme cavity residues of chlorite dismutase: effect on structure, redox chemistry, and reactivity."
    Hofbauer S., Gysel K., Bellei M., Hagmuller A., Schaffner I., Mlynek G., Kostan J., Pirker K.F., Daims H., Furtmuller P.G., Battistuzzi G., Djinovic-Carugo K., Obinger C.
    Biochemistry 53:77-89(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 27-264 IN COMPLEX WITH HEME.

Entry informationi

Entry nameiB3U4H7_9BACT
AccessioniPrimary (citable) accession number: B3U4H7
Entry historyi
Integrated into UniProtKB/TrEMBL: September 2, 2008
Last sequence update: September 2, 2008
Last modified: July 6, 2016
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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 one 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.