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Chlorite dismutase (EC 1.13.11.49)

 B3U4H7_9BACT            Unreviewed;       264 AA.
B3U4H7;
02-SEP-2008, integrated into UniProtKB/TrEMBL.
02-SEP-2008, sequence version 1.
28-FEB-2018, entry version 56.
SubName: Full=Chlorite dismutase {ECO:0000313|EMBL:ACE75544.1};
EC=1.13.11.49 {ECO:0000313|EMBL:ACE75544.1};
Name=cld {ECO:0000313|EMBL:ACE75544.1};
Synonyms=cld1 {ECO:0000313|EMBL:CBK41137.1};
ORFNames=NIDE1387 {ECO:0000313|EMBL:CBK41137.1};
Nitrospira defluvii.
Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Nitrospira.
NCBI_TaxID=330214 {ECO:0000313|EMBL:ACE75544.1};
[1] {ECO:0000313|EMBL:ACE75544.1}
NUCLEOTIDE SEQUENCE.
PubMed=18459973; DOI=10.1111/j.1462-2920.2008.01646.x;
Maixner F., Wagner M., Lucker S., Pelletier E., Schmitz-Esser S.,
Hace K., Spieck E., Konrat R., Le Paslier D., Daims H.;
"Environmental genomics reveals a functional chlorite dismutase in the
nitrite-oxidizing bacterium 'Candidatus Nitrospira defluvii'.";
Environ. Microbiol. 10:3043-3056(2008).
[2] {ECO:0000213|PDB:3NN1, ECO:0000213|PDB:3NN2, ECO:0000213|PDB:3NN3}
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 27-264 IN COMPLEX WITH HEME.
PubMed=20600954; DOI=10.1016/j.jsb.2010.06.014;
Kostan J., Sjoblom B., Maixner F., Mlynek G., Furtmuller P.G.,
Obinger C., Wagner M., Daims H., Djinovic-Carugo K.;
"Structural and functional characterisation of the chlorite dismutase
from the nitrite-oxidizing bacterium "Candidatus Nitrospira defluvii":
identification of a catalytically important amino acid residue.";
J. Struct. Biol. 172:331-342(2010).
[3] {ECO:0000313|EMBL:CBK41137.1, ECO:0000313|Proteomes:UP000001660}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.1003860107;
Lucker S., Wagner M., Maixner F., Pelletier E., Koch H., Vacherie B.,
Rattei T., Sinninghe Damste J., Spieck E., Le Paslier D., Daims H.;
"A Nitrospira metagenome illuminates the physiology and evolution of
globally important nitrite-oxidizing bacteria.";
Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2010).
[4] {ECO:0000313|EMBL:CBK41137.1}
NUCLEOTIDE SEQUENCE.
Itskovich V.B.;
Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000213|PDB:4M05, ECO:0000213|PDB:4M06, ECO:0000213|PDB:4M07}
X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 27-264 IN COMPLEX WITH HEME.
PubMed=24364531; DOI=10.1021/bi401042z;
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.;
"Manipulating conserved heme cavity residues of chlorite dismutase:
effect on structure, redox chemistry, and reactivity.";
Biochemistry 53:77-89(2014).
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EMBL; EU559167; ACE75544.1; -; Genomic_DNA.
EMBL; FP929003; CBK41137.1; -; Genomic_DNA.
RefSeq; WP_013247962.1; NC_014355.1.
PDB; 3NN1; X-ray; 1.85 A; A/B/C/D/E=27-264.
PDB; 3NN2; X-ray; 1.94 A; A/B/C/D/E=27-264.
PDB; 3NN3; X-ray; 2.60 A; A/B/C/D/E=27-264.
PDB; 3NN4; X-ray; 2.70 A; A/B/C/D/E=27-264.
PDB; 4M05; X-ray; 2.28 A; A/B/C/D/E=27-264.
PDB; 4M06; X-ray; 2.60 A; A/B/C/D/E=27-264.
PDB; 4M07; X-ray; 2.50 A; A/B/C/D/E=27-264.
PDB; 4M08; X-ray; 2.80 A; A/B/C/D/E=27-264.
PDB; 4M09; X-ray; 2.45 A; A/B/C/D/E=27-264.
PDBsum; 3NN1; -.
PDBsum; 3NN2; -.
PDBsum; 3NN3; -.
PDBsum; 3NN4; -.
PDBsum; 4M05; -.
PDBsum; 4M06; -.
PDBsum; 4M07; -.
PDBsum; 4M08; -.
PDBsum; 4M09; -.
SMR; B3U4H7; -.
STRING; 330214.NIDE1387; -.
EnsemblBacteria; CBK41137; CBK41137; NIDE1387.
KEGG; nde:NIDE1387; -.
eggNOG; ENOG4108VMV; Bacteria.
eggNOG; ENOG4111JF8; LUCA.
HOGENOM; HOG000068200; -.
KO; K09162; -.
OrthoDB; POG091H16SJ; -.
BioCyc; CNIT330214:G1GVO-1292-MONOMER; -.
BRENDA; 1.13.11.49; 9833.
Proteomes; UP000001660; Chromosome.
GO; GO:0050587; F:chlorite O2-lyase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
InterPro; IPR011008; Dimeric_a/b-barrel.
InterPro; IPR010644; Put_peroxidase/dismutase.
PANTHER; PTHR36843; PTHR36843; 1.
Pfam; PF06778; Chlor_dismutase; 1.
SUPFAM; SSF54909; SSF54909; 1.
1: Evidence at protein level;
3D-structure {ECO:0000213|PDB:3NN1, ECO:0000213|PDB:3NN2,
ECO:0000213|PDB:3NN3, ECO:0000213|PDB:3NN4};
Complete proteome {ECO:0000313|Proteomes:UP000001660};
Heme {ECO:0000213|PDB:3NN1, ECO:0000213|PDB:3NN2,
ECO:0000213|PDB:3NN3, ECO:0000213|PDB:3NN4};
Iron {ECO:0000213|PDB:3NN1, ECO:0000213|PDB:3NN2,
ECO:0000213|PDB:3NN3, ECO:0000213|PDB:3NN4};
Metal-binding {ECO:0000213|PDB:3NN1, ECO:0000213|PDB:3NN2,
ECO:0000213|PDB:3NN3, ECO:0000213|PDB:3NN4};
Oxidoreductase {ECO:0000313|EMBL:ACE75544.1};
Reference proteome {ECO:0000313|Proteomes:UP000001660};
Signal {ECO:0000256|SAM:SignalP}.
SIGNAL 1 26 {ECO:0000256|SAM:SignalP}.
CHAIN 27 264 {ECO:0000256|SAM:SignalP}.
/FTId=PRO_5010824435.
METAL 186 186 Iron (heme axial ligand); via tele
nitrogen. {ECO:0000213|PDB:3NN1,
ECO:0000213|PDB:3NN2,
ECO:0000213|PDB:3NN3}.
SEQUENCE 264 AA; 29857 MW; DE679F294DF38032 CRC64;
MNFRSAGRIA VLAGLLVLVA VWPAPAADRE KLLTESGVYG TFATFQMDHD WWDLPGESRV
ISVAEVKGLV EQWSGKILVE SYLLRGLSDH ADLMFRVHAR TLSDTQQFLS AFMGTRLGRH
LTSGGLLHGV SKKPTYVAGF PESMKTELQV NGESGSRPYA IVIPIKKDAE WWALDQEART
ALMQEHTQAA LPYLKTVKRK LYHSTGLDDV DFITYFETER LEDFHNLVRA LQQVKEFRHN
RRFGHPTLLG TMSPLDEILE KFAQ


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