Summary: Sulphur oxygenase reductase
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Sulphur oxygenase reductase Provide feedback
The sulphur oxygenase/reductase (SOR) of the thermo-acidophilic archaeon Acidianus ambivalens is an unusual enzyme consisting of 24 identical subunits arranged in a perfectly symmetrical hollow sphere and containing a mononuclear non-heme iron centre (personal communication: A. Kletzin). At 85 degrees C in vitro, elemental sulphur is oxidised to sulphite, thiosulphate and hydrogen sulphide with no external cofactors needed. The proposed equation is: 4S + O2 + 4 H2O ---> 2 HSO3- + 2 H2S + 2 H+.
Kletzin A; , J Bacteriol 1989;171:1638-1643.: Coupled enzymatic production of sulfite, thiosulfate, and hydrogen sulfide from sulfur: purification and properties of a sulfur oxygenase reductase from the facultatively anaerobic archaebacterium Desulfurolobus ambivalens. PUBMED:2493451 EPMC:2493451
He Z, Li Y, Zhou P, Liu S; , FEMS Microbiol Lett 2000;193:217-221.: Cloning and heterologous expression of a sulfur oxygenase/reductase gene from the thermoacidophilic archaeon Acidianus sp. S5 in Escherichia coli. PUBMED:11111027 EPMC:11111027
Sun CW, Chen ZW, He ZG, Zhou PJ, Liu SJ; , Extremophiles 2003;7:131-134.: Purification and properties of the sulfur oxygenase/reductase from the acidothermophilic archaeon, Acidianus strain S5. PUBMED:12664265 EPMC:12664265
Urich T, Bandeiras TM, Leal SS, Rachel R, Albrecht T, Zimmermann P, Scholz C, Teixeira M, Gomes CM, Kletzin A; , Biochem J 2004; [Epub ahead of print]: The sulphur oxygenase reductase from Acidianus ambivalens is a multimeric protein containing a low-potential mononuclear non-haem iron centre. PUBMED:15030315 EPMC:15030315
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This tab holds annotation information from the InterPro database.
InterPro entry IPR011661
The crystal structure of the sulphur oxygenase/reductase (SOR) of the thermo-acidophilic archaeon Acidianus ambivalens has been determined to 1.7-A resolution [PUBMED:16484493]. Twenty-four monomers form a large hollow sphere enclosing a positively charged nanocompartment. Apolar channels provide access for linear sulphur species. A cysteine persulphide and a low-potential mononuclear non-heme iron site ligated by a 2-His-1-carboxylate facial triad in a pocket of each subunit constitute the active sites, accessible from the inside of the sphere. The iron is likely the site of both sulphur oxidation and sulphur reduction.
At 85 degrees C in vitro, elemental sulphur is oxidised to sulphite, thiosulphate and hydrogen sulphide with no external cofactors needed. The proposed equation is: 4S + O2 + 4 H2O ---> 2 HSO3- + 2 H2S + 2 H+.
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This superfamily of proteins possess a Ferredoxin-like fold. Pairs of these assemble into a beta barrel. The function of this barrel is quite varied and includes Muconolactone isomerase as well as monooxygenases.
The clan contains the following 18 members:ABM AsnC_trans_reg Chlor_dismutase Dabb Dehydratase_hem DUF1330 DUF1428 DUF3291 DUF4188 DUF718 Dyp_perox EthD MIase MmlI NapD NIPSNAP SOR YCII
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Curation and family details
|Author:||Kletzin A, Studholme DJ|
|Number in seed:||10|
|Number in full:||29|
|Average length of the domain:||273.70 aa|
|Average identity of full alignment:||51 %|
|Average coverage of the sequence by the domain:||94.49 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||7|
|Download:||download the raw HMM for this family|
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