Sulfide-quinone reductase

Details

Name
Sulfide-quinone reductase
Synonyms
  • 1.8.5.4
  • SQR
  • Sulfide:quinone oxidoreductase
Gene Name
Not Available
Organism
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)
Amino acid sequence
>lcl|BSEQ0017301|Sulfide-quinone reductase
MAHVVILGAGTGGMPAAYEMKEALGSGHEVTLISANDYFQFVPSNPWVGVGWKERDDIAF
PIRHYVERKGIHFIAQSAEQIDAEAQNITLADGNTVHYDYLMIATGPKLAFENVPGSDPH
EGPVQSICTVDHAERAFAEYQALLREPGPIVIGAMAGASCFGPAYEYAMIVASDLKKRGM
RDKIPSFTFITSEPYIGHLGIQGVGDSKGILTKGLKEEGIEAYTNCKVTKVEDNKMYVTQ
VDEKGETIKEMVLPVKFGMMIPAFKGVPAVAGVEGLCNPGGFVLVDEHQRSKKYANIFAA
GIAIAIPPVETTPVPTGAPKTGYMIESMVSAAVHNIKADLEGRKGEQTMGTWNAVCFADM
GDRGAAFIALPQLKPRKVDVFAYGRWVHLAKVAFEKYFIRKMKMGVSEPFYEKVLFKMMG
ITRLKEEDTHRKAS
Number of residues
434
Molecular Weight
47405.465
Theoretical pI
6.8
GO Classification
Functions
nucleotide binding / oxidoreductase activity / quinone binding
Components
membrane
General Function
Quinone binding
Specific Function
Catalyzes the oxidation of hydrogen sulfide, with the help of a quinone. Consecutive reaction cycles lead to the accumulation of a polysulfide product on the active site Cys residues; these products are released when they exceed a critical length, typically as cyclooctasulfur.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Membrane
Gene sequence
>lcl|BSEQ0017302|Sulfide-quinone reductase
ATGGCACATGTGGTAATTTTGGGTGCGGGCACAGGCGGAATGCCGGCGGCCTACGAAATG
AAGGAAGCTCTGGGTTCTGGGCATGAGGTGACGCTGATCAGCGCCAATGATTATTTCCAG
TTCGTTCCGTCCAACCCGTGGGTGGGGGTGGGCTGGAAGGAGCGCGATGATATCGCTTTC
CCAATCCGGCACTATGTGGAACGTAAAGGAATACATTTTATCGCGCAGTCCGCCGAACAG
ATCGATGCCGAAGCGCAGAATATCACCCTTGCCGACGGCAACACGGTACATTACGACTAC
CTGATGATCGCGACAGGTCCGAAGCTGGCTTTCGAGAATGTACCGGGTTCCGATCCCCAT
GAAGGCCCGGTGCAGTCCATTTGTACGGTGGACCATGCGGAACGGGCCTTTGCCGAATAC
CAGGCTTTGTTGCGCGAGCCCGGCCCCATTGTCATCGGTGCCATGGCCGGCGCAAGTTGC
TTCGGACCGGCTTACGAATATGCCATGATCGTCGCTTCCGACCTCAAAAAACGGGGCATG
CGCGACAAGATTCCGTCCTTCACCTTTATCACCAGTGAGCCCTACATCGGTCATCTGGGC
ATTCAGGGCGTGGGCGATTCCAAGGGCATTCTGACGAAGGGCCTCAAGGAAGAAGGTATC
GAAGCGTACACGAACTGTAAGGTCACCAAGGTCGAAGACAACAAGATGTATGTAACCCAG
GTGGACGAGAAGGGTGAAACCATCAAGGAGATGGTTCTGCCGGTCAAGTTCGGGATGATG
ATCCCGGCTTTCAAGGGCGTGCCAGCGGTGGCGGGTGTCGAAGGATTGTGCAATCCCGGT
GGCTTCGTGCTGGTGGATGAGCACCAGCGCAGCAAGAAATACGCAAATATCTTTGCGGCG
GGTATCGCCATCGCCATTCCGCCGGTAGAGACGACCCCGGTGCCGACCGGCGCGCCCAAG
ACCGGTTATATGATCGAATCCATGGTGTCGGCGGCGGTGCACAACATCAAGGCGGATCTG
GAAGGCCGCAAGGGCGAGCAGACCATGGGCACCTGGAATGCGGTGTGTTTTGCCGATATG
GGTGATCGCGGCGCGGCATTTATCGCCTTGCCCCAGTTGAAGCCCCGTAAAGTGGACGTC
TTTGCCTACGGGCGCTGGGTGCATCTGGCGAAGGTGGCCTTTGAAAAATACTTTATCCGC
AAAATGAAGATGGGTGTCTCCGAGCCCTTCTATGAGAAGGTGCTGTTCAAGATGATGGGC
ATTACCCGTCTGAAGGAAGAAGATACCCATCGTAAGGCCTCCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDB7JBP8
UniProtKB Entry NameSQRD_ACIF2
GenBank Protein ID218519790
GenBank Gene IDCP001219
General References
  1. Valdes J, Pedroso I, Quatrini R, Dodson RJ, Tettelin H, Blake R 2nd, Eisen JA, Holmes DS: Acidithiobacillus ferrooxidans metabolism: from genome sequence to industrial applications. BMC Genomics. 2008 Dec 11;9:597. doi: 10.1186/1471-2164-9-597. [Article]
  2. Cherney MM, Zhang Y, Solomonson M, Weiner JH, James MN: Crystal structure of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans: insights into sulfidotrophic respiration and detoxification. J Mol Biol. 2010 Apr 30;398(2):292-305. doi: 10.1016/j.jmb.2010.03.018. Epub 2010 Mar 19. [Article]
  3. Cherney MM, Zhang Y, James MN, Weiner JH: Structure-activity characterization of sulfide:quinone oxidoreductase variants. J Struct Biol. 2012 Jun;178(3):319-28. doi: 10.1016/j.jsb.2012.04.007. Epub 2012 Apr 19. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB076402-decyl-5,6-dimethoxy-3-methylcyclohexa-2,5-diene-1,4-dioneexperimentalunknownDetails