Sulfide-quinone reductase

Details

Name
Sulfide-quinone reductase
Synonyms
  • 1.8.5.4
  • SQR
  • Sulfide:quinone oxidoreductase
Gene Name
sqr
Organism
Aquifex aeolicus (strain VF5)
Amino acid sequence
>lcl|BSEQ0012804|Sulfide-quinone reductase
MAKHVVVIGGGVGGIATAYNLRNLMPDLKITLISDRPYFGFTPAFPHLAMGWRKFEDISV
PLAPLLPKFNIEFINEKAESIDPDANTVTTQSGKKIEYDYLVIATGPKLVFGAEGQEENS
TSICTAEHALETQKKLQELYANPGPVVIGAIPGVSCFGPAYEFALMLHYELKKRGIRYKV
PMTFITSEPYLGHFGVGGIGASKRLVEDLFAERNIDWIANVAVKAIEPDKVIYEDLNGNT
HEVPAKFTMFMPSFQGPEVVASAGDKVANPANKMVIVNRCFQNPTYKNIFGVGVVTAIPP
IEKTPIPTGVPKTGMMIEQMAMAVAHNIVNDIRNNPDKYAPRLSAICIADFGEDAGFFFA
DPVIPPRERVITKMGKWAHYFKTAFEKYFLWKVRNGNIAPSFEEKVLEIFLKVHPIELCK
DCEGAPGSRC
Number of residues
430
Molecular Weight
47448.675
Theoretical pI
6.99
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|BSEQ0012805|Sulfide-quinone reductase (sqr)
ATGGCTAAGCACGTTGTAGTAATAGGAGGAGGAGTAGGCGGTATAGCAACCGCTTACAAC
CTCAGGAACTTAATGCCCGACCTTAAGATCACCTTAATTTCCGACAGGCCTTACTTCGGA
TTTACCCCTGCGTTCCCCCACCTCGCAATGGGATGGAGGAAGTTTGAAGACATTTCCGTA
CCACTCGCACCGTTACTTCCCAAGTTCAACATCGAGTTTATAAACGAAAAAGCCGAATCC
ATTGACCCTGACGCAAACACCGTAACGACCCAGTCCGGCAAGAAGATTGAGTACGACTAC
CTCGTAATAGCTACAGGACCCAAGCTCGTTTTCGGCGCGGAAGGACAGGAAGAGAACTCT
ACCTCCATATGTACGGCTGAACACGCACTAGAAACTCAGAAGAAGCTCCAGGAACTTTAC
GCAAATCCCGGACCGGTCGTAATAGGTGCTATCCCCGGAGTTAGCTGTTTCGGACCGGCT
TACGAGTTCGCTTTAATGCTTCACTACGAACTCAAAAAGAGAGGGATAAGGTACAAGGTT
CCCATGACCTTCATTACCTCCGAACCCTACCTTGGACACTTTGGAGTTGGTGGTATAGGT
GCTTCAAAGAGACTGGTAGAGGACCTTTTCGCTGAAAGGAACATAGATTGGATTGCAAAC
GTAGCAGTCAAGGCTATAGAACCTGACAAGGTTATATACGAAGACCTGAACGGAAACACC
CACGAAGTCCCCGCCAAGTTTACCATGTTCATGCCCAGCTTCCAAGGACCTGAGGTAGTT
GCTTCCGCGGGAGACAAAGTGGCAAACCCCGCAAACAAGATGGTTATAGTTAACAGGTGC
TTCCAGAACCCCACTTACAAGAACATATTCGGAGTAGGTGTTGTAACGGCTATACCCCCT
ATAGAAAAGACGCCTATACCCACCGGCGTACCAAAGACGGGTATGATGATTGAGCAAATG
GCTATGGCTGTAGCTCACAACATAGTAAACGACATAAGGAACAACCCCGACAAGTACGCT
CCGAGACTTTCCGCCATATGTATAGCTGACTTCGGAGAAGACGCTGGATTTTTCTTCGCA
GACCCCGTAATACCTCCGAGGGAAAGAGTAATAACCAAGATGGGCAAGTGGGCACACTAC
TTCAAGACCGCGTTTGAAAAGTACTTCCTCTGGAAGGTCAGGAACGGAAACATCGCACCC
TCCTTTGAAGAAAAGGTACTCGAAATATTCCTCAAGGTTCACCCCATAGAACTTTGTAAG
GACTGCGAAGGAGCACCCGGAAGTAGGTGTTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDO67931
UniProtKB Entry NameSQRD_AQUAE
GenBank Protein ID2982776
GenBank Gene IDAE000657
General References
  1. Deckert G, Warren PV, Gaasterland T, Young WG, Lenox AL, Graham DE, Overbeek R, Snead MA, Keller M, Aujay M, Huber R, Feldman RA, Short JM, Olsen GJ, Swanson RV: The complete genome of the hyperthermophilic bacterium Aquifex aeolicus. Nature. 1998 Mar 26;392(6674):353-8. [Article]
  2. Nubel T, Klughammer C, Huber R, Hauska G, Schutz M: Sulfide:quinone oxidoreductase in membranes of the hyperthermophilic bacterium Aquifex aeolicus (VF5). Arch Microbiol. 2000 Apr;173(4):233-44. [Article]
  3. Marcia M, Ermler U, Peng G, Michel H: The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration. Proc Natl Acad Sci U S A. 2009 Jun 16;106(24):9625-30. doi: 10.1073/pnas.0904165106. Epub 2009 Jun 1. [Article]

Drug Relations

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