NADH peroxidase

Details

Name
NADH peroxidase
Synonyms
  • 1.11.1.1
  • NPXase
Gene Name
npr
Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
Amino acid sequence
>lcl|BSEQ0011848|NADH peroxidase
MKVIVLGSSHGGYEAVEELLNLHPDAEIQWYEKGDFISFLSCGMQLYLEGKVKDVNSVRY
MTGEKMESRGVNVFSNTEITAIQPKEHQVTVKDLVSGEERVENYDKLIISPGAVPFELDI
PGKDLDNIYLMRGRQWAIKLKQKTVDPEVNNVVVIGSGYIGIEAAEAFAKAGKKVTVIDI
LDRPLGVYLDKEFTDVLTEEMEANNITIATGETVERYEGDGRVQKIVTDKNAYDADLVVV
AVGVRPNTAWLKGTLELHPNGLIKTDEYMRTSEPDVFAVGDATLIKYNPADTEVNIALAT
NARKQGRFAVKNLEEPVKPFPGVQGSSGLAVFDYKFASTGINEVMAQKLGKETKAVTVVE
DYLMDFNPDKQKAWFKLVYDPETTQILGAQLMSKADLTANINAISLAIQAKMTIEDLAYA
DFFFQPAFDKPWNIINTAALEAVKQER
Number of residues
447
Molecular Weight
49565.17
Theoretical pI
4.56
GO Classification
Functions
flavin adenine dinucleotide binding / NADH peroxidase activity
Processes
cell redox homeostasis
Components
cell
General Function
Nadh peroxidase activity
Specific Function
Peroxidase whose active site is a redox-active cysteine-sulfenic acid.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0011849|NADH peroxidase (npr)
ATGAAAGTTATTGTTTTAGGATCATCACATGGAGGTTATGAAGCGGTAGAGGAATTACTA
AATCTTCATCCTGATGCAGAAATTCAATGGTATGAGAAAGGTGATTTTATCTCATTCTTG
TCTTGTGGCATGCAGTTGTACCTAGAAGGAAAAGTGAAAGATGTTAATTCTGTTCGCTAT
ATGACTGGCGAAAAAATGGAGAGCCGTGGTGTAAATGTCTTTTCTAATACTGAAATTACA
GCGATTCAACCAAAAGAACATCAAGTGACAGTGAAAGATTTAGTGTCAGGTGAAGAACGT
GTTGAAAATTATGATAAATTAATCATCAGTCCCGGAGCTGTCCCATTTGAATTAGATATT
CCAGGTAAAGATTTGGATAATATTTACTTGATGCGTGGTCGTCAATGGGCCATTAAATTA
AAACAAAAAACAGTAGATCCAGAAGTCAATAATGTGGTTGTGATTGGTAGTGGTTATATT
GGGATTGAAGCTGCCGAAGCATTTGCAAAAGCCGGCAAAAAGGTTACTGTTATTGACATT
TTAGATCGTCCATTAGGGGTATATCTAGATAAAGAATTTACAGATGTTTTAACAGAAGAG
ATGGAAGCTAATAATATTACCATTGCAACTGGTGAAACAGTTGAACGTTACGAAGGCGAC
GGTCGTGTGCAAAAAATCGTTACAGATAAAAATGCGTACGATGCTGATTTGGTCGTTGTA
GCGGTTGGTGTCCGTCCAAACACTGCTTGGTTAAAAGGTACCTTGGAATTACATCCGAAT
GGCCTAATCAAGACGGATGAATACATGCGGACAAGTGAGCCGGATGTATTTGCAGTAGGG
GATGCTACGTTAATTAAATACAATCCTGCAGACACAGAAGTAAATATTGCCTTAGCAACG
AATGCTCGTAAACAAGGTCGCTTTGCTGTGAAAAACCTAGAGGAACCAGTTAAACCTTTC
CCTGGTGTTCAAGGATCTTCTGGCTTGGCCGTCTTTGATTATAAATTTGCTTCAACAGGG
ATTAACGAAGTCATGGCTCAAAAATTAGGAAAAGAAACAAAAGCGGTGACAGTAGTAGAA
GACTACTTGATGGACTTTAATCCAGACAAACAAAAAGCTTGGTTTAAATTAGTGTATGAT
CCTGAAACAACACAAATTTTAGGCGCTCAATTAATGTCGAAAGCAGATTTAACTGCAAAC
ATTAATGCTATTTCATTAGCGATTCAAGCCAAAATGACGATTGAAGACTTAGCCTATGCG
GACTTCTTCTTCCAACCAGCGTTTGACAAACCTTGGAATATTATTAATACAGCGGCTTTA
GAAGCGGTGAAACAAGAACGTTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP37062
UniProtKB Entry NameNAPE_ENTFA
GenBank Gene IDX62755
General References
  1. Ross RP, Claiborne A: Cloning, sequence and overexpression of NADH peroxidase from Streptococcus faecalis 10C1. Structural relationship with the flavoprotein disulfide reductases. J Mol Biol. 1991 Oct 5;221(3):857-71. [PubMed:1719212]
  2. Paulsen IT, Banerjei L, Myers GS, Nelson KE, Seshadri R, Read TD, Fouts DE, Eisen JA, Gill SR, Heidelberg JF, Tettelin H, Dodson RJ, Umayam L, Brinkac L, Beanan M, Daugherty S, DeBoy RT, Durkin S, Kolonay J, Madupu R, Nelson W, Vamathevan J, Tran B, Upton J, Hansen T, Shetty J, Khouri H, Utterback T, Radune D, Ketchum KA, Dougherty BA, Fraser CM: Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis. Science. 2003 Mar 28;299(5615):2071-4. [PubMed:12663927]
  3. Poole LB, Claiborne A: The non-flavin redox center of the streptococcal NADH peroxidase. I. Thiol reactivity and redox behavior in the presence of urea. J Biol Chem. 1989 Jul 25;264(21):12322-9. [PubMed:2501302]
  4. Stehle T, Ahmed SA, Claiborne A, Schulz GE: Structure of NADH peroxidase from Streptococcus faecalis 10C1 refined at 2.16 A resolution. J Mol Biol. 1991 Oct 20;221(4):1325-44. [PubMed:1942054]
  5. Stehle T, Claiborne A, Schulz GE: NADH binding site and catalysis of NADH peroxidase. Eur J Biochem. 1993 Jan 15;211(1-2):221-6. [PubMed:8425532]
  6. Yeh JI, Claiborne A, Hol WG: Structure of the native cysteine-sulfenic acid redox center of enterococcal NADH peroxidase refined at 2.8 A resolution. Biochemistry. 1996 Aug 6;35(31):9951-7. [PubMed:8756456]
  7. Crane EJ 3rd, Vervoort J, Claiborne A: 13C NMR analysis of the cysteine-sulfenic acid redox center of enterococcal NADH peroxidase. Biochemistry. 1997 Jul 15;36(28):8611-8. [PubMed:9214307]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03147Flavin adenine dinucleotideapprovedunknownDetails
DB03382S-oxy-L-cysteineexperimentalunknownDetails