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
- Functionsflavin adenine dinucleotide binding / NADH peroxidase activityProcessescell redox homeostasisComponentscell
- 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
Resource Link UniProtKB ID P37062 UniProtKB Entry Name NAPE_ENTFA GenBank Gene ID X62755 - General References
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]