Flavoprotein pyridine nucleotide cytochrome reductases

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FAD binding domain
Identifiers
SymbolFAD_binding_1
PfamPF00667
InterProIPR003097
SCOP21amo / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1ddiA:229-424 1ddgA:229-424 1f20A:985-1214

1tllB:985-1214 1ja1A:274-493 1ja0A:274-493 1j9zA:274-493 1amoA:274-493 2bf4B:261-481

2bn4A:261-481

Flavoprotein pyridine nucleotide cytochrome reductases[1] catalyse the interchange of reducing equivalents between one-electron carriers and the two-electron-carrying nicotinamide dinucleotides. The enzymes include ferredoxin-NADP+ reductases,[2] plant and fungal NAD(P)H:nitrate reductases,[1][3] cytochrome b5 reductases,[4] cytochrome P450 reductases,[5] sulphite reductases,[6] nitric oxide synthases,[7] phthalate dioxygenase reductase,[8] and various other flavoproteins.

Human proteins containing this domain[edit]

MTRR; NDOR1; NOS1; NOS2A; NOS3; NR1; POR;

References[edit]

  1. ^ a b Hyde GE, Crawford NM, Campbell WH (1991). "The sequence of squash NADH:nitrate reductase and its relationship to the sequences of other flavoprotein oxidoreductases. A family of flavoprotein pyridine nucleotide cytochrome reductases". J. Biol. Chem. 266 (35): 23542–23547. doi:10.1016/S0021-9258(18)54316-7. PMID 1748631.
  2. ^ Karplus PA, Bruns CM (1994). "Structure-function relations for ferredoxin reductase". J. Bioenerg. Biomembr. 26 (1): 89–99. doi:10.1007/BF00763221. PMID 8027025. S2CID 1004663.
  3. ^ Siverio JM (2002). "Assimilation of nitrate by yeasts". FEMS Microbiol. Rev. 26 (3): 277–284. doi:10.1111/j.1574-6976.2002.tb00615.x. PMID 12165428.
  4. ^ Iwanaga S, Miyata T, Yubisui T, Tamura M, Takeshita M (1986). "Complete amino acid sequence of NADH-cytochrome b5 reductase purified from human erythrocytes". J. Biochem. 99 (2): 407–422. doi:10.1093/oxfordjournals.jbchem.a135495. PMID 3700359.
  5. ^ Porter TD (1991). "An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals" (PDF). Trends Biochem. Sci. 16 (4): 154–158. doi:10.1016/0968-0004(91)90059-5. hdl:2027.42/29563. PMID 1908607.
  6. ^ Siegel LM, Ostrowski J, Rueger DC, Miller BE, Kredich NM, Barber MJ (1989). "Characterization of the flavoprotein moieties of NADPH-sulfite reductase from Salmonella typhimurium and Escherichia coli. Physicochemical and catalytic properties, amino acid sequence deduced from DNA sequence of cysJ, and comparison with NADPH-cytochrome P-450 reductase". J. Biol. Chem. 264 (27): 15796–15808. doi:10.1016/S0021-9258(18)71547-0. PMID 2550423.
  7. ^ Snyder SH, Reed RR, Bredt DS, Hwang PM, Glatt CE, Lowenstein C (1991). "Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase". Nature. 351 (6329): 714–718. Bibcode:1991Natur.351..714B. doi:10.1038/351714a0. PMID 1712077. S2CID 4356844.
  8. ^ Karplus PA, Bruns CM, Correll CC, Ludwig ML (1993). "Structural prototypes for an extended family of flavoprotein reductases: comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxin". Protein Sci. 2 (12): 2112–2133. doi:10.1002/pro.5560021212. PMC 2142325. PMID 8298460.
This article incorporates text from the public domain Pfam and InterPro: IPR003097
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