Summary
FAD/NAD(P)-binding Rossmann fold Superfamily
A class of redox enzymes are two domain proteins. One domain, termed the catalytic domain, confers substrate specificity and the precise reaction of the enzyme. The other domain, which is common to this class of redox enzymes, is a Rossmann-fold domain. The Rossmann domain binds nicotinamide adenine dinucleotide (NAD+) and it is this cofactor that reversibly accepts a hydride ion, which is lost or gained by the substrate in the redox reaction. Rossmann domains have an alpha/beta fold, which has a central beta sheet, with approximately five alpha helices found surrounding the beta sheet.The strands forming the beta sheet are found in the following characteristic order 654123. The inter sheet crossover of the stands in the sheet form the NAD+ binding site [1]. In some more distantly relate Rossmann domains the NAD+ cofactor is replaced by the functionally similar cofactor FAD.
This clan contains 148 families and the total number of domains in the clan is 362090.
Literature references
- Bashton M, Chothia C; , J Mol Biol 2002;315:927-939.: The geometry of domain combination in proteins. 11812158
Members
This clan contains the following 148 member families:
2-Hacid_dh_C 3Beta_HSD 3HCDH_N adh_short ADH_zinc_N AdoHcyase_NAD AdoMet_MTase AlaDh_PNT_C Amino_oxidase ApbA Bac_GDH Bin3 CheR CMAS CmcI CoA_binding Cons_hypoth95 DAO DapB_N DFP DNA_circ_N DNA_methylase DOT1 DREV DUF1442 DUF166 DUF1776 DUF185 DUF2431 DUF248 DUF268 DUF3321 DUF43 DUF519 DUF548 DUF574 DUF633 DUF752 DUF938 DXP_redisom_C DXP_reductoisom Eco57I ELFV_dehydrog Eno-Rase_FAD_bd Eno-Rase_NADH_b Enoyl_reductase Epimerase F420_oxidored FAD_binding_2 FAD_binding_3 Fibrillarin FMO-like FmrO FtsJ G6PD_N GCD14 GDI GFO_IDH_MocA GIDA GidB GLF Glyco_hydro_4 GMC_oxred_N Gp_dh_N GRDA HI0933_like HIM1 Hydrolase_5 Hydroxy-O-Methy IlvN KR LCM Ldh_1_N Lycopene_cycl Malic_M Mannitol_dh Met_10 Methyltrans_SAM Methyltransf_10 Methyltransf_11 Methyltransf_12 Methyltransf_15 Methyltransf_16 Methyltransf_2 Methyltransf_3 Methyltransf_4 Methyltransf_5 Methyltransf_8 Methyltransf_9 MethyltransfD12 MetW Mg-por_mtran_C Mqo MT-A70 MTS Mur_ligase N2227 N6-adenineMlase N6_Mtase N6_N4_Mtase NAD_binding_2 NAD_binding_3 NAD_binding_4 NAD_binding_5 NAD_Gly3P_dh_N NAS NmrA NNMT_PNMT_TEMT NodS Nol1_Nop2_Fmu NSP13 OCD_Mu_crystall PARP_regulatory PCMT PDH Polysacc_synt_2 Pox_MCEL Prenylcys_lyase PrmA PRMT5 Pyr_redox Pyr_redox_2 RmlD_sub_bind Rossmann-like rRNA_methylase RrnaAD Rsm22 Saccharop_dh SE Semialdhyde_dh Shikimate_DH Spermine_synth Strep_67kDa_ant TehB THF_DHG_CYH_C Thi4 ThiF TPMT TrkA_N TRM TRM13 tRNA_U5-meth_tr Trp_halogenase Ubie_methyltran UDPG_MGDP_dh_N UPF0020 UPF0146 V_cholerae_RfbTExternal database links
| CATH: | 3.40.50.1320 |
| SCOP: | 51734 |
Domain organisation
Below is a listing of the unique domain organisations or architectures from this clan. More...
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Alignments
The table below shows the number of occurrences of each domain throughout the sequence database. More...
Please note: Clan alignments can be very large and can cause problems for some browsers. Read the note above before viewing.
Family relationships
This diagram shows the relationships between members of this clan. More...
Species distribution
Tree controls
HideThis tree shows the occurrence of the domains in this clan across different species. More...
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Interactions
There are 171 interactions for this clan. More...
Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD group, to allow us to map Pfam domains onto UniProt three-dimensional structures. The table below shows the mapping between the Pfam families in this clan, the corresponding UniProt entries, and the region of the three-dimensional structures that are available for that sequence.
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