Summary
Oxidoreductase family, NAD-binding Rossmann fold
This family of enzymes utilise NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.
Literature references
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Kingston RL, Scopes RK, Baker EN; , Structure 1996;4:1413-1428.: The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP. PUBMED:8994968
InterPro entry IPR000683
This group of enzymes utilise NADP or NAD, and is known as the GFO/IDH/MOCA family in UniProtKB/Swiss-Prot. GFO is a glucose--fructose oxidoreductase, which converts D-glucose and D-fructose into D-gluconolactone and D-glucitol in the sorbitol-gluconate pathway. MOCA is a rhizopine catabolism protein which may catalyse the NADH-dependent dehydrogenase reaction involved in rhizopine catabolism. Other proteins belonging to this family include Gal80, a negative regulator for the expression of lactose and galactose metabolic genes; and several hypothetical proteins from yeast, Escherichia coli and Bacillus subtilis.
The oxidoreductase, N-terminal domain is almost always associated with the oxidoreductase, C-terminal domain (see ).
Clan
This family is a member of clan NADP_Rossmann (CL0063), which contains the following 148 members:
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_RfbTGene Ontology
| Molecular function | oxidoreductase activity (GO:0016491) |
External database links
| HOMSTRAD: | GFO_IDH_MocA GFO_IDH_MocA_NC |
| PANDIT: | PF01408 |
| SCOP: | 1ofg |
| SYSTERS: | GFO_IDH_MocA |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
View options
Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Pfam-B_342 (release 3.0) |
| Previous IDs: | none |
| Type: | Family |
| Author: | Bateman A, Griffiths-Jones SR |
| Number in seed: | 54 |
| Number in full: | 7416 |
| Average length of the domain: | 120.60 aa |
| Average identity of full alignment: | 23 % |
| Average coverage of the sequence by the domain: | 32.97 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
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| Model details: |
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| Model length: | 120 | ||||||||||||
| Family (HMM) version: | 15 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
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Interactions
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 PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the GFO_IDH_MocA domain has been found.
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