Summary: Oxidoreductase family, C-terminal alpha/beta domain
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Oxidoreductase family, C-terminal alpha/beta domain Provide feedback
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 EPMC:8994968
Internal database links
SCOOP: | GFO_IDH_MocA_C2 ox_reductase_C OxRdtase_C |
Similarity to PfamA using HHSearch: | GFO_IDH_MocA_C2 OxRdtase_C |
External database links
SCOP: | 1ofg |
This tab holds annotation information from the InterPro database.
InterPro entry IPR004104
In general, the Gfo/Idh/MocA protein family members are enzymes that catalyse various different chemical reactions such as oxidation and reduction of carbohydrates, oxidation of trans-dihydrodiols, reduction of biliverdin, and hydrolysation of glycosidic bonds. All the enzymes in this family utilise NAD(P) as a hydride donor or acceptor. However, despite the structural similarities, some member such as the transcriptional repressor Gal80p, does not have enzymatic activity [ PUBMED:26749496 ].
The Gfo/Idh/MocA protein family members consists of two main domains: an N-terminal dinucleotide-binding domain containing a typical Rossmann fold3 and a C-terminal alpha/beta-domain participating in substrate binding and oligomerisation. This entry represents the C-terminal domain [ PUBMED:26749496 ].
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan GADPH_aa-bio_dh (CL0139), which has the following description:
This clan contains the C terminal domains of dehydrogenase enzymes involved in the biosynthesis of arginine, aspartate and aspartate derived amino acids. It also contains the C terminal domain of GAPDH, a dehydrogenase involved in glycolysis and gluconeogenesis.
The clan contains the following 18 members:
AcetDehyd-dimer Asp_DH_C Biliv-reduc_cat DapB_C DAPDH_C DXP_redisom_C G6PD_C GFO_IDH_MocA_C GFO_IDH_MocA_C2 Gp_dh_C Homoserine_dh Inos-1-P_synth OpcA_G6PD_C ox_reductase_C Oxidoreduct_C OxRdtase_C Sacchrp_dh_C Semialdhyde_dhCAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...
View options
We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
Seed (20) |
Full (41850) |
Representative proteomes | UniProt (185446) |
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RP15 (4584) |
RP35 (19085) |
RP55 (42266) |
RP75 (72583) |
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Jalview | |||||||
HTML | |||||||
PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
Seed (20) |
Full (41850) |
Representative proteomes | UniProt (185446) |
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RP15 (4584) |
RP35 (19085) |
RP55 (42266) |
RP75 (72583) |
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Raw Stockholm | |||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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's seed alignment. 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 alignment.
Note: You can also download the data file for the tree.
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: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Bateman A |
Number in seed: | 20 |
Number in full: | 41850 |
Average length of the domain: | 206 aa |
Average identity of full alignment: | 15 % |
Average coverage of the sequence by the domain: | 56.14 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 220 | ||||||||||||
Family (HMM) version: | 20 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Selections
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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...
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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_C domain has been found. There are 348 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.