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961  structures 8904  species 0  interactions 127668  sequences 741  architectures

Family: Aminotran_1_2 (PF00155)

Summary: Aminotransferase class I and II

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Transaminase". More...

Transaminase Edit Wikipedia article

In biochemistry, a transaminase or an aminotransferase in an enzyme that catalyzes a type of reaction between an amino acid and an α-keto acid. Specifically, this reaction (transamination) involves removing the amino group from the amino acid, leaving behind an α-keto acid, and transferring it to the reactant αketo acid, converting it into an amino acid. The enzymes are important in the production of various amino acids, and measuring the concentrations of various transaminases in the blood is important in the diagnosing and tracking many diseases.

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Aminotransferase class I and II Provide feedback

No Pfam abstract.

Literature references

  1. Nakai T, Okada K, Akutsu S, Miyahara I, Kawaguchi S, Kato R, Kuramitsu S, Hirotsu K; , Biochemistry 1999;38:2413-2424.: Structure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate. PUBMED:10029535 EPMC:10029535

  2. Ko TP, Wu SP, Yang WZ, Tsai H, Yuan HS; , Acta Crystallogr D Biol Crystallogr 1999;55:1474-1477.: Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase. PUBMED:10417420 EPMC:10417420


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR004839

Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped [ PUBMED:1990006 ] into class I and class II. This entry includes proteins from both subfamilies.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

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 PLP_aminotran (CL0061), which has the following description:

This superfamily contains a variety of PLP-dependent enzymes.

The clan contains the following 16 members:

Alliinase_C Aminotran_1_2 Aminotran_3 Aminotran_5 Asp_aminotransf Beta_elim_lyase ComK Cys_Met_Meta_PP DegT_DnrJ_EryC1 GDC-P Met_gamma_lyase OKR_DC_1 Pyridoxal_deC SelA SepSecS SHMT

Alignments

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
(48)
Full
(127668)
Representative proteomes UniProt
(548488)
RP15
(16257)
RP35
(57649)
RP55
(123519)
RP75
(214787)
Jalview View  View  View  View  View  View  View 
HTML View             
PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(48)
Full
(127668)
Representative proteomes UniProt
(548488)
RP15
(16257)
RP35
(57649)
RP55
(123519)
RP75
(214787)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

Download options

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
(48)
Full
(127668)
Representative proteomes UniProt
(548488)
RP15
(16257)
RP35
(57649)
RP55
(123519)
RP75
(214787)
Raw Stockholm Download     Download   Download        
Gzipped Download     Download   Download        

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 View help on the curation process

Seed source: Prosite
Previous IDs: aminotran_1; aminotran_1_2;
Type: Domain
Sequence Ontology: SO:0000417
Author: Sonnhammer ELL , Griffiths-Jones SR
Number in seed: 48
Number in full: 127668
Average length of the domain: 338.8 aa
Average identity of full alignment: 17 %
Average coverage of the sequence by the domain: 80.02 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 19.7 19.7
Trusted cut-off 19.7 19.7
Noise cut-off 19.6 19.6
Model length: 363
Family (HMM) version: 24
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

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 Aminotran_1_2 domain has been found. There are 961 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.

Protein Predicted structure External Information
A0A044R6D4 View 3D Structure Click here
A0A044S7G0 View 3D Structure Click here
A0A044SWQ6 View 3D Structure Click here
A0A044UKQ0 View 3D Structure Click here
A0A077Z1P5 View 3D Structure Click here
A0A077Z1T7 View 3D Structure Click here
A0A077Z5G3 View 3D Structure Click here
A0A077Z5P8 View 3D Structure Click here
A0A077Z7I2 View 3D Structure Click here
A0A077ZCV8 View 3D Structure Click here
A0A077ZCZ3 View 3D Structure Click here
A0A077ZJH0 View 3D Structure Click here
A0A0D2DEG8 View 3D Structure Click here
A0A0D2DIT3 View 3D Structure Click here
A0A0D2DL55 View 3D Structure Click here
A0A0D2DV72 View 3D Structure Click here
A0A0D2E0S6 View 3D Structure Click here
A0A0D2E2H1 View 3D Structure Click here
A0A0D2E401 View 3D Structure Click here
A0A0D2E607 View 3D Structure Click here
A0A0D2E731 View 3D Structure Click here
A0A0D2EJY1 View 3D Structure Click here
A0A0D2ER68 View 3D Structure Click here
A0A0D2EUP6 View 3D Structure Click here
A0A0D2EZ61 View 3D Structure Click here
A0A0D2F1Q9 View 3D Structure Click here
A0A0D2GD43 View 3D Structure Click here
A0A0D2GGE9 View 3D Structure Click here
A0A0D2GHE8 View 3D Structure Click here
A0A0D2GQ02 View 3D Structure Click here
A0A0D2GRI0 View 3D Structure Click here
A0A0D2H3E4 View 3D Structure Click here
A0A0D2H6X5 View 3D Structure Click here
A0A0D2HM79 View 3D Structure Click here
A0A0D2HPU1 View 3D Structure Click here
A0A0G2K2Q2 View 3D Structure Click here
A0A0G2KZ36 View 3D Structure Click here
A0A0H3GJ88 View 3D Structure Click here
A0A0H3GKZ3 View 3D Structure Click here
A0A0H3GL11 View 3D Structure Click here