Pfam: Aminotran_1_2

Protein families database of alignments and HMMs

  Aminotran_1_2  


Figure 1: 2ay4
Aminotransferase

Aromatic amino acid aminotransferase with 3-(p-tolyl)propionic acid

Key:
DomainChainStart ResidueEnd Residue
Aminotran_1_2A 85 408
Aminotran_1_2B 85 408

The Swissprot/PDB mapping was provided by MSD

Accession number: PF00155
Previous identifiers: aminotran_1; aminotran_1_2;
Aminotransferase class I and II

INTERPRO description (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 MEDLINE:91115885 into class I and class II. This entry includes both subfamilies.
QuickGO
FUNCTION :transaminase activity (GO:0008483)
PROCESS :biosynthesis (GO:0009058)
For additional annotation, see the PROSITE document PDOC00098 [Expasy|SRS-UK|SRS-USA]

Alignment Domain organisation
Seed (48)  Full (1715)

Format

Further alignment options here
Help relating to Pfam alignments here
Seed (48)  Full (1715) Context (4)

As a Graphic As a Tree
Zoom pixels/aa.
Bootstrap tree

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Species DistributionPhylogenetic tree
View alignments & domain organisation by species
Tree depth :
Seed (48)  Full (1715)

The trees were generated using Quicktree
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Database References
PDB
You can find out how to set up Rasmol here

PROSITE
1-aminocyclopropane-1-carboxylate synthase signature
PDOC00518 [Expasy|SRS-UK|SRS-USA]
PRINTS PR00753
PROSITE PDOC00098 [Expasy|SRS-UK|SRS-USA]
PRINTS
aspartate aminotransferase signature
PR00799
COGS
COG0079 COG0156 COG0436 COG1168 COG1448
HOMSTRAD
aat
PFAMB
PB000347 PB003487 PB004037 PB021045 PB036387 PB041649 PB044383 PB051518 PB055703 PB059775 PB066709 PB068442 PB074045 PB099779 PB104904 PB105989 PB106250 PB108010 PB108157 PB108169 PB108171 PB108175 PB108179 PB108186 PB108371 PB108623
SYSTERSAminotran_1_2
PANDITAminotran_1_2

Literature References
1.
Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase.
Ko TP, Wu SP, Yang WZ, Tsai H, Yuan HS;
Acta Crystallogr D Biol Crystallogr 1999;55:1474-1477.
2.
Structure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate.
Nakai T, Okada K, Akutsu S, Miyahara I, Kawaguchi S, Kato R, Kuramitsu S, Hirotsu K;
Biochemistry 1999;38:2413-2424.
Pfam specific information
Author of entrySonnhammer ELL, Griffiths-Jones SR
Type definitionDomain
Alignment method of seedClustalw
Source of seed membersProsite
Average Length290.0
Average %id17
Average Coverage70.88%

HMMER build information
 Pfam_ls  [Download HMM]Pfam_fs  [Download HMM]
Gathering cutoff 5.0 5.0; 16.4 16.4
Trusted cutoff5.3 5.3; 16.5 16.5
Noise cutoff4.4 4.4; 16.3 16.3
Build method of HMMhmmbuild -F HMM_ls SEED
hmmcalibrate --seed 0 HMM_ls
hmmbuild -f -F HMM_fs SEED
hmmcalibrate --seed 0 HMM_fs

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