Summary: Saccharopine dehydrogenase
Saccharopine dehydrogenase Provide feedback
This family comprised of three structural domains that can not be separated in the linear sequence. In some organisms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.
Johansson E, Steffens JJ, Lindqvist Y, Schneider G; , Structure Fold Des 2000;8:1037-1047.: Crystal structure of saccharopine reductase from Magnaporthe grisea, an enzyme of the alpha-aminoadipate pathway of lysine biosynthesis. PUBMED:11080625 EPMC:11080625
Internal database links
|Similarity to PfamA using HHSearch:||3Beta_HSD DapB_N GFO_IDH_MocA ThiF adh_short DXP_reductoisom Epimerase F420_oxidored NAD_binding_2 NAD_binding_3 Polysacc_synt_2 RmlD_sub_bind Semialdhyde_dh Shikimate_DH TrkA_N NmrA KR NAD_binding_10|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR005097
This entry represents saccharopine dehydrogenase and homospermidine synthase.
Saccharopine dehydrogenase (EC) catalyses the condensation of l-alpha-aminoadipate-delta-semialdehyde (AASA) with l-glutamate to give an imine, which is reduced by NADPH to give saccharopine [PUBMED:19449898]. In some organisms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase (PF). Saccharopine dehydrogenase can also function as a saccharopine reductase. Saccharopine is an intermediate in lysine metabolism.
Homospermidine synthase (HSS) (EC) catalyses the synthesis of the polyamine homospermidine from 2 putrescine molecules in an NAD+-dependent reaction [PUBMED:8841401]. HSS evolved from the alternative spermidine biosynthetic pathway enzyme carboxyspermidine dehydrogenase [PUBMED:19196710, PUBMED:20194510] and the structure of HSS is related to lysine metabolic enzymes [PUBMED:20194510].
|Molecular function||oxidoreductase activity (GO:0016491)|
|Biological process||oxidation-reduction process (GO:0055114)|
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Curation and family details
|Seed source:||Pfam-B_4166 (release 6.6) & Pfam-B_6325 (Release 7.5)|
|Number in seed:||82|
|Number in full:||3742|
|Average length of the domain:||321.10 aa|
|Average identity of full alignment:||19 %|
|Average coverage of the sequence by the domain:||76.28 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
|Download:||download the raw HMM for this family|
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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 Saccharop_dh domain has been found. There are 17 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 seqence.
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