Blast Analysis : gnl|CDD|187541

Analysis  rpsblast_cdd Start  3
End  169 Strand  +
Length  167 Note  Gaps:1
Hit Coverage  38.36 Hit Length  305
Hit Pident  66.67 E Val  3e-42
Hit Description  cd05230 UGD_SDR_e UDP-glucuronate decarboxylase (UGD) and related proteins extended (e) SDRs. UGD catalyzes the formation of UDP-xylose from UDP-glucuronate it is an extended-SDR and has the characteristic glycine-rich NAD-binding pattern TGXXGXXG and active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins and include isomerases epimerases oxidoreductases and lyases they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold an NAD(P)(H)-binding region and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range they catalyze a wide range of activities including the metabolism of steroids cofactors carbohydrates lipids aromatic compounds and amino acids and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151 human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys there is often an upstream Ser and/or an Asn contributing to the active site while substrate binding is in the C-terminal region which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys a water molecule stabilized by Asn and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Hit Pcons  14.53
Name  Qrob_P0297350.2
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1 Protein

Protein Identifier
Organism . Name 		Score Score Type Protein Description Alias (in v1) Code Enzyme Gene Prediction Quality
Qrob_P0297350.2 Quercus robur 100.0 egn (M=1) KOG0747//KOG1429 - Putative NAD+-dependent epimerases [Carbohydrate transport and metabolism]. // dTDP-glucose 4-6-dehydratase/UDP-glucuronic acid decarboxylase [Carbohydrate transport and metabolism Cell wall/membrane/envelope biogenesis].   EC:4.1.1.35 validated