y
Basic Information | |
---|---|
Species | Selaginella moellendorffii |
Cazyme ID | 410382 |
Family | GT68 |
Protein Properties | Length: 400 Molecular Weight: 44271.3 Isoelectric Point: 5.5062 |
View CDS |
External Links |
---|
NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GT68 | 105 | 186 | 1e-22 |
SCFFPIPQAASCISRKIQEAKPRVIYISTDAAESEITLLQQLLGPDVVAMLDKTICAMAESFIGTPGSTFTDDIVRLRKEWG |
Full Sequence |
---|
Protein Sequence Length: 400 Download |
MSGCYLDEDH EKKIKALGLS WSSKNDAWPE EASLKGYPSH PRASEFVAKF SCEDEVLGIG 60 DVFYSDVESE LVAQIGGPLQ HSCKTIIRLN RLILLTVQSN VKNESCFFPI PQAASCISRK 120 IQEAKPRVIY ISTDAAESEI TLLQQLLGPD VVAMLDKTIC AMAESFIGTP GSTFTDDIVR 180 LRKEWGSSNS CDGVLCQGQY PNFIADTGRA LDLARRGGNI TIVCERDTSA FLFPVRYFPP 240 VEQVAKAFKE HKETFLRLDV CVNCAGIVEE RDFVSDDKWC KVLRIQAMRS QDSPGVAILN 300 LASTGGLFLV LLYPIYSASK GGLGSQGRLW NYRAKAYEQT FCIPGIISEL LLIQYVETPM 360 TAKEMIAATI PMKNPVYKFL LICHSILALI ELVFMFLLC* 420 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK05557 | fabG | 5.0e-10 | 242 | 373 | 162 | + 3-ketoacyl-(acyl-carrier-protein) reductase; Validated | ||
cd11296 | O-FucT_like | 2.0e-10 | 102 | 182 | 109 | + GDP-fucose protein O-fucosyltransferase and related proteins. O-fucosyltransferase-like proteins are GDP-fucose dependent enzymes with similarities to the family 1 glycosyltransferases (GT1). They are soluble ER proteins that may be proteolytically cleaved from a membrane-associated preprotein, and are involved in the O-fucosylation of protein substrates, the core fucosylation of growth factor receptors, and other processes. | ||
cd05233 | SDR_c | 9.0e-11 | 208 | 323 | 145 | + classical (c) SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. | ||
COG1028 | FabG | 3.0e-11 | 210 | 373 | 200 | + Dehydrogenases with different specificities (related to short-chain alcohol dehydrogenases) [Secondary metabolites biosynthesis, transport, and catabolism / General function prediction only] | ||
cd05323 | ADH_SDR_c_like | 8.0e-12 | 242 | 323 | 100 | + insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs. This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. |
Annotations - NR Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CAN80219.1 | 0 | 4 | 207 | 80 | 336 | hypothetical protein [Vitis vinifera] |
RefSeq | NP_001060060.1 | 0 | 4 | 206 | 298 | 555 | Os07g0572600 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_173170.2 | 0 | 4 | 207 | 306 | 563 | unknown protein [Arabidopsis thaliana] |
RefSeq | XP_002264087.1 | 0 | 4 | 207 | 302 | 558 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002460894.1 | 0 | 4 | 206 | 303 | 560 | hypothetical protein SORBIDRAFT_02g037060 [Sorghum bicolor] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2gdz_A | 0.00006 | 242 | 391 | 71 | 236 | A Chain A, Crystal Structure Of 15-Hydroxyprostaglandin Dehydrogenase Type1, Complexed With N |
PDB | 1gz6_D | 0.002 | 235 | 323 | 70 | 171 | A Chain A, (3r)-Hydroxyacyl-Coa Dehydrogenase Fragment Of Rat Peroxisomal Multifunctional Enzyme Type 2 |
PDB | 1gz6_C | 0.002 | 235 | 323 | 70 | 171 | A Chain A, (3r)-Hydroxyacyl-Coa Dehydrogenase Fragment Of Rat Peroxisomal Multifunctional Enzyme Type 2 |
PDB | 1gz6_B | 0.002 | 235 | 323 | 70 | 171 | A Chain A, (3r)-Hydroxyacyl-Coa Dehydrogenase Fragment Of Rat Peroxisomal Multifunctional Enzyme Type 2 |
PDB | 1gz6_A | 0.002 | 235 | 323 | 70 | 171 | A Chain A, (3r)-Hydroxyacyl-Coa Dehydrogenase Fragment Of Rat Peroxisomal Multifunctional Enzyme Type 2 |