uncharacterized protein [Oryza sativa Japonica Group]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| TIM super family | cl21457 | TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate ... |
381-613 | 4.73e-89 | |||||
TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate isomerase (TIM) which, in general, share an eight beta/alpha closed barrel structure. The actual alignment was detected with superfamily member pfam04481: Pssm-ID: 473867 Cd Length: 243 Bit Score: 276.63 E-value: 4.73e-89
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| MmsB | COG2084 | 3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
19-304 | 1.24e-84 | |||||
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism]; : Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 266.60 E-value: 1.24e-84
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| Name | Accession | Description | Interval | E-value | |||||
| DUF561 | pfam04481 | Protein of unknown function (DUF561); Protein of unknown function found in a cyanobacterium, ... |
381-613 | 4.73e-89 | |||||
Protein of unknown function (DUF561); Protein of unknown function found in a cyanobacterium, and the chloroplasts of algae. Pssm-ID: 113257 Cd Length: 243 Bit Score: 276.63 E-value: 4.73e-89
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| MmsB | COG2084 | 3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
19-304 | 1.24e-84 | |||||
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism]; Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 266.60 E-value: 1.24e-84
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| garR | PRK11559 | tartronate semialdehyde reductase; Provisional |
20-310 | 1.07e-53 | |||||
tartronate semialdehyde reductase; Provisional Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 185.64 E-value: 1.07e-53
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| NAD_binding_2 | pfam03446 | NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
20-179 | 6.26e-41 | |||||
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold. Pssm-ID: 427298 [Multi-domain] Cd Length: 159 Bit Score: 146.08 E-value: 6.26e-41
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| GDH_like_2 | cd12164 | Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ... |
13-51 | 2.97e-05 | |||||
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy dehydrogenase family; This group contains a variety of proteins variously identified as glycerate dehydrogenase (GDH, also known as hydroxypyruvate reductase) and other enzymes of the 2-hydroxyacid dehydrogenase family. GDH catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. 2-hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. Pssm-ID: 240641 [Multi-domain] Cd Length: 306 Bit Score: 46.34 E-value: 2.97e-05
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| gnd_rel | TIGR00872 | 6-phosphogluconate dehydrogenase (decarboxylating); This family resembles a larger family (gnd) ... |
20-189 | 5.87e-05 | |||||
6-phosphogluconate dehydrogenase (decarboxylating); This family resembles a larger family (gnd) of bacterial and eukaryotic 6-phosphogluconate dehydrogenases but differs from it by a deep split in a UPGMA similarity clustering tree and the lack of a central region of about 140 residues. Among complete genomes, it is found is found in Bacillus subtilis and Mycobacterium tuberculosis, both of which also contain gnd, and in Aquifex aeolicus. The protein from Methylobacillus flagellatus KT has been characterized as a decarboxylating 6-phosphogluconate dehydrogenase as part of an unusual formaldehyde oxidation cycle. In some sequenced organisms members of this family are the sole 6-phosphogluconate dehydrogenase present and are probably active in the pentose phosphate cycle. [Energy metabolism, Pentose phosphate pathway] Pssm-ID: 273313 [Multi-domain] Cd Length: 298 Bit Score: 45.61 E-value: 5.87e-05
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| ThiE | COG0352 | Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
534-612 | 7.25e-03 | |||||
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis Pssm-ID: 440121 [Multi-domain] Cd Length: 206 Bit Score: 38.24 E-value: 7.25e-03
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| Name | Accession | Description | Interval | E-value | |||||
| DUF561 | pfam04481 | Protein of unknown function (DUF561); Protein of unknown function found in a cyanobacterium, ... |
381-613 | 4.73e-89 | |||||
Protein of unknown function (DUF561); Protein of unknown function found in a cyanobacterium, and the chloroplasts of algae. Pssm-ID: 113257 Cd Length: 243 Bit Score: 276.63 E-value: 4.73e-89
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| MmsB | COG2084 | 3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
19-304 | 1.24e-84 | |||||
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism]; Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 266.60 E-value: 1.24e-84
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| garR | PRK11559 | tartronate semialdehyde reductase; Provisional |
20-310 | 1.07e-53 | |||||
tartronate semialdehyde reductase; Provisional Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 185.64 E-value: 1.07e-53
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| PRK15059 | PRK15059 | 2-hydroxy-3-oxopropionate reductase; |
20-305 | 5.90e-42 | |||||
2-hydroxy-3-oxopropionate reductase; Pssm-ID: 185019 [Multi-domain] Cd Length: 292 Bit Score: 153.64 E-value: 5.90e-42
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| NAD_binding_2 | pfam03446 | NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
20-179 | 6.26e-41 | |||||
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold. Pssm-ID: 427298 [Multi-domain] Cd Length: 159 Bit Score: 146.08 E-value: 6.26e-41
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| PLN02858 | PLN02858 | fructose-bisphosphate aldolase |
18-311 | 1.01e-26 | |||||
fructose-bisphosphate aldolase Pssm-ID: 215463 [Multi-domain] Cd Length: 1378 Bit Score: 116.49 E-value: 1.01e-26
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| NAD_binding_11 | pfam14833 | NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ... |
182-301 | 6.97e-24 | |||||
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a central metabolite in the valine catabolic pathway, and is reversibly oxidized to methylmalonate semi-aldehyde by a specific dehydrogenase belonging to the 3-hydroxyacid dehydrogenase family. The reaction is NADP-dependent and this region of the enzyme binds NAD. The NAD-binding domain of 6-phosphogluconate dehydrogenase adopts an alpha helical structure. Pssm-ID: 434252 [Multi-domain] Cd Length: 122 Bit Score: 96.83 E-value: 6.97e-24
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| PLN02858 | PLN02858 | fructose-bisphosphate aldolase |
18-310 | 1.32e-20 | |||||
fructose-bisphosphate aldolase Pssm-ID: 215463 [Multi-domain] Cd Length: 1378 Bit Score: 96.84 E-value: 1.32e-20
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| PRK15461 | PRK15461 | sulfolactaldehyde 3-reductase; |
21-313 | 2.73e-20 | |||||
sulfolactaldehyde 3-reductase; Pssm-ID: 185358 [Multi-domain] Cd Length: 296 Bit Score: 91.84 E-value: 2.73e-20
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| PRK09599 | PRK09599 | NADP-dependent phosphogluconate dehydrogenase; |
20-184 | 8.00e-15 | |||||
NADP-dependent phosphogluconate dehydrogenase; Pssm-ID: 236582 [Multi-domain] Cd Length: 301 Bit Score: 75.56 E-value: 8.00e-15
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| YqeC | COG1023 | 6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism]; |
20-184 | 4.34e-14 | |||||
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism]; Pssm-ID: 440646 [Multi-domain] Cd Length: 300 Bit Score: 73.20 E-value: 4.34e-14
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| GDH_like_2 | cd12164 | Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ... |
13-51 | 2.97e-05 | |||||
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy dehydrogenase family; This group contains a variety of proteins variously identified as glycerate dehydrogenase (GDH, also known as hydroxypyruvate reductase) and other enzymes of the 2-hydroxyacid dehydrogenase family. GDH catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. 2-hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. Pssm-ID: 240641 [Multi-domain] Cd Length: 306 Bit Score: 46.34 E-value: 2.97e-05
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| gnd_rel | TIGR00872 | 6-phosphogluconate dehydrogenase (decarboxylating); This family resembles a larger family (gnd) ... |
20-189 | 5.87e-05 | |||||
6-phosphogluconate dehydrogenase (decarboxylating); This family resembles a larger family (gnd) of bacterial and eukaryotic 6-phosphogluconate dehydrogenases but differs from it by a deep split in a UPGMA similarity clustering tree and the lack of a central region of about 140 residues. Among complete genomes, it is found is found in Bacillus subtilis and Mycobacterium tuberculosis, both of which also contain gnd, and in Aquifex aeolicus. The protein from Methylobacillus flagellatus KT has been characterized as a decarboxylating 6-phosphogluconate dehydrogenase as part of an unusual formaldehyde oxidation cycle. In some sequenced organisms members of this family are the sole 6-phosphogluconate dehydrogenase present and are probably active in the pentose phosphate cycle. [Energy metabolism, Pentose phosphate pathway] Pssm-ID: 273313 [Multi-domain] Cd Length: 298 Bit Score: 45.61 E-value: 5.87e-05
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| NmrA_TMR_like_1_SDR_a | cd05231 | NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, ... |
27-65 | 3.04e-04 | |||||
NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, subgroup 1, atypical (a) SDRs; Atypical SDRs related to NMRa, TMR, and HSCARG (an NADPH sensor). This subgroup resembles the SDRs and has a partially conserved characteristic [ST]GXXGXXG NAD-binding motif, but lacks the conserved active site residues. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. 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. Atypical SDRs are distinct from classical SDRs. 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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. Pssm-ID: 187542 [Multi-domain] Cd Length: 259 Bit Score: 43.08 E-value: 3.04e-04
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| PRK06522 | PRK06522 | 2-dehydropantoate 2-reductase; Reviewed |
20-68 | 1.37e-03 | |||||
2-dehydropantoate 2-reductase; Reviewed Pssm-ID: 235821 [Multi-domain] Cd Length: 304 Bit Score: 40.99 E-value: 1.37e-03
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| Gnd | COG0362 | 6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate ... |
21-184 | 1.43e-03 | |||||
6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate dehydrogenase is part of the Pathway/BioSystem: Pentose phosphate pathway Pssm-ID: 440131 [Multi-domain] Cd Length: 467 Bit Score: 41.60 E-value: 1.43e-03
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| YbjT | COG0702 | Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ... |
17-65 | 2.38e-03 | |||||
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only]; Pssm-ID: 440466 [Multi-domain] Cd Length: 215 Bit Score: 39.83 E-value: 2.38e-03
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| SDR_a7 | cd05262 | atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. ... |
25-63 | 2.48e-03 | |||||
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. 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. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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. Pssm-ID: 187572 [Multi-domain] Cd Length: 291 Bit Score: 40.41 E-value: 2.48e-03
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| PRK09287 | PRK09287 | NADP-dependent phosphogluconate dehydrogenase; |
139-184 | 3.65e-03 | |||||
NADP-dependent phosphogluconate dehydrogenase; Pssm-ID: 236453 [Multi-domain] Cd Length: 459 Bit Score: 40.11 E-value: 3.65e-03
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| PanE | COG1893 | Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ... |
24-110 | 5.46e-03 | |||||
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis Pssm-ID: 441497 [Multi-domain] Cd Length: 305 Bit Score: 39.45 E-value: 5.46e-03
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| ProC | COG0345 | Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
19-57 | 6.77e-03 | |||||
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis Pssm-ID: 440114 [Multi-domain] Cd Length: 267 Bit Score: 38.89 E-value: 6.77e-03
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| PLN02350 | PLN02350 | phosphogluconate dehydrogenase (decarboxylating) |
16-184 | 7.20e-03 | |||||
phosphogluconate dehydrogenase (decarboxylating) Pssm-ID: 215200 [Multi-domain] Cd Length: 493 Bit Score: 39.31 E-value: 7.20e-03
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| ThiE | COG0352 | Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
534-612 | 7.25e-03 | |||||
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis Pssm-ID: 440121 [Multi-domain] Cd Length: 206 Bit Score: 38.24 E-value: 7.25e-03
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| Blast search parameters | ||||
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