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sn-glycerol-1-phosphate dehydrogenase [Bacillus amyloliquefaciens]
sn-glycerol-1-phosphate dehydrogenase( domain architecture ID 10169355)
sn-glycerol-1-phosphate dehydrogenase catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-phosphate (G1P)
List of domain hits
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Name | Accession | Description | Interval | E-value | ||||||
G1PDH | cd08175 | Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
24-383 | 1.70e-152 | ||||||
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in an NADH-dependent manner; Glycerol-1-phosphate dehydrogenase (G1PDH) plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires a Ni++ ion. In Bacillus subtilis, it has been described as AraM gene in L-arabinose (ara) operon. AraM protein forms homodimer. : Pssm-ID: 341454 Cd Length: 340 Bit Score: 433.86 E-value: 1.70e-152
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Name | Accession | Description | Interval | E-value | ||||||
G1PDH | cd08175 | Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
24-383 | 1.70e-152 | ||||||
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in an NADH-dependent manner; Glycerol-1-phosphate dehydrogenase (G1PDH) plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires a Ni++ ion. In Bacillus subtilis, it has been described as AraM gene in L-arabinose (ara) operon. AraM protein forms homodimer. Pssm-ID: 341454 Cd Length: 340 Bit Score: 433.86 E-value: 1.70e-152
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Fe-ADH_2 | pfam13685 | Iron-containing alcohol dehydrogenase; |
28-295 | 1.52e-75 | ||||||
Iron-containing alcohol dehydrogenase; Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 234.89 E-value: 1.52e-75
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GldA | COG0371 | Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
27-376 | 2.91e-62 | ||||||
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and conversion]; Glycerol dehydrogenase or related enzyme, iron-containing ADH family is part of the Pathway/BioSystem: Isoprenoid biosynthesis Pssm-ID: 440140 [Multi-domain] Cd Length: 355 Bit Score: 203.86 E-value: 2.91e-62
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egsA | PRK00843 | NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
26-386 | 6.55e-62 | ||||||
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed Pssm-ID: 179139 Cd Length: 350 Bit Score: 202.82 E-value: 6.55e-62
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Name | Accession | Description | Interval | E-value | ||||||
G1PDH | cd08175 | Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
24-383 | 1.70e-152 | ||||||
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in an NADH-dependent manner; Glycerol-1-phosphate dehydrogenase (G1PDH) plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires a Ni++ ion. In Bacillus subtilis, it has been described as AraM gene in L-arabinose (ara) operon. AraM protein forms homodimer. Pssm-ID: 341454 Cd Length: 340 Bit Score: 433.86 E-value: 1.70e-152
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G1PDH_related | cd08549 | Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
24-386 | 7.82e-90 | ||||||
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and archeal glycerol-1-phosphate dehydrogenase-like oxidoreductases. These proteins have similarity with glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion. It also contains archaeal Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) that plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. Pssm-ID: 341479 [Multi-domain] Cd Length: 331 Bit Score: 274.06 E-value: 7.82e-90
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Fe-ADH_2 | pfam13685 | Iron-containing alcohol dehydrogenase; |
28-295 | 1.52e-75 | ||||||
Iron-containing alcohol dehydrogenase; Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 234.89 E-value: 1.52e-75
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Gro1PDH | cd08173 | Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
27-384 | 3.20e-66 | ||||||
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya. Pssm-ID: 341452 Cd Length: 343 Bit Score: 213.95 E-value: 3.20e-66
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GldA | COG0371 | Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
27-376 | 2.91e-62 | ||||||
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and conversion]; Glycerol dehydrogenase or related enzyme, iron-containing ADH family is part of the Pathway/BioSystem: Isoprenoid biosynthesis Pssm-ID: 440140 [Multi-domain] Cd Length: 355 Bit Score: 203.86 E-value: 2.91e-62
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egsA | PRK00843 | NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
26-386 | 6.55e-62 | ||||||
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed Pssm-ID: 179139 Cd Length: 350 Bit Score: 202.82 E-value: 6.55e-62
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G1PDH-like | cd08174 | Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
27-391 | 9.33e-49 | ||||||
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion. Pssm-ID: 341453 [Multi-domain] Cd Length: 332 Bit Score: 168.08 E-value: 9.33e-49
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DHQS | cd08195 | Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
26-138 | 7.89e-13 | ||||||
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway. Pssm-ID: 341474 Cd Length: 343 Bit Score: 69.01 E-value: 7.89e-13
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AroB | COG0337 | 3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
26-189 | 1.21e-11 | ||||||
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis Pssm-ID: 440106 Cd Length: 355 Bit Score: 65.50 E-value: 1.21e-11
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DHQ_Fe-ADH | cd07766 | Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
25-199 | 1.46e-10 | ||||||
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H. Pssm-ID: 341447 [Multi-domain] Cd Length: 271 Bit Score: 61.23 E-value: 1.46e-10
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GlyDH-like | cd08550 | Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
47-194 | 6.49e-10 | ||||||
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized. Pssm-ID: 341480 [Multi-domain] Cd Length: 347 Bit Score: 59.86 E-value: 6.49e-10
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GlyDH | cd08170 | Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
28-194 | 7.08e-10 | ||||||
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in glycerol dissmilation; Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Pssm-ID: 341449 [Multi-domain] Cd Length: 351 Bit Score: 60.12 E-value: 7.08e-10
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DHQ_synthase | pfam01761 | 3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
108-358 | 1.47e-09 | ||||||
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in isolation in various bacterial 3-dehydroquinate synthases and also present as a domain in the pentafunctional AROM polypeptide. 3-dehydroquinate (DHQ) synthase catalyzes the formation of dehydroquinate (DHQ) and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Pssm-ID: 426414 Cd Length: 260 Bit Score: 58.28 E-value: 1.47e-09
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EEVS | cd08199 | 2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ... |
50-302 | 3.00e-09 | ||||||
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the cyclization of sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in the biosynthesis of C(7)N-aminocyclitol-containing products. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety. The valienamine unit is responsible for their biological activities as various glycosidic hydrolases inhibitors. Two important microbial secondary metabolites, validamycin and acarbose, are used in agricultural and biomedical applications. Validamycin A is an antifungal antibiotic which has a strong trehalase inhibitory activity and has been used to control sheath blight disease in rice caused by Rhizoctonia solani. Acarbose is an alpha-glucosidase inhibitor used for the treatment of type II insulin-independent diabetes. Salbostatin produced by Streptomyces albus also belongs to this family. It exhibits strong trehalase inhibitory activity. Pssm-ID: 341478 Cd Length: 349 Bit Score: 57.92 E-value: 3.00e-09
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Fe-ADH | pfam00465 | Iron-containing alcohol dehydrogenase; |
27-371 | 2.16e-08 | ||||||
Iron-containing alcohol dehydrogenase; Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 55.30 E-value: 2.16e-08
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GlyDH-like | cd08172 | Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
35-224 | 3.87e-08 | ||||||
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Pssm-ID: 341451 [Multi-domain] Cd Length: 346 Bit Score: 54.45 E-value: 3.87e-08
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gldA | PRK09423 | glycerol dehydrogenase; Provisional |
28-192 | 5.71e-07 | ||||||
glycerol dehydrogenase; Provisional Pssm-ID: 181843 Cd Length: 366 Bit Score: 50.97 E-value: 5.71e-07
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PLN02834 | PLN02834 | 3-dehydroquinate synthase |
27-192 | 9.59e-07 | ||||||
3-dehydroquinate synthase Pssm-ID: 215448 Cd Length: 433 Bit Score: 50.54 E-value: 9.59e-07
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DOIS | cd08197 | 2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ... |
24-180 | 1.26e-06 | ||||||
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose; 2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose through a multistep reaction in the biosynthesis of aminoglycoside antibiotics. 2-deoxystreptamine (DOS)-containing aminoglycoside antibiotics includes neomycin, kanamycin, gentamicin, and ribostamycin. They are important antibacterial agents. DOIS is a homolog of the dehydroquinate synthase which catalyzes the cyclization of 3-deoxy-D-arabino-heputulosonate-7-phosphate to dehydroquinate (DHQ) in the shikimate pathway. Pssm-ID: 341476 Cd Length: 355 Bit Score: 49.89 E-value: 1.26e-06
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DHQ-like | cd08169 | Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ... |
110-294 | 1.63e-06 | ||||||
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase; This group contains dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. These proteins exhibit the dehydroquinate synthase structural fold. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. 2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose through a multi-step reaction in the biosynthesis of aminoglycoside antibiotics. 2-deoxystreptamine (DOS)-containing aminoglycoside antibiotics includes neomycin, kanamycin, gentamicin, and ribostamycin. 2-epi-5-epi-valiolone synthases catalyze the cyclization of sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in the biosynthesis of C(7)N-aminocyclitol-containing products. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety. The valienamine unit is responsible for their biological activities as various glycosidic hydrolases inhibitors. Two important microbial secondary metabolites, validamycin and acarbose, are used in agricultural and biomedical applications. Pssm-ID: 341448 [Multi-domain] Cd Length: 328 Bit Score: 49.33 E-value: 1.63e-06
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PRK14021 | PRK14021 | bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
22-207 | 6.12e-04 | ||||||
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 41.77 E-value: 6.12e-04
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