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unnamed protein product [Homo sapiens]
2OG-Fe(II) oxygenase family protein( domain architecture ID 18133971)
2OG-Fe(II) oxygenase family protein, similar to procollagen-lysine, 2-oxoglutarate 5-dioxygenase 1 (PLOD1) catalyzes the hydroxylation of lysyl residues in collagen-like peptides
List of domain hits
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Name | Accession | Description | Interval | E-value | ||||
GT_LH super family | cl45890 | catalytic glycosyltransferase (GT) domain found in the lysyl hydroxylase (LH) family; The ... |
26-151 | 2.89e-82 | ||||
catalytic glycosyltransferase (GT) domain found in the lysyl hydroxylase (LH) family; The lysyl hydroxylase (LH) family includes LH1-3. LH1 (EC 1.14.11.4, also called procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 or PLOD1) and LH2 (EC 1.14.11.4, also called procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 or PLOD2) form hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines may serve as sites of attachment for carbohydrate units and are essential for stability of the intermolecular collagen cross-links. LH1 is part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linking of collagen fibrils. LH3 (EC 1.14.11.4/EC 2.4.1.50/EC 2.4.1.66), also called procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 (PLOD3), or multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3, is a multifunctional enzyme that catalyzes a series of essential post-translational modifications on Lys residues in procollagen. It converts collagen lysines into 1,2-glucosylgalactosyl-5-hydroxylysines through three consecutive reactions: hydroxylation of collagen lysines (LH activity), N-linked conjugation of galactose to hydroxylysines (GT activity), and conjugation of glucose to galactosyl-5-hydroxylysines (GGT activity). LH3 monomer encompasses three domains; the first two N-terminal domains (catalytic glycosyltransferase domain and accessory domain) show Rossmann-fold architectures reminiscent of glycosyltransferases, whereas the C-terminal domain is characterized by a double-stranded beta-helix (DSBH) fold, highly conserved among the 2-oxoglutarate, Fe2+-dependent dioxygenases. This model corresponds to the N-terminal catalytic glycosyltransferase (GT) domain, which is solely responsible for glycosyltransferase activities (both GT and GGT). The actual alignment was detected with superfamily member cd23004: Pssm-ID: 459235 Cd Length: 230 Bit Score: 251.26 E-value: 2.89e-82
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P4Hc | smart00702 | Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ... |
226-389 | 1.48e-26 | ||||
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor. : Pssm-ID: 214780 Cd Length: 165 Bit Score: 104.01 E-value: 1.48e-26
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Name | Accession | Description | Interval | E-value | ||||
GT_LH1 | cd23004 | catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 1 (LH1) and similar ... |
26-151 | 2.89e-82 | ||||
catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 1 (LH1) and similar proteins; LH1 (EC 1.14.11.4), also called procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 (PLOD1), forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines may serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links. LH1 is part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linkling of collagen fibrils. This model corresponds to the N-terminal conserved domain of LH1, which shows high sequence similarity with catalytic glycosyltransferase (GT) domain of LH3. Pssm-ID: 438560 Cd Length: 230 Bit Score: 251.26 E-value: 2.89e-82
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P4Hc | smart00702 | Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ... |
226-389 | 1.48e-26 | ||||
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor. Pssm-ID: 214780 Cd Length: 165 Bit Score: 104.01 E-value: 1.48e-26
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2OG-FeII_Oxy | pfam03171 | 2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ... |
301-391 | 1.15e-10 | ||||
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily. This family includes the C-terminal of prolyl 4-hydroxylase alpha subunit. The holoenzyme has the activity EC:1.14.11.2 catalysing the reaction: Procollagen L-proline + 2-oxoglutarate + O2 <=> procollagen trans- 4-hydroxy-L-proline + succinate + CO2. The full enzyme consists of a alpha2 beta2 complex with the alpha subunit contributing most of the parts of the active site. The family also includes lysyl hydrolases, isopenicillin synthases and AlkB. Pssm-ID: 397334 [Multi-domain] Cd Length: 101 Bit Score: 57.85 E-value: 1.15e-10
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Name | Accession | Description | Interval | E-value | ||||
GT_LH1 | cd23004 | catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 1 (LH1) and similar ... |
26-151 | 2.89e-82 | ||||
catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 1 (LH1) and similar proteins; LH1 (EC 1.14.11.4), also called procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 (PLOD1), forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines may serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links. LH1 is part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linkling of collagen fibrils. This model corresponds to the N-terminal conserved domain of LH1, which shows high sequence similarity with catalytic glycosyltransferase (GT) domain of LH3. Pssm-ID: 438560 Cd Length: 230 Bit Score: 251.26 E-value: 2.89e-82
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GT_LH2 | cd23003 | catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 2 (LH2) and similar ... |
26-158 | 1.75e-56 | ||||
catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 2 (LH2) and similar proteins; Lysyl hydroxylase 2 (LH2; EC 1.14.11.4), also called procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 (PLOD2), forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links. The model corresponds to the N-terminal conserved domain of LH2, which shows high sequence similarity with catalytic glycosyltransferase (GT) domain of LH3. Pssm-ID: 438559 Cd Length: 230 Bit Score: 185.03 E-value: 1.75e-56
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GT_LH3 | cd23002 | catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 3 (LH3) and similar ... |
26-207 | 1.04e-55 | ||||
catalytic glycosyltransferase (GT) domain found in lysyl hydroxylase 3 (LH3) and similar proteins; Lysyl hydroxylase 3 (LH3; EC 1.14.11.4/EC 2.4.1.50/EC 2.4.1.66), also called procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 (PLOD3), or multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3, is a multifunctional enzyme that catalyzes a series of essential post-translational modifications on Lys residues in procollagen. It converts collagen lysines into 1,2-glucosylgalactosyl-5-hydroxylysines through three consecutive reactions: hydroxylation of collagen lysines (LH activity), N-linked conjugation of galactose to hydroxylysines (GT activity), and conjugation of glucose to galactosyl-5-hydroxylysines (GGT activity). LH3 monomer encompasses three domains; the first two N-terminal domains (catalytic glycosyltransferase domain and accessory domain) show Rossmann-fold architectures reminiscent of glycosyltransferases, whereas the C-terminal domain is characterized by a double-stranded beta-helix (DSBH) fold, highly conserved among the 2-oxoglutarate, Fe2+-dependent dioxygenases. This model corresponds to the N-terminal catalytic glycosyltransferase (GT) domain, which is solely responsible for glycosyltransferase activities (both GT and GGT). Pssm-ID: 438558 Cd Length: 230 Bit Score: 182.70 E-value: 1.04e-55
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GT_LH | cd22997 | catalytic glycosyltransferase (GT) domain found in the lysyl hydroxylase (LH) family; The ... |
30-145 | 1.08e-27 | ||||
catalytic glycosyltransferase (GT) domain found in the lysyl hydroxylase (LH) family; The lysyl hydroxylase (LH) family includes LH1-3. LH1 (EC 1.14.11.4, also called procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 or PLOD1) and LH2 (EC 1.14.11.4, also called procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 or PLOD2) form hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines may serve as sites of attachment for carbohydrate units and are essential for stability of the intermolecular collagen cross-links. LH1 is part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linking of collagen fibrils. LH3 (EC 1.14.11.4/EC 2.4.1.50/EC 2.4.1.66), also called procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 (PLOD3), or multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3, is a multifunctional enzyme that catalyzes a series of essential post-translational modifications on Lys residues in procollagen. It converts collagen lysines into 1,2-glucosylgalactosyl-5-hydroxylysines through three consecutive reactions: hydroxylation of collagen lysines (LH activity), N-linked conjugation of galactose to hydroxylysines (GT activity), and conjugation of glucose to galactosyl-5-hydroxylysines (GGT activity). LH3 monomer encompasses three domains; the first two N-terminal domains (catalytic glycosyltransferase domain and accessory domain) show Rossmann-fold architectures reminiscent of glycosyltransferases, whereas the C-terminal domain is characterized by a double-stranded beta-helix (DSBH) fold, highly conserved among the 2-oxoglutarate, Fe2+-dependent dioxygenases. This model corresponds to the N-terminal catalytic glycosyltransferase (GT) domain, which is solely responsible for glycosyltransferase activities (both GT and GGT). Pssm-ID: 438557 Cd Length: 247 Bit Score: 109.41 E-value: 1.08e-27
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P4Hc | smart00702 | Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ... |
226-389 | 1.48e-26 | ||||
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor. Pssm-ID: 214780 Cd Length: 165 Bit Score: 104.01 E-value: 1.48e-26
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2OG-FeII_Oxy | pfam03171 | 2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ... |
301-391 | 1.15e-10 | ||||
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily. This family includes the C-terminal of prolyl 4-hydroxylase alpha subunit. The holoenzyme has the activity EC:1.14.11.2 catalysing the reaction: Procollagen L-proline + 2-oxoglutarate + O2 <=> procollagen trans- 4-hydroxy-L-proline + succinate + CO2. The full enzyme consists of a alpha2 beta2 complex with the alpha subunit contributing most of the parts of the active site. The family also includes lysyl hydrolases, isopenicillin synthases and AlkB. Pssm-ID: 397334 [Multi-domain] Cd Length: 101 Bit Score: 57.85 E-value: 1.15e-10
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2OG-FeII_Oxy_3 | pfam13640 | 2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ... |
304-389 | 1.36e-03 | ||||
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily. Pssm-ID: 463943 Cd Length: 94 Bit Score: 37.74 E-value: 1.36e-03
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Blast search parameters | ||||
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