clavaminate synthase family protein is an Fe(II)-2OG dependent oxygenase that may catalyze a hydroxylation reaction, similar to Streptomyces clavuligerus clavaminate synthases 1 and 2
Clavaminic acid synthetase (CAS) -like; CAS is a trifunctional Fe(II)/ 2-oxoglutarate (2OG) ...
127-395
1.57e-102
Clavaminic acid synthetase (CAS) -like; CAS is a trifunctional Fe(II)/ 2-oxoglutarate (2OG) oxygenase carrying out three reactions in the biosynthesis of clavulanic acid, an inhibitor of class A serine beta-lactamases. In general, Fe(II)-2OG oxygenases catalyze a hydroxylation reaction, which leads to the incorporation of an oxygen atom from dioxygen into a hydroxyl group and conversion of 2OG to succinate and CO2
:
Pssm-ID: 238154 Cd Length: 262 Bit Score: 304.71 E-value: 1.57e-102
Gamma-butyrobetaine hydroxylase-like, N-terminal; This domain is found in several proteins ...
42-113
2.05e-06
Gamma-butyrobetaine hydroxylase-like, N-terminal; This domain is found in several proteins including gamma-butyrobetaine dioxygenase, Fe-S cluster assembly factor HCF101 and trimethyllysine dioxygenase proteins. Gamma-butyrobetaine hydroxylase (GBBH) is a alpha-ketoglutarate-dependent dioxygenase that catalyzes the biosynthesis of L-carnitine by hydroxylation of gamma-butyrobetaine (GBB). GBBH is a dimeric enzyme. The monomer consists of a catalytic double-stranded beta-helix domain and a smaller N-terminal domain. The N-terminal domain has a bound Zn ion, which is coordinated by three cysteines and one histidine. The N-terminal domain could facilitate dimer formation, but its precise function is not known. Other family members have been suggested to be involved in FeS cluster maintenance (see Supplementary note 5 in.)
The actual alignment was detected with superfamily member pfam06155:
Pssm-ID: 461840 [Multi-domain] Cd Length: 87 Bit Score: 45.68 E-value: 2.05e-06
Clavaminic acid synthetase (CAS) -like; CAS is a trifunctional Fe(II)/ 2-oxoglutarate (2OG) ...
127-395
1.57e-102
Clavaminic acid synthetase (CAS) -like; CAS is a trifunctional Fe(II)/ 2-oxoglutarate (2OG) oxygenase carrying out three reactions in the biosynthesis of clavulanic acid, an inhibitor of class A serine beta-lactamases. In general, Fe(II)-2OG oxygenases catalyze a hydroxylation reaction, which leads to the incorporation of an oxygen atom from dioxygen into a hydroxyl group and conversion of 2OG to succinate and CO2
Pssm-ID: 238154 Cd Length: 262 Bit Score: 304.71 E-value: 1.57e-102
gamma-butyrobetaine hydroxylase; Members of this protein family are gamma-butyrobetaine ...
42-405
3.58e-98
gamma-butyrobetaine hydroxylase; Members of this protein family are gamma-butyrobetaine hydroxylase, both bacterial and eukarytotic. This enzyme catalyzes the last step in the conversion of lysine to carnitine. Carnitine can serve as a compatible solvent in bacteria and also participates in fatty acid metabolism.
Pssm-ID: 274118 [Multi-domain] Cd Length: 366 Bit Score: 297.45 E-value: 3.58e-98
Taurine catabolism dioxygenase TauD, TfdA family; This family consists of taurine catabolism ...
147-390
2.27e-41
Taurine catabolism dioxygenase TauD, TfdA family; This family consists of taurine catabolism dioxygenases of the TauD, TfdA family. TauD from E. coli is a alpha-ketoglutarate-dependent taurine dioxygenase. This enzyme catalyzes the oxygenolytic release of sulfite from taurine. TfdA from Burkholderia sp. is a 2,4-dichlorophenoxyacetic acid/alpha-ketoglutarate dioxygenase. TfdA from Alcaligenes eutrophus JMP134 is a 2,4-dichlorophenoxyacetate monooxygenase. Also included are gamma-Butyrobetaine hydroxylase enzymes EC:1.14.11.1.
Pssm-ID: 367137 [Multi-domain] Cd Length: 264 Bit Score: 147.21 E-value: 2.27e-41
Gamma-butyrobetaine hydroxylase-like, N-terminal; This domain is found in several proteins ...
42-113
2.05e-06
Gamma-butyrobetaine hydroxylase-like, N-terminal; This domain is found in several proteins including gamma-butyrobetaine dioxygenase, Fe-S cluster assembly factor HCF101 and trimethyllysine dioxygenase proteins. Gamma-butyrobetaine hydroxylase (GBBH) is a alpha-ketoglutarate-dependent dioxygenase that catalyzes the biosynthesis of L-carnitine by hydroxylation of gamma-butyrobetaine (GBB). GBBH is a dimeric enzyme. The monomer consists of a catalytic double-stranded beta-helix domain and a smaller N-terminal domain. The N-terminal domain has a bound Zn ion, which is coordinated by three cysteines and one histidine. The N-terminal domain could facilitate dimer formation, but its precise function is not known. Other family members have been suggested to be involved in FeS cluster maintenance (see Supplementary note 5 in.)
Pssm-ID: 461840 [Multi-domain] Cd Length: 87 Bit Score: 45.68 E-value: 2.05e-06
Clavaminic acid synthetase (CAS) -like; CAS is a trifunctional Fe(II)/ 2-oxoglutarate (2OG) ...
127-395
1.57e-102
Clavaminic acid synthetase (CAS) -like; CAS is a trifunctional Fe(II)/ 2-oxoglutarate (2OG) oxygenase carrying out three reactions in the biosynthesis of clavulanic acid, an inhibitor of class A serine beta-lactamases. In general, Fe(II)-2OG oxygenases catalyze a hydroxylation reaction, which leads to the incorporation of an oxygen atom from dioxygen into a hydroxyl group and conversion of 2OG to succinate and CO2
Pssm-ID: 238154 Cd Length: 262 Bit Score: 304.71 E-value: 1.57e-102
gamma-butyrobetaine hydroxylase; Members of this protein family are gamma-butyrobetaine ...
42-405
3.58e-98
gamma-butyrobetaine hydroxylase; Members of this protein family are gamma-butyrobetaine hydroxylase, both bacterial and eukarytotic. This enzyme catalyzes the last step in the conversion of lysine to carnitine. Carnitine can serve as a compatible solvent in bacteria and also participates in fatty acid metabolism.
Pssm-ID: 274118 [Multi-domain] Cd Length: 366 Bit Score: 297.45 E-value: 3.58e-98
trimethyllysine dioxygenase; Members of this family with known function act as trimethyllysine ...
49-404
7.97e-61
trimethyllysine dioxygenase; Members of this family with known function act as trimethyllysine dioxygenase, an enzyme in the pathway for carnitine biosynthesis from lysine. This enzyme is homologous to gamma-butyrobetaine,2-oxoglutarate dioxygenase, which catalyzes the last step in carnitine biosynthesis. Members of this family appear to be eukaryotic only.
Pssm-ID: 274119 [Multi-domain] Cd Length: 362 Bit Score: 201.16 E-value: 7.97e-61
Taurine catabolism dioxygenase TauD, TfdA family; This family consists of taurine catabolism ...
147-390
2.27e-41
Taurine catabolism dioxygenase TauD, TfdA family; This family consists of taurine catabolism dioxygenases of the TauD, TfdA family. TauD from E. coli is a alpha-ketoglutarate-dependent taurine dioxygenase. This enzyme catalyzes the oxygenolytic release of sulfite from taurine. TfdA from Burkholderia sp. is a 2,4-dichlorophenoxyacetic acid/alpha-ketoglutarate dioxygenase. TfdA from Alcaligenes eutrophus JMP134 is a 2,4-dichlorophenoxyacetate monooxygenase. Also included are gamma-Butyrobetaine hydroxylase enzymes EC:1.14.11.1.
Pssm-ID: 367137 [Multi-domain] Cd Length: 264 Bit Score: 147.21 E-value: 2.27e-41
Gamma-butyrobetaine hydroxylase-like, N-terminal; This domain is found in several proteins ...
42-113
2.05e-06
Gamma-butyrobetaine hydroxylase-like, N-terminal; This domain is found in several proteins including gamma-butyrobetaine dioxygenase, Fe-S cluster assembly factor HCF101 and trimethyllysine dioxygenase proteins. Gamma-butyrobetaine hydroxylase (GBBH) is a alpha-ketoglutarate-dependent dioxygenase that catalyzes the biosynthesis of L-carnitine by hydroxylation of gamma-butyrobetaine (GBB). GBBH is a dimeric enzyme. The monomer consists of a catalytic double-stranded beta-helix domain and a smaller N-terminal domain. The N-terminal domain has a bound Zn ion, which is coordinated by three cysteines and one histidine. The N-terminal domain could facilitate dimer formation, but its precise function is not known. Other family members have been suggested to be involved in FeS cluster maintenance (see Supplementary note 5 in.)
Pssm-ID: 461840 [Multi-domain] Cd Length: 87 Bit Score: 45.68 E-value: 2.05e-06
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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