N-terminal nucleotide-binding domain (NBD) of nebramycin 5' synthase (TobZ) and similar ...
2-336
3.83e-112
N-terminal nucleotide-binding domain (NBD) of nebramycin 5' synthase (TobZ) and similar proteins; TobZ (EC 6.1.2.2), also called kanamycin A carbamoyltransferase, or tobramycin carbamoyltransferase, is involved in the biosynthesis of the 2-deoxystreptamine-containing aminoglycoside antibiotics such as nebramycin 5 and 6-O-carbamoylkanamycin. It catalyzes the hydrolysis of carbamoyl phosphate and its subsequent adenylation by ATP to yield O-carbamoyladenylate. Then it catalyzes the transfer of the carbamoyl moiety from O-carbamoyladenylate to the tobramycin 6-hydroxy group to yield nebramycin 5'. It catalyzes the same reaction with kanamycin A. These reactions are considerably slower in the presence of deoxy-ATP. TobZ consists of two major domains: the N-terminal Kae1-like domain is involved in the transfer of carbamoyl from O-carbamoyladenylate to tobramycin or kanamycin; the C-terminal YrdC-like domain is involved in the hydrolysis of carbamoyl phosphate and its subsequent adenylation by ATP. The model corresponds to the N-terminal domain.
Pssm-ID: 466948 [Multi-domain] Cd Length: 243 Bit Score: 333.27 E-value: 3.83e-112
Carbamoyltransferase C-terminus; This domain is found in NodU from Rhizobium, CmcH from ...
381-549
1.69e-82
Carbamoyltransferase C-terminus; This domain is found in NodU from Rhizobium, CmcH from Nocardia lactamdurans and the bifunctional carbamoyltransferase TobZ from Streptoalloteichus tenebrarius. NodU a Rhizobium nodulation protein involved in the synthesis of nodulation factors has 6-O-carbamoyltransferase-like activity. CmcH is involved in cephamycin (antibiotic) biosynthesis and has 3-hydroxymethylcephem carbamoyltransferase activity, EC:2.1.3.7 catalysing the reaction: Carbamoyl phosphate + 3-hydroxymethylceph-3-EM-4-carboxylate <=> phosphate + 3-carbamoyloxymethylcephem. TobZ functions as an ATP carbamoyltransferase and tobramycin carbamoyltransferase. These proteins contain two domains, this is the smaller, C-terminal, domain.
Pssm-ID: 435610 [Multi-domain] Cd Length: 169 Bit Score: 254.29 E-value: 1.69e-82
N-terminal nucleotide-binding domain (NBD) of nebramycin 5' synthase (TobZ) and similar ...
2-336
3.83e-112
N-terminal nucleotide-binding domain (NBD) of nebramycin 5' synthase (TobZ) and similar proteins; TobZ (EC 6.1.2.2), also called kanamycin A carbamoyltransferase, or tobramycin carbamoyltransferase, is involved in the biosynthesis of the 2-deoxystreptamine-containing aminoglycoside antibiotics such as nebramycin 5 and 6-O-carbamoylkanamycin. It catalyzes the hydrolysis of carbamoyl phosphate and its subsequent adenylation by ATP to yield O-carbamoyladenylate. Then it catalyzes the transfer of the carbamoyl moiety from O-carbamoyladenylate to the tobramycin 6-hydroxy group to yield nebramycin 5'. It catalyzes the same reaction with kanamycin A. These reactions are considerably slower in the presence of deoxy-ATP. TobZ consists of two major domains: the N-terminal Kae1-like domain is involved in the transfer of carbamoyl from O-carbamoyladenylate to tobramycin or kanamycin; the C-terminal YrdC-like domain is involved in the hydrolysis of carbamoyl phosphate and its subsequent adenylation by ATP. The model corresponds to the N-terminal domain.
Pssm-ID: 466948 [Multi-domain] Cd Length: 243 Bit Score: 333.27 E-value: 3.83e-112
Carbamoyltransferase C-terminus; This domain is found in NodU from Rhizobium, CmcH from ...
381-549
1.69e-82
Carbamoyltransferase C-terminus; This domain is found in NodU from Rhizobium, CmcH from Nocardia lactamdurans and the bifunctional carbamoyltransferase TobZ from Streptoalloteichus tenebrarius. NodU a Rhizobium nodulation protein involved in the synthesis of nodulation factors has 6-O-carbamoyltransferase-like activity. CmcH is involved in cephamycin (antibiotic) biosynthesis and has 3-hydroxymethylcephem carbamoyltransferase activity, EC:2.1.3.7 catalysing the reaction: Carbamoyl phosphate + 3-hydroxymethylceph-3-EM-4-carboxylate <=> phosphate + 3-carbamoyloxymethylcephem. TobZ functions as an ATP carbamoyltransferase and tobramycin carbamoyltransferase. These proteins contain two domains, this is the smaller, C-terminal, domain.
Pssm-ID: 435610 [Multi-domain] Cd Length: 169 Bit Score: 254.29 E-value: 1.69e-82
N-terminal nucleotide-binding domain (NBD) of the NodU/CmcH family proteins; The NodU/CmcH ...
2-335
7.35e-76
N-terminal nucleotide-binding domain (NBD) of the NodU/CmcH family proteins; The NodU/CmcH family includes NodU from Rhizobium, CmcH from Amycolatopsis lactamdurans, the bifunctional carbamoyltransferase TobZ from Streptoalloteichus tenebrarius, NovN from Streptomyces niveus and NolNO from Sinorhizobium fredii. NodU is a Rhizobium nodulation protein involved in the synthesis of nodulation factors has 6-O-carbamoyltransferase-like activity. 3'-hydroxymethylcephem-O-carbamoyltransferase CmcH (EC 2.1.3.7), also called 3'-hydroxymethylcephem-O-CASE (CCT), is involved in cephamycin (antibiotic) biosynthesis and has 3-hydroxymethylcephem carbamoyltransferase activity. nebramycin 5' synthase TobZ (EC 6.1.2.2), also called kanamycin A carbamoyltransferase, or tobramycin carbamoyltransferase, functions as an ATP carbamoyltransferase and tobramycin carbamoyltransferase. Novobiocin biosynthesis protein NovN (EC 2.1.3.12), also called decarbamoylnovobiocin carbamoyltransferase, acts as a carbamoyltransferase that mediates 3'-carbamoylation of the noviosyl ring to produce novobiocin, the final step in the novobiocin biosynthesis pathway. Nodulation protein NolNO (EC 2.1.3.-), also called NolO or Y4hD, is involved in the O-carbamoylation of nod factors. Members in this family consist of two domains. The model corresponds to the N-terminal Kae1-like domain.
Pssm-ID: 466883 [Multi-domain] Cd Length: 268 Bit Score: 241.05 E-value: 7.35e-76
N-terminal nucleotide-binding domain (NBD) of Streptomyces niveus novobiocin biosynthesis ...
3-333
7.69e-71
N-terminal nucleotide-binding domain (NBD) of Streptomyces niveus novobiocin biosynthesis protein N (NovN) and similar proteins; The family includes a group of proteins similar to Streptomyces niveus novobiocin biosynthesis protein N (NovN) and Sinorhizobium fredii nodulation protein NolNO. NovN (EC 2.1.3.12), also called decarbamoylnovobiocin carbamoyltransferase, acts as a carbamoyltransferase that mediates 3'-carbamoylation of the noviosyl ring to produce novobiocin, the final step in the novobiocin biosynthesis pathway. Novobiocincin is an aminocoumarin family antibiotic that targets bacterial DNA gyrases. NolNO (EC 2.1.3.-), also called NolO or Y4hD, is involved in the O-carbamoylation of nod factors. Members of this family consist of two domains. The model corresponds to the N-terminal Kae1-like domain.
Pssm-ID: 466949 [Multi-domain] Cd Length: 340 Bit Score: 230.58 E-value: 7.69e-71
N-terminal nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ1051 and ...
2-335
1.84e-65
N-terminal nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ1051 and similar proteins; The family includes a group of uncharacterized proteins similar to Methanocaldococcus jannaschii protein MJ1051 and protein MJ1058. Members of this family consist of two domains. The model corresponds to the N-terminal Kae1-like domain.
Pssm-ID: 466950 [Multi-domain] Cd Length: 238 Bit Score: 212.72 E-value: 1.84e-65
Carbamoyltransferase N-terminus; This domain is found in NodU from Rhizobium, CmcH from ...
14-328
1.68e-38
Carbamoyltransferase N-terminus; This domain is found in NodU from Rhizobium, CmcH from Nocardia lactamdurans and the bifunctional carbamoyltransferase TobZ from Streptoalloteichus tenebrarius. NodU a Rhizobium nodulation protein involved in the synthesis of nodulation factors has 6-O-carbamoyltransferase-like activity. CmcH is involved in cephamycin (antibiotic) biosynthesis and has 3-hydroxymethylcephem carbamoyltransferase activity, EC:2.1.3.7 catalysing the reaction: Carbamoyl phosphate + 3-hydroxymethylceph-3-EM-4-carboxylate <=> phosphate + 3-carbamoyloxymethylcephem. TobZ functions as an ATP carbamoyltransferase and tobramycin carbamoyltransferase. These proteins contain two domains, this is the larger, N-terminal, domain.
Pssm-ID: 426823 [Multi-domain] Cd Length: 352 Bit Score: 144.71 E-value: 1.68e-38
nucleotide-binding domain (NBD) of the Kae1/TsaB-like domain family; The family includes tRNA ...
3-138
4.57e-13
nucleotide-binding domain (NBD) of the Kae1/TsaB-like domain family; The family includes tRNA N6-adenosine threonylcarbamoyltransferase Kae1/TsaD, tRNA threonylcarbamoyladenosine biosynthesis protein TsaB (previously known as YeaZ), as well as proteins from the NodU/CmcH subfamily. tRNA N6-adenosine threonylcarbamoyltransferase (EC 2.3.1.234) is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. TsaB is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It may be involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE. TsaB seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD. The NodU/CmcH family includes NodU from Rhizobium, CmcH from Amycolatopsis lactamdurans, the bifunctional carbamoyltransferase TobZ from Streptoalloteichus tenebrarius, NovN from Streptomyces niveus and NolNO from Sinorhizobium fredii. NodU is a Rhizobium nodulation protein involved in the synthesis of nodulation factors has 6-O-carbamoyltransferase-like activity. 3'-hydroxymethylcephem-O-carbamoyltransferase CmcH (EC 2.1.3.7) is involved in cephamycin (antibiotic) biosynthesis and has 3-hydroxymethylcephem carbamoyltransferase activity. nebramycin 5' synthase TobZ (EC 6.1.2.2) functions as an ATP carbamoyltransferase and tobramycin carbamoyltransferase. Novobiocin biosynthesis protein NovN (EC 2.1.3.12) acts as a carbamoyltransferase that mediates 3'-carbamoylation of the noviosyl ring to produce novobiocin, the final step in the novobiocin biosynthesis pathway. nodulation protein NolNO (EC 2.1.3.-) is involved in the O-carbamoylation of nod factors. The NodU/CmcH subfamily proteins consist of two domains. Only the N-terminal domain shows similarity with Kae1/TsaB-like domain, which belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466851 [Multi-domain] Cd Length: 186 Bit Score: 67.86 E-value: 4.57e-13
N-terminal nucleotide-binding domain (NBD) of nodulation protein U (NodU) and similar proteins; ...
14-328
5.80e-12
N-terminal nucleotide-binding domain (NBD) of nodulation protein U (NodU) and similar proteins; NodU (EC 2.1.3.-) is a Rhizobium nodulation protein involved in the synthesis of nodulation factors has 6-O-carbamoyltransferase-like activity. Members of this family consist of two domains. The model corresponds to the N-terminal Kae1-like domain.
Pssm-ID: 466951 [Multi-domain] Cd Length: 346 Bit Score: 66.98 E-value: 5.80e-12
N-terminal nucleotide-binding domain (NBD) of 3'-hydroxymethylcephem-O-carbamoyltransferase ...
290-327
4.43e-03
N-terminal nucleotide-binding domain (NBD) of 3'-hydroxymethylcephem-O-carbamoyltransferase (CmcH) and similar proteins; CmcH (EC 2.1.3.7), also called 3'-hydroxymethylcephem-O-CASE (CCT), has 3-hydroxymethylcephem carbamoyltransferase activity. It catalyzes the carbamoylation reaction in the cephamycin (antibiotic) biosynthesis. Members of this family consist of two domains. The model corresponds to the N-terminal Kae1-like domain.
Pssm-ID: 466952 [Multi-domain] Cd Length: 316 Bit Score: 39.23 E-value: 4.43e-03
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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