amidohydrolase family protein [Citrobacter sp. Cf136]
Protein Classification
N-acyl-D-amino-acid deacylase family protein( domain architecture ID 10790308)
N-acyl-D-amino-acid deacylase family protein may catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||
| COG3653 | COG3653 | N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
3-528 | 0e+00 | ||||||||
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism]; : Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 691.53 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||||
| COG3653 | COG3653 | N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
3-528 | 0e+00 | ||||||||
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 691.53 E-value: 0e+00
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| D-aminoacylase | cd01297 | D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
2-515 | 2.32e-157 | ||||||||
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics. Pssm-ID: 238622 [Multi-domain] Cd Length: 415 Bit Score: 454.83 E-value: 2.32e-157
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| PRK09061 | PRK09061 | D-glutamate deacylase; Validated |
1-515 | 1.12e-65 | ||||||||
D-glutamate deacylase; Validated Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 221.49 E-value: 1.12e-65
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| Amidohydro_3 | pfam07969 | Amidohydrolase family; |
43-510 | 5.64e-21 | ||||||||
Amidohydrolase family; Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 95.68 E-value: 5.64e-21
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| pyrC_multi | TIGR00857 | dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
21-491 | 3.18e-11 | ||||||||
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis] Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 65.16 E-value: 3.18e-11
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| Name | Accession | Description | Interval | E-value | |||||||||
| COG3653 | COG3653 | N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
3-528 | 0e+00 | |||||||||
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 691.53 E-value: 0e+00
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| D-aminoacylase | cd01297 | D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
2-515 | 2.32e-157 | |||||||||
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics. Pssm-ID: 238622 [Multi-domain] Cd Length: 415 Bit Score: 454.83 E-value: 2.32e-157
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| PRK09061 | PRK09061 | D-glutamate deacylase; Validated |
1-515 | 1.12e-65 | |||||||||
D-glutamate deacylase; Validated Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 221.49 E-value: 1.12e-65
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| Amidohydro_3 | pfam07969 | Amidohydrolase family; |
43-510 | 5.64e-21 | |||||||||
Amidohydrolase family; Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 95.68 E-value: 5.64e-21
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| AllB | COG0044 | Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
4-516 | 4.45e-20 | |||||||||
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis Pssm-ID: 439814 [Multi-domain] Cd Length: 439 Bit Score: 92.85 E-value: 4.45e-20
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| pyrC | PRK09357 | dihydroorotase; Validated |
1-484 | 2.35e-15 | |||||||||
dihydroorotase; Validated Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 78.31 E-value: 2.35e-15
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| HutI | COG1228 | Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
3-510 | 3.24e-13 | |||||||||
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 71.15 E-value: 3.24e-13
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| COG3964 | COG3964 | Predicted amidohydrolase [General function prediction only]; |
4-83 | 9.64e-13 | |||||||||
Predicted amidohydrolase [General function prediction only]; Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 69.81 E-value: 9.64e-13
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| D-HYD | cd01314 | D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
3-65 | 2.24e-11 | |||||||||
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues. Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 65.70 E-value: 2.24e-11
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| pyrC_multi | TIGR00857 | dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
21-491 | 3.18e-11 | |||||||||
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis] Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 65.16 E-value: 3.18e-11
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| PRK09237 | PRK09237 | amidohydrolase/deacetylase family metallohydrolase; |
4-62 | 8.29e-11 | |||||||||
amidohydrolase/deacetylase family metallohydrolase; Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 63.72 E-value: 8.29e-11
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| PRK08323 | PRK08323 | phenylhydantoinase; Validated |
1-65 | 8.74e-11 | |||||||||
phenylhydantoinase; Validated Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 64.04 E-value: 8.74e-11
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| SsnA | COG0402 | Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
2-72 | 1.57e-10 | |||||||||
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 62.92 E-value: 1.57e-10
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| AdeC | COG1001 | Adenine deaminase [Nucleotide transport and metabolism]; |
3-83 | 1.17e-09 | |||||||||
Adenine deaminase [Nucleotide transport and metabolism]; Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 60.88 E-value: 1.17e-09
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| NagA | COG1820 | N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
4-62 | 2.39e-09 | |||||||||
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 59.34 E-value: 2.39e-09
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| NagA | cd00854 | N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
3-62 | 5.92e-09 | |||||||||
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling. Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 57.97 E-value: 5.92e-09
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| PRK07627 | PRK07627 | dihydroorotase; Provisional |
1-79 | 7.21e-09 | |||||||||
dihydroorotase; Provisional Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 57.76 E-value: 7.21e-09
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| L-HYD_ALN | cd01315 | L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
3-62 | 1.77e-08 | |||||||||
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid. Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 56.91 E-value: 1.77e-08
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| DHOase_IIa | cd01317 | Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
429-484 | 6.63e-08 | |||||||||
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth. Pssm-ID: 238642 [Multi-domain] Cd Length: 374 Bit Score: 54.55 E-value: 6.63e-08
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| PRK08044 | PRK08044 | allantoinase AllB; |
3-62 | 1.27e-07 | |||||||||
allantoinase AllB; Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 54.09 E-value: 1.27e-07
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| PRK08204 | PRK08204 | hypothetical protein; Provisional |
1-62 | 1.37e-07 | |||||||||
hypothetical protein; Provisional Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 53.85 E-value: 1.37e-07
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| ATZ_TRZ_like | cd01298 | TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
3-63 | 1.47e-07 | |||||||||
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD. Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 53.75 E-value: 1.47e-07
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| Amidohydro_1 | pfam01979 | Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
411-510 | 1.64e-07 | |||||||||
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included. Pssm-ID: 460401 [Multi-domain] Cd Length: 334 Bit Score: 53.27 E-value: 1.64e-07
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| PRK08393 | PRK08393 | N-ethylammeline chlorohydrolase; Provisional |
1-63 | 1.76e-07 | |||||||||
N-ethylammeline chlorohydrolase; Provisional Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 53.65 E-value: 1.76e-07
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| ade | TIGR01178 | adenine deaminase; The family described by this model includes an experimentally characterized ... |
4-93 | 2.18e-07 | |||||||||
adenine deaminase; The family described by this model includes an experimentally characterized adenine deaminase of Bacillus subtilis. It also include a member from Methanobacterium thermoautotrophicum, in which adenine deaminase activity has been detected. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides] Pssm-ID: 130246 [Multi-domain] Cd Length: 552 Bit Score: 53.62 E-value: 2.18e-07
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| PRK09236 | PRK09236 | dihydroorotase; Reviewed |
1-62 | 4.68e-07 | |||||||||
dihydroorotase; Reviewed Pssm-ID: 181716 Cd Length: 444 Bit Score: 52.18 E-value: 4.68e-07
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| PLN02942 | PLN02942 | dihydropyrimidinase |
2-62 | 5.64e-07 | |||||||||
dihydropyrimidinase Pssm-ID: 178530 Cd Length: 486 Bit Score: 52.15 E-value: 5.64e-07
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| Urease_alpha | cd00375 | Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
1-257 | 6.54e-07 | |||||||||
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, fungi and plants. Their primary role is to allow the use of external and internally generated urea as a nitrogen source. The enzyme consists of 3 subunits, alpha, beta and gamma, which can be fused and present on a single protein chain and which in turn forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers. Pssm-ID: 238221 [Multi-domain] Cd Length: 567 Bit Score: 51.95 E-value: 6.54e-07
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| YtcJ | COG1574 | Predicted amidohydrolase YtcJ [General function prediction only]; |
1-62 | 8.95e-07 | |||||||||
Predicted amidohydrolase YtcJ [General function prediction only]; Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 51.34 E-value: 8.95e-07
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| ureC | PRK13207 | urease subunit alpha; Reviewed |
1-88 | 9.21e-07 | |||||||||
urease subunit alpha; Reviewed Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 51.33 E-value: 9.21e-07
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| FMDH_A | cd01304 | Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
6-78 | 9.69e-07 | |||||||||
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen. Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 51.26 E-value: 9.69e-07
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| PRK07228 | PRK07228 | 5'-deoxyadenosine deaminase; |
1-63 | 2.38e-06 | |||||||||
5'-deoxyadenosine deaminase; Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 50.00 E-value: 2.38e-06
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| PRK06038 | PRK06038 | N-ethylammeline chlorohydrolase; Provisional |
4-62 | 3.32e-06 | |||||||||
N-ethylammeline chlorohydrolase; Provisional Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 49.36 E-value: 3.32e-06
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| PRK12394 | PRK12394 | metallo-dependent hydrolase; |
1-62 | 3.96e-06 | |||||||||
metallo-dependent hydrolase; Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 48.99 E-value: 3.96e-06
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| Bact_CD | cd01293 | Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
4-64 | 5.07e-06 | |||||||||
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric. Pssm-ID: 238618 [Multi-domain] Cd Length: 398 Bit Score: 48.78 E-value: 5.07e-06
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| PRK06380 | PRK06380 | metal-dependent hydrolase; Provisional |
1-67 | 6.12e-06 | |||||||||
metal-dependent hydrolase; Provisional Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 48.73 E-value: 6.12e-06
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| PRK09060 | PRK09060 | dihydroorotase; Validated |
3-62 | 6.78e-06 | |||||||||
dihydroorotase; Validated Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 48.38 E-value: 6.78e-06
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| PLN02303 | PLN02303 | urease |
3-92 | 9.38e-06 | |||||||||
urease Pssm-ID: 215172 [Multi-domain] Cd Length: 837 Bit Score: 48.59 E-value: 9.38e-06
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| PRK13404 | PRK13404 | dihydropyrimidinase; Provisional |
3-64 | 1.13e-05 | |||||||||
dihydropyrimidinase; Provisional Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 47.77 E-value: 1.13e-05
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| PRK09236 | PRK09236 | dihydroorotase; Reviewed |
441-523 | 1.41e-05 | |||||||||
dihydroorotase; Reviewed Pssm-ID: 181716 Cd Length: 444 Bit Score: 47.56 E-value: 1.41e-05
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| Met_dep_hydrolase_C | cd01309 | Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
27-71 | 1.42e-05 | |||||||||
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown. Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 47.31 E-value: 1.42e-05
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| Met_dep_hydrolase_C | cd01309 | Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
435-510 | 1.73e-05 | |||||||||
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown. Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 46.92 E-value: 1.73e-05
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| PRK02382 | PRK02382 | dihydroorotase; Provisional |
6-62 | 2.10e-05 | |||||||||
dihydroorotase; Provisional Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 46.95 E-value: 2.10e-05
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| NagA | COG1820 | N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
436-493 | 2.87e-05 | |||||||||
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 46.25 E-value: 2.87e-05
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| Cyclic_amidohydrolases | cd01302 | Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
431-483 | 4.35e-05 | |||||||||
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines. Pssm-ID: 238627 [Multi-domain] Cd Length: 337 Bit Score: 45.85 E-value: 4.35e-05
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| Imidazolone-5PH | cd01296 | Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
23-62 | 6.09e-05 | |||||||||
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon. Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 45.33 E-value: 6.09e-05
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| Isoaspartyl-dipeptidase | cd01308 | Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
22-104 | 6.34e-05 | |||||||||
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides. Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 45.46 E-value: 6.34e-05
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| PRK15446 | PRK15446 | phosphonate metabolism protein PhnM; Provisional |
440-482 | 7.41e-05 | |||||||||
phosphonate metabolism protein PhnM; Provisional Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 45.17 E-value: 7.41e-05
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| ureC | PRK13206 | urease subunit alpha; Reviewed |
21-92 | 7.70e-05 | |||||||||
urease subunit alpha; Reviewed Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 45.47 E-value: 7.70e-05
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| ureC | PRK13308 | urease subunit alpha; Reviewed |
4-90 | 7.96e-05 | |||||||||
urease subunit alpha; Reviewed Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 45.47 E-value: 7.96e-05
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| Met_dep_hydrolase_B | cd01307 | Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
22-62 | 8.37e-05 | |||||||||
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown. Pssm-ID: 238632 [Multi-domain] Cd Length: 338 Bit Score: 44.63 E-value: 8.37e-05
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| PRK06151 | PRK06151 | N-ethylammeline chlorohydrolase; Provisional |
1-69 | 9.13e-05 | |||||||||
N-ethylammeline chlorohydrolase; Provisional Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 45.03 E-value: 9.13e-05
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| PRK12393 | PRK12393 | amidohydrolase; Provisional |
14-62 | 1.02e-04 | |||||||||
amidohydrolase; Provisional Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 44.67 E-value: 1.02e-04
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| NagA | cd00854 | N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
436-483 | 1.60e-04 | |||||||||
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling. Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 44.11 E-value: 1.60e-04
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| hutI | TIGR01224 | imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
23-62 | 1.68e-04 | |||||||||
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy metabolism, Amino acids and amines] Pssm-ID: 273512 [Multi-domain] Cd Length: 377 Bit Score: 43.94 E-value: 1.68e-04
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| PRK07572 | PRK07572 | cytosine deaminase; Validated |
1-64 | 1.90e-04 | |||||||||
cytosine deaminase; Validated Pssm-ID: 181039 Cd Length: 426 Bit Score: 43.85 E-value: 1.90e-04
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| PRK05985 | PRK05985 | cytosine deaminase; Provisional |
11-64 | 1.99e-04 | |||||||||
cytosine deaminase; Provisional Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 43.77 E-value: 1.99e-04
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| PRK09228 | PRK09228 | guanine deaminase; Provisional |
23-62 | 2.71e-04 | |||||||||
guanine deaminase; Provisional Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 43.26 E-value: 2.71e-04
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| PRK04250 | PRK04250 | dihydroorotase; Provisional |
4-62 | 3.16e-04 | |||||||||
dihydroorotase; Provisional Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 43.22 E-value: 3.16e-04
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| FwdA | COG1229 | Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
439-483 | 5.00e-04 | |||||||||
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; Pssm-ID: 440842 Cd Length: 554 Bit Score: 42.87 E-value: 5.00e-04
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| ATZ_TRZ_like | cd01298 | TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
458-515 | 6.22e-04 | |||||||||
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD. Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 42.19 E-value: 6.22e-04
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| DHOase_IIb | cd01318 | Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
441-483 | 7.93e-04 | |||||||||
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family. Pssm-ID: 238643 [Multi-domain] Cd Length: 361 Bit Score: 41.94 E-value: 7.93e-04
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| PRK09237 | PRK09237 | amidohydrolase/deacetylase family metallohydrolase; |
444-481 | 9.79e-04 | |||||||||
amidohydrolase/deacetylase family metallohydrolase; Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 41.37 E-value: 9.79e-04
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| PRK08203 | PRK08203 | hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
1-62 | 9.81e-04 | |||||||||
hydroxydechloroatrazine ethylaminohydrolase; Reviewed Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 41.76 E-value: 9.81e-04
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| YtcJ_like | cd01300 | YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
22-62 | 1.06e-03 | |||||||||
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling. Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 41.53 E-value: 1.06e-03
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| Met_dep_hydrolase_B | cd01307 | Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
444-481 | 1.21e-03 | |||||||||
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown. Pssm-ID: 238632 [Multi-domain] Cd Length: 338 Bit Score: 41.16 E-value: 1.21e-03
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| PRK06189 | PRK06189 | allantoinase; Provisional |
4-62 | 1.67e-03 | |||||||||
allantoinase; Provisional Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 40.84 E-value: 1.67e-03
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| PRK15446 | PRK15446 | phosphonate metabolism protein PhnM; Provisional |
1-61 | 1.79e-03 | |||||||||
phosphonate metabolism protein PhnM; Provisional Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 40.55 E-value: 1.79e-03
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| PRK08417 | PRK08417 | metal-dependent hydrolase; |
437-510 | 1.89e-03 | |||||||||
metal-dependent hydrolase; Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 40.84 E-value: 1.89e-03
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| Isoaspartyl-dipeptidase | cd01308 | Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
433-491 | 2.74e-03 | |||||||||
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides. Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 40.07 E-value: 2.74e-03
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| PRK07575 | PRK07575 | dihydroorotase; Provisional |
1-62 | 2.92e-03 | |||||||||
dihydroorotase; Provisional Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 40.04 E-value: 2.92e-03
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| PRK07203 | PRK07203 | putative aminohydrolase SsnA; |
4-62 | 3.65e-03 | |||||||||
putative aminohydrolase SsnA; Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 39.92 E-value: 3.65e-03
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| ureB | PRK13985 | urease subunit alpha; |
4-92 | 5.33e-03 | |||||||||
urease subunit alpha; Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 39.49 E-value: 5.33e-03
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| AdeC | cd01295 | Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
47-83 | 5.39e-03 | |||||||||
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea. Pssm-ID: 238620 [Multi-domain] Cd Length: 422 Bit Score: 39.13 E-value: 5.39e-03
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| guan_deamin | TIGR02967 | guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ... |
23-62 | 5.46e-03 | |||||||||
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to xanthine and ammonia. Xanthine can then be converted to urate by xanthine dehydrogenase, and urate subsequently degraded. In some bacteria, the guanine deaminase gene is found near the xdhABC genes for xanthine dehydrogenase. Non-homologous forms of guanine deaminase also exist, as well as distantly related forms outside the scope of this model. [Purines, pyrimidines, nucleosides, and nucleotides, Other] Pssm-ID: 132012 [Multi-domain] Cd Length: 401 Bit Score: 39.16 E-value: 5.46e-03
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| isoAsp_dipep | TIGR01975 | isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically ... |
3-104 | 5.82e-03 | |||||||||
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically over time as a form of protein damage. In this isomerization, the connectivity of the polypeptide changes to pass through the beta-carboxyl of the side chain. Much but not all of this damage can be repaired by protein-L-isoaspartate (D-aspartate) O-methyltransferase. This model describes the isoaspartyl dipeptidase IadA, apparently one of two such enzymes in E. coli, an enzyme that degrades isoaspartyl dipeptides and may unblock degradation of proteins that cannot be repaired. This model also describes closely related proteins from other species (e.g. Clostridium perfringens, Thermoanaerobacter tengcongensis) that we assume to be equivalent in function. This family shows homology to dihydroorotases. [Protein fate, Degradation of proteins, peptides, and glycopeptides] Pssm-ID: 131030 Cd Length: 389 Bit Score: 39.00 E-value: 5.82e-03
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| PhnM | cd01306 | PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ... |
440-483 | 5.89e-03 | |||||||||
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is thought to catalyze the direct cleavage of inactivated C-P bonds to yield inorganic phosphate and the corresponding hydrocarbons. It is responsible for cleavage of alkylphosphonates, which are utilized as sole phosphorus sources by many bacteria. Pssm-ID: 238631 Cd Length: 325 Bit Score: 38.80 E-value: 5.89e-03
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| PRK07369 | PRK07369 | dihydroorotase; Provisional |
1-64 | 5.98e-03 | |||||||||
dihydroorotase; Provisional Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 39.20 E-value: 5.98e-03
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| PRK08203 | PRK08203 | hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
458-515 | 8.44e-03 | |||||||||
hydroxydechloroatrazine ethylaminohydrolase; Reviewed Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 38.68 E-value: 8.44e-03
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| PRK09059 | PRK09059 | dihydroorotase; Validated |
442-484 | 8.65e-03 | |||||||||
dihydroorotase; Validated Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 38.48 E-value: 8.65e-03
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| Blast search parameters | ||||
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