MULTISPECIES: amidohydrolase [Klebsiella]
Protein Classification
amidohydrolase( domain architecture ID 10101347)
metal-dependent amidohydrolase similar to Bacillus subtilis YtcJ and Arthrobacter pascens N-substituted formamide deformylase that catalyzes the hydrolysis of N-benzylformamide (an N-substituted formamide) to benzylamine and formate
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||
| YtcJ_like | cd01300 | YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
26-507 | 3.50e-153 | ||||||||
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: 449.84 E-value: 3.50e-153
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| Name | Accession | Description | Interval | E-value | ||||||||
| YtcJ_like | cd01300 | YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
26-507 | 3.50e-153 | ||||||||
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: 449.84 E-value: 3.50e-153
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| YtcJ | COG1574 | Predicted amidohydrolase YtcJ [General function prediction only]; |
2-539 | 2.51e-148 | ||||||||
Predicted amidohydrolase YtcJ [General function prediction only]; Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 439.23 E-value: 2.51e-148
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| Amidohydro_3 | pfam07969 | Amidohydrolase family; |
52-536 | 5.15e-121 | ||||||||
Amidohydrolase family; Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 366.86 E-value: 5.15e-121
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| PRK09228 | PRK09228 | guanine deaminase; Provisional |
26-71 | 1.65e-06 | ||||||||
guanine deaminase; Provisional Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 50.96 E-value: 1.65e-06
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| pyrC_multi | TIGR00857 | dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
26-79 | 6.48e-03 | ||||||||
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: 39.35 E-value: 6.48e-03
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| Name | Accession | Description | Interval | E-value | |||||||||
| YtcJ_like | cd01300 | YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
26-507 | 3.50e-153 | |||||||||
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: 449.84 E-value: 3.50e-153
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| YtcJ | COG1574 | Predicted amidohydrolase YtcJ [General function prediction only]; |
2-539 | 2.51e-148 | |||||||||
Predicted amidohydrolase YtcJ [General function prediction only]; Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 439.23 E-value: 2.51e-148
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| Amidohydro_3 | pfam07969 | Amidohydrolase family; |
52-536 | 5.15e-121 | |||||||||
Amidohydrolase family; Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 366.86 E-value: 5.15e-121
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| HutI | COG1228 | Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
2-538 | 1.11e-17 | |||||||||
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 85.40 E-value: 1.11e-17
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| SsnA | COG0402 | Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
6-537 | 6.12e-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: 61.77 E-value: 6.12e-10
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| COG3964 | COG3964 | Predicted amidohydrolase [General function prediction only]; |
7-94 | 8.66e-09 | |||||||||
Predicted amidohydrolase [General function prediction only]; Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 57.87 E-value: 8.66e-09
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| Imidazolone-5PH | cd01296 | Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
27-89 | 2.65e-08 | |||||||||
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: 56.11 E-value: 2.65e-08
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| AdeC | COG1001 | Adenine deaminase [Nucleotide transport and metabolism]; |
5-71 | 2.46e-07 | |||||||||
Adenine deaminase [Nucleotide transport and metabolism]; Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 53.57 E-value: 2.46e-07
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| PRK09228 | PRK09228 | guanine deaminase; Provisional |
26-71 | 1.65e-06 | |||||||||
guanine deaminase; Provisional Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 50.96 E-value: 1.65e-06
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| ATZ_TRZ_like | cd01298 | TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
7-72 | 1.81e-06 | |||||||||
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: 50.66 E-value: 1.81e-06
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| PRK09237 | PRK09237 | amidohydrolase/deacetylase family metallohydrolase; |
7-71 | 1.94e-06 | |||||||||
amidohydrolase/deacetylase family metallohydrolase; Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 50.23 E-value: 1.94e-06
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| AllB | COG0044 | Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
8-72 | 3.68e-06 | |||||||||
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: 49.70 E-value: 3.68e-06
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| Isoaspartyl-dipeptidase | cd01308 | Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
27-76 | 4.95e-06 | |||||||||
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: 49.31 E-value: 4.95e-06
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| Amidohydro_1 | pfam01979 | Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
417-535 | 2.63e-05 | |||||||||
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: 46.73 E-value: 2.63e-05
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| PRK09060 | PRK09060 | dihydroorotase; Validated |
1-77 | 4.54e-05 | |||||||||
dihydroorotase; Validated Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 46.07 E-value: 4.54e-05
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| NagA | cd00854 | N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
26-96 | 4.78e-05 | |||||||||
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: 46.03 E-value: 4.78e-05
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| PRK12394 | PRK12394 | metallo-dependent hydrolase; |
7-94 | 4.94e-05 | |||||||||
metallo-dependent hydrolase; Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 45.91 E-value: 4.94e-05
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| PRK05985 | PRK05985 | cytosine deaminase; Provisional |
24-72 | 5.57e-05 | |||||||||
cytosine deaminase; Provisional Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 45.69 E-value: 5.57e-05
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| PRK08204 | PRK08204 | hypothetical protein; Provisional |
5-75 | 8.87e-05 | |||||||||
hypothetical protein; Provisional Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 45.38 E-value: 8.87e-05
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| L-HYD_ALN | cd01315 | L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
27-87 | 9.70e-05 | |||||||||
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: 45.36 E-value: 9.70e-05
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| PRK07203 | PRK07203 | putative aminohydrolase SsnA; |
7-75 | 1.86e-04 | |||||||||
putative aminohydrolase SsnA; Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 44.16 E-value: 1.86e-04
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| NagA | COG1820 | N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
8-71 | 3.40e-04 | |||||||||
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 43.16 E-value: 3.40e-04
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| Met_dep_hydrolase_B | cd01307 | Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
26-90 | 3.93e-04 | |||||||||
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: 43.09 E-value: 3.93e-04
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| GDEase | cd01303 | Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
26-71 | 4.67e-04 | |||||||||
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool. Pssm-ID: 238628 [Multi-domain] Cd Length: 429 Bit Score: 43.04 E-value: 4.67e-04
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| PRK06038 | PRK06038 | N-ethylammeline chlorohydrolase; Provisional |
4-75 | 5.00e-04 | |||||||||
N-ethylammeline chlorohydrolase; Provisional Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 42.82 E-value: 5.00e-04
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| PRK08323 | PRK08323 | phenylhydantoinase; Validated |
27-72 | 5.65e-04 | |||||||||
phenylhydantoinase; Validated Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 42.85 E-value: 5.65e-04
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| PRK08044 | PRK08044 | allantoinase AllB; |
27-87 | 5.87e-04 | |||||||||
allantoinase AllB; Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 42.54 E-value: 5.87e-04
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| D-HYD | cd01314 | D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
7-72 | 8.91e-04 | |||||||||
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: 42.20 E-value: 8.91e-04
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| pyrC | PRK09357 | dihydroorotase; Validated |
6-72 | 1.05e-03 | |||||||||
dihydroorotase; Validated Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 41.72 E-value: 1.05e-03
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| metallo-dependent_hydrolases | cd01292 | Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
215-454 | 1.62e-03 | |||||||||
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is 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 family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others. Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 40.78 E-value: 1.62e-03
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| PRK09045 | PRK09045 | TRZ/ATZ family hydrolase; |
1-75 | 2.18e-03 | |||||||||
TRZ/ATZ family hydrolase; Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 41.05 E-value: 2.18e-03
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| Bact_CD | cd01293 | Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
27-72 | 5.92e-03 | |||||||||
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: 39.54 E-value: 5.92e-03
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| Met_dep_hydrolase_C | cd01309 | Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
31-88 | 5.95e-03 | |||||||||
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: 39.22 E-value: 5.95e-03
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| PRK07228 | PRK07228 | 5'-deoxyadenosine deaminase; |
6-72 | 6.01e-03 | |||||||||
5'-deoxyadenosine deaminase; Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 39.60 E-value: 6.01e-03
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| pyrC_multi | TIGR00857 | dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
26-79 | 6.48e-03 | |||||||||
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: 39.35 E-value: 6.48e-03
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| D-aminoacylase | cd01297 | D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
21-86 | 7.46e-03 | |||||||||
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: 39.20 E-value: 7.46e-03
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| PRK09059 | PRK09059 | dihydroorotase; Validated |
27-72 | 7.47e-03 | |||||||||
dihydroorotase; Validated Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 39.25 E-value: 7.47e-03
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| Blast search parameters | ||||
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