MULTISPECIES: amidohydrolase [Klebsiella]
Protein Classification
amidohydrolase( domain architecture ID 11446324)
metal-dependent amidohydrolase similar to Bacillus subtilis YtcJ and Arthrobacter pascens N-substituted formamide deformylase, which catalyzes the hydrolysis of N-substituted formamides
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||||
| YtcJ | COG1574 | Predicted amidohydrolase YtcJ [General function prediction only]; |
7-567 | 1.41e-168 | |||||||||
Predicted amidohydrolase YtcJ [General function prediction only]; : Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 489.31 E-value: 1.41e-168
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| Name | Accession | Description | Interval | E-value | |||||||||
| YtcJ | COG1574 | Predicted amidohydrolase YtcJ [General function prediction only]; |
7-567 | 1.41e-168 | |||||||||
Predicted amidohydrolase YtcJ [General function prediction only]; Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 489.31 E-value: 1.41e-168
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| YtcJ_like | cd01300 | YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
28-535 | 1.73e-115 | |||||||||
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: 351.23 E-value: 1.73e-115
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| Amidohydro_3 | pfam07969 | Amidohydrolase family; |
54-566 | 1.48e-63 | |||||||||
Amidohydrolase family; Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 215.47 E-value: 1.48e-63
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| PRK13404 | PRK13404 | dihydropyrimidinase; Provisional |
8-74 | 3.11e-06 | |||||||||
dihydropyrimidinase; Provisional Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 49.70 E-value: 3.11e-06
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| Name | Accession | Description | Interval | E-value | |||||||||
| YtcJ | COG1574 | Predicted amidohydrolase YtcJ [General function prediction only]; |
7-567 | 1.41e-168 | |||||||||
Predicted amidohydrolase YtcJ [General function prediction only]; Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 489.31 E-value: 1.41e-168
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| YtcJ_like | cd01300 | YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
28-535 | 1.73e-115 | |||||||||
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: 351.23 E-value: 1.73e-115
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| Amidohydro_3 | pfam07969 | Amidohydrolase family; |
54-566 | 1.48e-63 | |||||||||
Amidohydrolase family; Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 215.47 E-value: 1.48e-63
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| Amidohydro_1 | pfam01979 | Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
343-565 | 2.61e-12 | |||||||||
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: 68.30 E-value: 2.61e-12
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| HutI | COG1228 | Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
352-568 | 2.76e-11 | |||||||||
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 65.37 E-value: 2.76e-11
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| Met_dep_hydrolase_A | cd01299 | Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
362-541 | 9.02e-08 | |||||||||
Metallo-dependent hydrolases, subgroup A 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: 238624 [Multi-domain] Cd Length: 342 Bit Score: 54.22 E-value: 9.02e-08
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| AdeC | COG1001 | Adenine deaminase [Nucleotide transport and metabolism]; |
7-74 | 2.80e-07 | |||||||||
Adenine deaminase [Nucleotide transport and metabolism]; Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 53.18 E-value: 2.80e-07
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| NagA | COG1820 | N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
501-563 | 2.50e-06 | |||||||||
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 49.71 E-value: 2.50e-06
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| Imidazolone-5PH | cd01296 | Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
454-539 | 2.92e-06 | |||||||||
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: 49.56 E-value: 2.92e-06
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| SsnA | COG0402 | Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
453-568 | 3.00e-06 | |||||||||
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: 49.83 E-value: 3.00e-06
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| PRK13404 | PRK13404 | dihydropyrimidinase; Provisional |
8-74 | 3.11e-06 | |||||||||
dihydropyrimidinase; Provisional Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 49.70 E-value: 3.11e-06
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| PRK07228 | PRK07228 | 5'-deoxyadenosine deaminase; |
455-568 | 9.01e-06 | |||||||||
5'-deoxyadenosine deaminase; Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 48.46 E-value: 9.01e-06
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| ATZ_TRZ_like | cd01298 | TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
454-568 | 1.67e-05 | |||||||||
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: 47.20 E-value: 1.67e-05
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| Met_dep_hydrolase_C | cd01309 | Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
502-566 | 2.73e-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: 46.54 E-value: 2.73e-05
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| PRK09228 | PRK09228 | guanine deaminase; Provisional |
28-73 | 3.77e-05 | |||||||||
guanine deaminase; Provisional Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 46.34 E-value: 3.77e-05
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| SsnA | COG0402 | Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
8-73 | 7.19e-05 | |||||||||
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: 45.20 E-value: 7.19e-05
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| NagA | cd00854 | N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
501-562 | 7.65e-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: 45.26 E-value: 7.65e-05
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| PRK07203 | PRK07203 | putative aminohydrolase SsnA; |
13-74 | 7.77e-05 | |||||||||
putative aminohydrolase SsnA; Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 45.31 E-value: 7.77e-05
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| D-HYD | cd01314 | D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
13-74 | 1.88e-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: 44.13 E-value: 1.88e-04
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| L-HYD_ALN | cd01315 | L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
8-74 | 4.19e-04 | |||||||||
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: 43.05 E-value: 4.19e-04
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| AllB | COG0044 | Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
10-75 | 6.64e-04 | |||||||||
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: 42.39 E-value: 6.64e-04
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| GDEase | cd01303 | Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
28-73 | 9.35e-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: 41.88 E-value: 9.35e-04
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| Imidazolone-5PH | cd01296 | Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
29-76 | 9.78e-04 | |||||||||
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: 41.47 E-value: 9.78e-04
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| PRK08204 | PRK08204 | hypothetical protein; Provisional |
488-564 | 1.86e-03 | |||||||||
hypothetical protein; Provisional Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 40.76 E-value: 1.86e-03
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| PRK09237 | PRK09237 | amidohydrolase/deacetylase family metallohydrolase; |
10-83 | 2.96e-03 | |||||||||
amidohydrolase/deacetylase family metallohydrolase; Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 40.22 E-value: 2.96e-03
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| metallo-dependent_hydrolases | cd01292 | Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
310-515 | 4.91e-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: 39.24 E-value: 4.91e-03
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| ureC | PRK13309 | urease subunit alpha; Reviewed |
458-545 | 7.77e-03 | |||||||||
urease subunit alpha; Reviewed Pssm-ID: 183966 [Multi-domain] Cd Length: 572 Bit Score: 39.09 E-value: 7.77e-03
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| Urease_alpha | cd00375 | Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
510-545 | 8.46e-03 | |||||||||
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: 38.85 E-value: 8.46e-03
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| Blast search parameters | ||||
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