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Conserved domains on  [gi|1141055502|ref|WP_076879552|]
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amidohydrolase family protein [Bordetella pertussis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YtcJ super family cl34308
Predicted amidohydrolase YtcJ [General function prediction only];
1-113 5.43e-48

Predicted amidohydrolase YtcJ [General function prediction only];


The actual alignment was detected with superfamily member COG1574:

Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 160.73  E-value: 5.43e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141055502   1 MLDRGVLVCAHSDAPVCERNPFLGMWSMVTRKTASGASLGAGQAITPLEAMRCYTANPARAEGQAARKGTLSPGKLADLI 80
Cdd:COG1574   423 LLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRTPSGRGLGPEERLTVEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFV 502

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1141055502  81 VLDRDPCAVDPDEIRHTQVLATLVGGQATYRAA 113
Cdd:COG1574   503 VLDRDPLTVPPEEIKDIKVLLTVVGGRVVYEAE 535
 
Name Accession Description Interval E-value
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
1-113 5.43e-48

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 160.73  E-value: 5.43e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141055502   1 MLDRGVLVCAHSDAPVCERNPFLGMWSMVTRKTASGASLGAGQAITPLEAMRCYTANPARAEGQAARKGTLSPGKLADLI 80
Cdd:COG1574   423 LLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRTPSGRGLGPEERLTVEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFV 502

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1141055502  81 VLDRDPCAVDPDEIRHTQVLATLVGGQATYRAA 113
Cdd:COG1574   503 VLDRDPLTVPPEEIKDIKVLLTVVGGRVVYEAE 535
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 1-81 1.08e-29

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: 110.86  E-value: 1.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141055502   1 MLDRGVLVCAHSDAPVCERNPFLGMWSMVTRKTASGASLG-AGQAITPLEAMRCYTANPARAEGQAARKGTLSPGKLADL 79
Cdd:cd01300   398 LLDAGVPVALGSDAPVAPPDPLLGIWAAVTRKTPGGGVLGnPEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGKLADF 477


                  ..
gi 1141055502  80 IV 81
Cdd:cd01300   478 VV 479
Amidohydro_3 pfam07969
Amidohydrolase family;
1-110 7.10e-28

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 105.69  E-value: 7.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141055502   1 MLDRGVLVCAHSDAPVCERNPFLGMWSMVTRKTA-SGASLGAGQAITPLEAMRCYTANPARAEGQAARKGTLSPGKLADL 79
Cdd:pfam07969 354 LLNAGVKVALGSDAPVGPFDPWPRIGAAVMRQTAgGGEVLGPDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADL 433

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1141055502  80 IVLDRDPCAVDPDEIRHTQVLATLVGGQATY 110
Cdd:pfam07969 434 VVLDDDPLTVDPPAIADIRVRLTVVDGRVVY 464
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
 41-113 2.05e-06

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 45.17  E-value: 2.05e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1141055502  41 AGQAITPL-EAMRCYTANPARAEGQAARkGTLSPGKLADLIVLDRDPcavdpdeiRHTQVLATLVGGQATYRAA 113
Cdd:PRK15446  319 ADDGGLDLpQAVALVTANPARAAGLDDR-GEIAPGKRADLVRVRRAG--------GLPVVRAVWRGGRRVFLAG 383
 
Name Accession Description Interval E-value
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
1-113 5.43e-48

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 160.73  E-value: 5.43e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141055502   1 MLDRGVLVCAHSDAPVCERNPFLGMWSMVTRKTASGASLGAGQAITPLEAMRCYTANPARAEGQAARKGTLSPGKLADLI 80
Cdd:COG1574   423 LLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRTPSGRGLGPEERLTVEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFV 502

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1141055502  81 VLDRDPCAVDPDEIRHTQVLATLVGGQATYRAA 113
Cdd:COG1574   503 VLDRDPLTVPPEEIKDIKVLLTVVGGRVVYEAE 535
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 1-81 1.08e-29

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: 110.86  E-value: 1.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141055502   1 MLDRGVLVCAHSDAPVCERNPFLGMWSMVTRKTASGASLG-AGQAITPLEAMRCYTANPARAEGQAARKGTLSPGKLADL 79
Cdd:cd01300   398 LLDAGVPVALGSDAPVAPPDPLLGIWAAVTRKTPGGGVLGnPEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGKLADF 477


                  ..
gi 1141055502  80 IV 81
Cdd:cd01300   478 VV 479
Amidohydro_3 pfam07969
Amidohydrolase family;
1-110 7.10e-28

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 105.69  E-value: 7.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141055502   1 MLDRGVLVCAHSDAPVCERNPFLGMWSMVTRKTA-SGASLGAGQAITPLEAMRCYTANPARAEGQAARKGTLSPGKLADL 79
Cdd:pfam07969 354 LLNAGVKVALGSDAPVGPFDPWPRIGAAVMRQTAgGGEVLGPDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADL 433

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1141055502  80 IVLDRDPCAVDPDEIRHTQVLATLVGGQATY 110
Cdd:pfam07969 434 VVLDDDPLTVDPPAIADIRVRLTVVDGRVVY 464
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 1-112 3.58e-12

Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 61.52  E-value: 3.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141055502   1 MLDRGVLVCAHSDAPVcERNPFLGMWSMVTRKTASGaslgagqaITPLEAMRCYTANPARAEGQAARKGTLSPGKLADLI 80
Cdd:COG1228   287 LHDAGVPVALGTDAGV-GVPPGRSLHRELALAVEAG--------LTPEEALRAATINAAKALGLDDDVGSLEPGKLADLV 357

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1141055502  81 VLDRDPcavdPDEIRHTQ-VLATLVGGQATYRA 112
Cdd:COG1228   358 LLDGDP----LEDIAYLEdVRAVMKDGRVVDRS 386
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 1-107 2.12e-10

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: 56.36  E-value: 2.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141055502   1 MLDRGVLVCAHSDAPVCERNPflgmwSMVTR-KTASGASLGAGQAITPLEAMRCYTANPARAEGQAARKGTLSPGKLADL 79
Cdd:pfam01979 230 ALEDGVKVGLGTDGAGSGNSL-----NMLEElRLALELQFDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADL 304

                          90       100
                  ....*....|....*....|....*...
gi 1141055502  80 IVLDRDPCAVDPDEIRHTQVLATLVGGQ 107
Cdd:pfam01979 305 VVVDLDPLAAFFGLKPDGNVKKVIVKGK 332
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
45-107 6.44e-09

N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 52.41  E-value: 6.44e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1141055502  45 ITPLEAMRCYTANPARAEGQAARKGTLSPGKLADLIVLDRDpcavdpdeirhTQVLATLVGGQ 107
Cdd:COG1820   322 LPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD-----------LNVRATWVGGE 373
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 37-110 2.46e-08

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: 50.77  E-value: 2.46e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1141055502  37 ASLGAGQAITPLEAMRCYTANPARAEGQAARKGTLSPGKLADLIVLDRDPCAVDpdeirhTQVLATLVGGQATY 110
Cdd:cd01309   292 AAKAVKYGLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWNGDPLEPT------SKPEQVYIDGRLVY 359
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 46-86 5.69e-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: 49.60  E-value: 5.69e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1141055502  46 TPLEAMRCYTANPARAEGQAARKGTLSPGKLADLIVLDRDP 86
Cdd:cd01299   295 TPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVDGDP 335
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 1-111 9.44e-08

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: 49.05  E-value: 9.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141055502   1 MLDRGVLVCAHSDAPVCerNPFLGMWS-MvtrKTASG---ASLGAGQAITPLEAMRCYTANPARAEGQAARKGTLSPGKL 76
Cdd:COG0402   297 LLAAGVRVGLGTDGAAS--NNSLDMFEeM---RLAALlqrLRGGDPTALSAREALEMATLGGARALGLDDEIGSLEPGKR 371

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1141055502  77 ADLIVLDRDPCAVDP--DEIRH-------TQVLATLVGGQATYR 111
Cdd:COG0402   372 ADLVVLDLDAPHLAPlhDPLSAlvyaadgRDVRTVWVAGRVVVR 415
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 45-106 3.64e-07

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: 47.19  E-value: 3.64e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1141055502  45 ITPLEAMRCYTANPARAEGQAARKGTLSPGKLADLIVLDRDpcavdpdeirhTQVLATLVGG 106
Cdd:cd00854   324 CPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDD-----------LNVKATWING 374
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
 43-111 1.42e-06

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: 45.75  E-value: 1.42e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1141055502  43 QAITPLEAMRCYTANPARAEGQAARkGTLSPGKLADLIVLDRDPCAVDPDEIRHTQ----VLATLVGGQATYR 111
Cdd:cd01297   333 KLLSLEEAVRKMTGLPARVFGLADR-GRIAPGYRADIVVFDPDTLADRATFTRPNQpaegIEAVLVNGVPVVR 404
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
 41-113 2.05e-06

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 45.17  E-value: 2.05e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1141055502  41 AGQAITPL-EAMRCYTANPARAEGQAARkGTLSPGKLADLIVLDRDPcavdpdeiRHTQVLATLVGGQATYRAA 113
Cdd:PRK15446  319 ADDGGLDLpQAVALVTANPARAAGLDDR-GEIAPGKRADLVRVRRAG--------GLPVVRAVWRGGRRVFLAG 383
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 46-83 4.28e-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: 44.17  E-value: 4.28e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1141055502  46 TPLEAMRCYTANPARAEGQAARKGTLSPGKLADLIVLD 83
Cdd:cd01296   311 TPEEALTAATINAAAALGLGETVGSLEVGKQADLVILD 348
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
 33-107 4.36e-06

N-acetylglucosamine-6-phosphate deacetylase; Provisional


Pssm-ID: 183010  Cd Length: 382  Bit Score: 44.20  E-value: 4.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141055502  33 TASGASLGAGQAIT--------PL-EAMRCYTANPARAEGQAARKGTLSPGKLADLIVLDRDpcavdpdeirhTQVLATL 103
Cdd:PRK11170  305 TLSGSALTMIEAVRnlvehvgiALdEALRMATLYPARAIGVDKRLGSIEAGKVANLTAFTRD-----------FKITKTI 373


                  ....
gi 1141055502 104 VGGQ 107
Cdd:PRK11170  374 VNGN 377
PRK08204 PRK08204
hypothetical protein; Provisional
 45-85 1.15e-05

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 43.07  E-value: 1.15e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1141055502  45 ITPLEAMRCYTANPARAEGQAARKGTLSPGKLADLIVLDRD 85
Cdd:PRK08204  342 LTARQVLEWATIEGARALGLEDRIGSLTPGKQADLVLIDAT 382
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 45-111 1.25e-05

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: 42.77  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141055502  45 ITPLEAMRCYTANPARAEGQAaRKGTLSPGKLADLIVLDRD-PCAVDPDEIRHT-------------QVLATLVGGQATY 110
Cdd:COG0044   345 LSLERLVELLSTNPARIFGLP-RKGRIAVGADADLVLFDPDaEWTVTAEDLHSKskntpfegreltgRVVATIVRGRVVY 423


                  .
gi 1141055502 111 R 111
Cdd:COG0044   424 E 424
PRK09228 PRK09228
guanine deaminase; Provisional
 42-119 5.87e-05

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 40.94  E-value: 5.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141055502  42 GQAITPLEAMRCYTANPARAEGQAARKGTLSPGKLADLIVLdrDPCAVDPDEIRHTQ---------VLATLVGGQATYR- 111
Cdd:PRK09228  345 GYRLSPFQAFYLATLGGARALGLDDRIGNLAPGKEADFVVL--DPAATPLLALRTARaesleellfALMTLGDDRAVAEt 422


                  ....*....
gi 1141055502 112 -AAGAPSWA 119
Cdd:PRK09228  423 yVAGRPVYR 431
PRK12394 PRK12394
metallo-dependent hydrolase;
47-111 6.52e-05

metallo-dependent hydrolase;


Pssm-ID: 183497 [Multi-domain]  Cd Length: 379  Bit Score: 40.90  E-value: 6.52e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1141055502  47 PLE-AMRCYTANPARAEGQAARKGTLSPGKLADL-IVLDRDPCAVDPDEIRHT----QVL---ATLVGGQATYR 111
Cdd:PRK12394  302 ALEdVINACTHTPAVLMGMAAEIGTLAPGAFADIaIFKLKNRHVEFADIHGETltgtHVLvpqMTIKSGEILYR 375
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
2-85 8.35e-05

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 40.37  E-value: 8.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141055502   2 LDRGVLVCAHSDAPVCERN--PFLGMwsmvtrKTAS----GASLGAgQAITPLEAMRCYTANPARAEGQAARKGTLSPGK 75
Cdd:PRK07228  295 LERGINVALGADGAPCNNTldPFTEM------RQAAliqkVDRLGP-TAMPARTVFEMATLGGAKAAGFEDEIGSLEEGK 367

                          90
                  ....*....|
gi 1141055502  76 LADLIVLDRD 85
Cdd:PRK07228  368 KADLAILDLD 377
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 56-117 2.61e-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: 39.19  E-value: 2.61e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1141055502  56 ANPARAEGQAARKGTLSPGKLADLIVLDRDP-CAVDPDEIRHT-------------QVLATLVGGQATYRAAGAPS 117
Cdd:cd01315   364 ENPAKLFGLSHQKGRIAVGYDADFVVWDPEEeFTVDAEDLYYKnkispyvgrtlkgRVHATILRGTVVYQDGEVVG 439
PRK06038 PRK06038
N-ethylammeline chlorohydrolase; Provisional
 1-83 3.14e-04

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180363 [Multi-domain]  Cd Length: 430  Bit Score: 38.96  E-value: 3.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141055502   1 MLDRGVLVCAHSDApvCERNPFLGMWSMVtrKTAS---GASLGAGQAITPLEAMRCYTANPARAEGQAArkGTLSPGKLA 77
Cdd:PRK06038  285 LLERGVNVSLGTDG--CASNNNLDMFEEM--KTAAllhKVNTMDPTALPARQVLEMATVNGAKALGINT--GMLKEGYLA 358


                  ....*.
gi 1141055502  78 DLIVLD 83
Cdd:PRK06038  359 DIIIVD 364
Urease_alpha cd00375
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ...
 54-117 3.75e-04

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: 3.75e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1141055502  54 YTANPARAEGQAARKGTLSPGKLADLIVLDRDPCAVDPDEIrhtqvlatLVGGQATYRAAGAPS 117
Cdd:cd00375   408 YTINPAIAHGISHEVGSVEVGKLADLVLWEPAFFGVKPEMV--------LKGGFIAYAQMGDPN 463
PhnM cd01306
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ...
 49-106 4.60e-04

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: 38.42  E-value: 4.60e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1141055502  49 EAMRCYTANPARAEGQAARkGTLSPGKLADLIVLDRDPcavdpdeiRHTQVLATLVGG 106
Cdd:cd01306   277 EAVALVSANPARAVGLTDR-GSIAPGKRADLILVDDMD--------GVPVVRTVWRGG 325
ureC PRK13206
urease subunit alpha; Reviewed
 54-117 8.47e-04

urease subunit alpha; Reviewed


Pssm-ID: 237304 [Multi-domain]  Cd Length: 573  Bit Score: 37.77  E-value: 8.47e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1141055502  54 YTANPARAEGQAARKGTLSPGKLADLIVLDRDPCAVDPDeirhtqvlATLVGGQATYRAAGAPS 117
Cdd:PRK13206  413 YTICPAVAHGIDHEIGSVEVGKLADLVLWEPAFFGVRPH--------AVLKGGAIAWAAMGDAN 468
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
 47-85 1.11e-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: 37.37  E-value: 1.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1141055502  47 PLE-AMRCYTANPARAEgQAARKGTLSPGKLADLIVLDRD 85
Cdd:cd01308   323 PLEvALRVITSNVARIL-KLRKKGEIQPGFDADLVILDKD 361
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 1-85 1.35e-03

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: 37.18  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141055502   1 MLDRGVLVCAHSDAPVCerNPFLGMWSMVtrKTASG---ASLGAGQAITPLEAMRCYTANPARAEGqaaRK--GTLSPGK 75
Cdd:cd01298   289 MLEAGVNVGLGTDGAAS--NNNLDMFEEM--RLAALlqkLAHGDPTALPAEEALEMATIGGAKALG---LDeiGSLEVGK 361

                          90
                  ....*....|
gi 1141055502  76 LADLIVLDRD 85
Cdd:cd01298   362 KADLILIDLD 371
ureC PRK13308
urease subunit alpha; Reviewed
 54-84 1.47e-03

urease subunit alpha; Reviewed


Pssm-ID: 183965 [Multi-domain]  Cd Length: 569  Bit Score: 36.99  E-value: 1.47e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1141055502  54 YTANPARAEGQAARKGTLSPGKLADLIVLDR 84
Cdd:PRK13308  409 YTINPAITFGIDDHIGSLEPGKLADIVLWRP 439
PRK09059 PRK09059
dihydroorotase; Validated
 58-112 1.48e-03

dihydroorotase; Validated


Pssm-ID: 181631 [Multi-domain]  Cd Length: 429  Bit Score: 36.94  E-value: 1.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1141055502  58 PARAEGQAArkGTLSPGKLADLIVLDRD-PCAVDPDEI----RHT---------QVLATLVGGQATYRA 112
Cdd:PRK09059  363 PAEIFGLPA--GTLKPGAPADIIVIDLDePWVVDPEDLksrsKNTpfeearfqgRVVRTIVAGKTVYEL 429
ureC PRK13207
urease subunit alpha; Reviewed
 54-81 1.49e-03

urease subunit alpha; Reviewed


Pssm-ID: 237305 [Multi-domain]  Cd Length: 568  Bit Score: 37.08  E-value: 1.49e-03
                          10        20
                  ....*....|....*....|....*...
gi 1141055502  54 YTANPARAEGQAARKGTLSPGKLADLIV 81
Cdd:PRK13207  408 YTINPAIAHGISHEVGSVEVGKLADLVL 435
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
30-83 1.54e-03

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 36.81  E-value: 1.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1141055502  30 TRKTASGASLGAGQA--ITPLEAMRCYTANPARAEGQAARKGTLSPGKLADLIVLD 83
Cdd:PRK09045  323 MRTAALLAKAVAGDAtaLPAHTALRMATLNGARALGLDDEIGSLEPGKQADLVAVD 378
AdeC cd01295
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ...
 43-101 1.66e-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: 36.82  E-value: 1.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1141055502  43 QAITPLEAMRCYTANPARAEGqAARKGTLSPGKLADLIVLDrdpcavDPDEIRHTQVLA 101
Cdd:cd01295   233 AGIPPEDAIQMATINPAECYG-LHDLGAIAPGRIADIVILD------DLENFNITTVLA 284
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
49-119 2.23e-03

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 36.37  E-value: 2.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1141055502  49 EAMRCYTANPARAEGQAaRKGTLSPGKLADLIVLD--RDPC-AVDP--DEIRHTQVL---ATLVGGQATYRAAGAPSWA 119
Cdd:PRK09237  300 EVIAAVTKNAADALRLP-ELGRLQVGSDADLTLFTlkDGPFtLTDSegDSLIGERLLtplATVRGGKVVLTEQGSAEHA 377
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
47-83 2.42e-03

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 36.23  E-value: 2.42e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1141055502  47 PLEAMRCYTANPARAEGqAARKGTLSPGKLADLIVLD 83
Cdd:COG1001   286 PVTAIQMATLNAAEHFG-LKDLGAIAPGRRADIVLLD 321
UreC COG0804
Urease alpha subunit [Amino acid transport and metabolism];
54-116 2.77e-03

Urease alpha subunit [Amino acid transport and metabolism];


Pssm-ID: 440567 [Multi-domain]  Cd Length: 570  Bit Score: 36.27  E-value: 2.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1141055502  54 YTANPARAEGQAARKGTLSPGKLADLIVLDRDPCAVDPDEIrhtqvlatLVGGQATYRAAGAP 116
Cdd:COG0804   410 YTINPAIAHGISHEVGSVEVGKLADLVLWDPAFFGVKPELV--------IKGGMIAWAQMGDP 464
PRK07627 PRK07627
dihydroorotase; Provisional
 41-110 3.44e-03

dihydroorotase; Provisional


Pssm-ID: 181059 [Multi-domain]  Cd Length: 425  Bit Score: 35.81  E-value: 3.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141055502  41 AGQAITPL-EAMRCYTANPARAEGQAArkGTLSPGKLADLIVLDRDP-CAVDPDEIR----HT---------QVLATLVG 105
Cdd:PRK07627  340 ADEAKVPLaRALARITSAPARVLGLPA--GRLAEGAPADLCVFDPDAhWRVEPRALKsqgkNTpflgyelpgRVRATLVA 417


                  ....*
gi 1141055502 106 GQATY 110
Cdd:PRK07627  418 GQVAF 422
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
 1-107 4.15e-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: 35.69  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1141055502   1 MLDRGVLVCAHSDapvCERNPF--LGMWSMVTRktaSGASLGAGQAITPLEAMRCY---TANPARAEGQAarKGTLSPGK 75
Cdd:cd01293   295 LRAAGVNVALGSD---NVRDPWypFGSGDMLEV---ANLAAHIAQLGTPEDLALALdliTGNAARALGLE--DYGIKVGC 366

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1141055502  76 LADLIVLDrdpcAVDPDEI--RHTQVLATLVGGQ 107
Cdd:cd01293   367 PADLVLLD----AEDVAEAvaRQPPRRVVIRKGR 396
PRK02382 PRK02382
dihydroorotase; Provisional
 47-95 7.44e-03

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 35.01  E-value: 7.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1141055502  47 PLEAMRCYT-ANPARAEGqAARKGTLSPGKLADLIVldrdpcaVDPDEIR 95
Cdd:PRK02382  342 PLERVRDVTaANPARIFG-LDGKGRIAEGYDADLVL-------VDPDAAR 383
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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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