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Conserved domains on  [gi|15599041|ref|NP_252535|]
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hypothetical protein PA3846 [Pseudomonas aeruginosa PAO1]

Protein Classification

hydrolase( domain architecture ID 10099061)

putative YcaC-like hydrolase with unknown specificity

CATH:  3.40.50.850
Gene Ontology:  GO:0016787
PubMed:  9782055
SCOP:  4000591

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 9-164 1.78e-67

YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown specificity. Despite its weak sequence similarity, it is structurally related to other amidohydrolases and shares conserved active site residues with them. Multimerisation interface seems not to be conserved in all members.


:

Pssm-ID: 238494 [Multi-domain]  Cd Length: 157  Bit Score: 202.82  E-value: 1.78e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599041   9 TLLVVDIQERLLPAIDDGPALVEYSQWLLRVARALDVPVLASEQYSKGLGPTVAALRDELEPTQILEKLDFSAAADGALL 88
Cdd:cd01012   1 ALLLVDVQEKLAPAIKSFDELINNTVKLAKAAKLLDVPVILTEQYPKGLGPTVPELREVFPDAPVIEKTSFSCWEDEAFR 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599041  89 RAPGGD-RRQFVVCGSEAHVCVLQTVLDLLGRGREVFVVEEAIGSRRPSDKALAVERMRQAGAMIVSREMVAFEWME 164
Cdd:cd01012  81 KALKATgRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRSKEDHELALARMRQAGAVLTTSESVLFELQR 157
 
Name Accession Description Interval E-value
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 9-164 1.78e-67

YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown specificity. Despite its weak sequence similarity, it is structurally related to other amidohydrolases and shares conserved active site residues with them. Multimerisation interface seems not to be conserved in all members.


Pssm-ID: 238494 [Multi-domain]  Cd Length: 157  Bit Score: 202.82  E-value: 1.78e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599041   9 TLLVVDIQERLLPAIDDGPALVEYSQWLLRVARALDVPVLASEQYSKGLGPTVAALRDELEPTQILEKLDFSAAADGALL 88
Cdd:cd01012   1 ALLLVDVQEKLAPAIKSFDELINNTVKLAKAAKLLDVPVILTEQYPKGLGPTVPELREVFPDAPVIEKTSFSCWEDEAFR 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599041  89 RAPGGD-RRQFVVCGSEAHVCVLQTVLDLLGRGREVFVVEEAIGSRRPSDKALAVERMRQAGAMIVSREMVAFEWME 164
Cdd:cd01012  81 KALKATgRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRSKEDHELALARMRQAGAVLTTSESVLFELQR 157
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 10-153 1.02e-31

Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction only]; Nicotinamidase-related amidase is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440946 [Multi-domain]  Cd Length: 169  Bit Score: 112.31  E-value: 1.02e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599041  10 LLVVDIQERLLP----AIDDGPALVEYSQWLLRVARALDVPVLASEQYS----------------KGLGPTVAALRDELE 69
Cdd:COG1335   2 LLVIDVQNDFVPpgalAVPGADAVVANIARLLAAARAAGVPVIHTRDWHppdgsefaefdlwpphCVPGTPGAELVPELA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599041  70 PTQ---ILEKLDFSAAADGAL---LRAPGgdRRQFVVCGSEAHVCVLQTVLDLLGRGREVFVVEEAIGSRRPSDKALAVE 143
Cdd:COG1335  82 PLPgdpVVDKTRYSAFYGTDLdelLRERG--IDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAALA 159

                       170
                ....*....|
gi 15599041 144 RMRQAGAMIV 153
Cdd:COG1335 160 RLRAAGATVV 169
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 10-156 5.77e-26

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 97.47  E-value: 5.77e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599041    10 LLVVDIQERLL----PAIDDGPALVEYSQWLLRVARALDVPVLASEQYSK----------------GLGPTVAALRDELE 69
Cdd:pfam00857   3 LLVIDMQNDFVdsggPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEpddadfalkdrpspafPPGTTGAELVPELA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599041    70 P---TQILEKLDFSAAADGAL---LRAPGgdRRQFVVCGSEAHVCVLQTVLDLLGRGREVFVVEEAIGSRRPSDKALAVE 143
Cdd:pfam00857  83 PlpgDLVVDKTRFSAFAGTDLdeiLRELG--IDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDAALE 160

                         170
                  ....*....|...
gi 15599041   144 RMRQAGAMIVSRE 156
Cdd:pfam00857 161 RLAQRGAEVTTTE 173
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 86-160 1.43e-03

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 37.74  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599041   86 ALLRAPGGDRrqFVVCGSEAHVCVLQTVLDLLGRGREVFVVEEAIgsrRPSDKAlAVERMRQ----AGAMIV-SREMVAF 160
Cdd:PTZ00331 139 QILKAHGVRR--VFICGLAFDFCVLFTALDAVKLGFKVVVLEDAT---RAVDPD-AISKQRAelleAGVILLtSSDLVAS 212
 
Name Accession Description Interval E-value
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 9-164 1.78e-67

YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown specificity. Despite its weak sequence similarity, it is structurally related to other amidohydrolases and shares conserved active site residues with them. Multimerisation interface seems not to be conserved in all members.


Pssm-ID: 238494 [Multi-domain]  Cd Length: 157  Bit Score: 202.82  E-value: 1.78e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599041   9 TLLVVDIQERLLPAIDDGPALVEYSQWLLRVARALDVPVLASEQYSKGLGPTVAALRDELEPTQILEKLDFSAAADGALL 88
Cdd:cd01012   1 ALLLVDVQEKLAPAIKSFDELINNTVKLAKAAKLLDVPVILTEQYPKGLGPTVPELREVFPDAPVIEKTSFSCWEDEAFR 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599041  89 RAPGGD-RRQFVVCGSEAHVCVLQTVLDLLGRGREVFVVEEAIGSRRPSDKALAVERMRQAGAMIVSREMVAFEWME 164
Cdd:cd01012  81 KALKATgRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRSKEDHELALARMRQAGAVLTTSESVLFELQR 157
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 10-153 1.02e-31

Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction only]; Nicotinamidase-related amidase is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440946 [Multi-domain]  Cd Length: 169  Bit Score: 112.31  E-value: 1.02e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599041  10 LLVVDIQERLLP----AIDDGPALVEYSQWLLRVARALDVPVLASEQYS----------------KGLGPTVAALRDELE 69
Cdd:COG1335   2 LLVIDVQNDFVPpgalAVPGADAVVANIARLLAAARAAGVPVIHTRDWHppdgsefaefdlwpphCVPGTPGAELVPELA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599041  70 PTQ---ILEKLDFSAAADGAL---LRAPGgdRRQFVVCGSEAHVCVLQTVLDLLGRGREVFVVEEAIGSRRPSDKALAVE 143
Cdd:COG1335  82 PLPgdpVVDKTRYSAFYGTDLdelLRERG--IDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAALA 159

                       170
                ....*....|
gi 15599041 144 RMRQAGAMIV 153
Cdd:COG1335 160 RLRAAGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 10-146 1.83e-26

Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine amidohydrolase), involved in creatine metabolism and nicotinamidase, converting nicotinamide to nicotinic acid and ammonia in the pyridine nucleotide cycle. It also contains isochorismatase, an enzyme that catalyzes the conversion of isochorismate to 2,3-dihydroxybenzoate and pyruvate, via the hydrolysis of the vinyl ether bond, and other related enzymes with unknown function.


Pssm-ID: 238245 [Multi-domain]  Cd Length: 161  Bit Score: 98.49  E-value: 1.83e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599041  10 LLVVDIQERLLPAID----DGPALVEYSQWLLRVARALDVPVLASEQYSKGLGPTV---------------AALRDELEP 70
Cdd:cd00431   2 LLVVDMQNDFVPGGGlllpGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFaellwpphcvkgtegAELVPELAP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599041  71 T---QILEKLDFSAAADGAL---LRAPGgdRRQFVVCGSEAHVCVLQTVLDLLGRGREVFVVEEAIGSRRPSDKALAVER 144
Cdd:cd00431  82 LpddLVIEKTRYSAFYGTDLdelLRERG--IDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEAALER 159


                ..
gi 15599041 145 MR 146
Cdd:cd00431 160 LA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 10-156 5.77e-26

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 97.47  E-value: 5.77e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599041    10 LLVVDIQERLL----PAIDDGPALVEYSQWLLRVARALDVPVLASEQYSK----------------GLGPTVAALRDELE 69
Cdd:pfam00857   3 LLVIDMQNDFVdsggPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEpddadfalkdrpspafPPGTTGAELVPELA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599041    70 P---TQILEKLDFSAAADGAL---LRAPGgdRRQFVVCGSEAHVCVLQTVLDLLGRGREVFVVEEAIGSRRPSDKALAVE 143
Cdd:pfam00857  83 PlpgDLVVDKTRFSAFAGTDLdeiLRELG--IDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDAALE 160

                         170
                  ....*....|...
gi 15599041   144 RMRQAGAMIVSRE 156
Cdd:pfam00857 161 RLAQRGAEVTTTE 173
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
4-167 3.52e-10

Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 56.40  E-value: 3.52e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599041   4 RAAtstLLVVDIQERLL----PAIDDGPALVEYSQWLLRVARALDVPVLASEQ---------------YSKGL--GPTVA 62
Cdd:COG1535  19 RAA---LLIHDMQNYFLrpydPDEPPIRELVANIARLRDACRAAGIPVVYTAQpgdqtpedrgllndfWGPGLtaGPEGQ 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599041  63 ALRDELEPTQ---ILEKLDFSA--AAD-GALLRAPGGDrrQFVVCGSEAHVCVLQTVLDLLGRGREVFVVEEAIGSRRPS 136
Cdd:COG1535  96 EIVDELAPAPgdtVLTKWRYSAfqRTDlEERLRELGRD--QLIITGVYAHIGCLATAVDAFMRDIQPFVVADAVADFSRE 173

                       170       180       190
                ....*....|....*....|....*....|.
gi 15599041 137 DKALAVERMRQAGAMIVSREMVaFEWMERAG 167
Cdd:COG1535 174 EHRMALEYVAGRCGVVVTTDEV-LEALRAAG 203
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 9-133 2.97e-06

Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share the catalytic triad with other amidohydrolases, like nicotinamidase, which converts nicotinamide to nicotinic acid and ammonia.


Pssm-ID: 238496 [Multi-domain]  Cd Length: 155  Bit Score: 44.89  E-value: 2.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599041   9 TLLVVDIQERLLP---AIDDGPALVEYSQWLLRVARALDVPV-----LASEQYSKGLGPTVAALRDELEPTQ---ILEKl 77
Cdd:cd01014   1 ALLVIDVQNGYFDgglPPLNNEAALENIAALIAAARAAGIPVihvrhIDDEGGSFAPGSEGWEIHPELAPLEgetVIEK- 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599041  78 dfsAAAD-------GALLRAPGgdRRQFVVCGSEAHVCVLQTVLDLLGRGREVFVVEEAIGSR 133
Cdd:cd01014  80 ---TVPNafygtdlEEWLREAG--IDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATF 137
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
 3-154 3.26e-05

Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the conversion of isochorismate, in the presence of water, to 2,3-dihydroxybenzoate and pyruvate, via the hydrolysis of a vinyl ether, an uncommon reaction in biological systems. Isochorismatase is part of the phenazine biosynthesis pathway. Phenazines are antimicrobial compounds that provide the competitive advantage for certain bacteria.


Pssm-ID: 238495  Cd Length: 203  Bit Score: 42.71  E-value: 3.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599041   3 IRAATSTLLVVDIQERLLPAIDDG----PALVEYSQWLLRVARALDVPVLASEQ---------------YSKGL--GPTV 61
Cdd:cd01013  25 IDPKRAVLLVHDMQRYFLDFYDESaepvPQLIANIARLRDWCRQAGIPVVYTAQpgnqtpeqrallndfWGPGLtaSPEE 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599041  62 AALRDELEPTQ---ILEKLDFSAAADGAL---LRAPGgdRRQFVVCGSEAHVCVLQTVLDLLGRGREVFVVEEAIGSRRP 135
Cdd:cd01013 105 TKIVTELAPQPddtVLTKWRYSAFKRSPLlerLKESG--RDQLIITGVYAHIGCLSTAVDAFMRDIQPFVVADAIADFSL 182

                       170
                ....*....|....*....
gi 15599041 136 SDKALAVERMRQAGAMIVS 154
Cdd:cd01013 183 EEHRMALKYAATRCAMVVS 201
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 87-153 1.14e-04

Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, converts nicotinamide to nicotinic acid (niacin) and ammonia, which in turn can be recycled to make nicotinamide adenine dinucleotide (NAD). The same enzyme is also called pyrazinamidase, because in converts the tuberculosis drug pyrazinamide (PZA) into its active form pyrazinoic acid (POA).


Pssm-ID: 238493  Cd Length: 196  Bit Score: 41.10  E-value: 1.14e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599041  87 LLRAPGGDRrqFVVCGSEAHVCVLQTVLDLLGRGREVFVVEEAIGSRRPSDKALAVERMRQAGAMIV 153
Cdd:cd01011 132 YLRERGIDR--VDVVGLATDYCVKATALDALKAGFEVRVLEDACRAVDPETIERAIEEMKEAGVVLV 196
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 10-135 2.10e-04

N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, carbon dioxide and ammonia. CSHase is involved in one of the two alternative pathways for creatinine degradation to glycine in microorganisms.This CSHase-containing pathway degrades creatinine via N-methylhydantoin N-carbamoylsarcosine and sarcosine to glycine. Enzymes of this pathway are used in the diagnosis for renal disfunction, for determining creatinine levels in urine and serum.


Pssm-ID: 238497 [Multi-domain]  Cd Length: 179  Bit Score: 40.08  E-value: 2.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599041  10 LLVVDIQERLL----PAIDDGPALVEYSQWLLRVARALDVPVL------ASEQYSKGLG----PTVAALRDELEPTQILE 75
Cdd:cd01015   2 LLVIDLVEGYTqpgsYLAPGIAAALENVQRLLAAARAAGVPVIhttvvyDPDGADGGLWarkvPAMSDLVEGSPLAAICD 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599041  76 KLdfSAAADGALLRA------PGGDRRQF---------VVCGSEAHVCVLQTVLDLLGRGREVFVVEEAIGSRRP 135
Cdd:cd01015  82 EL--APQEDEMVLVKkyasafFGTSLAATltargvdtlIVAGCSTSGCIRATAVDAMQHGFRPIVVRECVGDRAP 154
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 86-160 1.43e-03

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 37.74  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599041   86 ALLRAPGGDRrqFVVCGSEAHVCVLQTVLDLLGRGREVFVVEEAIgsrRPSDKAlAVERMRQ----AGAMIV-SREMVAF 160
Cdd:PTZ00331 139 QILKAHGVRR--VFICGLAFDFCVLFTALDAVKLGFKVVVLEDAT---RAVDPD-AISKQRAelleAGVILLtSSDLVAS 212
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
108-154 2.92e-03

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 36.89  E-value: 2.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15599041  108 CVLQTVLDLLGRGREVFVVEEaiGSR----RPSDKALAVERMRQAGAMIVS 154
Cdd:PRK11609 155 CVKFTVLDALALGYQVNVITD--GCRgvnlQPQDSAHAFMEMSAAGATLYT 203
 
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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