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Conserved domains on  [gi|221235821|ref|YP_002518258|]
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pyrimidine utilization protein B [Caulobacter vibrioides NA1000]

Protein Classification

peroxyureidoacrylate/ureidoacrylate amidohydrolase RutB( domain architecture ID 10799479)

peroxyureidoacrylate/ureidoacrylate amidohydrolase RutB hydrolyzes ureidoacrylate to form aminoacrylate and carbamate, the latter hydrolyzes spontaneously, releasing one of the nitrogen atoms of the pyrimidine ring as ammonia and one of its carbon atoms as CO2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RutB TIGR03614
pyrimidine utilization protein B;
14-238 2.05e-175

pyrimidine utilization protein B;


:

Pssm-ID: 163356  Cd Length: 226  Bit Score: 480.87  E-value: 2.05e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821   14 MLPARPEPLPVDPKTTAVIVIDMQNAYASPGGYLDLAGFDISGAAKVTHEIKGVLEVARSAGMTVIYFQNGWDDGYVEAG 93
Cdd:TIGR03614   1 TLPARPEPITLDPEQTALIVVDMQNAYATPGGYLDLAGFDVSGTKPVIENIKKAVTAARAAGIQVIYFQNGWDNDYVEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821   94 GPGSPNWWKSNALKTMRARPELQGKLLARGQWDYELVDDLTPQPGDIRLHKTRYSGFFNSQLDSVLRARGIRHLVFTGIA 173
Cdd:TIGR03614  81 GPGSPNWHKSNALKTMRKRPELQGKLLAKGTWDYELVDELQPQPGDIVLPKPRYSGFFNTPLDSMLRARGIRNLVFTGIA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221235821  174 TNVCVESTLRDGFMLEYFGTVLEDATHQAGPDFVQKAALFNIETFFGWVSTTADFKGTFGQLAPG 238
Cdd:TIGR03614 161 TNVCVESTLRDGFHLEYFGVVLEDATHQAGPDFMQKAALYNIETFFGWVSDVADFCGTFSQNAPL 225
 
Name Accession Description Interval E-value
RutB TIGR03614
pyrimidine utilization protein B;
14-238 2.05e-175

pyrimidine utilization protein B;


Pssm-ID: 163356  Cd Length: 226  Bit Score: 480.87  E-value: 2.05e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821   14 MLPARPEPLPVDPKTTAVIVIDMQNAYASPGGYLDLAGFDISGAAKVTHEIKGVLEVARSAGMTVIYFQNGWDDGYVEAG 93
Cdd:TIGR03614   1 TLPARPEPITLDPEQTALIVVDMQNAYATPGGYLDLAGFDVSGTKPVIENIKKAVTAARAAGIQVIYFQNGWDNDYVEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821   94 GPGSPNWWKSNALKTMRARPELQGKLLARGQWDYELVDDLTPQPGDIRLHKTRYSGFFNSQLDSVLRARGIRHLVFTGIA 173
Cdd:TIGR03614  81 GPGSPNWHKSNALKTMRKRPELQGKLLAKGTWDYELVDELQPQPGDIVLPKPRYSGFFNTPLDSMLRARGIRNLVFTGIA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221235821  174 TNVCVESTLRDGFMLEYFGTVLEDATHQAGPDFVQKAALFNIETFFGWVSTTADFKGTFGQLAPG 238
Cdd:TIGR03614 161 TNVCVESTLRDGFHLEYFGVVLEDATHQAGPDFMQKAALYNIETFFGWVSDVADFCGTFSQNAPL 225
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 30-222 1.56e-49

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: 159.68  E-value: 1.56e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821  30 AVIVIDMQNAYASPGGyldlagFDISGAAKVTHEIKGVLEVARSAGMTVIYFQNGWDDGYVEaggpgspnwwksnalktm 109
Cdd:COG1335    1 ALLVIDVQNDFVPPGA------LAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSE------------------ 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821 110 RARPELQGKLLARGQWDYELVDDLTPQPGDIRLHKTRYSGFFNSQLDSVLRARGIRHLVFTGIATNVCVESTLRDGFMLE 189
Cdd:COG1335   57 FAEFDLWPPHCVPGTPGAELVPELAPLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLG 136

                        170       180       190
                 ....*....|....*....|....*....|...
gi 221235821 190 YFGTVLEDATHqAGPDFVQKAALFNIETFFGWV 222
Cdd:COG1335  137 YEVTVVEDACA-SRDPEAHEAALARLRAAGATV 168
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 29-226 2.51e-45

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 149.09  E-value: 2.51e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821   29 TAVIVIDMQNayaspgGYLDLAGFDISGAAKVTHEIKGVLEVARSAGMTVIYFQNGWDDGYVEAGGPGSPNWWksnalkt 108
Cdd:pfam00857   1 TALLVIDMQN------DFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDRPSPA------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821  109 mrarpelqgklLARGQWDYELVDDLTPQPGDIRLHKTRYSGFFNSQLDSVLRARGIRHLVFTGIATNVCVESTLRDGFML 188
Cdd:pfam00857  68 -----------FPPGTTGAELVPELAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDR 136

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 221235821  189 EYFGTVLEDATHQAGPDFvQKAALFNIETFFGWVSTTA 226
Cdd:pfam00857 137 GYEVVVVSDACASLSPEA-HDAALERLAQRGAEVTTTE 173
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 30-216 2.92e-43

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: 143.56  E-value: 2.92e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821  30 AVIVIDMQNAYASPGGYLDlagfdiSGAAKVTHEIKGVLEVARSAGMTVIYFQNGWDDGYVEAGgpgsPNWWksnalktm 109
Cdd:cd00431    1 ALLVVDMQNDFVPGGGLLL------PGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFA----ELLW-------- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821 110 rarpelqGKLLARGQWDYELVDDLTPQPGDIRLHKTRYSGFFNSQLDSVLRARGIRHLVFTGIATNVCVESTLRDGFMLE 189
Cdd:cd00431   63 -------PPHCVKGTEGAELVPELAPLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLG 135

                        170       180
                 ....*....|....*....|....*...
gi 221235821 190 YFGTVLEDAThqAGPD-FVQKAALFNIE 216
Cdd:cd00431  136 YRVIVVEDAC--ATRDeEDHEAALERLA 161
PRK11440 PRK11440
putative hydrolase; Provisional
 22-227 1.12e-21

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 88.63  E-value: 1.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821  22 LPVDPKTTAVIVIDMQNayaspgGYLDLAGFDISGAAKVTHEIKgVLEVARSAGMTVIYFQNGWDDGYVEA--------- 92
Cdd:PRK11440   2 LELNAKTTALVVIDLQE------GILPFAGGPHTADEVVARAAR-LAAKFRASGSPVVLVRVGWSADYAEAlkqpvdaps 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821  93 -GGPGSPNWWKSNAlktmrarpelqgkllargqwdyelvdDLTPQPGDIRLHKTRYSGFFNSQLDSVLRARGIRHLVFTG 171
Cdd:PRK11440  75 pAKVLPENWWQHPA--------------------------ALGKTDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCG 128

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 221235821 172 IATNVCVESTLRDGFMLEYFGTVLEDATHQAGPDfVQKAALFNIETFFGWVSTTAD 227
Cdd:PRK11440 129 ISTNIGVESTARNAWELGFNLVIAEDACSAASAE-QHQNSMNHIFPRIARVRSVEE 183
 
Name Accession Description Interval E-value
RutB TIGR03614
pyrimidine utilization protein B;
14-238 2.05e-175

pyrimidine utilization protein B;


Pssm-ID: 163356  Cd Length: 226  Bit Score: 480.87  E-value: 2.05e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821   14 MLPARPEPLPVDPKTTAVIVIDMQNAYASPGGYLDLAGFDISGAAKVTHEIKGVLEVARSAGMTVIYFQNGWDDGYVEAG 93
Cdd:TIGR03614   1 TLPARPEPITLDPEQTALIVVDMQNAYATPGGYLDLAGFDVSGTKPVIENIKKAVTAARAAGIQVIYFQNGWDNDYVEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821   94 GPGSPNWWKSNALKTMRARPELQGKLLARGQWDYELVDDLTPQPGDIRLHKTRYSGFFNSQLDSVLRARGIRHLVFTGIA 173
Cdd:TIGR03614  81 GPGSPNWHKSNALKTMRKRPELQGKLLAKGTWDYELVDELQPQPGDIVLPKPRYSGFFNTPLDSMLRARGIRNLVFTGIA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221235821  174 TNVCVESTLRDGFMLEYFGTVLEDATHQAGPDFVQKAALFNIETFFGWVSTTADFKGTFGQLAPG 238
Cdd:TIGR03614 161 TNVCVESTLRDGFHLEYFGVVLEDATHQAGPDFMQKAALYNIETFFGWVSDVADFCGTFSQNAPL 225
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 30-222 1.56e-49

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: 159.68  E-value: 1.56e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821  30 AVIVIDMQNAYASPGGyldlagFDISGAAKVTHEIKGVLEVARSAGMTVIYFQNGWDDGYVEaggpgspnwwksnalktm 109
Cdd:COG1335    1 ALLVIDVQNDFVPPGA------LAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSE------------------ 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821 110 RARPELQGKLLARGQWDYELVDDLTPQPGDIRLHKTRYSGFFNSQLDSVLRARGIRHLVFTGIATNVCVESTLRDGFMLE 189
Cdd:COG1335   57 FAEFDLWPPHCVPGTPGAELVPELAPLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLG 136

                        170       180       190
                 ....*....|....*....|....*....|...
gi 221235821 190 YFGTVLEDATHqAGPDFVQKAALFNIETFFGWV 222
Cdd:COG1335  137 YEVTVVEDACA-SRDPEAHEAALARLRAAGATV 168
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 29-226 2.51e-45

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 149.09  E-value: 2.51e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821   29 TAVIVIDMQNayaspgGYLDLAGFDISGAAKVTHEIKGVLEVARSAGMTVIYFQNGWDDGYVEAGGPGSPNWWksnalkt 108
Cdd:pfam00857   1 TALLVIDMQN------DFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDRPSPA------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821  109 mrarpelqgklLARGQWDYELVDDLTPQPGDIRLHKTRYSGFFNSQLDSVLRARGIRHLVFTGIATNVCVESTLRDGFML 188
Cdd:pfam00857  68 -----------FPPGTTGAELVPELAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDR 136

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 221235821  189 EYFGTVLEDATHQAGPDFvQKAALFNIETFFGWVSTTA 226
Cdd:pfam00857 137 GYEVVVVSDACASLSPEA-HDAALERLAQRGAEVTTTE 173
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 30-216 2.92e-43

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: 143.56  E-value: 2.92e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821  30 AVIVIDMQNAYASPGGYLDlagfdiSGAAKVTHEIKGVLEVARSAGMTVIYFQNGWDDGYVEAGgpgsPNWWksnalktm 109
Cdd:cd00431    1 ALLVVDMQNDFVPGGGLLL------PGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFA----ELLW-------- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821 110 rarpelqGKLLARGQWDYELVDDLTPQPGDIRLHKTRYSGFFNSQLDSVLRARGIRHLVFTGIATNVCVESTLRDGFMLE 189
Cdd:cd00431   63 -------PPHCVKGTEGAELVPELAPLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLG 135

                        170       180
                 ....*....|....*....|....*...
gi 221235821 190 YFGTVLEDAThqAGPD-FVQKAALFNIE 216
Cdd:cd00431  136 YRVIVVEDAC--ATRDeEDHEAALERLA 161
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
14-237 7.37e-33

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 118.03  E-value: 7.37e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821  14 MLPARPEPLPVDPKTTAVIVIDMQNAYASPGGyldlagFDISGAAKVTHEIKGVLEVARSAGMTVIYF-----QNGWDDG 88
Cdd:COG1535    5 DLPANKVSWTLDPARAALLIHDMQNYFLRPYD------PDEPPIRELVANIARLRDACRAAGIPVVYTaqpgdQTPEDRG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821  89 YVEaggpgspNWWKSnalkTMRARPELQgkllargqwdyELVDDLTPQPGDIRLHKTRYSGFFNSQLDSVLRARGIRHLV 168
Cdd:COG1535   79 LLN-------DFWGP----GLTAGPEGQ-----------EIVDELAPAPGDTVLTKWRYSAFQRTDLEERLRELGRDQLI 136

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221235821 169 FTGIATNVCVESTLRDGFMLEYFGTVLEDAThqAgpDF---VQKAALFNIETFFGWVSTTADFKGTFGQLAP 237
Cdd:COG1535  137 ITGVYAHIGCLATAVDAFMRDIQPFVVADAV--A--DFsreEHRMALEYVAGRCGVVVTTDEVLEALRAAGP 204
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 30-199 8.43e-23

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: 90.34  E-value: 8.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821  30 AVIVIDMQNAYASPGGYLDlagfdisGAAKVTHEIKGVLEVARSAGMTVIYFQNgwddgyvEAGGPGSpnwwksnalktm 109
Cdd:cd01014    1 ALLVIDVQNGYFDGGLPPL-------NNEAALENIAALIAAARAAGIPVIHVRH-------IDDEGGS------------ 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821 110 rarpelqgklLARGQWDYELVDDLTPQPGDIRLHKTRYSGFFNSQLDSVLRARGIRHLVFTGIATNVCVESTLRDGFMLE 189
Cdd:cd01014   55 ----------FAPGSEGWEIHPELAPLEGETVIEKTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLG 124

                        170
                 ....*....|
gi 221235821 190 YFGTVLEDAT 199
Cdd:cd01014  125 YDVTVVADAC 134
PRK11440 PRK11440
putative hydrolase; Provisional
 22-227 1.12e-21

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 88.63  E-value: 1.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821  22 LPVDPKTTAVIVIDMQNayaspgGYLDLAGFDISGAAKVTHEIKgVLEVARSAGMTVIYFQNGWDDGYVEA--------- 92
Cdd:PRK11440   2 LELNAKTTALVVIDLQE------GILPFAGGPHTADEVVARAAR-LAAKFRASGSPVVLVRVGWSADYAEAlkqpvdaps 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821  93 -GGPGSPNWWKSNAlktmrarpelqgkllargqwdyelvdDLTPQPGDIRLHKTRYSGFFNSQLDSVLRARGIRHLVFTG 171
Cdd:PRK11440  75 pAKVLPENWWQHPA--------------------------ALGKTDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCG 128

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 221235821 172 IATNVCVESTLRDGFMLEYFGTVLEDATHQAGPDfVQKAALFNIETFFGWVSTTAD 227
Cdd:PRK11440 129 ISTNIGVESTARNAWELGFNLVIAEDACSAASAE-QHQNSMNHIFPRIARVRSVEE 183
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 30-227 3.02e-20

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: 84.38  E-value: 3.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821  30 AVIVIDMQNAYASPGGYLdlagfdISGAAKVTHEIKGVLEVARSAGMTVIYFQNGWDDGyveagGPGSPNWW-KSNALKT 108
Cdd:cd01015    1 ALLVIDLVEGYTQPGSYL------APGIAAALENVQRLLAAARAAGVPVIHTTVVYDPD-----GADGGLWArKVPAMSD 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821 109 MRARPELQgkllargqwdyELVDDLTPQPGDIRLHKTRYSGFFNSQLDSVLRARGIRHLVFTGIATNVCVESTLRDGFML 188
Cdd:cd01015   70 LVEGSPLA-----------AICDELAPQEDEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQH 138

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 221235821 189 EYFGTVLEDATHQAGPDFVQkAALFNIETFFGWVSTTAD 227
Cdd:cd01015  139 GFRPIVVRECVGDRAPAPHE-ANLFDIDNKYGDVVSTDD 176
PLN02621 PLN02621
nicotinamidase
 25-222 1.14e-15

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 72.89  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821  25 DPKTTAVIVIDMQNAYASPggyldlagfdisgAAKVTHEIKGVLEVARSAGMTVIYFQNGwDDGYVEAGGPGSpnWWksn 104
Cdd:PLN02621  17 DPKQAALLVIDMQNYFSSM-------------AEPILPALLTTIDLCRRASIPVFFTRHS-HKSPSDYGMLGE--WW--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821 105 alktmrarpelQGKLLARGQWDYELVDDLT-PQPGDIRLHKTRYSGFFNSQLDSVLRARGIRHLVFTGIATNVCVESTLR 183
Cdd:PLN02621  78 -----------DGDLILDGTTEAELMPEIGrVTGPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAR 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 221235821 184 DGFMLE---YFGTvleDATHQAGPDfVQKAALFNIETFFGWV 222
Cdd:PLN02621 147 EAFVRGfrvFFST---DATATANEE-LHEATLKNLAYGFAYL 184
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
 5-189 2.82e-15

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: 71.60  E-value: 2.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821   5 ITPLS-PGCVMLPARPEPLPVDPKTTAVIVIDMQNAYASPggyldlagFDISGA--AKVTHEIKGVLEVARSAGMTVIYF 81
Cdd:cd01013    5 IASYPlPTAESFPANKVDWQIDPKRAVLLVHDMQRYFLDF--------YDESAEpvPQLIANIARLRDWCRQAGIPVVYT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821  82 -----QNGWDDGYV-EAGGPGspnwwksnalktMRARPELQgkllargqwdyELVDDLTPQPGDIRLHKTRYSGFFNSQL 155
Cdd:cd01013   77 aqpgnQTPEQRALLnDFWGPG------------LTASPEET-----------KIVTELAPQPDDTVLTKWRYSAFKRSPL 133

                        170       180       190
                 ....*....|....*....|....*....|....
gi 221235821 156 DSVLRARGIRHLVFTGIATNVCVESTLRDGFMLE 189
Cdd:cd01013  134 LERLKESGRDQLIITGVYAHIGCLSTAVDAFMRD 167
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 28-199 8.00e-12

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: 62.28  E-value: 8.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821  28 TTAVIVIDMQNAYaSPGGYLDlagfdISGAAKVTHEIKGVLEVARSAgmTVIYFQngwdDGYVEAGGPgspnwWKSNALK 107
Cdd:cd01011    1 TDALLVVDVQNDF-CPGGALA-----VPGGDAIVPLINALLSLFQYD--LVVATQ----DWHPANHAS-----FASNHPG 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821 108 TMRARPELQGKLL------ARGQWDYELVDDLTPQPGDIRLHK-TR-----YSGFF-NSQLDSV-----LRARGIRHLVF 169
Cdd:cd01011   64 QMPFITLPPGPQVlwpdhcVQGTPGAELHPGLPVPDIDLIVRKgTNpdidsYSAFFdNDRRSSTglaeyLRERGIDRVDV 143

                        170       180       190
                 ....*....|....*....|....*....|
gi 221235821 170 TGIATNVCVESTLRDGFMLEYFGTVLEDAT 199
Cdd:cd01011  144 VGLATDYCVKATALDALKAGFEVRVLEDAC 173
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 17-210 1.29e-11

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 62.01  E-value: 1.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821  17 ARPEPLPVDPKTTAVIVIDMQNAYASPGGyldLAgfdISGAAKVTHEIKGVleVARSAGMTVIYFQNGWDDGYVEAGGPG 96
Cdd:PTZ00331   1 MSTSCITVSSTNDALIIVDVQNDFCKGGS---LA---VPDAEEVIPVINQV--RQSHHFDLVVATQDWHPPNHISFASNH 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221235821  97 SPNWWKSNALKTMRARPE-LQGKLLArgqwdyELVDDLTPQPGDIRLHK------TRYSGFFNSQ-----LDSVLRARGI 164
Cdd:PTZ00331  73 GKPKILPDGTTQGLWPPHcVQGTKGA------QLHKDLVVERIDIIIRKgtnrdvDSYSAFDNDKgsktgLAQILKAHGV 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 221235821 165 RHLVFTGIATNVCVESTLRDGFMLEYFGTVLEDATHQAGPDFVQKA 210
Cdd:PTZ00331 147 RRVFICGLAFDFCVLFTALDAVKLGFKVVVLEDATRAVDPDAISKQ 192
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
147-197 2.35e-07

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 49.61  E-value: 2.35e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 221235821 147 YSGFFN------SQLDSVLRARGIRHLVFTGIATNVCVESTLRDGFMLEYFGTVLED 197
Cdd:PRK11609 119 YSAFFDnghrqkTALDDWLREHGITELIVMGLATDYCVKFTVLDALALGYQVNVITD 175
 
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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