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Conserved domains on  [gi|654544949|ref|WP_028012657|]
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MULTISPECIES: pyrimidine utilization protein B [Enterobacter]

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;
3-223 1.92e-167

pyrimidine utilization protein B;


:

Pssm-ID: 163356  Cd Length: 226  Bit Score: 460.45  E-value: 1.92e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949    3 TLNARPEAITFAPQQSALIVVDMQNAYASQGGYLDLAGFDVSATRPVIENIKTAVAAARAAGMLIIWFQNGWDDQYVEAG 82
Cdd:TIGR03614   1 TLPARPEPITLDPEQTALIVVDMQNAYATPGGYLDLAGFDVSGTKPVIENIKKAVTAARAAGIQVIYFQNGWDNDYVEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949   83 GPGSPNFHKSNALKTMRKRPELQGKLLAKGGWDYQLVDELVPQAGDIVLPKPRYSGFFNTPLDSLLRSRGIRHLVFTGIA 162
Cdd:TIGR03614  81 GPGSPNWHKSNALKTMRKRPELQGKLLAKGTWDYELVDELQPQPGDIVLPKPRYSGFFNTPLDSMLRARGIRNLVFTGIA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654544949  163 TNVCVESTLRDGFFLEYFGVVLEDATHQAGPEFAQKAALFNIETFFGWVSNVADFCDALNP 223
Cdd:TIGR03614 161 TNVCVESTLRDGFHLEYFGVVLEDATHQAGPDFMQKAALYNIETFFGWVSDVADFCGTFSQ 221
 
Name Accession Description Interval E-value
RutB TIGR03614
pyrimidine utilization protein B;
3-223 1.92e-167

pyrimidine utilization protein B;


Pssm-ID: 163356  Cd Length: 226  Bit Score: 460.45  E-value: 1.92e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949    3 TLNARPEAITFAPQQSALIVVDMQNAYASQGGYLDLAGFDVSATRPVIENIKTAVAAARAAGMLIIWFQNGWDDQYVEAG 82
Cdd:TIGR03614   1 TLPARPEPITLDPEQTALIVVDMQNAYATPGGYLDLAGFDVSGTKPVIENIKKAVTAARAAGIQVIYFQNGWDNDYVEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949   83 GPGSPNFHKSNALKTMRKRPELQGKLLAKGGWDYQLVDELVPQAGDIVLPKPRYSGFFNTPLDSLLRSRGIRHLVFTGIA 162
Cdd:TIGR03614  81 GPGSPNWHKSNALKTMRKRPELQGKLLAKGTWDYELVDELQPQPGDIVLPKPRYSGFFNTPLDSMLRARGIRNLVFTGIA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654544949  163 TNVCVESTLRDGFFLEYFGVVLEDATHQAGPEFAQKAALFNIETFFGWVSNVADFCDALNP 223
Cdd:TIGR03614 161 TNVCVESTLRDGFHLEYFGVVLEDATHQAGPDFMQKAALYNIETFFGWVSDVADFCGTFSQ 221
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 19-211 5.32e-45

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: 147.74  E-value: 5.32e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949  19 ALIVVDMQNAYASQGGyldlagFDVSATRPVIENIKTAVAAARAAGMLIIWFQNGWDDQYVEAGGPGSPNFHksnalktm 98
Cdd:COG1335    1 ALLVIDVQNDFVPPGA------LAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPH-------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949  99 rkrpelqgklLAKGGWDYQLVDELVPQAGDIVLPKPRYSGFFNTPLDSLLRSRGIRHLVFTGIATNVCVESTLRDGFFLE 178
Cdd:COG1335   67 ----------CVPGTPGAELVPELAPLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLG 136

                        170       180       190
                 ....*....|....*....|....*....|...
gi 654544949 179 YFGVVLEDATHQAGPEfAQKAALFNIETFFGWV 211
Cdd:COG1335  137 YEVTVVEDACASRDPE-AHEAALARLRAAGATV 168
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 18-215 6.82e-43

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 142.54  E-value: 6.82e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949   18 SALIVVDMQNayasqgGYLDLAGFDVSATRPVIENIKTAVAAARAAGMLIIWFQngwddQYVEAGGPGSPnfhksnalkt 97
Cdd:pfam00857   1 TALLVIDMQN------DFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTR-----QVPEPDDADFA---------- 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949   98 mrkRPELQGKLLAKGGWDYQLVDELVPQAGDIVLPKPRYSGFFNTPLDSLLRSRGIRHLVFTGIATNVCVESTLRDGFFL 177
Cdd:pfam00857  60 ---LKDRPSPAFPPGTTGAELVPELAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDR 136

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 654544949  178 EYFGVVLEDATHQAGPEfAQKAALFNIETFFGWVSNVA 215
Cdd:pfam00857 137 GYEVVVVSDACASLSPE-AHDAALERLAQRGAEVTTTE 173
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 19-205 1.50e-41

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: 138.94  E-value: 1.50e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949  19 ALIVVDMQNAYASQGGYLdlagfdVSATRPVIENIKTAVAAARAAGMLIIWFQNGWDDQYVEAGGPGSPNFhksnalktm 98
Cdd:cd00431    1 ALLVVDMQNDFVPGGGLL------LPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAELLWPPH--------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949  99 rkrpelqgklLAKGGWDYQLVDELVPQAGDIVLPKPRYSGFFNTPLDSLLRSRGIRHLVFTGIATNVCVESTLRDGFFLE 178
Cdd:cd00431   66 ----------CVKGTEGAELVPELAPLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLG 135

                        170       180
                 ....*....|....*....|....*..
gi 654544949 179 YFGVVLEDATHQAGPEfAQKAALFNIE 205
Cdd:cd00431  136 YRVIVVEDACATRDEE-DHEAALERLA 161
PRK11440 PRK11440
putative hydrolase; Provisional
 15-221 1.85e-16

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 74.38  E-value: 1.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949  15 PQQSALIVVDMQNayasqgGYLDLAGFDVSATRpVIENIKTAVAAARAAGMLIIWFQNGWDDQYVEAggpgspnfhksna 94
Cdd:PRK11440   6 AKTTALVVIDLQE------GILPFAGGPHTADE-VVARAARLAAKFRASGSPVVLVRVGWSADYAEA------------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949  95 LKTMRKRPElQGKLLAKGGWDYQLvdELVPQAGDIVLPKPRYSGFFNTPLDSLLRSRGIRHLVFTGIATNVCVESTLRDG 174
Cdd:PRK11440  66 LKQPVDAPS-PAKVLPENWWQHPA--ALGKTDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNA 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 654544949 175 FFLEYFGVVLEDATHQAGPEfAQKAALFNIETFFGWVSNVADFCDAL 221
Cdd:PRK11440 143 WELGFNLVIAEDACSAASAE-QHQNSMNHIFPRIARVRSVEEILNAL 188
 
Name Accession Description Interval E-value
RutB TIGR03614
pyrimidine utilization protein B;
3-223 1.92e-167

pyrimidine utilization protein B;


Pssm-ID: 163356  Cd Length: 226  Bit Score: 460.45  E-value: 1.92e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949    3 TLNARPEAITFAPQQSALIVVDMQNAYASQGGYLDLAGFDVSATRPVIENIKTAVAAARAAGMLIIWFQNGWDDQYVEAG 82
Cdd:TIGR03614   1 TLPARPEPITLDPEQTALIVVDMQNAYATPGGYLDLAGFDVSGTKPVIENIKKAVTAARAAGIQVIYFQNGWDNDYVEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949   83 GPGSPNFHKSNALKTMRKRPELQGKLLAKGGWDYQLVDELVPQAGDIVLPKPRYSGFFNTPLDSLLRSRGIRHLVFTGIA 162
Cdd:TIGR03614  81 GPGSPNWHKSNALKTMRKRPELQGKLLAKGTWDYELVDELQPQPGDIVLPKPRYSGFFNTPLDSMLRARGIRNLVFTGIA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654544949  163 TNVCVESTLRDGFFLEYFGVVLEDATHQAGPEFAQKAALFNIETFFGWVSNVADFCDALNP 223
Cdd:TIGR03614 161 TNVCVESTLRDGFHLEYFGVVLEDATHQAGPDFMQKAALYNIETFFGWVSDVADFCGTFSQ 221
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 19-211 5.32e-45

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: 147.74  E-value: 5.32e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949  19 ALIVVDMQNAYASQGGyldlagFDVSATRPVIENIKTAVAAARAAGMLIIWFQNGWDDQYVEAGGPGSPNFHksnalktm 98
Cdd:COG1335    1 ALLVIDVQNDFVPPGA------LAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPH-------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949  99 rkrpelqgklLAKGGWDYQLVDELVPQAGDIVLPKPRYSGFFNTPLDSLLRSRGIRHLVFTGIATNVCVESTLRDGFFLE 178
Cdd:COG1335   67 ----------CVPGTPGAELVPELAPLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLG 136

                        170       180       190
                 ....*....|....*....|....*....|...
gi 654544949 179 YFGVVLEDATHQAGPEfAQKAALFNIETFFGWV 211
Cdd:COG1335  137 YEVTVVEDACASRDPE-AHEAALARLRAAGATV 168
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 18-215 6.82e-43

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 142.54  E-value: 6.82e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949   18 SALIVVDMQNayasqgGYLDLAGFDVSATRPVIENIKTAVAAARAAGMLIIWFQngwddQYVEAGGPGSPnfhksnalkt 97
Cdd:pfam00857   1 TALLVIDMQN------DFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTR-----QVPEPDDADFA---------- 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949   98 mrkRPELQGKLLAKGGWDYQLVDELVPQAGDIVLPKPRYSGFFNTPLDSLLRSRGIRHLVFTGIATNVCVESTLRDGFFL 177
Cdd:pfam00857  60 ---LKDRPSPAFPPGTTGAELVPELAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDR 136

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 654544949  178 EYFGVVLEDATHQAGPEfAQKAALFNIETFFGWVSNVA 215
Cdd:pfam00857 137 GYEVVVVSDACASLSPE-AHDAALERLAQRGAEVTTTE 173
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 19-205 1.50e-41

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: 138.94  E-value: 1.50e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949  19 ALIVVDMQNAYASQGGYLdlagfdVSATRPVIENIKTAVAAARAAGMLIIWFQNGWDDQYVEAGGPGSPNFhksnalktm 98
Cdd:cd00431    1 ALLVVDMQNDFVPGGGLL------LPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAELLWPPH--------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949  99 rkrpelqgklLAKGGWDYQLVDELVPQAGDIVLPKPRYSGFFNTPLDSLLRSRGIRHLVFTGIATNVCVESTLRDGFFLE 178
Cdd:cd00431   66 ----------CVKGTEGAELVPELAPLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLG 135

                        170       180
                 ....*....|....*....|....*..
gi 654544949 179 YFGVVLEDATHQAGPEfAQKAALFNIE 205
Cdd:cd00431  136 YRVIVVEDACATRDEE-DHEAALERLA 161
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
12-224 1.21e-28

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 106.86  E-value: 1.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949  12 TFAPQQSALIVVDMQNAYasqggyLDLAGFDVSATRPVIENIKTAVAAARAAGMLIIWFQNGWDDQYVEAG------GPG 85
Cdd:COG1535   14 TLDPARAALLIHDMQNYF------LRPYDPDEPPIRELVANIARLRDACRAAGIPVVYTAQPGDQTPEDRGllndfwGPG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949  86 spnfhksnalktMRKRPELQgkllakggwdyQLVDELVPQAGDIVLPKPRYSGFFNTPLDSLLRSRGIRHLVFTGIATNV 165
Cdd:COG1535   88 ------------LTAGPEGQ-----------EIVDELAPAPGDTVLTKWRYSAFQRTDLEERLRELGRDQLIITGVYAHI 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654544949 166 CVESTLRDGFFLEYFGVVLEDAT-------HQagpefaqkAALFNIETFFGWVSNVADFCDALNPP 224
Cdd:COG1535  145 GCLATAVDAFMRDIQPFVVADAVadfsreeHR--------MALEYVAGRCGVVVTTDEVLEALRAA 202
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 19-188 1.44e-20

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: 84.56  E-value: 1.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949  19 ALIVVDMQNAYASQGGYLDlagfdvsATRPVIENIKTAVAAARAAGMLIIWFQngwddqyveaggpgspnfHKSNAlktm 98
Cdd:cd01014    1 ALLVIDVQNGYFDGGLPPL-------NNEAALENIAALIAAARAAGIPVIHVR------------------HIDDE---- 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949  99 rkrpelqGKLLAKGGWDYQLVDELVPQAGDIVLPKPRYSGFFNTPLDSLLRSRGIRHLVFTGIATNVCVESTLRDGFFLE 178
Cdd:cd01014   52 -------GGSFAPGSEGWEIHPELAPLEGETVIEKTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLG 124

                        170
                 ....*....|
gi 654544949 179 YFGVVLEDAT 188
Cdd:cd01014  125 YDVTVVADAC 134
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 19-219 2.83e-18

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: 78.98  E-value: 2.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949  19 ALIVVDMQNAYASQGGYLdLAGFD--VSATRPVIENIKtavaaarAAGMLIIWFQNGWDDQYVEAGgpgspnfhksnalK 96
Cdd:cd01015    1 ALLVIDLVEGYTQPGSYL-APGIAaaLENVQRLLAAAR-------AAGVPVIHTTVVYDPDGADGG-------------L 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949  97 TMRKRPELqgKLLAKGGWDYQLVDELVPQAGDIVLPKPRYSGFFNTPLDSLLRSRGIRHLVFTGIATNVCVESTLRDGFF 176
Cdd:cd01015   60 WARKVPAM--SDLVEGSPLAAICDELAPQEDEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQ 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 654544949 177 LEYFGVVLEDATHQAGPEFAQkAALFNIETFFGWVSNVADFCD 219
Cdd:cd01015  138 HGFRPIVVRECVGDRAPAPHE-ANLFDIDNKYGDVVSTDDALA 179
PRK11440 PRK11440
putative hydrolase; Provisional
 15-221 1.85e-16

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 74.38  E-value: 1.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949  15 PQQSALIVVDMQNayasqgGYLDLAGFDVSATRpVIENIKTAVAAARAAGMLIIWFQNGWDDQYVEAggpgspnfhksna 94
Cdd:PRK11440   6 AKTTALVVIDLQE------GILPFAGGPHTADE-VVARAARLAAKFRASGSPVVLVRVGWSADYAEA------------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949  95 LKTMRKRPElQGKLLAKGGWDYQLvdELVPQAGDIVLPKPRYSGFFNTPLDSLLRSRGIRHLVFTGIATNVCVESTLRDG 174
Cdd:PRK11440  66 LKQPVDAPS-PAKVLPENWWQHPA--ALGKTDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNA 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 654544949 175 FFLEYFGVVLEDATHQAGPEfAQKAALFNIETFFGWVSNVADFCDAL 221
Cdd:PRK11440 143 WELGFNLVIAEDACSAASAE-QHQNSMNHIFPRIARVRSVEEILNAL 188
PLN02621 PLN02621
nicotinamidase
 15-227 2.16e-14

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 69.04  E-value: 2.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949  15 PQQSALIVVDMQNAYASQggyldlagfdvsaTRPVIENIKTAVAAARAAGMliiwfqngwddqyveaggpgsPNFHKSNA 94
Cdd:PLN02621  18 PKQAALLVIDMQNYFSSM-------------AEPILPALLTTIDLCRRASI---------------------PVFFTRHS 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949  95 LKTMRKRPEL----QGKLLAKGGWDYQLVDELVPQAG-DIVLPKPRYSGFFNTPLDSLLRSRGIRHLVFTGIATNVCVES 169
Cdd:PLN02621  64 HKSPSDYGMLgewwDGDLILDGTTEAELMPEIGRVTGpDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCET 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654544949 170 TLRDGF---FLEYFGVvleDATHQAGPEFaQKAALFNIETFFGWVSNvadfCDALNPPLAR 227
Cdd:PLN02621 144 TAREAFvrgFRVFFST---DATATANEEL-HEATLKNLAYGFAYLVD----CDRLEAGLLK 196
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
 15-188 5.25e-11

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: 59.66  E-value: 5.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949  15 PQQSALIVVDMQNaYasqggYLDLAGFDVSATRPVIENIKTAVAAARAAGMLIIwfqngwddqYVEAGGPGSPNfhkSNA 94
Cdd:cd01013   27 PKRAVLLVHDMQR-Y-----FLDFYDESAEPVPQLIANIARLRDWCRQAGIPVV---------YTAQPGNQTPE---QRA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949  95 LKTmrkrpELQGKLLAKGGWDYQLVDELVPQAGDIVLPKPRYSGFFNTPLDSLLRSRGIRHLVFTGIATNVCVESTLRDG 174
Cdd:cd01013   89 LLN-----DFWGPGLTASPEETKIVTELAPQPDDTVLTKWRYSAFKRSPLLERLKESGRDQLIITGVYAHIGCLSTAVDA 163

                        170
                 ....*....|....
gi 654544949 175 FFLEYFGVVLEDAT 188
Cdd:cd01013  164 FMRDIQPFVVADAI 177
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 111-188 1.16e-09

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: 56.12  E-value: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949 111 KGGWDYQLVDELVPQAGDIVLPK------PRYSGFF------NTPLDSLLRSRGIRHLVFTGIATNVCVESTLRDGFFLE 178
Cdd:cd01011   84 QGTPGAELHPGLPVPDIDLIVRKgtnpdiDSYSAFFdndrrsSTGLAEYLRERGIDRVDVVGLATDYCVKATALDALKAG 163

                         90
                 ....*....|
gi 654544949 179 YFGVVLEDAT 188
Cdd:cd01011  164 FEVRVLEDAC 173
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 6-199 3.29e-09

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 55.07  E-value: 3.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949   6 ARPEAITFAPQQSALIVVDMQNAYASQGGyldLAGFDVSATRPVIENIKTavaaaraagmliiwfQNGWDdqYVEAGGPG 85
Cdd:PTZ00331   1 MSTSCITVSSTNDALIIVDVQNDFCKGGS---LAVPDAEEVIPVINQVRQ---------------SHHFD--LVVATQDW 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654544949  86 SPNFHKSNALKTMRKRPELQGKLL----------AKGGwdyQLVDELVPQAGDIVLPK------PRYSGFFN-----TPL 144
Cdd:PTZ00331  61 HPPNHISFASNHGKPKILPDGTTQglwpphcvqgTKGA---QLHKDLVVERIDIIIRKgtnrdvDSYSAFDNdkgskTGL 137

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 654544949 145 DSLLRSRGIRHLVFTGIATNVCVESTLRDGFFLEYFGVVLEDATHQAGPEFAQKA 199
Cdd:PTZ00331 138 AQILKAHGVRRVFICGLAFDFCVLFTALDAVKLGFKVVVLEDATRAVDPDAISKQ 192
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
136-186 2.37e-06

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 46.91  E-value: 2.37e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 654544949 136 YSGFFN------TPLDSLLRSRGIRHLVFTGIATNVCVESTLRDGFFLEYFGVVLED 186
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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