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Conserved domains on  [gi|518752642|ref|WP_019910611|]
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cysteine hydrolase family protein [Paenibacillus sp. HW567]

Protein Classification

cysteine hydrolase family protein( domain architecture ID 10003554)

cysteine hydrolase family protein related to isochorismatase and nicotinamidase; catalyzes the hydrolysis of a chemical bond using an active site cysteinyl residue

CATH:  3.40.50.850
EC:  3.-.-.-
Gene Ontology:  GO:0016787

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
3-177 9.79e-54

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: 168.16  E-value: 9.79e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642   3 ALIVIDFTNDFVD-GSLPVgQPGIDIAPRVSELTEAFVGSGDYVVMAVDLHETNDPYHPESSLFPPHNLRGTRGRELYGS 81
Cdd:COG1335    1 ALLVIDVQNDFVPpGALAV-PGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPHCVPGTPGAELVPE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642  82 LntvyeQNRESIYWMDKTRYSAFSGTDLELKLRERGITELHLIGVCTDICVLHTAVDAYNKGFSLTIHEDAVASFNPDGH 161
Cdd:COG1335   80 L-----APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAH 154
                        170
                 ....*....|....*.
gi 518752642 162 SWALGHFRGsLGAGVV 177
Cdd:COG1335  155 EAALARLRA-AGATVV 169
 
Name Accession Description Interval E-value
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
3-177 9.79e-54

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: 168.16  E-value: 9.79e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642   3 ALIVIDFTNDFVD-GSLPVgQPGIDIAPRVSELTEAFVGSGDYVVMAVDLHETNDPYHPESSLFPPHNLRGTRGRELYGS 81
Cdd:COG1335    1 ALLVIDVQNDFVPpGALAV-PGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPHCVPGTPGAELVPE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642  82 LntvyeQNRESIYWMDKTRYSAFSGTDLELKLRERGITELHLIGVCTDICVLHTAVDAYNKGFSLTIHEDAVASFNPDGH 161
Cdd:COG1335   80 L-----APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAH 154
                        170
                 ....*....|....*.
gi 518752642 162 SWALGHFRGsLGAGVV 177
Cdd:COG1335  155 EAALARLRA-AGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
3-169 7.06e-49

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: 155.50  E-value: 7.06e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642   3 ALIVIDFTNDFVDGSLPVGQPGIDIAPRVSELTEAFVGSGDYVVMAVDLHETNDPYHPESsLFPPHNLRGTRGRELYGSL 82
Cdd:cd00431    1 ALLVVDMQNDFVPGGGLLLPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAEL-LWPPHCVKGTEGAELVPEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642  83 ntvyeQNRESIYWMDKTRYSAFSGTDLELKLRERGITELHLIGVCTDICVLHTAVDAYNKGFSLTIHEDAVASFNPDGHS 162
Cdd:cd00431   80 -----APLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHE 154

                 ....*..
gi 518752642 163 WALGHFR 169
Cdd:cd00431  155 AALERLA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
3-180 3.26e-46

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 149.48  E-value: 3.26e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642    3 ALIVIDFTNDFVDGSLPVGQPGIDIAPRVSELTEAFVGSGDYVVMAVDLHETNDPYHPESSLFPPHNLRGTRGRELYGSL 82
Cdd:pfam00857   2 ALLVIDMQNDFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDRPSPAFPPGTTGAELVPEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642   83 nTVYEQNRESiywmDKTRYSAFSGTDLELKLRERGITELHLIGVCTDICVLHTAVDAYNKGFSLTIHEDAVASFNPDGHS 162
Cdd:pfam00857  82 -APLPGDLVV----DKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHD 156
                         170
                  ....*....|....*...
gi 518752642  163 WALGHFRGSlGAGVVSGE 180
Cdd:pfam00857 157 AALERLAQR-GAEVTTTE 173
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
1-177 1.27e-22

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 89.74  E-value: 1.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642   1 MRALIVIDFTNDFV-DGSLPVgQPGIDIAPRVSELTE--AFvgsgDYVVMAVDLHETN-------------DPYHPESSL 64
Cdd:PTZ00331  12 NDALIIVDVQNDFCkGGSLAV-PDAEEVIPVINQVRQshHF----DLVVATQDWHPPNhisfasnhgkpkiLPDGTTQGL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642  65 FPPHNLRGTRGRELYGSL-----NTVYE--QNREsiywMDKtrYSAFSG-----TDLELKLRERGITELHLIGVCTDICV 132
Cdd:PTZ00331  87 WPPHCVQGTKGAQLHKDLvveriDIIIRkgTNRD----VDS--YSAFDNdkgskTGLAQILKAHGVRRVFICGLAFDFCV 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 518752642 133 LHTAVDAYNKGFSLTIHEDAVASFNPDGHSWALGHFrgsLGAGVV 177
Cdd:PTZ00331 161 LFTALDAVKLGFKVVVLEDATRAVDPDAISKQRAEL---LEAGVI 202
 
Name Accession Description Interval E-value
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
3-177 9.79e-54

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: 168.16  E-value: 9.79e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642   3 ALIVIDFTNDFVD-GSLPVgQPGIDIAPRVSELTEAFVGSGDYVVMAVDLHETNDPYHPESSLFPPHNLRGTRGRELYGS 81
Cdd:COG1335    1 ALLVIDVQNDFVPpGALAV-PGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPHCVPGTPGAELVPE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642  82 LntvyeQNRESIYWMDKTRYSAFSGTDLELKLRERGITELHLIGVCTDICVLHTAVDAYNKGFSLTIHEDAVASFNPDGH 161
Cdd:COG1335   80 L-----APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAH 154
                        170
                 ....*....|....*.
gi 518752642 162 SWALGHFRGsLGAGVV 177
Cdd:COG1335  155 EAALARLRA-AGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
3-169 7.06e-49

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: 155.50  E-value: 7.06e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642   3 ALIVIDFTNDFVDGSLPVGQPGIDIAPRVSELTEAFVGSGDYVVMAVDLHETNDPYHPESsLFPPHNLRGTRGRELYGSL 82
Cdd:cd00431    1 ALLVVDMQNDFVPGGGLLLPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAEL-LWPPHCVKGTEGAELVPEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642  83 ntvyeQNRESIYWMDKTRYSAFSGTDLELKLRERGITELHLIGVCTDICVLHTAVDAYNKGFSLTIHEDAVASFNPDGHS 162
Cdd:cd00431   80 -----APLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHE 154

                 ....*..
gi 518752642 163 WALGHFR 169
Cdd:cd00431  155 AALERLA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
3-180 3.26e-46

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 149.48  E-value: 3.26e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642    3 ALIVIDFTNDFVDGSLPVGQPGIDIAPRVSELTEAFVGSGDYVVMAVDLHETNDPYHPESSLFPPHNLRGTRGRELYGSL 82
Cdd:pfam00857   2 ALLVIDMQNDFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDRPSPAFPPGTTGAELVPEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642   83 nTVYEQNRESiywmDKTRYSAFSGTDLELKLRERGITELHLIGVCTDICVLHTAVDAYNKGFSLTIHEDAVASFNPDGHS 162
Cdd:pfam00857  82 -APLPGDLVV----DKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHD 156
                         170
                  ....*....|....*...
gi 518752642  163 WALGHFRGSlGAGVVSGE 180
Cdd:pfam00857 157 AALERLAQR-GAEVTTTE 173
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
1-177 7.69e-28

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: 103.11  E-value: 7.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642   1 MRALIVIDFTNDFVD-GSLPVGQpGIDIAPRVSELTEAFvgSGDYVVMAVDLHETN---------------DPYHPESSL 64
Cdd:cd01011    1 TDALLVVDVQNDFCPgGALAVPG-GDAIVPLINALLSLF--QYDLVVATQDWHPANhasfasnhpgqmpfiTLPPGPQVL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642  65 FPPHNLRGTRGRELYGSLNTV---------YEQNRESiywmdktrYSAF------SGTDLELKLRERGITELHLIGVCTD 129
Cdd:cd01011   78 WPDHCVQGTPGAELHPGLPVPdidlivrkgTNPDIDS--------YSAFfdndrrSSTGLAEYLRERGIDRVDVVGLATD 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 518752642 130 ICVLHTAVDAYNKGFSLTIHEDAVASFNPDGHSWALGHFRgslGAGVV 177
Cdd:cd01011  150 YCVKATALDALKAGFEVRVLEDACRAVDPETIERAIEEMK---EAGVV 194
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
1-177 1.27e-22

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 89.74  E-value: 1.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642   1 MRALIVIDFTNDFV-DGSLPVgQPGIDIAPRVSELTE--AFvgsgDYVVMAVDLHETN-------------DPYHPESSL 64
Cdd:PTZ00331  12 NDALIIVDVQNDFCkGGSLAV-PDAEEVIPVINQVRQshHF----DLVVATQDWHPPNhisfasnhgkpkiLPDGTTQGL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642  65 FPPHNLRGTRGRELYGSL-----NTVYE--QNREsiywMDKtrYSAFSG-----TDLELKLRERGITELHLIGVCTDICV 132
Cdd:PTZ00331  87 WPPHCVQGTKGAQLHKDLvveriDIIIRkgTNRD----VDS--YSAFDNdkgskTGLAQILKAHGVRRVFICGLAFDFCV 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 518752642 133 LHTAVDAYNKGFSLTIHEDAVASFNPDGHSWALGHFrgsLGAGVV 177
Cdd:PTZ00331 161 LFTALDAVKLGFKVVVLEDATRAVDPDAISKQRAEL---LEAGVI 202
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
3-165 1.42e-17

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: 75.32  E-value: 1.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642   3 ALIVIDFTNDFVDGSLPvGQPGIDIAPRVSELTEAFVGSGDYVVMAVDLHETNDPYHPESSLFPPHNLRGTRGRELYgsl 82
Cdd:cd01014    1 ALLVIDVQNGYFDGGLP-PLNNEAALENIAALIAAARAAGIPVIHVRHIDDEGGSFAPGSEGWEIHPELAPLEGETV--- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642  83 ntvyeqnresiywMDKTRYSAFSGTDLELKLRERGITELHLIGVCTDICVLHTAVDAYNKGFSLTIHEDAVASFNPDGHS 162
Cdd:cd01014   77 -------------IEKTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDHG 143

                 ...
gi 518752642 163 WAL 165
Cdd:cd01014  144 GVL 146
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
3-165 1.51e-17

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 76.43  E-value: 1.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642   3 ALIVIDFTNDFVDGSLPVGQPGIDIAPRVSELTEAFVGSGD---YVVMAVDLHETNDPYHPEssLFPPHNLRGTRGRELY 79
Cdd:COG1535   21 ALLIHDMQNYFLRPYDPDEPPIRELVANIARLRDACRAAGIpvvYTAQPGDQTPEDRGLLND--FWGPGLTAGPEGQEIV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642  80 GSLnTVYEQNRESIYWmdktRYSAFSGTDLELKLRERGITELHLIGVCTDICVLHTAVDAYNKGFSLTIHEDAVASFNPD 159
Cdd:COG1535   99 DEL-APAPGDTVLTKW----RYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDIQPFVVADAVADFSRE 173

                 ....*.
gi 518752642 160 GHSWAL 165
Cdd:COG1535  174 EHRMAL 179
PRK11440 PRK11440
putative hydrolase; Provisional
3-167 5.03e-16

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 72.07  E-value: 5.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642   3 ALIVIDFTNdfvdGSLPV-GQP--GIDIAPRVSELTEAFVGSGDYVVM-----AVDLHETndPYHPESSLFPPHNLRGTR 74
Cdd:PRK11440  10 ALVVIDLQE----GILPFaGGPhtADEVVARAARLAAKFRASGSPVVLvrvgwSADYAEA--LKQPVDAPSPAKVLPENW 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642  75 GRelYGSLNTVYEQNRESIywmdKTRYSAFSGTDLELKLRERGITELHLIGVCTDICVLHTAVDAYNKGFSLTIHEDAVA 154
Cdd:PRK11440  84 WQ--HPAALGKTDSDIEVT----KRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACS 157
                        170
                 ....*....|...
gi 518752642 155 SFNPDGHSWALGH 167
Cdd:PRK11440 158 AASAEQHQNSMNH 170
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
3-178 1.36e-14

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: 67.81  E-value: 1.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642   3 ALIVIDFTNDFVDGSLPVGqPGID-IAPRVSELTEAFVGSGDYVVMAVDLHETNDPYHPESSLFPPHNLRGTRGRELYGS 81
Cdd:cd01015    1 ALLVIDLVEGYTQPGSYLA-PGIAaALENVQRLLAAARAAGVPVIHTTVVYDPDGADGGLWARKVPAMSDLVEGSPLAAI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642  82 LNTVYEQNRESIywMDKTRYSAFSGTDLELKLRERGITELHLIGVCTDICVLHTAVDAYNKGFSLTIHEDAVASFNPDGH 161
Cdd:cd01015   80 CDELAPQEDEMV--LVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVRECVGDRAPAPH 157
                        170
                 ....*....|....*..
gi 518752642 162 SWALGHFRGSLGAgVVS 178
Cdd:cd01015  158 EANLFDIDNKYGD-VVS 173
PLN02621 PLN02621
nicotinamidase
3-161 8.34e-14

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 66.34  E-value: 8.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642   3 ALIVIDFTNDF---VDGSLPVGQPGIDIAPRVSelteafvgsgdyVVMAVDLHETNDPY-HPESSLFPPHNL--RGTRGR 76
Cdd:PLN02621  22 ALLVIDMQNYFssmAEPILPALLTTIDLCRRAS------------IPVFFTRHSHKSPSdYGMLGEWWDGDLilDGTTEA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642  77 ELYGSLNTVYEQNResiyWMDKTRYSAFSGTDLELKLRERGITELHLIGVCTDICVLHTAVDAYNKGFSLTIHEDAVASF 156
Cdd:PLN02621  90 ELMPEIGRVTGPDE----VVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATA 165

                 ....*
gi 518752642 157 NPDGH 161
Cdd:PLN02621 166 NEELH 170
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
2-148 1.65e-10

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 57.69  E-value: 1.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642   2 RALIVIDFTNDFV-DGSLPV--GQPGIDIAPRvseLTEAFVGSGDYVVMAVDLHETN----------DPYH-------PE 61
Cdd:PRK11609   3 RALLLVDLQNDFCaGGALAVpeGDSTIDVANR---LIDWCQSRGIPVIASQDWHPANhgsfasnhgaEPGTqgeldglPQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642  62 SsLFPPHNLRGTRGRELYGSLNtvyeqnRESIYWM-------DKTRYSAF------SGTDLELKLRERGITELHLIGVCT 128
Cdd:PRK11609  80 T-WWPDHCVQNSEGAALHPLLN------QKAIDAVfhkgenpLIDSYSAFfdnghrQKTALDDWLREHGITELIVMGLAT 152
                        170       180
                 ....*....|....*....|
gi 518752642 129 DICVLHTAVDAYNKGFSLTI 148
Cdd:PRK11609 153 DYCVKFTVLDALALGYQVNV 172
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
96-165 2.94e-10

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: 56.58  E-value: 2.94e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642  96 MDKTRYSAFSGTDLELKLRERGITELHLIGVCTDICVLHTAVDAYNKGFSLTIHEDAVASFNPDGHSWAL 165
Cdd:cd01013  120 LTKWRYSAFKRSPLLERLKESGRDQLIITGVYAHIGCLSTAVDAFMRDIQPFVVADAIADFSLEEHRMAL 189
PLN02743 PLN02743
nicotinamidase
4-153 4.20e-07

nicotinamidase


Pssm-ID: 215396  Cd Length: 239  Bit Score: 48.20  E-value: 4.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642   4 LIVIDFTNDFVD---GSLPVGQPGIDIAPRVSE---LTEAFVGSGDYVVMAVDLHETNDPYHPesslFPPHNLRGTRGRE 77
Cdd:PLN02743  30 LVLVDEVNGFCTvgaGNLAPREPDKQISKMVDEsarLAREFCERKWPVLAFLDSHHPDKPEHP----YPPHCIVGTGEEN 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642  78 LYGSLNtvYEQNRESIYWMDKTRYSAF------SGTDLELK-LRERGITELHLIGVCTDICVLH---TAVDAYNKGFSLT 147
Cdd:PLN02743 106 LVPALQ--WLENDPNVTLRRKDCIDGFvgaiekDGSNVFVDwVNNNKIKVILVVGICTDICVLDfvaSALSARNHGILPP 183

                 ....*.
gi 518752642 148 IhEDAV 153
Cdd:PLN02743 184 L-EDVV 188
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
96-177 2.14e-06

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: 45.28  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518752642  96 MDKTRYSAFSGTDLELKLRERGITELHLIGVCTDICVLHTAVDAYNKGFSLTIHEDAVASFNPDGHSWALGHFRgslGAG 175
Cdd:cd01012   66 IEKTSFSCWEDEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRSKEDHELALARMR---QAG 142

                 ..
gi 518752642 176 VV 177
Cdd:cd01012  143 AV 144
 
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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