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Conserved domains on  [gi|738808103|ref|WP_036699095|]
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MULTISPECIES: cysteine hydrolase family protein [unclassified Paenibacillus]

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 5.37e-53

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: 166.62  E-value: 5.37e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103   3 ALIVIDFTNDFID-GNLPVgQPGIDIAPRVSELTEQFVRSGDYVVMAVDLHEADDPYHPEAKLFPPHNLRGSQGRELYGS 81
Cdd:COG1335    1 ALLVIDVQNDFVPpGALAV-PGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPHCVPGTPGAELVPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103  82 LKAvyeenREAIYWMDKTRYSAFCGTDLALKLRERGITEVHLIGVCTDICVLHTAVDAYNHGFGITVHEDAVASFNPDGH 161
Cdd:COG1335   80 LAP-----LPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAH 154

                        170
                 ....*....|....*.
gi 738808103 162 VWALGHFRGsLGAKVV 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 5.37e-53

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: 166.62  E-value: 5.37e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103   3 ALIVIDFTNDFID-GNLPVgQPGIDIAPRVSELTEQFVRSGDYVVMAVDLHEADDPYHPEAKLFPPHNLRGSQGRELYGS 81
Cdd:COG1335    1 ALLVIDVQNDFVPpGALAV-PGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPHCVPGTPGAELVPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103  82 LKAvyeenREAIYWMDKTRYSAFCGTDLALKLRERGITEVHLIGVCTDICVLHTAVDAYNHGFGITVHEDAVASFNPDGH 161
Cdd:COG1335   80 LAP-----LPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAH 154

                        170
                 ....*....|....*.
gi 738808103 162 VWALGHFRGsLGAKVV 177
Cdd:COG1335  155 EAALARLRA-AGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 3-169 3.83e-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: 156.66  E-value: 3.83e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103   3 ALIVIDFTNDFIDGNLPVGQPGIDIAPRVSELTEQFVRSGDYVVMAVDLHEADDPYHPEAkLFPPHNLRGSQGRELYGSL 82
Cdd:cd00431    1 ALLVVDMQNDFVPGGGLLLPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAEL-LWPPHCVKGTEGAELVPEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103  83 KavyeeNREAIYWMDKTRYSAFCGTDLALKLRERGITEVHLIGVCTDICVLHTAVDAYNHGFGITVHEDAVASFNPDGHV 162
Cdd:cd00431   80 A-----PLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHE 154


                 ....*..
gi 738808103 163 WALGHFR 169
Cdd:cd00431  155 AALERLA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 3-179 7.02e-44

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 143.70  E-value: 7.02e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103    3 ALIVIDFTNDFIDGNLPVGQPGIDIAPRVSELTEQFVRSGDYVVMAVDLHEADDPYHPEAKLFPPHNLRGSQGRELYGSL 82
Cdd:pfam00857   2 ALLVIDMQNDFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDRPSPAFPPGTTGAELVPEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103   83 KAVYEEnreaiYWMDKTRYSAFCGTDLALKLRERGITEVHLIGVCTDICVLHTAVDAYNHGFGITVHEDAVASFNPDGHV 162
Cdd:pfam00857  82 APLPGD-----LVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHD 156

                         170
                  ....*....|....*..
gi 738808103  163 WALGHFRGSlGAKVVTA 179
Cdd:pfam00857 157 AALERLAQR-GAEVTTT 172
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 1-160 3.29e-21

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 86.27  E-value: 3.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103   1 MRALIVIDFTNDFI-DGNLPVgQPGIDIAPRVSELTEQfvRSGDYVVMAVDLHEAD-------------DPYHPEAKLFP 66
Cdd:PTZ00331  12 NDALIIVDVQNDFCkGGSLAV-PDAEEVIPVINQVRQS--HHFDLVVATQDWHPPNhisfasnhgkpkiLPDGTTQGLWP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103  67 PHNLRGSQGRELYGSLkaVYEENREAI-----YWMDKtrYSAFCG-----TDLALKLRERGITEVHLIGVCTDICVLHTA 136
Cdd:PTZ00331  89 PHCVQGTKGAQLHKDL--VVERIDIIIrkgtnRDVDS--YSAFDNdkgskTGLAQILKAHGVRRVFICGLAFDFCVLFTA 164

                        170       180
                 ....*....|....*....|....
gi 738808103 137 VDAYNHGFGITVHEDAVASFNPDG 160
Cdd:PTZ00331 165 LDAVKLGFKVVVLEDATRAVDPDA 188
 
Name Accession Description Interval E-value
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 3-177 5.37e-53

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: 166.62  E-value: 5.37e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103   3 ALIVIDFTNDFID-GNLPVgQPGIDIAPRVSELTEQFVRSGDYVVMAVDLHEADDPYHPEAKLFPPHNLRGSQGRELYGS 81
Cdd:COG1335    1 ALLVIDVQNDFVPpGALAV-PGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPHCVPGTPGAELVPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103  82 LKAvyeenREAIYWMDKTRYSAFCGTDLALKLRERGITEVHLIGVCTDICVLHTAVDAYNHGFGITVHEDAVASFNPDGH 161
Cdd:COG1335   80 LAP-----LPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAH 154

                        170
                 ....*....|....*.
gi 738808103 162 VWALGHFRGsLGAKVV 177
Cdd:COG1335  155 EAALARLRA-AGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 3-169 3.83e-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: 156.66  E-value: 3.83e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103   3 ALIVIDFTNDFIDGNLPVGQPGIDIAPRVSELTEQFVRSGDYVVMAVDLHEADDPYHPEAkLFPPHNLRGSQGRELYGSL 82
Cdd:cd00431    1 ALLVVDMQNDFVPGGGLLLPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAEL-LWPPHCVKGTEGAELVPEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103  83 KavyeeNREAIYWMDKTRYSAFCGTDLALKLRERGITEVHLIGVCTDICVLHTAVDAYNHGFGITVHEDAVASFNPDGHV 162
Cdd:cd00431   80 A-----PLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHE 154


                 ....*..
gi 738808103 163 WALGHFR 169
Cdd:cd00431  155 AALERLA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 3-179 7.02e-44

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 143.70  E-value: 7.02e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103    3 ALIVIDFTNDFIDGNLPVGQPGIDIAPRVSELTEQFVRSGDYVVMAVDLHEADDPYHPEAKLFPPHNLRGSQGRELYGSL 82
Cdd:pfam00857   2 ALLVIDMQNDFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDRPSPAFPPGTTGAELVPEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103   83 KAVYEEnreaiYWMDKTRYSAFCGTDLALKLRERGITEVHLIGVCTDICVLHTAVDAYNHGFGITVHEDAVASFNPDGHV 162
Cdd:pfam00857  82 APLPGD-----LVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHD 156

                         170
                  ....*....|....*..
gi 738808103  163 WALGHFRGSlGAKVVTA 179
Cdd:pfam00857 157 AALERLAQR-GAEVTTT 172
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 1-177 2.19e-27

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: 101.96  E-value: 2.19e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103   1 MRALIVIDFTNDFID-GNLPVGQpGIDIAPRVSELTEQFvrSGDYVVMAVDLHEAD---------------DPYHPEAKL 64
Cdd:cd01011    1 TDALLVVDVQNDFCPgGALAVPG-GDAIVPLINALLSLF--QYDLVVATQDWHPANhasfasnhpgqmpfiTLPPGPQVL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103  65 FPPHNLRGSQGRELygsLKAVYEENREAIYW----MDKTRYSAF------CGTDLALKLRERGITEVHLIGVCTDICVLH 134
Cdd:cd01011   78 WPDHCVQGTPGAEL---HPGLPVPDIDLIVRkgtnPDIDSYSAFfdndrrSSTGLAEYLRERGIDRVDVVGLATDYCVKA 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 738808103 135 TAVDAYNHGFGITVHEDAVASFNPDGHVWALGHFRgSLGAKVV 177
Cdd:cd01011  155 TALDALKAGFEVRVLEDACRAVDPETIERAIEEMK-EAGVVLV 196
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 1-160 3.29e-21

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 86.27  E-value: 3.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103   1 MRALIVIDFTNDFI-DGNLPVgQPGIDIAPRVSELTEQfvRSGDYVVMAVDLHEAD-------------DPYHPEAKLFP 66
Cdd:PTZ00331  12 NDALIIVDVQNDFCkGGSLAV-PDAEEVIPVINQVRQS--HHFDLVVATQDWHPPNhisfasnhgkpkiLPDGTTQGLWP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103  67 PHNLRGSQGRELYGSLkaVYEENREAI-----YWMDKtrYSAFCG-----TDLALKLRERGITEVHLIGVCTDICVLHTA 136
Cdd:PTZ00331  89 PHCVQGTKGAQLHKDL--VVERIDIIIrkgtnRDVDS--YSAFDNdkgskTGLAQILKAHGVRRVFICGLAFDFCVLFTA 164

                        170       180
                 ....*....|....*....|....
gi 738808103 137 VDAYNHGFGITVHEDAVASFNPDG 160
Cdd:PTZ00331 165 LDAVKLGFKVVVLEDATRAVDPDA 188
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 3-165 4.20e-19

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: 79.17  E-value: 4.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103   3 ALIVIDFTNDFIDGNLPvGQPGIDIAPRVSELTEQFVRSGDYVVMAVdlHEADDPYhpeakLFPPhnlrGSQGRELYGSL 82
Cdd:cd01014    1 ALLVIDVQNGYFDGGLP-PLNNEAALENIAALIAAARAAGIPVIHVR--HIDDEGG-----SFAP----GSEGWEIHPEL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103  83 KAVYEENReaiywMDKTRYSAFCGTDLALKLRERGITEVHLIGVCTDICVLHTAVDAYNHGFGITVHEDAVASFNPDGHV 162
Cdd:cd01014   69 APLEGETV-----IEKTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDHG 143


                 ...
gi 738808103 163 WAL 165
Cdd:cd01014  144 GVL 146
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
3-182 2.31e-17

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 76.04  E-value: 2.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103   3 ALIVIDFTNDFIDGNLPVGQPGIDIAPRVSELTEQFVRSGD---YVVMAVDLHEADDPYhpEAKLFPPHNLRGSQGRELY 79
Cdd:COG1535   21 ALLIHDMQNYFLRPYDPDEPPIRELVANIARLRDACRAAGIpvvYTAQPGDQTPEDRGL--LNDFWGPGLTAGPEGQEIV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103  80 GSLkAVYEENREAIYWmdktRYSAFCGTDLALKLRERGITEVHLIGVCTDICVLHTAVDAYNHGFGITVHEDAVASFNPD 159
Cdd:COG1535   99 DEL-APAPGDTVLTKW----RYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDIQPFVVADAVADFSRE 173

                        170       180
                 ....*....|....*....|...
gi 738808103 160 GHVWALGHFRGSLGakVVTALGE 182
Cdd:COG1535  174 EHRMALEYVAGRCG--VVVTTDE 194
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 3-179 8.05e-16

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: 71.28  E-value: 8.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103   3 ALIVIDFTNDFIDGNLPVGqPGID-IAPRVSELTEQFVRSGDYVVMAVDLHEADDPYHPEAKLFPPHNLRGSQGRELYGS 81
Cdd:cd01015    1 ALLVIDLVEGYTQPGSYLA-PGIAaALENVQRLLAAARAAGVPVIHTTVVYDPDGADGGLWARKVPAMSDLVEGSPLAAI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103  82 LKAVYEENREAIywMDKTRYSAFCGTDLALKLRERGITEVHLIGVCTDICVLHTAVDAYNHGFGITVHEDAVASFNPDGH 161
Cdd:cd01015   80 CDELAPQEDEMV--LVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVRECVGDRAPAPH 157

                        170
                 ....*....|....*...
gi 738808103 162 VWALGHFRGSLGAKVVTA 179
Cdd:cd01015  158 EANLFDIDNKYGDVVSTD 175
PRK11440 PRK11440
putative hydrolase; Provisional
 3-167 1.03e-14

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 68.60  E-value: 1.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103   3 ALIVIDFTNdfidGNLPV-GQP--GIDIAPRVSELTEQFVRSGDYVVM-----AVDLHEAddPYHPEAKLFPPHNLRGSQ 74
Cdd:PRK11440  10 ALVVIDLQE----GILPFaGGPhtADEVVARAARLAAKFRASGSPVVLvrvgwSADYAEA--LKQPVDAPSPAKVLPENW 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103  75 GRelYGSLKAVYEENREAIywmdKTRYSAFCGTDLALKLRERGITEVHLIGVCTDICVLHTAVDAYNHGFGITVHEDAVA 154
Cdd:PRK11440  84 WQ--HPAALGKTDSDIEVT----KRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACS 157

                        170
                 ....*....|...
gi 738808103 155 SFNPDGHVWALGH 167
Cdd:PRK11440 158 AASAEQHQNSMNH 170
PLN02621 PLN02621
nicotinamidase
 97-165 2.67e-12

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 62.11  E-value: 2.67e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738808103  97 DKTRYSAFCGTDLALKLRERGITEVHLIGVCTDICVLHTAVDAYNHGFGITVHEDAVASFNPDGHVWAL 165
Cdd:PLN02621 106 EKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATANEELHEATL 174
PLN02743 PLN02743
nicotinamidase
 4-162 5.72e-11

nicotinamidase


Pssm-ID: 215396  Cd Length: 239  Bit Score: 59.37  E-value: 5.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103   4 LIVIDFTNDFID---GNLPVGQPGIDIAPRVSE---LTEQFvRSGDYVVMA-VDLHEADDPYHPeaklFPPHNLRGSQGR 76
Cdd:PLN02743  30 LVLVDEVNGFCTvgaGNLAPREPDKQISKMVDEsarLAREF-CERKWPVLAfLDSHHPDKPEHP----YPPHCIVGTGEE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103  77 ELYGSLKavYEENREAIYWMDKTRYSAFCGtdlALK----------LRERGITEVHLIGVCTDICVLH---TAVDAYNHG 143
Cdd:PLN02743 105 NLVPALQ--WLENDPNVTLRRKDCIDGFVG---AIEkdgsnvfvdwVNNNKIKVILVVGICTDICVLDfvaSALSARNHG 179

                        170       180
                 ....*....|....*....|....
gi 738808103 144 F-----GITVHEDAVASFNPDGHV 162
Cdd:PLN02743 180 IlppleDVVVYSRGCATYDLPLHV 203
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
2-148 8.65e-11

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 58.46  E-value: 8.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103   2 RALIVIDFTNDFIDGN-LPV--GQPGIDIAPRvseLTEQFVRSGDYVVMAVDLHEAD----------DPYH-------PE 61
Cdd:PRK11609   3 RALLLVDLQNDFCAGGaLAVpeGDSTIDVANR---LIDWCQSRGIPVIASQDWHPANhgsfasnhgaEPGTqgeldglPQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103  62 AkLFPPHNLRGSQGRELYGSLkavyeeNREAIYWM-------DKTRYSAF------CGTDLALKLRERGITEVHLIGVCT 128
Cdd:PRK11609  80 T-WWPDHCVQNSEGAALHPLL------NQKAIDAVfhkgenpLIDSYSAFfdnghrQKTALDDWLREHGITELIVMGLAT 152

                        170       180
                 ....*....|....*....|
gi 738808103 129 DICVLHTAVDAYNHGFGITV 148
Cdd:PRK11609 153 DYCVKFTVLDALALGYQVNV 172
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
 96-178 9.86e-09

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: 52.73  E-value: 9.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103  96 MDKTRYSAFCGTDLALKLRERGITEVHLIGVCTDICVLHTAVDAYNHGFGITVHEDAVASFNPDGHVWALgHFRGSLGAK 175
Cdd:cd01013  120 LTKWRYSAFKRSPLLERLKESGRDQLIITGVYAHIGCLSTAVDAFMRDIQPFVVADAIADFSLEEHRMAL-KYAATRCAM 198


                 ...
gi 738808103 176 VVT 178
Cdd:cd01013  199 VVS 201
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 96-178 3.21e-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: 44.89  E-value: 3.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738808103  96 MDKTRYSAFCGTDLALKLRERGITEVHLIGVCTDICVLHTAVDAYNHGFGITVHEDAVASFNPDGHVWALGHFRGSlGAK 175
Cdd:cd01012   66 IEKTSFSCWEDEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRSKEDHELALARMRQA-GAV 144


                 ...
gi 738808103 176 VVT 178
Cdd:cd01012  145 LTT 147
 
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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