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Conserved domains on  [gi|1264924599|gb|PGO59341|]
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cysteine hydrolase [Priestia megaterium]

Protein Classification

cysteine hydrolase family protein( domain architecture ID 10099067)

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

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

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 7-164 2.75e-58

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: 180.09  E-value: 2.75e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599   7 VLLLIDVQEGFYSPEWGERNNLDAEKHMLTLLQAWRRQDYPVIHVQHASGNPnSPLHPSSKGFQFKEGFGPQEDEYLIRK 86
Cdd:cd01014     1 ALLVIDVQNGYFDGGLPPLNNEAALENIAALIAAARAAGIPVIHVRHIDDEG-GSFAPGSEGWEIHPELAPLEGETVIEK 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1264924599  87 HVNSCFIGTELDSYLKANGYDTLILIGLTTNHCVSTTARMAGNLGYRTYVVNDATACFDCMsyDGKTRLPAEDVHTFA 164
Cdd:cd01014    80 TVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLP--DHGGVLSAEEIHAHY 155
 
Name Accession Description Interval E-value
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 7-164 2.75e-58

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: 180.09  E-value: 2.75e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599   7 VLLLIDVQEGFYSPEWGERNNLDAEKHMLTLLQAWRRQDYPVIHVQHASGNPnSPLHPSSKGFQFKEGFGPQEDEYLIRK 86
Cdd:cd01014     1 ALLVIDVQNGYFDGGLPPLNNEAALENIAALIAAARAAGIPVIHVRHIDDEG-GSFAPGSEGWEIHPELAPLEGETVIEK 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1264924599  87 HVNSCFIGTELDSYLKANGYDTLILIGLTTNHCVSTTARMAGNLGYRTYVVNDATACFDCMsyDGKTRLPAEDVHTFA 164
Cdd:cd01014    80 TVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLP--DHGGVLSAEEIHAHY 155
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 7-176 1.97e-51

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: 163.15  E-value: 1.97e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599   7 VLLLIDVQEGFYSP-EWGERNNLDAEKHMLTLLQAWRRQDYPVIHVQHASGNPNS----------PLHPSSKGFQFKEGF 75
Cdd:COG1335     1 ALLVIDVQNDFVPPgALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSefaefdlwppHCVPGTPGAELVPEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599  76 GPQEDEYLIRKHVNSCFIGTELDSYLKANGYDTLILIGLTTNHCVSTTARMAGNLGYRTYVVNDATACFDcmsydgktrl 155
Cdd:COG1335    81 APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRD---------- 150

                         170       180
                  ....*....|....*....|.
gi 1264924599 156 paEDVHTFALSSLHEEFATVV 176
Cdd:COG1335   151 --PEAHEAALARLRAAGATVV 169
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 6-178 4.66e-33

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 116.35  E-value: 4.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599   6 PVLLLIDVQEGFYSpeWGERNNLDAEKhMLT----LLQAWRRQDYPVIHVQHaSGNPNSPLHPSSK-----------GFQ 70
Cdd:pfam00857   1 TALLVIDMQNDFVD--SGGPKVEGIAA-ILEninrLLKAARKAGIPVIFTRQ-VPEPDDADFALKDrpspafppgttGAE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599  71 FKEGFGPQEDEYLIRKHVNSCFIGTELDSYLKANGYDTLILIGLTTNHCVSTTARMAGNLGYRTYVVNDATACFDcmsyd 150
Cdd:pfam00857  77 LVPELAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLS----- 151

                         170       180
                  ....*....|....*....|....*...
gi 1264924599 151 gktrlpaEDVHTFALSSLHEEFATVVST 178
Cdd:pfam00857 152 -------PEAHDAALERLAQRGAEVTTT 172
PLN02621 PLN02621
nicotinamidase
 7-176 8.20e-15

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 69.42  E-value: 8.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599   7 VLLLIDVQEGFYSPEWGERNNLdaekhmLTLLQAWRRQDYPVIHVQHA--------------------SGNPNSPLHPSS 66
Cdd:PLN02621   22 ALLVIDMQNYFSSMAEPILPAL------LTTIDLCRRASIPVFFTRHShkspsdygmlgewwdgdlilDGTTEAELMPEI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599  67 KGFQfkegfgpqEDEYLIRKHVNSCFIGTELDSYLKANGYDTLILIGLTTNHCVSTTARMAGNLGYRTYVVNDATACFDc 146
Cdd:PLN02621   96 GRVT--------GPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATAN- 166

                         170       180       190
                  ....*....|....*....|....*....|
gi 1264924599 147 msydgktrlpaEDVHTFALSSLHEEFATVV 176
Cdd:PLN02621  167 -----------EELHEATLKNLAYGFAYLV 185
 
Name Accession Description Interval E-value
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 7-164 2.75e-58

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: 180.09  E-value: 2.75e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599   7 VLLLIDVQEGFYSPEWGERNNLDAEKHMLTLLQAWRRQDYPVIHVQHASGNPnSPLHPSSKGFQFKEGFGPQEDEYLIRK 86
Cdd:cd01014     1 ALLVIDVQNGYFDGGLPPLNNEAALENIAALIAAARAAGIPVIHVRHIDDEG-GSFAPGSEGWEIHPELAPLEGETVIEK 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1264924599  87 HVNSCFIGTELDSYLKANGYDTLILIGLTTNHCVSTTARMAGNLGYRTYVVNDATACFDCMsyDGKTRLPAEDVHTFA 164
Cdd:cd01014    80 TVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLP--DHGGVLSAEEIHAHY 155
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 7-176 1.97e-51

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: 163.15  E-value: 1.97e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599   7 VLLLIDVQEGFYSP-EWGERNNLDAEKHMLTLLQAWRRQDYPVIHVQHASGNPNS----------PLHPSSKGFQFKEGF 75
Cdd:COG1335     1 ALLVIDVQNDFVPPgALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSefaefdlwppHCVPGTPGAELVPEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599  76 GPQEDEYLIRKHVNSCFIGTELDSYLKANGYDTLILIGLTTNHCVSTTARMAGNLGYRTYVVNDATACFDcmsydgktrl 155
Cdd:COG1335    81 APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRD---------- 150

                         170       180
                  ....*....|....*....|.
gi 1264924599 156 paEDVHTFALSSLHEEFATVV 176
Cdd:COG1335   151 --PEAHEAALARLRAAGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 7-169 4.13e-45

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: 146.64  E-value: 4.13e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599   7 VLLLIDVQEGFYSPEWGERNNLD-AEKHMLTLLQAWRRQDYPVIHVQH---------ASGNPNSPLHPSSKGFQFKEGFG 76
Cdd:cd00431     1 ALLVVDMQNDFVPGGGLLLPGADeLVPNINRLLAAARAAGIPVIFTRDwhppddpefAELLWPPHCVKGTEGAELVPELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599  77 PQEDEYLIRKHVNSCFIGTELDSYLKANGYDTLILIGLTTNHCVSTTARMAGNLGYRTYVVNDATACFDcmsydgktrlp 156
Cdd:cd00431    81 PLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRD----------- 149

                         170
                  ....*....|...
gi 1264924599 157 aEDVHTFALSSLH 169
Cdd:cd00431   150 -EEDHEAALERLA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 6-178 4.66e-33

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 116.35  E-value: 4.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599   6 PVLLLIDVQEGFYSpeWGERNNLDAEKhMLT----LLQAWRRQDYPVIHVQHaSGNPNSPLHPSSK-----------GFQ 70
Cdd:pfam00857   1 TALLVIDMQNDFVD--SGGPKVEGIAA-ILEninrLLKAARKAGIPVIFTRQ-VPEPDDADFALKDrpspafppgttGAE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599  71 FKEGFGPQEDEYLIRKHVNSCFIGTELDSYLKANGYDTLILIGLTTNHCVSTTARMAGNLGYRTYVVNDATACFDcmsyd 150
Cdd:pfam00857  77 LVPELAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLS----- 151

                         170       180
                  ....*....|....*....|....*...
gi 1264924599 151 gktrlpaEDVHTFALSSLHEEFATVVST 178
Cdd:pfam00857 152 -------PEAHDAALERLAQRGAEVTTT 172
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
3-187 3.09e-23

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 91.84  E-value: 3.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599   3 RSRPVLLLIDVQE---GFYSPewGERNNLDAEKHMLTLLQAWRRQDYPVIHVQHAsGNPNSP------------LHPSSK 67
Cdd:COG1535    17 PARAALLIHDMQNyflRPYDP--DEPPIRELVANIARLRDACRAAGIPVVYTAQP-GDQTPEdrgllndfwgpgLTAGPE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599  68 GFQFKEGFGPQEDEYLIRKHVNSCFIGTELDSYLKANGYDTLILIGLTTNHCVSTTARMAGNLGYRTYVVNDATACFDcm 147
Cdd:COG1535    94 GQEIVDELAPAPGDTVLTKWRYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDIQPFVVADAVADFS-- 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1264924599 148 sydgktrlpaEDVHTFALSSLHEEFATVVSTKETLQVLQT 187
Cdd:COG1535   172 ----------REEHRMALEYVAGRCGVVVTTDEVLEALRA 201
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 8-183 5.05e-22

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: 87.84  E-value: 5.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599   8 LLLIDVQEGFYSP-EWGERNNLDAEKHMLTLLQAWRRQDYPVIH--VQHASGNPNSPL------------HPSSKGfQFK 72
Cdd:cd01015     2 LLVIDLVEGYTQPgSYLAPGIAAALENVQRLLAAARAAGVPVIHttVVYDPDGADGGLwarkvpamsdlvEGSPLA-AIC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599  73 EGFGPQEDEYLIRKHVNSCFIGTELDSYLKANGYDTLILIGLTTNHCVSTTARMAGNLGYRTYVVNDATAcfdcmsyDGk 152
Cdd:cd01015    81 DELAPQEDEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVRECVG-------DR- 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1264924599 153 trlpAEDVHTFALSSLHEEFATVVSTKETLQ 183
Cdd:cd01015   153 ----APAPHEANLFDIDNKYGDVVSTDDALA 179
PLN02621 PLN02621
nicotinamidase
 7-176 8.20e-15

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 69.42  E-value: 8.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599   7 VLLLIDVQEGFYSPEWGERNNLdaekhmLTLLQAWRRQDYPVIHVQHA--------------------SGNPNSPLHPSS 66
Cdd:PLN02621   22 ALLVIDMQNYFSSMAEPILPAL------LTTIDLCRRASIPVFFTRHShkspsdygmlgewwdgdlilDGTTEAELMPEI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599  67 KGFQfkegfgpqEDEYLIRKHVNSCFIGTELDSYLKANGYDTLILIGLTTNHCVSTTARMAGNLGYRTYVVNDATACFDc 146
Cdd:PLN02621   96 GRVT--------GPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATAN- 166

                         170       180       190
                  ....*....|....*....|....*....|
gi 1264924599 147 msydgktrlpaEDVHTFALSSLHEEFATVV 176
Cdd:PLN02621  167 -----------EELHEATLKNLAYGFAYLV 185
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 5-142 9.40e-14

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: 66.52  E-value: 9.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599   5 RPVLLLIDVQEGFYS------PEwGER-----NNL--DAEKHMLTLLQAWrrqdYPVIHVQHASGNPNSPLHPS------ 65
Cdd:cd01011     1 TDALLVVDVQNDFCPggalavPG-GDAivpliNALlsLFQYDLVVATQDW----HPANHASFASNHPGQMPFITlppgpq 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599  66 ----------SKGFQFKEGFGPQEDEYLIRKHVN------SCFIG------TELDSYLKANGYDTLILIGLTTNHCVSTT 123
Cdd:cd01011    76 vlwpdhcvqgTPGAELHPGLPVPDIDLIVRKGTNpdidsySAFFDndrrssTGLAEYLRERGIDRVDVVGLATDYCVKAT 155

                         170
                  ....*....|....*....
gi 1264924599 124 ARMAGNLGYRTYVVNDATA 142
Cdd:cd01011   156 ALDALKAGFEVRVLEDACR 174
PRK11440 PRK11440
putative hydrolase; Provisional
 8-185 1.59e-12

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 62.82  E-value: 1.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599   8 LLLIDVQEGFYSPEWGERNNLDAEKHMLTLLQAWRRQDYPVIHVQ---HASGN--PNSPLHPSSKG-------FQFKEGF 75
Cdd:PRK11440   11 LVVIDLQEGILPFAGGPHTADEVVARAARLAAKFRASGSPVVLVRvgwSADYAeaLKQPVDAPSPAkvlpenwWQHPAAL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599  76 GPQEDEYLIRKHVNSCFIGTELDSYLKANGYDTLILIGLTTNHCVSTTARMAGNLGYRTYVVNDATACfdcmsydgktrl 155
Cdd:PRK11440   91 GKTDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSA------------ 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 1264924599 156 PAEDVHTFALSSLHEEFATVVSTKETLQVL 185
Cdd:PRK11440  159 ASAEQHQNSMNHIFPRIARVRSVEEILNAL 188
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 7-145 3.52e-11

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 59.70  E-value: 3.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599   7 VLLLIDVQEGFYSP-----EWGER-----NNLDAEKH--MLTLLQAWrrqdYPVIHVQHASGNPNSPLHPS--------- 65
Cdd:PTZ00331   14 ALIIVDVQNDFCKGgslavPDAEEvipviNQVRQSHHfdLVVATQDW----HPPNHISFASNHGKPKILPDgttqglwpp 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599  66 -----SKGFQFKEGFGPQEDEYLIRKHVN------SCFIG-----TELDSYLKANGYDTLILIGLTTNHCVSTTARMAGN 129
Cdd:PTZ00331   90 hcvqgTKGAQLHKDLVVERIDIIIRKGTNrdvdsySAFDNdkgskTGLAQILKAHGVRRVFICGLAFDFCVLFTALDAVK 169

                         170
                  ....*....|....*.
gi 1264924599 130 LGYRTYVVNDATACFD 145
Cdd:PTZ00331  170 LGFKVVVLEDATRAVD 185
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
37-139 2.55e-10

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 57.31  E-value: 2.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599  37 LLQAWrrqdYPVIHVQHASGnpnSPLHP----SSKGFQFKEGFGPQEDEYlirkhvnSCFIG------TELDSYLKANGY 106
Cdd:PRK11609   77 LPQTW----WPDHCVQNSEG---AALHPllnqKAIDAVFHKGENPLIDSY-------SAFFDnghrqkTALDDWLREHGI 142

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1264924599 107 DTLILIGLTTNHCVSTTARMAGNLGYRTYVVND 139
Cdd:PRK11609  143 TELIVMGLATDYCVKFTVLDALALGYQVNVITD 175
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 7-142 3.49e-10

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: 56.06  E-value: 3.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599   7 VLLLIDVQEGFySPEWGERNNLdaEKHMLTLLQAWRRQDYPVIHVQHASGnPNSPLHPsskgfQFKEGFGpqEDEYLIRK 86
Cdd:cd01012     1 ALLLVDVQEKL-APAIKSFDEL--INNTVKLAKAAKLLDVPVILTEQYPK-GLGPTVP-----ELREVFP--DAPVIEKT 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1264924599  87 HVNSCfIGTELDSYLKANGYDTLILIGLTTNHCVSTTARMAGNLGYRTYVVNDATA 142
Cdd:cd01012    70 SFSCW-EDEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACG 124
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
 4-178 1.55e-05

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


Pssm-ID: 238495  Cd Length: 203  Bit Score: 43.87  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599   4 SRPVLLLIDVQEGFYSPeWGERNNLDAE--KHMLTLLQAWRRQDYPVIH-VQHASGNPNS---------P-LHPSSKGFQ 70
Cdd:cd01013    28 KRAVLLVHDMQRYFLDF-YDESAEPVPQliANIARLRDWCRQAGIPVVYtAQPGNQTPEQrallndfwgPgLTASPEETK 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264924599  71 FKEGFGPQEDEYLIRKHVNSCFIGTELDSYLKANGYDTLILIGLTTNHCVSTTARMAGNLGYRTYVVNDATACFdcmsyd 150
Cdd:cd01013   107 IVTELAPQPDDTVLTKWRYSAFKRSPLLERLKESGRDQLIITGVYAHIGCLSTAVDAFMRDIQPFVVADAIADF------ 180

                         170       180
                  ....*....|....*....|....*...
gi 1264924599 151 gktrlpAEDVHTFALSSLHEEFATVVST 178
Cdd:cd01013   181 ------SLEEHRMALKYAATRCAMVVST 202
 
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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