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Conserved domains on  [gi|18401044|ref|NP_566539|]
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Isochorismatase family protein [Arabidopsis thaliana]

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 ...
 9-184 1.30e-52

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: 166.23  E-value: 1.30e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044   9 ALLVIDMQNDFIEEGAVTqVKGGKSIVPNVIRVVELARQRGILVIWVVREHDRQGRDVELFRRhnysseKVGPVIKGTVG 88
Cdd:COG1335   1 ALLVIDVQNDFVPPGALA-VPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDL------WPPHCVPGTPG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044  89 AELVDGLMInEEDDYKIVKTRFSAFFSTNLHSFLQTSGVTKLVIAGVQTPNCIRQTVFDAVALDYpNVTVITDATAAATP 168
Cdd:COG1335  74 AELVPELAP-LPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGY-EVTVVEDACASRDP 151

                       170
                ....*....|....*.
gi 18401044 169 EIHTANILDMKNIGVK 184
Cdd:COG1335 152 EAHEAALARLRAAGAT 167
 
Name Accession Description Interval E-value
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 9-184 1.30e-52

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: 166.23  E-value: 1.30e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044   9 ALLVIDMQNDFIEEGAVTqVKGGKSIVPNVIRVVELARQRGILVIWVVREHDRQGRDVELFRRhnysseKVGPVIKGTVG 88
Cdd:COG1335   1 ALLVIDVQNDFVPPGALA-VPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDL------WPPHCVPGTPG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044  89 AELVDGLMInEEDDYKIVKTRFSAFFSTNLHSFLQTSGVTKLVIAGVQTPNCIRQTVFDAVALDYpNVTVITDATAAATP 168
Cdd:COG1335  74 AELVPELAP-LPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGY-EVTVVEDACASRDP 151

                       170
                ....*....|....*.
gi 18401044 169 EIHTANILDMKNIGVK 184
Cdd:COG1335 152 EAHEAALARLRAAGAT 167
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 9-179 1.51e-47

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: 152.81  E-value: 1.51e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044   9 ALLVIDMQNDFIEEGAVTqVKGGKSIVPNVIRVVELARQRGILVIWVVREHDRQGRDVELFRrhnysseKVGPVIKGTVG 88
Cdd:cd00431   1 ALLVVDMQNDFVPGGGLL-LPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAELL-------WPPHCVKGTEG 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044  89 AELVDGLmINEEDDYKIVKTRFSAFFSTNLHSFLQTSGVTKLVIAGVQTPNCIRQTVFDAVALDYpNVTVITDATAAATP 168
Cdd:cd00431  73 AELVPEL-APLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGY-RVIVVEDACATRDE 150

                       170
                ....*....|.
gi 18401044 169 EIHTANILDMK 179
Cdd:cd00431 151 EDHEAALERLA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 8-183 5.85e-43

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 141.77  E-value: 5.85e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044     8 TALLVIDMQNDFIEEGAVtQVKGGKSIVPNVIRVVELARQRGILVIWVVREHDRQGRDVELFRRhnysseKVGPVIKGTV 87
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGP-KVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDR------PSPAFPPGTT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044    88 GAELVDGLmINEEDDYKIVKTRFSAFFSTNLHSFLQTSGVTKLVIAGVQTPNCIRQTVFDAVALDYpNVTVITDATAAAT 167
Cdd:pfam00857  74 GAELVPEL-APLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGY-EVVVVSDACASLS 151

                         170
                  ....*....|....*.
gi 18401044   168 PEIHTANILDMKNIGV 183
Cdd:pfam00857 152 PEAHDAALERLAQRGA 167
PLN02621 PLN02621
nicotinamidase
 6-178 1.90e-22

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 89.45  E-value: 1.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044    6 RNTALLVIDMQNDFieegavtqVKGGKSIVPNVIRVVELARQRGILVIwvvrehdrqgrdvelFRRHNYSSEKVGP---- 81
Cdd:PLN02621  19 KQAALLVIDMQNYF--------SSMAEPILPALLTTIDLCRRASIPVF---------------FTRHSHKSPSDYGmlge 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044   82 ------VIKGTVGAELVDGLMINEEDDYKIVKTRFSAFFSTNLHSFLQTSGVTKLVIAGVQTPNCIRQTVFDAVALDYpN 155
Cdd:PLN02621  76 wwdgdlILDGTTEAELMPEIGRVTGPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGF-R 154

                        170       180
                 ....*....|....*....|...
gi 18401044  156 VTVITDATAAATPEIHTANILDM 178
Cdd:PLN02621 155 VFFSTDATATANEELHEATLKNL 177
 
Name Accession Description Interval E-value
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 9-184 1.30e-52

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: 166.23  E-value: 1.30e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044   9 ALLVIDMQNDFIEEGAVTqVKGGKSIVPNVIRVVELARQRGILVIWVVREHDRQGRDVELFRRhnysseKVGPVIKGTVG 88
Cdd:COG1335   1 ALLVIDVQNDFVPPGALA-VPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDL------WPPHCVPGTPG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044  89 AELVDGLMInEEDDYKIVKTRFSAFFSTNLHSFLQTSGVTKLVIAGVQTPNCIRQTVFDAVALDYpNVTVITDATAAATP 168
Cdd:COG1335  74 AELVPELAP-LPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGY-EVTVVEDACASRDP 151

                       170
                ....*....|....*.
gi 18401044 169 EIHTANILDMKNIGVK 184
Cdd:COG1335 152 EAHEAALARLRAAGAT 167
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 9-179 1.51e-47

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: 152.81  E-value: 1.51e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044   9 ALLVIDMQNDFIEEGAVTqVKGGKSIVPNVIRVVELARQRGILVIWVVREHDRQGRDVELFRrhnysseKVGPVIKGTVG 88
Cdd:cd00431   1 ALLVVDMQNDFVPGGGLL-LPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAELL-------WPPHCVKGTEG 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044  89 AELVDGLmINEEDDYKIVKTRFSAFFSTNLHSFLQTSGVTKLVIAGVQTPNCIRQTVFDAVALDYpNVTVITDATAAATP 168
Cdd:cd00431  73 AELVPEL-APLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGY-RVIVVEDACATRDE 150

                       170
                ....*....|.
gi 18401044 169 EIHTANILDMK 179
Cdd:cd00431 151 EDHEAALERLA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 8-183 5.85e-43

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 141.77  E-value: 5.85e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044     8 TALLVIDMQNDFIEEGAVtQVKGGKSIVPNVIRVVELARQRGILVIWVVREHDRQGRDVELFRRhnysseKVGPVIKGTV 87
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGP-KVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDR------PSPAFPPGTT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044    88 GAELVDGLmINEEDDYKIVKTRFSAFFSTNLHSFLQTSGVTKLVIAGVQTPNCIRQTVFDAVALDYpNVTVITDATAAAT 167
Cdd:pfam00857  74 GAELVPEL-APLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGY-EVVVVSDACASLS 151

                         170
                  ....*....|....*.
gi 18401044   168 PEIHTANILDMKNIGV 183
Cdd:pfam00857 152 PEAHDAALERLAQRGA 167
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
8-178 2.19e-31

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 113.02  E-value: 2.19e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044   8 TALLVIDMQNDFIEEGAVTQvKGGKSIVPNVIRVVELARQRGILVIWVVREHDRQGRDVELFrrhnysSEKVGPVIK-GT 86
Cdd:COG1535  20 AALLIHDMQNYFLRPYDPDE-PPIRELVANIARLRDACRAAGIPVVYTAQPGDQTPEDRGLL------NDFWGPGLTaGP 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044  87 VGAELVDGLMiNEEDDYKIVKTRFSAFFSTNLHSFLQTSGVTKLVIAGVQTPNCIRQTVFDAVALDYpNVTVITDATAAA 166
Cdd:COG1535  93 EGQEIVDELA-PAPGDTVLTKWRYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDI-QPFVVADAVADF 170

                       170
                ....*....|..
gi 18401044 167 TPEIHTANILDM 178
Cdd:COG1535 171 SREEHRMALEYV 182
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 9-164 1.84e-26

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: 98.82  E-value: 1.84e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044   9 ALLVIDMQNDFIEEGAvtQVKGGKSIVPNVIRVVELARQRGILVIWVvrehdrqgrdvelfrRHNysSEKVGPVIKGTVG 88
Cdd:cd01014   1 ALLVIDVQNGYFDGGL--PPLNNEAALENIAALIAAARAAGIPVIHV---------------RHI--DDEGGSFAPGSEG 61

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18401044  89 AELVDGLmINEEDDYKIVKTRFSAFFSTNLHSFLQTSGVTKLVIAGVQTPNCIRQTVFDAVALDYPnVTVITDATA 164
Cdd:cd01014  62 WEIHPEL-APLEGETVIEKTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYD-VTVVADACA 135
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 9-180 1.95e-25

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: 96.70  E-value: 1.95e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044   9 ALLVIDMQNDFIEEGAVTqVKGGKSIVPNVIRVVELARQRGILVIWVVREHDRQGRDVELFRRhNYSSEKVgpVIKGTVG 88
Cdd:cd01015   1 ALLVIDLVEGYTQPGSYL-APGIAAALENVQRLLAAARAAGVPVIHTTVVYDPDGADGGLWAR-KVPAMSD--LVEGSPL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044  89 AELVDGLMiNEEDDYKIVKTRFSAFFSTNLHSFLQTSGVTKLVIAGVQTPNCIRQTVFDAVALDYpNVTVITDATAAATP 168
Cdd:cd01015  77 AAICDELA-PQEDEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGF-RPIVVRECVGDRAP 154

                       170
                ....*....|..
gi 18401044 169 EIHTANILDMKN 180
Cdd:cd01015 155 APHEANLFDIDN 166
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 7-184 9.46e-24

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: 92.71  E-value: 9.46e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044   7 NTALLVIDMQNDFIEEGAVTqVKGGKSIVPNVIRVVELARQRgiLVI----WVVREH---DRQGRDVELFRRHNYSSEKV 79
Cdd:cd01011   1 TDALLVVDVQNDFCPGGALA-VPGGDAIVPLINALLSLFQYD--LVVatqdWHPANHasfASNHPGQMPFITLPPGPQVL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044  80 GPV--IKGTVGAELVDGLMInEEDDYKIVK-TR-----FSAFF------STNLHSFLQTSGVTKLVIAGVQTPNCIRQTV 145
Cdd:cd01011  78 WPDhcVQGTPGAELHPGLPV-PDIDLIVRKgTNpdidsYSAFFdndrrsSTGLAEYLRERGIDRVDVVGLATDYCVKATA 156

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 18401044 146 FDAVALDYpNVTVITDATAAATPEIHTANILDMKNIGVK 184
Cdd:cd01011 157 LDALKAGF-EVRVLEDACRAVDPETIERAIEEMKEAGVV 194
PLN02621 PLN02621
nicotinamidase
 6-178 1.90e-22

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 89.45  E-value: 1.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044    6 RNTALLVIDMQNDFieegavtqVKGGKSIVPNVIRVVELARQRGILVIwvvrehdrqgrdvelFRRHNYSSEKVGP---- 81
Cdd:PLN02621  19 KQAALLVIDMQNYF--------SSMAEPILPALLTTIDLCRRASIPVF---------------FTRHSHKSPSDYGmlge 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044   82 ------VIKGTVGAELVDGLMINEEDDYKIVKTRFSAFFSTNLHSFLQTSGVTKLVIAGVQTPNCIRQTVFDAVALDYpN 155
Cdd:PLN02621  76 wwdgdlILDGTTEAELMPEIGRVTGPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGF-R 154

                        170       180
                 ....*....|....*....|...
gi 18401044  156 VTVITDATAAATPEIHTANILDM 178
Cdd:PLN02621 155 VFFSTDATATANEELHEATLKNL 177
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 6-184 6.38e-20

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 83.19  E-value: 6.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044    6 RNTALLVIDMQNDFIEEGAVTqVKGGKSIVPNVIRVVELARQRGILVI--WVVREH------------DRQGRDVELFRR 71
Cdd:PTZ00331  11 TNDALIIVDVQNDFCKGGSLA-VPDAEEVIPVINQVRQSHHFDLVVATqdWHPPNHisfasnhgkpkiLPDGTTQGLWPP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044   72 HnyssekvgpVIKGTVGAELVDGLMInEEDDYKIVK------TRFSAFF-----STNLHSFLQTSGVTKLVIAGVQTPNC 140
Cdd:PTZ00331  90 H---------CVQGTKGAQLHKDLVV-ERIDIIIRKgtnrdvDSYSAFDndkgsKTGLAQILKAHGVRRVFICGLAFDFC 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 18401044  141 IRQTVFDAVALDYpNVTVITDATAAATPEIHTANILDMKNIGVK 184
Cdd:PTZ00331 160 VLFTALDAVKLGF-KVVVLEDATRAVDPDAISKQRAELLEAGVI 202
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
7-196 9.77e-18

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 77.34  E-value: 9.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044    7 NTALLVIDMQNDFIEEGAVTqVKGGKSIVPNVIRVVELARQRGILVI----WVVREHDRqgrdvelFRRHnySSEKVG-- 80
Cdd:PRK11609   2 KRALLLVDLQNDFCAGGALA-VPEGDSTIDVANRLIDWCQSRGIPVIasqdWHPANHGS-------FASN--HGAEPGtq 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044   81 -----------PV--IKGTVGAELVDGLmiNEEDDYKIVKT-------RFSAFF------STNLHSFLQTSGVTKLVIAG 134
Cdd:PRK11609  72 geldglpqtwwPDhcVQNSEGAALHPLL--NQKAIDAVFHKgenplidSYSAFFdnghrqKTALDDWLREHGITELIVMG 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18401044  135 VQTPNCIRQTVFDAVALDYpNVTVITDATAAA--TPEIHTANILDMKNIGVKTPTLHEWSEELA 196
Cdd:PRK11609 150 LATDYCVKFTVLDALALGY-QVNVITDGCRGVnlQPQDSAHAFMEMSAAGATLYTLADWEETQG 212
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 9-184 3.73e-11

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: 58.76  E-value: 3.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044   9 ALLVIDMQndfieEGAVTQVKGGKSIVPNVIRVVELARQRGILVIWVvrEHdrqgrdvelfrrhnySSEKVGPvikgtvg 88
Cdd:cd01012   1 ALLLVDVQ-----EKLAPAIKSFDELINNTVKLAKAAKLLDVPVILT--EQ---------------YPKGLGP------- 51

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044  89 aeLVDGLMINEEDDYKIVKTRFSAFFSTNLHSFLQTSGVTKLVIAGVQTPNCIRQTVFDAVALDYpNVTVITDATAAATP 168
Cdd:cd01012  52 --TVPELREVFPDAPVIEKTSFSCWEDEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGY-EVFVVADACGSRSK 128

                       170
                ....*....|....*.
gi 18401044 169 EIHTANILDMKNIGVK 184
Cdd:cd01012 129 EDHELALARMRQAGAV 144
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
 9-171 1.62e-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: 55.04  E-value: 1.62e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044   9 ALLVIDMQN---DFIEEGA--VTQVkggksiVPNVIRVVELARQRGILVIWVVREHDRQGRDVELFrrhnysSEKVGPVI 83
Cdd:cd01013  31 VLLVHDMQRyflDFYDESAepVPQL------IANIARLRDWCRQAGIPVVYTAQPGNQTPEQRALL------NDFWGPGL 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044  84 KGT-VGAELVDGLMiNEEDDYKIVKTRFSAFFSTNLHSFLQTSGVTKLVIAGVQTPNCIRQTVFDAVALDYPNVtVITDA 162
Cdd:cd01013  99 TASpEETKIVTELA-PQPDDTVLTKWRYSAFKRSPLLERLKESGRDQLIITGVYAHIGCLSTAVDAFMRDIQPF-VVADA 176


                ....*....
gi 18401044 163 TAAATPEIH 171
Cdd:cd01013 177 IADFSLEEH 185
PRK11440 PRK11440
putative hydrolase; Provisional
 6-181 7.71e-04

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 38.56  E-value: 7.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044    6 RNTALLVIDMQndfieEGAVTQVKG---GKSIVPNVIRVVELARQRGILVIWVvrehdRQGRDVElfrrhnYSSEKVGPV 82
Cdd:PRK11440   7 KTTALVVIDLQ-----EGILPFAGGphtADEVVARAARLAAKFRASGSPVVLV-----RVGWSAD------YAEALKQPV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401044   83 IKGTVGAELVDGL------MINEEDDYKIVKTRFSAFFSTNLHSFLQTSGVTKLVIAGVQTPNCIRQTVFDAVALDYpNV 156
Cdd:PRK11440  71 DAPSPAKVLPENWwqhpaaLGKTDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGF-NL 149

                        170       180
                 ....*....|....*....|....*
gi 18401044  157 TVITDATAAATPEIHTANildMKNI 181
Cdd:PRK11440 150 VIAEDACSAASAEQHQNS---MNHI 171
 
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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