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Conserved domains on  [gi|599619755|gb|EYF50723|]
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isochorismatase [Staphylococcus aureus T35604]

Protein Classification

cysteine hydrolase family protein( domain architecture ID 726)

cysteine hydrolase family protein, such as isochorismatase and nicotinamidase, catalyzes the hydrolysis of a chemical bond using an active site cysteinyl residue

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
cysteine_hydrolases super family cl00220
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
2-184 2.69e-54

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.


The actual alignment was detected with superfamily member PRK11440:

Pssm-ID: 444760  Cd Length: 188  Bit Score: 170.68  E-value: 2.69e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755   2 INFNKTALVLIDLQEGILKMDYAPHTAENVVQNANKLIDVFRKNNGFIAFVRVNFY-DGKDVLQ-----PNAMISLPpke 75
Cdd:PRK11440   4 LNAKTTALVVIDLQEGILPFAGGPHTADEVVARAARLAAKFRASGSPVVLVRVGWSaDYAEALKqpvdaPSPAKVLP--- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755  76 gDDYSRFHHLLDKRDDDFVIDKRHFSAFVGTDLDLQLRRRGIDTIVLGGVATHIGVDTTARDAYQLNYNQFFVTDMMSAQ 155
Cdd:PRK11440  81 -ENWWQHPAALGKTDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAA 159
                        170       180
                 ....*....|....*....|....*....
gi 599619755 156 NETLHQFPIDNVFPLMGQTITTNDFLNIL 184
Cdd:PRK11440 160 SAEQHQNSMNHIFPRIARVRSVEEILNAL 188
 
Name Accession Description Interval E-value
PRK11440 PRK11440
putative hydrolase; Provisional
2-184 2.69e-54

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 170.68  E-value: 2.69e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755   2 INFNKTALVLIDLQEGILKMDYAPHTAENVVQNANKLIDVFRKNNGFIAFVRVNFY-DGKDVLQ-----PNAMISLPpke 75
Cdd:PRK11440   4 LNAKTTALVVIDLQEGILPFAGGPHTADEVVARAARLAAKFRASGSPVVLVRVGWSaDYAEALKqpvdaPSPAKVLP--- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755  76 gDDYSRFHHLLDKRDDDFVIDKRHFSAFVGTDLDLQLRRRGIDTIVLGGVATHIGVDTTARDAYQLNYNQFFVTDMMSAQ 155
Cdd:PRK11440  81 -ENWWQHPAALGKTDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAA 159
                        170       180
                 ....*....|....*....|....*....
gi 599619755 156 NETLHQFPIDNVFPLMGQTITTNDFLNIL 184
Cdd:PRK11440 160 SAEQHQNSMNHIFPRIARVRSVEEILNAL 188
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
8-175 1.44e-47

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: 152.75  E-value: 1.44e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755   8 ALVLIDLQEGILK-MDYAPHTAENVVQNANKLIDVFRKNNGFIAFVRVNFYDGKDVLQPNAMISLPPKEGDDYSRFHHLL 86
Cdd:COG1335    1 ALLVIDVQNDFVPpGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPHCVPGTPGAELVPEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755  87 DKRDDDFVIDKRHFSAFVGTDLDLQLRRRGIDTIVLGGVATHIGVDTTARDAYQLNYNQFFVTDMMSAQNETLHQFPIDN 166
Cdd:COG1335   81 APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAALAR 160

                 ....*....
gi 599619755 167 VFPLMGQTI 175
Cdd:COG1335  161 LRAAGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
8-168 8.21e-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: 150.50  E-value: 8.21e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755   8 ALVLIDLQEGILK-MDYAPHTAENVVQNANKLIDVFRKNNGFIAFVRVNFYDGKDVLQPNAMISLPPKEGDDySRFHHLL 86
Cdd:cd00431    1 ALLVVDMQNDFVPgGGLLLPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAELLWPPHCVKGTEG-AELVPEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755  87 DKRDDDFVIDKRHFSAFVGTDLDLQLRRRGIDTIVLGGVATHIGVDTTARDAYQLNYNQFFVTDMMSAQNETLHQFPIDN 166
Cdd:cd00431   80 APLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEAALER 159

                 ..
gi 599619755 167 VF 168
Cdd:cd00431  160 LA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
7-178 3.29e-44

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 144.47  E-value: 3.29e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755    7 TALVLIDLQEGILK-MDYAPHTAENVVQNANKLIDVFRKNNGFIAFVRVNFYDGKDVLQPNAMISLPPKEGDDYSRFHHL 85
Cdd:pfam00857   1 TALLVIDMQNDFVDsGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDRPSPAFPPGTTGAELVPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755   86 LDKRDDDFVIDKRHFSAFVGTDLDLQLRRRGIDTIVLGGVATHIGVDTTARDAYQLNYNQFFVTDMMSAQNETLHQFPID 165
Cdd:pfam00857  81 LAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDAALE 160
                         170
                  ....*....|...
gi 599619755  166 NVFPLMGQTITTN 178
Cdd:pfam00857 161 RLAQRGAEVTTTE 173
 
Name Accession Description Interval E-value
PRK11440 PRK11440
putative hydrolase; Provisional
2-184 2.69e-54

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 170.68  E-value: 2.69e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755   2 INFNKTALVLIDLQEGILKMDYAPHTAENVVQNANKLIDVFRKNNGFIAFVRVNFY-DGKDVLQ-----PNAMISLPpke 75
Cdd:PRK11440   4 LNAKTTALVVIDLQEGILPFAGGPHTADEVVARAARLAAKFRASGSPVVLVRVGWSaDYAEALKqpvdaPSPAKVLP--- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755  76 gDDYSRFHHLLDKRDDDFVIDKRHFSAFVGTDLDLQLRRRGIDTIVLGGVATHIGVDTTARDAYQLNYNQFFVTDMMSAQ 155
Cdd:PRK11440  81 -ENWWQHPAALGKTDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAA 159
                        170       180
                 ....*....|....*....|....*....
gi 599619755 156 NETLHQFPIDNVFPLMGQTITTNDFLNIL 184
Cdd:PRK11440 160 SAEQHQNSMNHIFPRIARVRSVEEILNAL 188
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
8-175 1.44e-47

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: 152.75  E-value: 1.44e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755   8 ALVLIDLQEGILK-MDYAPHTAENVVQNANKLIDVFRKNNGFIAFVRVNFYDGKDVLQPNAMISLPPKEGDDYSRFHHLL 86
Cdd:COG1335    1 ALLVIDVQNDFVPpGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPHCVPGTPGAELVPEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755  87 DKRDDDFVIDKRHFSAFVGTDLDLQLRRRGIDTIVLGGVATHIGVDTTARDAYQLNYNQFFVTDMMSAQNETLHQFPIDN 166
Cdd:COG1335   81 APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAALAR 160

                 ....*....
gi 599619755 167 VFPLMGQTI 175
Cdd:COG1335  161 LRAAGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
8-168 8.21e-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: 150.50  E-value: 8.21e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755   8 ALVLIDLQEGILK-MDYAPHTAENVVQNANKLIDVFRKNNGFIAFVRVNFYDGKDVLQPNAMISLPPKEGDDySRFHHLL 86
Cdd:cd00431    1 ALLVVDMQNDFVPgGGLLLPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAELLWPPHCVKGTEG-AELVPEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755  87 DKRDDDFVIDKRHFSAFVGTDLDLQLRRRGIDTIVLGGVATHIGVDTTARDAYQLNYNQFFVTDMMSAQNETLHQFPIDN 166
Cdd:cd00431   80 APLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEAALER 159

                 ..
gi 599619755 167 VF 168
Cdd:cd00431  160 LA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
7-178 3.29e-44

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 144.47  E-value: 3.29e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755    7 TALVLIDLQEGILK-MDYAPHTAENVVQNANKLIDVFRKNNGFIAFVRVNFYDGKDVLQPNAMISLPPKEGDDYSRFHHL 85
Cdd:pfam00857   1 TALLVIDMQNDFVDsGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDRPSPAFPPGTTGAELVPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755   86 LDKRDDDFVIDKRHFSAFVGTDLDLQLRRRGIDTIVLGGVATHIGVDTTARDAYQLNYNQFFVTDMMSAQNETLHQFPID 165
Cdd:pfam00857  81 LAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDAALE 160
                         170
                  ....*....|...
gi 599619755  166 NVFPLMGQTITTN 178
Cdd:pfam00857 161 RLAQRGAEVTTTE 173
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
6-185 2.05e-29

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 107.24  E-value: 2.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755   6 KTALVLIDLQEGILK---MDYAPHTAenVVQNANKLIDVFRKNNgfiafVRVnFYdgkdVLQPNAMISL---------PP 73
Cdd:COG1535   19 RAALLIHDMQNYFLRpydPDEPPIRE--LVANIARLRDACRAAG-----IPV-VY----TAQPGDQTPEdrgllndfwGP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755  74 --KEGDDYSRFHHLLDKRDDDFVIDKRHFSAFVGTDLDLQLRRRGIDTIVLGGVATHIGVDTTARDAYQLNYNQFFVTDM 151
Cdd:COG1535   87 glTAGPEGQEIVDELAPAPGDTVLTKWRYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDIQPFVVADA 166
                        170       180       190
                 ....*....|....*....|....*....|....
gi 599619755 152 MSAQNETLHQFPIDNVFPLMGQTITTNDFLNILN 185
Cdd:COG1535  167 VADFSREEHRMALEYVAGRCGVVVTTDEVLEALR 200
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
8-150 5.25e-28

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: 102.28  E-value: 5.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755   8 ALVLIDLQEGILKMDYAPHTAENVVQNANKLIDVFRKNNGFIAFVRVNFYDGKdvlqpnamiSLPP-KEGDDysrFHHLL 86
Cdd:cd01014    1 ALLVIDVQNGYFDGGLPPLNNEAALENIAALIAAARAAGIPVIHVRHIDDEGG---------SFAPgSEGWE---IHPEL 68
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 599619755  87 DKRDDDFVIDKRHFSAFVGTDLDLQLRRRGIDTIVLGGVATHIGVDTTARDAYQLNYNQFFVTD 150
Cdd:cd01014   69 APLEGETVIEKTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVAD 132
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
8-181 2.65e-17

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: 75.13  E-value: 2.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755   8 ALVLIDLQEGIL--KMDYAPHTaENVVQNANKLIDVFRKNNGFIAFVRVNFYD-----GKDVLQPNAMisLPPKEGDDYS 80
Cdd:cd01015    1 ALLVIDLVEGYTqpGSYLAPGI-AAALENVQRLLAAARAAGVPVIHTTVVYDPdgadgGLWARKVPAM--SDLVEGSPLA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755  81 RFHHLLDKRDDDFVIDKRHFSAFVGTDLDLQLRRRGIDTIVLGGVATHIGVDTTARDAYQLNYNQFFVTDMMSAQNETLH 160
Cdd:cd01015   78 AICDELAPQEDEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVRECVGDRAPAPH 157
                        170       180
                 ....*....|....*....|....
gi 599619755 161 Q---FPIDNVFplmGQTITTNDFL 181
Cdd:cd01015  158 EanlFDIDNKY---GDVVSTDDAL 178
PLN02621 PLN02621
nicotinamidase
6-167 3.78e-14

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 67.50  E-value: 3.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755   6 KTALVLIDLQEGILKMdyaphtAENVVQNANKLIDVFRKNNGFIAFVRVN------------FYDGKDVLQPNAMISLPP 73
Cdd:PLN02621  20 QAALLVIDMQNYFSSM------AEPILPALLTTIDLCRRASIPVFFTRHShkspsdygmlgeWWDGDLILDGTTEAELMP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755  74 KEGDdysrfhhlldKRDDDFVIDKRHFSAFVGTDLDLQLRRRGIDTIVLGGVATHIGVDTTARDAYQLNYNQFFVTDMMS 153
Cdd:PLN02621  94 EIGR----------VTGPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATA 163
                        170
                 ....*....|....
gi 599619755 154 AQNETLHQFPIDNV 167
Cdd:PLN02621 164 TANEELHEATLKNL 177
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
5-177 2.98e-13

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: 65.05  E-value: 2.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755   5 NKTALVLIDLQEGILkmDYAPHTAE---NVVQNANKLIDVFRKNNgfiafVRVnFYDGkdvlQPNAMislPP-------- 73
Cdd:cd01013   28 KRAVLLVHDMQRYFL--DFYDESAEpvpQLIANIARLRDWCRQAG-----IPV-VYTA----QPGNQ---TPeqrallnd 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755  74 ------KEGDDYSRFHHLLDKRDDDFVIDKRHFSAFVGTDLDLQLRRRGIDTIVLGGVATHIGVDTTARDAYQLNYNQFF 147
Cdd:cd01013   93 fwgpglTASPEETKIVTELAPQPDDTVLTKWRYSAFKRSPLLERLKESGRDQLIITGVYAHIGCLSTAVDAFMRDIQPFV 172
                        170       180       190
                 ....*....|....*....|....*....|
gi 599619755 148 VTDMMSAQNETLHQFPIDNVFPLMGQTITT 177
Cdd:cd01013  173 VADAIADFSLEEHRMALKYAATRCAMVVST 202
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
8-162 3.02e-09

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: 53.37  E-value: 3.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755   8 ALVLIDLQEGIlkmdyAPHTA--ENVVQNANKLIDVFRknngfiafvrvnfydgkdVLQPNAMIS--LPPKEGddysrfh 83
Cdd:cd01012    1 ALLLVDVQEKL-----APAIKsfDELINNTVKLAKAAK------------------LLDVPVILTeqYPKGLG------- 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755  84 HLLDKRDDDF----VIDKRHFSAFVGTDLDLQLRRRGIDTIVLGGVATHIGVDTTARDAYQLNYNQFFVTDMMSAQNETL 159
Cdd:cd01012   51 PTVPELREVFpdapVIEKTSFSCWEDEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRSKED 130

                 ...
gi 599619755 160 HQF 162
Cdd:cd01012  131 HEL 133
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
80-150 8.08e-09

Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, converts nicotinamide to nicotinic acid (niacin) and ammonia, which in turn can be recycled to make nicotinamide adenine dinucleotide (NAD). The same enzyme is also called pyrazinamidase, because in converts the tuberculosis drug pyrazinamide (PZA) into its active form pyrazinoic acid (POA).


Pssm-ID: 238493  Cd Length: 196  Bit Score: 52.65  E-value: 8.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755  80 SRFHHLLDKRDDDFVIDK------------RHFSAFVGTDLDLQLRRRGIDTIVLGGVATHIGVDTTARDAYQLNYNQFF 147
Cdd:cd01011   89 AELHPGLPVPDIDLIVRKgtnpdidsysafFDNDRRSSTGLAEYLRERGIDRVDVVGLATDYCVKATALDALKAGFEVRV 168

                 ...
gi 599619755 148 VTD 150
Cdd:cd01011  169 LED 171
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
6-150 6.47e-06

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 44.67  E-value: 6.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755   6 KTALVLIDLQEGILKmdyaPHTAEnvVQNANKLIDVF---RKNNGFIAFV---------RVNF--YDGKDVLQPNAMISL 71
Cdd:PTZ00331  12 NDALIIVDVQNDFCK----GGSLA--VPDAEEVIPVInqvRQSHHFDLVVatqdwhppnHISFasNHGKPKILPDGTTQG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755  72 --PPK--EGDDYSRFHHLLDKRDDDFVIDK------RHFSAFVG-----TDLDLQLRRRGIDTIVLGGVATHIGVDTTAR 136
Cdd:PTZ00331  86 lwPPHcvQGTKGAQLHKDLVVERIDIIIRKgtnrdvDSYSAFDNdkgskTGLAQILKAHGVRRVFICGLAFDFCVLFTAL 165
                        170
                 ....*....|....
gi 599619755 137 DAYQLNYNQFFVTD 150
Cdd:PTZ00331 166 DAVKLGFKVVVLED 179
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
6-150 1.24e-05

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 43.83  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755   6 KTALVLIDLQEgilkmDYAPHTA------ENVVQNANKLIDVFRKNN-GFIA-----------FVrVNfyDGKDVLQPNA 67
Cdd:PRK11609   2 KRALLLVDLQN-----DFCAGGAlavpegDSTIDVANRLIDWCQSRGiPVIAsqdwhpanhgsFA-SN--HGAEPGTQGE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599619755  68 MISLP----PK---EGDDYSRFHHLLDKRDDDFVIDK------RHFSAF------VGTDLDLQLRRRGIDTIVLGGVATH 128
Cdd:PRK11609  74 LDGLPqtwwPDhcvQNSEGAALHPLLNQKAIDAVFHKgenpliDSYSAFfdnghrQKTALDDWLREHGITELIVMGLATD 153
                        170       180
                 ....*....|....*....|..
gi 599619755 129 IGVDTTARDAYQLNYNQFFVTD 150
Cdd:PRK11609 154 YCVKFTVLDALALGYQVNVITD 175
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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