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Conserved domains on  [gi|446529545|ref|WP_000606891|]
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MULTISPECIES: isochorismatase family protein [Staphylococcus]

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 1.89e-58

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: 181.08  E-value: 1.89e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545   2 INFNKTALVLIDLQEGILKMDYAPYTAENVVQNANKLIDVFRKNNSFIVFVRVKFY-DGKDALK-----PNSMVSLPpke 75
Cdd:PRK11440   4 LNAKTTALVVIDLQEGILPFAGGPHTADEVVARAARLAAKFRASGSPVVLVRVGWSaDYAEALKqpvdaPSPAKVLP--- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545  76 gDDYSRFHHLLDKRDGDFVIDKRQFSAFVGTDLDLQLRRRGIDTIVLGGVATHVGVDTTARDAYQLNYDQYFVTDMMSAQ 155
Cdd:PRK11440  81 -ENWWQHPAALGKTDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAA 159
                        170       180
                 ....*....|....*....|....*....
gi 446529545 156 NETLHQFPIDNLFPIMGQTVTTSELLNIL 184
Cdd:PRK11440 160 SAEQHQNSMNHIFPRIARVRSVEEILNAL 188
 
Name Accession Description Interval E-value
PRK11440 PRK11440
putative hydrolase; Provisional
2-184 1.89e-58

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 181.08  E-value: 1.89e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545   2 INFNKTALVLIDLQEGILKMDYAPYTAENVVQNANKLIDVFRKNNSFIVFVRVKFY-DGKDALK-----PNSMVSLPpke 75
Cdd:PRK11440   4 LNAKTTALVVIDLQEGILPFAGGPHTADEVVARAARLAAKFRASGSPVVLVRVGWSaDYAEALKqpvdaPSPAKVLP--- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545  76 gDDYSRFHHLLDKRDGDFVIDKRQFSAFVGTDLDLQLRRRGIDTIVLGGVATHVGVDTTARDAYQLNYDQYFVTDMMSAQ 155
Cdd:PRK11440  81 -ENWWQHPAALGKTDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAA 159
                        170       180
                 ....*....|....*....|....*....
gi 446529545 156 NETLHQFPIDNLFPIMGQTVTTSELLNIL 184
Cdd:PRK11440 160 SAEQHQNSMNHIFPRIARVRSVEEILNAL 188
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
8-175 3.01e-49

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: 156.99  E-value: 3.01e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545   8 ALVLIDLQEGILK-MDYAPYTAENVVQNANKLIDVFRKNNSFIVFVRVKFYDGKDALKPNSMVSLPPKEGDDYSRFHHLL 86
Cdd:COG1335    1 ALLVIDVQNDFVPpGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPHCVPGTPGAELVPEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545  87 DKRDGDFVIDKRQFSAFVGTDLDLQLRRRGIDTIVLGGVATHVGVDTTARDAYQLNYDQYFVTDMMSAQNETLHQFPIDN 166
Cdd:COG1335   81 APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAALAR 160

                 ....*....
gi 446529545 167 LFPIMGQTV 175
Cdd:COG1335  161 LRAAGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
8-168 2.98e-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: 151.65  E-value: 2.98e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545   8 ALVLIDLQEGILK-MDYAPYTAENVVQNANKLIDVFRKNNSFIVFVRVKFYDGKDALKPNSMVSLPPKEGDDySRFHHLL 86
Cdd:cd00431    1 ALLVVDMQNDFVPgGGLLLPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAELLWPPHCVKGTEG-AELVPEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545  87 DKRDGDFVIDKRQFSAFVGTDLDLQLRRRGIDTIVLGGVATHVGVDTTARDAYQLNYDQYFVTDMMSAQNETLHQFPIDN 166
Cdd:cd00431   80 APLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEAALER 159

                 ..
gi 446529545 167 LF 168
Cdd:cd00431  160 LA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
7-177 3.06e-43

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 142.16  E-value: 3.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545    7 TALVLIDLQEGILK-MDYAPYTAENVVQNANKLIDVFRKNNSFIVFVRVKFYDGKDALKPNSMVSLPPKEGDDYSRFHHL 85
Cdd:pfam00857   1 TALLVIDMQNDFVDsGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDRPSPAFPPGTTGAELVPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545   86 LDKRDGDFVIDKRQFSAFVGTDLDLQLRRRGIDTIVLGGVATHVGVDTTARDAYQLNYDQYFVTDMMSAQNETLHQFPID 165
Cdd:pfam00857  81 LAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDAALE 160
                         170
                  ....*....|..
gi 446529545  166 NLFPIMGQTVTT 177
Cdd:pfam00857 161 RLAQRGAEVTTT 172
 
Name Accession Description Interval E-value
PRK11440 PRK11440
putative hydrolase; Provisional
2-184 1.89e-58

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 181.08  E-value: 1.89e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545   2 INFNKTALVLIDLQEGILKMDYAPYTAENVVQNANKLIDVFRKNNSFIVFVRVKFY-DGKDALK-----PNSMVSLPpke 75
Cdd:PRK11440   4 LNAKTTALVVIDLQEGILPFAGGPHTADEVVARAARLAAKFRASGSPVVLVRVGWSaDYAEALKqpvdaPSPAKVLP--- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545  76 gDDYSRFHHLLDKRDGDFVIDKRQFSAFVGTDLDLQLRRRGIDTIVLGGVATHVGVDTTARDAYQLNYDQYFVTDMMSAQ 155
Cdd:PRK11440  81 -ENWWQHPAALGKTDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAA 159
                        170       180
                 ....*....|....*....|....*....
gi 446529545 156 NETLHQFPIDNLFPIMGQTVTTSELLNIL 184
Cdd:PRK11440 160 SAEQHQNSMNHIFPRIARVRSVEEILNAL 188
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
8-175 3.01e-49

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: 156.99  E-value: 3.01e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545   8 ALVLIDLQEGILK-MDYAPYTAENVVQNANKLIDVFRKNNSFIVFVRVKFYDGKDALKPNSMVSLPPKEGDDYSRFHHLL 86
Cdd:COG1335    1 ALLVIDVQNDFVPpGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPHCVPGTPGAELVPEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545  87 DKRDGDFVIDKRQFSAFVGTDLDLQLRRRGIDTIVLGGVATHVGVDTTARDAYQLNYDQYFVTDMMSAQNETLHQFPIDN 166
Cdd:COG1335   81 APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAALAR 160

                 ....*....
gi 446529545 167 LFPIMGQTV 175
Cdd:COG1335  161 LRAAGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
8-168 2.98e-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: 151.65  E-value: 2.98e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545   8 ALVLIDLQEGILK-MDYAPYTAENVVQNANKLIDVFRKNNSFIVFVRVKFYDGKDALKPNSMVSLPPKEGDDySRFHHLL 86
Cdd:cd00431    1 ALLVVDMQNDFVPgGGLLLPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAELLWPPHCVKGTEG-AELVPEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545  87 DKRDGDFVIDKRQFSAFVGTDLDLQLRRRGIDTIVLGGVATHVGVDTTARDAYQLNYDQYFVTDMMSAQNETLHQFPIDN 166
Cdd:cd00431   80 APLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEAALER 159

                 ..
gi 446529545 167 LF 168
Cdd:cd00431  160 LA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
7-177 3.06e-43

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 142.16  E-value: 3.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545    7 TALVLIDLQEGILK-MDYAPYTAENVVQNANKLIDVFRKNNSFIVFVRVKFYDGKDALKPNSMVSLPPKEGDDYSRFHHL 85
Cdd:pfam00857   1 TALLVIDMQNDFVDsGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDRPSPAFPPGTTGAELVPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545   86 LDKRDGDFVIDKRQFSAFVGTDLDLQLRRRGIDTIVLGGVATHVGVDTTARDAYQLNYDQYFVTDMMSAQNETLHQFPID 165
Cdd:pfam00857  81 LAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDAALE 160
                         170
                  ....*....|..
gi 446529545  166 NLFPIMGQTVTT 177
Cdd:pfam00857 161 RLAQRGAEVTTT 172
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
8-150 5.63e-29

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: 104.98  E-value: 5.63e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545   8 ALVLIDLQEGILKMDYAPYTAENVVQNANKLIDVFRKNNSFIVFVRvKFYDGKDALKPNSmvslppkEGDDysrFHHLLD 87
Cdd:cd01014    1 ALLVIDVQNGYFDGGLPPLNNEAALENIAALIAAARAAGIPVIHVR-HIDDEGGSFAPGS-------EGWE---IHPELA 69
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446529545  88 KRDGDFVIDKRQFSAFVGTDLDLQLRRRGIDTIVLGGVATHVGVDTTARDAYQLNYDQYFVTD 150
Cdd:cd01014   70 PLEGETVIEKTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVAD 132
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
6-185 1.10e-27

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 103.01  E-value: 1.10e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545   6 KTALVLIDLQEGILK---MDYAPYTAenVVQNANKLIDVFRKNNSFIVFVRVKFY-DGKDALKPNSMVSLPPKEGDDYSR 81
Cdd:COG1535   19 RAALLIHDMQNYFLRpydPDEPPIRE--LVANIARLRDACRAAGIPVVYTAQPGDqTPEDRGLLNDFWGPGLTAGPEGQE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545  82 FHHLLDKRDGDFVIDKRQFSAFVGTDLDLQLRRRGIDTIVLGGVATHVGVDTTARDAYQLNYDQYFVTDMMSAQNETLHQ 161
Cdd:COG1535   97 IVDELAPAPGDTVLTKWRYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDIQPFVVADAVADFSREEHR 176
                        170       180
                 ....*....|....*....|....
gi 446529545 162 FPIDNLFPIMGQTVTTSELLNILN 185
Cdd:COG1535  177 MALEYVAGRCGVVVTTDEVLEALR 200
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
8-181 1.93e-19

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: 80.91  E-value: 1.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545   8 ALVLIDLQEGILkmDYAPYTAENV---VQNANKLIDVFRKNNSFIVFVRVKFYD-----GKDALKPNSMvsLPPKEGDDY 79
Cdd:cd01015    1 ALLVIDLVEGYT--QPGSYLAPGIaaaLENVQRLLAAARAAGVPVIHTTVVYDPdgadgGLWARKVPAM--SDLVEGSPL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545  80 SRFHHLLDKRDGDFVIDKRQFSAFVGTDLDLQLRRRGIDTIVLGGVATHVGVDTTARDAYQLNYDQYFVTDMMSAQNETL 159
Cdd:cd01015   77 AAICDELAPQEDEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVRECVGDRAPAP 156
                        170       180
                 ....*....|....*....|....*
gi 446529545 160 HQ---FPIDNLFpimGQTVTTSELL 181
Cdd:cd01015  157 HEanlFDIDNKY---GDVVSTDDAL 178
PLN02621 PLN02621
nicotinamidase
6-167 1.78e-13

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 65.57  E-value: 1.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545   6 KTALVLIDLQEGILKMdyapytAENVVQNANKLIDVFRKNNSFIVFVR------------VKFYDGKDALKPNSMVSLPP 73
Cdd:PLN02621  20 QAALLVIDMQNYFSSM------AEPILPALLTTIDLCRRASIPVFFTRhshkspsdygmlGEWWDGDLILDGTTEAELMP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545  74 KEGDdysrfhhlldKRDGDFVIDKRQFSAFVGTDLDLQLRRRGIDTIVLGGVATHVGVDTTARDAYQLNYDQYFVTDMMS 153
Cdd:PLN02621  94 EIGR----------VTGPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATA 163
                        170
                 ....*....|....
gi 446529545 154 AQNETLHQFPIDNL 167
Cdd:PLN02621 164 TANEELHEATLKNL 177
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
5-177 1.48e-11

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: 60.43  E-value: 1.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545   5 NKTALVLIDLQEGILkmDYAPYTAE---NVVQNANKLIDVFRKNNSFIVFvrvkfydgkdALKPNSMvslPP-------- 73
Cdd:cd01013   28 KRAVLLVHDMQRYFL--DFYDESAEpvpQLIANIARLRDWCRQAGIPVVY----------TAQPGNQ---TPeqrallnd 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545  74 ------KEGDDYSRFHHLLDKRDGDFVIDKRQFSAFVGTDLDLQLRRRGIDTIVLGGVATHVGVDTTARDAYQLNYDQYF 147
Cdd:cd01013   93 fwgpglTASPEETKIVTELAPQPDDTVLTKWRYSAFKRSPLLERLKESGRDQLIITGVYAHIGCLSTAVDAFMRDIQPFV 172
                        170       180       190
                 ....*....|....*....|....*....|
gi 446529545 148 VTDMMSAQNETLHQFPIDNLFPIMGQTVTT 177
Cdd:cd01013  173 VADAIADFSLEEHRMALKYAATRCAMVVST 202
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
6-150 3.46e-09

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 53.92  E-value: 3.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545   6 KTALVLIDLQEGILKMDYAPytaenvVQNANKLIDVF---RKNNSF-IVFV--------RVKF---YDGKDALKPNSMVS 70
Cdd:PTZ00331  12 NDALIIVDVQNDFCKGGSLA------VPDAEEVIPVInqvRQSHHFdLVVAtqdwhppnHISFasnHGKPKILPDGTTQG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545  71 LPPK---EGDDYSRFHHLLDKRDGDFVIDKRQ------FSAFVG-----TDLDLQLRRRGIDTIVLGGVATHVGVDTTAR 136
Cdd:PTZ00331  86 LWPPhcvQGTKGAQLHKDLVVERIDIIIRKGTnrdvdsYSAFDNdkgskTGLAQILKAHGVRRVFICGLAFDFCVLFTAL 165
                        170
                 ....*....|....
gi 446529545 137 DAYQLNYDQYFVTD 150
Cdd:PTZ00331 166 DAVKLGFKVVVLED 179
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
6-150 9.48e-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: 9.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545   6 KTALVLIDLQEGILKMDYAPYT-AENVVQNANKLIDVFRK-------------NNSFIVFVRVKFYDGKdaLKPNSMVSL 71
Cdd:cd01011    1 TDALLVVDVQNDFCPGGALAVPgGDAIVPLINALLSLFQYdlvvatqdwhpanHASFASNHPGQMPFIT--LPPGPQVLW 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545  72 PPK--EGDDYSRFHHLLDKRDGDFVIDKRQ------FSAFVG------TDLDLQLRRRGIDTIVLGGVATHVGVDTTARD 137
Cdd:cd01011   79 PDHcvQGTPGAELHPGLPVPDIDLIVRKGTnpdidsYSAFFDndrrssTGLAEYLRERGIDRVDVVGLATDYCVKATALD 158
                        170
                 ....*....|...
gi 446529545 138 AYQLNYDQYFVTD 150
Cdd:cd01011  159 ALKAGFEVRVLED 171
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
6-150 1.32e-08

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 52.30  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545   6 KTALVLIDLQEgilkmDYAPYTA------ENVVQNANKLIDVFRKNN---------------SFIVFVRVKFYD-GK-DA 62
Cdd:PRK11609   2 KRALLLVDLQN-----DFCAGGAlavpegDSTIDVANRLIDWCQSRGipviasqdwhpanhgSFASNHGAEPGTqGElDG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545  63 LK----PNSMVslppkEGDDYSRFHHLLDKRDGDFVIDKRQ------FSAF------VGTDLDLQLRRRGIDTIVLGGVA 126
Cdd:PRK11609  77 LPqtwwPDHCV-----QNSEGAALHPLLNQKAIDAVFHKGEnplidsYSAFfdnghrQKTALDDWLREHGITELIVMGLA 151
                        170       180
                 ....*....|....*....|....
gi 446529545 127 THVGVDTTARDAYQLNYDQYFVTD 150
Cdd:PRK11609 152 TDYCVKFTVLDALALGYQVNVITD 175
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
8-179 2.01e-08

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: 51.06  E-value: 2.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545   8 ALVLIDLQEGILK-MDYAPytaeNVVQNANKLIDVFRknnsfivfvrvkfydgkdALKPNSMVS--LPPKEGDdysRFHH 84
Cdd:cd01012    1 ALLLVDVQEKLAPaIKSFD----ELINNTVKLAKAAK------------------LLDVPVILTeqYPKGLGP---TVPE 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446529545  85 LLDKRDGDFVIDKRQFSAFVGTDLDLQLRRRGIDTIVLGGVATHVGVDTTARDAYQLNYDQYFVTDMMSAQNETLHQFPI 164
Cdd:cd01012   56 LREVFPDAPVIEKTSFSCWEDEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRSKEDHELAL 135
                        170
                 ....*....|....*...
gi 446529545 165 DNlfpiMGQT---VTTSE 179
Cdd:cd01012  136 AR----MRQAgavLTTSE 149
 
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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