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Conserved domains on  [gi|1476636192|gb|AXZ47799|]
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cysteine hydrolase [Citrobacter freundii]

Protein Classification

cysteine hydrolase( domain architecture ID 10467615)

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
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 5-178 4.01e-36

Isochorismatase family; This family are hydrolase enzymes.


:

Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 124.44  E-value: 4.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192   5 AVLTNDLQYEFTYKITYSTQELEQKLTAFNQFLDGIRNQNQAVIHLQLINDPADPAVQRRYKNRDAGIPalaGRPENRII 84
Cdd:pfam00857   2 ALLVIDMQNDFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDRPSPAFPP---GTTGAELV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192  85 DSI-CAPSDLIVVKGRDSGFFNNNLDETLQKLGVKTVIVTGLQTHVCVQTTAADAFFRGYNVWVPEDCVFAPSADDTTRA 163
Cdd:pfam00857  79 PELaPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDAA 158

                         170
                  ....*....|....*
gi 1476636192 164 LEWLASYCATVAPSA 178
Cdd:pfam00857 159 LERLAQRGAEVTTTE 173
 
Name Accession Description Interval E-value
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 5-178 4.01e-36

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 124.44  E-value: 4.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192   5 AVLTNDLQYEFTYKITYSTQELEQKLTAFNQFLDGIRNQNQAVIHLQLINDPADPAVQRRYKNRDAGIPalaGRPENRII 84
Cdd:pfam00857   2 ALLVIDMQNDFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDRPSPAFPP---GTTGAELV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192  85 DSI-CAPSDLIVVKGRDSGFFNNNLDETLQKLGVKTVIVTGLQTHVCVQTTAADAFFRGYNVWVPEDCVFAPSADDTTRA 163
Cdd:pfam00857  79 PELaPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDAA 158

                         170
                  ....*....|....*
gi 1476636192 164 LEWLASYCATVAPSA 178
Cdd:pfam00857 159 LERLAQRGAEVTTTE 173
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 5-168 8.20e-35

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: 120.45  E-value: 8.20e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192   5 AVLTNDLQYEFTYKITYSTQELEQKLTAFNQFLDGIRNQNQAVIHLQLINDPADPAVQRRyknrDAGIPALAGRPENRII 84
Cdd:cd00431     1 ALLVVDMQNDFVPGGGLLLPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAEL----LWPPHCVKGTEGAELV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192  85 DSI-CAPSDLIVVKGRDSGFFNNNLDETLQKLGVKTVIVTGLQTHVCVQTTAADAFFRGYNVWVPEDCVFAPSADDTTRA 163
Cdd:cd00431    77 PELaPLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEAA 156


                  ....*
gi 1476636192 164 LEWLA 168
Cdd:cd00431   157 LERLA 161
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 5-175 1.12e-34

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: 120.39  E-value: 1.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192   5 AVLTNDLQYEFTYKITYSTQELEQKLTAFNQFLDGIRNQNQAVIHLQLINDPADPavqRRYKNRDAGIPALAGRPENRII 84
Cdd:COG1335     1 ALLVIDVQNDFVPPGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGS---EFAEFDLWPPHCVPGTPGAELV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192  85 DSI-CAPSDLIVVKGRDSGFFNNNLDETLQKLGVKTVIVTGLQTHVCVQTTAADAFFRGYNVWVPEDCVFAPSADDTTRA 163
Cdd:COG1335    78 PELaPLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAA 157

                         170
                  ....*....|..
gi 1476636192 164 LEWLASYCATVA 175
Cdd:COG1335   158 LARLRAAGATVV 169
PLN02621 PLN02621
nicotinamidase
 30-150 2.51e-16

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 73.66  E-value: 2.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192  30 LTAFNQFLDGIRNQNQAVIHLQLI-NDPADPAVQRRYKNRDAgipALAGRPENRIIDSI--CAPSDLIVVKGRDSGFFNN 106
Cdd:PLN02621   40 LPALLTTIDLCRRASIPVFFTRHShKSPSDYGMLGEWWDGDL---ILDGTTEAELMPEIgrVTGPDEVVEKSTYSAFYNT 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1476636192 107 NLDETLQKLGVKTVIVTGLQTHVCVQTTAADAFFRGYNVWVPED 150
Cdd:PLN02621  117 RLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTD 160
 
Name Accession Description Interval E-value
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 5-178 4.01e-36

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 124.44  E-value: 4.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192   5 AVLTNDLQYEFTYKITYSTQELEQKLTAFNQFLDGIRNQNQAVIHLQLINDPADPAVQRRYKNRDAGIPalaGRPENRII 84
Cdd:pfam00857   2 ALLVIDMQNDFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDRPSPAFPP---GTTGAELV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192  85 DSI-CAPSDLIVVKGRDSGFFNNNLDETLQKLGVKTVIVTGLQTHVCVQTTAADAFFRGYNVWVPEDCVFAPSADDTTRA 163
Cdd:pfam00857  79 PELaPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDAA 158

                         170
                  ....*....|....*
gi 1476636192 164 LEWLASYCATVAPSA 178
Cdd:pfam00857 159 LERLAQRGAEVTTTE 173
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 5-168 8.20e-35

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: 120.45  E-value: 8.20e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192   5 AVLTNDLQYEFTYKITYSTQELEQKLTAFNQFLDGIRNQNQAVIHLQLINDPADPAVQRRyknrDAGIPALAGRPENRII 84
Cdd:cd00431     1 ALLVVDMQNDFVPGGGLLLPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAEL----LWPPHCVKGTEGAELV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192  85 DSI-CAPSDLIVVKGRDSGFFNNNLDETLQKLGVKTVIVTGLQTHVCVQTTAADAFFRGYNVWVPEDCVFAPSADDTTRA 163
Cdd:cd00431    77 PELaPLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEAA 156


                  ....*
gi 1476636192 164 LEWLA 168
Cdd:cd00431   157 LERLA 161
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 5-175 1.12e-34

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: 120.39  E-value: 1.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192   5 AVLTNDLQYEFTYKITYSTQELEQKLTAFNQFLDGIRNQNQAVIHLQLINDPADPavqRRYKNRDAGIPALAGRPENRII 84
Cdd:COG1335     1 ALLVIDVQNDFVPPGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGS---EFAEFDLWPPHCVPGTPGAELV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192  85 DSI-CAPSDLIVVKGRDSGFFNNNLDETLQKLGVKTVIVTGLQTHVCVQTTAADAFFRGYNVWVPEDCVFAPSADDTTRA 163
Cdd:COG1335    78 PELaPLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAA 157

                         170
                  ....*....|..
gi 1476636192 164 LEWLASYCATVA 175
Cdd:COG1335   158 LARLRAAGATVV 169
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
73-185 2.02e-25

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 97.61  E-value: 2.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192  73 PALAGRPENR-IIDSIC-APSDLIVVKGRDSGFFNNNLDETLQKLGVKTVIVTGLQTHVCVQTTAADAFFRGYNVWVPED 150
Cdd:COG1535    86 PGLTAGPEGQeIVDELApAPGDTVLTKWRYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDIQPFVVAD 165

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1476636192 151 CVFAPSADDTTRALEWLASYCATVAPSAEILSLLA 185
Cdd:COG1535   166 AVADFSREEHRMALEYVAGRCGVVVTTDEVLEALR 200
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 10-164 8.09e-17

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: 73.78  E-value: 8.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192  10 DLQYEFTYKITYStQELEQKLTAFNQFLDGIRNQNQAVIHLQLINDPADPAVQrryknrdagipalaGRPENRIIDSICA 89
Cdd:cd01014     6 DVQNGYFDGGLPP-LNNEAALENIAALIAAARAAGIPVIHVRHIDDEGGSFAP--------------GSEGWEIHPELAP 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1476636192  90 -PSDLIVVKGRDSGFFNNNLDETLQKLGVKTVIVTGLQTHVCVQTTAADAFFRGYNVWVPEDCVFAPSADDTTRAL 164
Cdd:cd01014    71 lEGETVIEKTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDHGGVL 146
PLN02621 PLN02621
nicotinamidase
 30-150 2.51e-16

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 73.66  E-value: 2.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192  30 LTAFNQFLDGIRNQNQAVIHLQLI-NDPADPAVQRRYKNRDAgipALAGRPENRIIDSI--CAPSDLIVVKGRDSGFFNN 106
Cdd:PLN02621   40 LPALLTTIDLCRRASIPVFFTRHShKSPSDYGMLGEWWDGDL---ILDGTTEAELMPEIgrVTGPDEVVEKSTYSAFYNT 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1476636192 107 NLDETLQKLGVKTVIVTGLQTHVCVQTTAADAFFRGYNVWVPED 150
Cdd:PLN02621  117 RLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTD 160
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 5-152 1.38e-15

N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, carbon dioxide and ammonia. CSHase is involved in one of the two alternative pathways for creatinine degradation to glycine in microorganisms.This CSHase-containing pathway degrades creatinine via N-methylhydantoin N-carbamoylsarcosine and sarcosine to glycine. Enzymes of this pathway are used in the diagnosis for renal disfunction, for determining creatinine levels in urine and serum.


Pssm-ID: 238497 [Multi-domain]  Cd Length: 179  Bit Score: 71.28  E-value: 1.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192   5 AVLTNDLQYEFTYKITYSTQELEQKLTAFNQFLDGIRNQNQAVIHLQLINDPADPAVQRRYKnrdaGIPALAGRPENRII 84
Cdd:cd01015     1 ALLVIDLVEGYTQPGSYLAPGIAAALENVQRLLAAARAAGVPVIHTTVVYDPDGADGGLWAR----KVPAMSDLVEGSPL 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1476636192  85 DSIC-----APSDLIVVKGRDSGFFNNNLDETLQKLGVKTVIVTGLQTHVCVQTTAADAFFRGYNVWVPEDCV 152
Cdd:cd01015    77 AAICdelapQEDEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVRECV 149
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 89-165 7.87e-14

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: 66.08  E-value: 7.87e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1476636192  89 APSDLIVVKGRDSGFFNNNLDETLQKLGVKTVIVTGLQTHVCVQTTAADAFFRGYNVWVPEDCVFAPSADDTTRALE 165
Cdd:cd01012    60 FPDAPVIEKTSFSCWEDEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRSKEDHELALA 136
PRK11440 PRK11440
putative hydrolase; Provisional
 89-184 3.95e-13

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 64.75  E-value: 3.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192  89 APSDLIVVKGRDSGFFNNNLDETLQKLGVKTVIVTGLQTHVCVQTTAADAFFRGYNVWVPEDCVFAPSADDTTRALEWLA 168
Cdd:PRK11440   93 TDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAASAEQHQNSMNHIF 172

                          90
                  ....*....|....*.
gi 1476636192 169 SYCATVAPSAEILSLL 184
Cdd:PRK11440  173 PRIARVRSVEEILNAL 188
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
 73-174 2.51e-12

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: 62.74  E-value: 2.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192  73 PALAGRPENR-IIDSIC-APSDLIVVKGRDSGFFNNNLDETLQKLGVKTVIVTGLQTHVCVQTTAADAFFRGYNVWVPED 150
Cdd:cd01013    96 PGLTASPEETkIVTELApQPDDTVLTKWRYSAFKRSPLLERLKESGRDQLIITGVYAHIGCLSTAVDAFMRDIQPFVVAD 175

                          90       100
                  ....*....|....*....|....
gi 1476636192 151 CVFAPSADDTTRALEWLASYCATV 174
Cdd:cd01013   176 AIADFSLEEHRMALKYAATRCAMV 199
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 90-163 3.48e-11

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 59.70  E-value: 3.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192  90 PSDLIVVKGRD------SGFFNNN-----LDETLQKLGVKTVIVTGLQTHVCVQTTAADAFFRGYNVWVPEDCVfAPSAD 158
Cdd:PTZ00331  108 RIDIIIRKGTNrdvdsySAFDNDKgsktgLAQILKAHGVRRVFICGLAFDFCVLFTALDAVKLGFKVVVLEDAT-RAVDP 186


                  ....*
gi 1476636192 159 DTTRA 163
Cdd:PTZ00331  187 DAISK 191
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 92-165 1.83e-10

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: 57.66  E-value: 1.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192  92 DLIVVKGRD------SGFFNNN------LDETLQKLGVKTVIVTGLQTHVCVQTTAADAFFRGYNVWVPEDCVFAPSADD 159
Cdd:cd01011   101 DLIVRKGTNpdidsySAFFDNDrrsstgLAEYLRERGIDRVDVVGLATDYCVKATALDALKAGFEVRVLEDACRAVDPET 180


                  ....*.
gi 1476636192 160 TTRALE 165
Cdd:cd01011   181 IERAIE 186
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
92-185 1.21e-07

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 49.99  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636192  92 DLIVVKGRD------SGFFNNN------LDETLQKLGVKTVIVTGLQTHVCVQTTAADAFFRGYNVWVPED-C--VfAPS 156
Cdd:PRK11609  105 DAVFHKGENplidsySAFFDNGhrqktaLDDWLREHGITELIVMGLATDYCVKFTVLDALALGYQVNVITDgCrgV-NLQ 183

                          90       100
                  ....*....|....*....|....*....
gi 1476636192 157 ADDTTRALEWLASYCATVAPSAEILSLLA 185
Cdd:PRK11609  184 PQDSAHAFMEMSAAGATLYTLADWEETQG 212
 
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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