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Conserved domains on  [gi|1198899064|ref|WP_087014505|]
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nitrilase-related carbon-nitrogen hydrolase [Leucobacter sp. 7(1)]

Protein Classification

carbon-nitrogen hydrolase family protein( domain architecture ID 27728)

carbon-nitrogen hydrolase family protein similar to nitrilase, which is involved in the reduction of organic nitrogen compounds and ammonia production, breaks carbon-nitrogen bonds and depends on a Glu-Lys-Cys catalytic triad

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nitrilase super family cl11424
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
 2-261 2.51e-70

Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes; This superfamily (also known as the C-N hydrolase superfamily) contains hydrolases that break carbon-nitrogen bonds; it includes nitrilases, cyanide dihydratases, aliphatic amidases, N-terminal amidases, beta-ureidopropionases, biotinidases, pantotheinase, N-carbamyl-D-amino acid amidohydrolases, the glutaminase domain of glutamine-dependent NAD+ synthetase, apolipoprotein N-acyltransferases, and N-carbamoylputrescine amidohydrolases, among others. These enzymes depend on a Glu-Lys-Cys catalytic triad, and work through a thiol acylenzyme intermediate. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. These oligomers include dimers, tetramers, hexamers, octamers, tetradecamers, octadecamers, as well as variable length helical arrangements and homo-oligomeric spirals. These proteins have roles in vitamin and co-enzyme metabolism, in detoxifying small molecules, in the synthesis of signaling molecules, and in the post-translational modification of proteins. They are used industrially, as biocatalysts in the fine chemical and pharmaceutical industry, in cyanide remediation, and in the treatment of toxic effluent. This superfamily has been classified previously in the literature, based on global and structure-based sequence analysis, into thirteen different enzyme classes (referred to as 1-13). This hierarchy includes those thirteen classes and a few additional subfamilies. A putative distant relative, the plasmid-borne TraB family, has not been included in the hierarchy.


The actual alignment was detected with superfamily member cd07576:

Pssm-ID: 448250  Cd Length: 254  Bit Score: 217.06  E-value: 2.51e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064   2 KIALLQAAATPLDPEANLAALREAAATAQAAGAELILTPELFLSGYAPRELASWLTPERVTGIPDAAAEIARDTGIAIAA 81
Cdd:cd07576     1 RLALYQGPARDGDVAANLARLDEAAARAAAAGADLLVFPELFLTGYNIGDAVARLAEPADGPALQALRAIARRHGIAIVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  82 SFPLaRADGTFAIAAELWDASGASVLRYEKVHLWGDLEPLAFTPStAAPAVAAWNGRSVGFQICYDIEFPEPARALAAGG 161
Cdd:cd07576    81 GYPE-RAGGAVYNAAVLIDEDGTVLANYRKTHLFGDSERAAFTPG-DRFPVVELRGLRVGLLICYDVEFPELVRALALAG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 162 VDLLLVPTAIDGHSAYVPELLVRARAAENALVVAYADHAGqaepsADPAADFTGLSTVAGREGRVLAVAGRTAELLCAEL 241
Cdd:cd07576   159 ADLVLVPTALMEPYGFVARTLVPARAFENQIFVAYANRCG-----AEDGLTYVGLSSIAGPDGTVLARAGRGEALLVADL 233

                         250       260
                  ....*....|....*....|..
gi 1198899064 242 pDVTPIAAG--EANYLRDRRPD 261
Cdd:cd07576   234 -DPAALAAArrENPYLADRRPE 254
 
Name Accession Description Interval E-value
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
 2-261 2.51e-70

Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); Pseudomonas sp. MCI3434 R-amidase hydrolyzes (R,S)-piperazine-2-tert-butylcarboxamide to form (R)-piperazine-2-carboxylic acid. It does so with strict R-stereoselectively. Its preferred substrates are carboxamide compounds which have the amino or imino group connected to their beta- or gamma-carbon. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), class 13 represents proteins that at the time were difficult to place in a distinct similarity group. It has been suggested that this subgroup represents a new class. Members of the nitrilase superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Native R-amidase however appears to be a monomer.


Pssm-ID: 143600  Cd Length: 254  Bit Score: 217.06  E-value: 2.51e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064   2 KIALLQAAATPLDPEANLAALREAAATAQAAGAELILTPELFLSGYAPRELASWLTPERVTGIPDAAAEIARDTGIAIAA 81
Cdd:cd07576     1 RLALYQGPARDGDVAANLARLDEAAARAAAAGADLLVFPELFLTGYNIGDAVARLAEPADGPALQALRAIARRHGIAIVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  82 SFPLaRADGTFAIAAELWDASGASVLRYEKVHLWGDLEPLAFTPStAAPAVAAWNGRSVGFQICYDIEFPEPARALAAGG 161
Cdd:cd07576    81 GYPE-RAGGAVYNAAVLIDEDGTVLANYRKTHLFGDSERAAFTPG-DRFPVVELRGLRVGLLICYDVEFPELVRALALAG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 162 VDLLLVPTAIDGHSAYVPELLVRARAAENALVVAYADHAGqaepsADPAADFTGLSTVAGREGRVLAVAGRTAELLCAEL 241
Cdd:cd07576   159 ADLVLVPTALMEPYGFVARTLVPARAFENQIFVAYANRCG-----AEDGLTYVGLSSIAGPDGTVLARAGRGEALLVADL 233

                         250       260
                  ....*....|....*....|..
gi 1198899064 242 pDVTPIAAG--EANYLRDRRPD 261
Cdd:cd07576   234 -DPAALAAArrENPYLADRRPE 254
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
1-263 4.45e-53

Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 173.13  E-value: 4.45e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064   1 MKIALLQAAATPLDPEANLAALREAAATAQAAGAELILTPELFLSGYAPRELASWLTPERVTG-IPDAAAEIARDTGIAI 79
Cdd:COG0388     2 MRIALAQLNPTVGDIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDGpALAALAELARELGIAV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  80 AASFPLARADGTFAIAAELWDASGASVLRYEKVHLWGDL---EPLAFTPSTAAPaVAAWNGRSVGFQICYDIEFPEPARA 156
Cdd:COG0388    82 VVGLPERDEGGRLYNTALVIDPDGEILGRYRKIHLPNYGvfdEKRYFTPGDELV-VFDTDGGRIGVLICYDLWFPELARA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 157 LAAGGVDLLLVPTAIDGHSAY-VPELLVRARAAENALVVAYADHAGqaepsADPAADFTGLSTVAGREGRVLAVAGRTAE 235
Cdd:COG0388   161 LALAGADLLLVPSASPFGRGKdHWELLLRARAIENGCYVVAANQVG-----GEDGLVFDGGSMIVDPDGEVLAEAGDEEG 235

                         250       260       270
                  ....*....|....*....|....*....|
gi 1198899064 236 LLCAELpDVTPIAAGEAN--YLRDRRPDVY 263
Cdd:COG0388   236 LLVADI-DLDRLREARRRfpVLRDRRPDLY 264
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
 2-235 5.39e-22

Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. The family includes: Nitrilase EC:3.5.5.1, Aliphatic amidase EC:3.5.1.4, Biotidinase EC:3.5.1.12, Beta-ureidopropionase EC:3.5.1.6. Nitrilase-related proteins generally have a conserved E-K-C catalytic triad, and are multimeric alpha-beta-beta-alpha sandwich proteins.


Pssm-ID: 425873 [Multi-domain]  Cd Length: 257  Bit Score: 91.65  E-value: 5.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064   2 KIALLQAAATPLDPEANLAALREAAATAQAAGAELILTPELFLSGYA----PRELASWLTPERVTGIpdaaAEIARDTGI 77
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQKALELIEEAARYGADLIVLPELFITGYPcwahFLEAAEVGDGETLAGL----AALARKNGI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  78 AIAASFP-LARADGTFAIAAELWDASGASVLRYEKVHLW------GDLEPLAFTPSTAAPAVAAWNGRsVGFQICYDIEF 150
Cdd:pfam00795  77 AIVIGLIeRWLTGGRLYNTAVLLDPDGKLVGKYRKLHLFpeprppGFRERVLFEPGDGGTVFDTPLGK-IGAAICYEIRF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 151 PEPARALAAGGVDLLLVPTAIDGH----SAYVPELLVRARAAENALVVAYADHAGQAEpsadPAADFTGLSTVAGREGRV 226
Cdd:pfam00795 156 PELLRALALKGAEILINPSARAPFpgslGPPQWLLLARARALENGCFVIAANQVGGEE----DAPWPYGHSMIIDPDGRI 231


                  ....*....
gi 1198899064 227 LAVAGRTAE 235
Cdd:pfam00795 232 LAGAGEWEE 240
PRK13981 PRK13981
NAD synthetase; Provisional
 35-197 9.60e-19

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 85.21  E-value: 9.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  35 ELILTPELFLSGYAPRELAswLTPERVTGIPDAAAEIARDT--GIAIAASFPLARADGTFAIAAELWDasGASVLRYEKV 112
Cdd:PRK13981   35 DLLLFPELFLSGYPPEDLL--LRPAFLAACEAALERLAAATagGPAVLVGHPWREGGKLYNAAALLDG--GEVLATYRKQ 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 113 HL--WG--DlEPLAFTPSTaAPAVAAWNGRSVGFQICYDIEFPEPARALAAGGVDLLLVPTAidghSAY------VPELL 182
Cdd:PRK13981  111 DLpnYGvfD-EKRYFAPGP-EPGVVELKGVRIGVPICEDIWNPEPAETLAEAGAELLLVPNA----SPYhrgkpdLREAV 184

                         170
                  ....*....|....*
gi 1198899064 183 VRARAAENALVVAYA 197
Cdd:PRK13981  185 LRARVRETGLPLVYL 199
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
 35-197 4.44e-08

apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the lgt/lsp/lnt system which is found broadly in bacteria but not in archaea. This model represents one component of the "lipoprotein lgt/lsp/lnt system" genome property. [Protein fate, Protein modification and repair]


Pssm-ID: 273129 [Multi-domain]  Cd Length: 391  Bit Score: 53.13  E-value: 4.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  35 ELILTPE---LFLSGYAPRELASWLtpervtgipdaaAEIARDTGIAIAASFPLARADGTFAI--AAELWDASGASVLRY 109
Cdd:TIGR00546 199 DLVVWPEtafPFDLENSPQKLADRL------------KLLVLSKGIPILIGAPDAVPGGPYHYynSAYLVDPGGEVVQRY 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 110 EKVHL------------WGDLEPLAFTPSTAAPA------VAAWNGRSVGFQICYDIEFPEPARALAAGGVDLLLVPTAi 171
Cdd:TIGR00546 267 DKVKLvpfgeyiplgflFKWLSKLFFLLSQEDFSrgpgpqVLKLPGGKIAPLICYESIFPDLVRASARQGAELLVNLTN- 345

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1198899064 172 DGHSAYVPELLV-----RARAAENALVVAYA 197
Cdd:TIGR00546 346 DAWFGDSSGPWQhfalaRFRAIENGRPLVRA 376
 
Name Accession Description Interval E-value
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
 2-261 2.51e-70

Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); Pseudomonas sp. MCI3434 R-amidase hydrolyzes (R,S)-piperazine-2-tert-butylcarboxamide to form (R)-piperazine-2-carboxylic acid. It does so with strict R-stereoselectively. Its preferred substrates are carboxamide compounds which have the amino or imino group connected to their beta- or gamma-carbon. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), class 13 represents proteins that at the time were difficult to place in a distinct similarity group. It has been suggested that this subgroup represents a new class. Members of the nitrilase superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Native R-amidase however appears to be a monomer.


Pssm-ID: 143600  Cd Length: 254  Bit Score: 217.06  E-value: 2.51e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064   2 KIALLQAAATPLDPEANLAALREAAATAQAAGAELILTPELFLSGYAPRELASWLTPERVTGIPDAAAEIARDTGIAIAA 81
Cdd:cd07576     1 RLALYQGPARDGDVAANLARLDEAAARAAAAGADLLVFPELFLTGYNIGDAVARLAEPADGPALQALRAIARRHGIAIVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  82 SFPLaRADGTFAIAAELWDASGASVLRYEKVHLWGDLEPLAFTPStAAPAVAAWNGRSVGFQICYDIEFPEPARALAAGG 161
Cdd:cd07576    81 GYPE-RAGGAVYNAAVLIDEDGTVLANYRKTHLFGDSERAAFTPG-DRFPVVELRGLRVGLLICYDVEFPELVRALALAG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 162 VDLLLVPTAIDGHSAYVPELLVRARAAENALVVAYADHAGqaepsADPAADFTGLSTVAGREGRVLAVAGRTAELLCAEL 241
Cdd:cd07576   159 ADLVLVPTALMEPYGFVARTLVPARAFENQIFVAYANRCG-----AEDGLTYVGLSSIAGPDGTVLARAGRGEALLVADL 233

                         250       260
                  ....*....|....*....|..
gi 1198899064 242 pDVTPIAAG--EANYLRDRRPD 261
Cdd:cd07576   234 -DPAALAAArrENPYLADRRPE 254
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
1-263 4.45e-53

Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 173.13  E-value: 4.45e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064   1 MKIALLQAAATPLDPEANLAALREAAATAQAAGAELILTPELFLSGYAPRELASWLTPERVTG-IPDAAAEIARDTGIAI 79
Cdd:COG0388     2 MRIALAQLNPTVGDIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDGpALAALAELARELGIAV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  80 AASFPLARADGTFAIAAELWDASGASVLRYEKVHLWGDL---EPLAFTPSTAAPaVAAWNGRSVGFQICYDIEFPEPARA 156
Cdd:COG0388    82 VVGLPERDEGGRLYNTALVIDPDGEILGRYRKIHLPNYGvfdEKRYFTPGDELV-VFDTDGGRIGVLICYDLWFPELARA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 157 LAAGGVDLLLVPTAIDGHSAY-VPELLVRARAAENALVVAYADHAGqaepsADPAADFTGLSTVAGREGRVLAVAGRTAE 235
Cdd:COG0388   161 LALAGADLLLVPSASPFGRGKdHWELLLRARAIENGCYVVAANQVG-----GEDGLVFDGGSMIVDPDGEVLAEAGDEEG 235

                         250       260       270
                  ....*....|....*....|....*....|
gi 1198899064 236 LLCAELpDVTPIAAGEAN--YLRDRRPDVY 263
Cdd:COG0388   236 LLVADI-DLDRLREARRRfpVLRDRRPDLY 264
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
 3-259 2.20e-48

Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes; This superfamily (also known as the C-N hydrolase superfamily) contains hydrolases that break carbon-nitrogen bonds; it includes nitrilases, cyanide dihydratases, aliphatic amidases, N-terminal amidases, beta-ureidopropionases, biotinidases, pantotheinase, N-carbamyl-D-amino acid amidohydrolases, the glutaminase domain of glutamine-dependent NAD+ synthetase, apolipoprotein N-acyltransferases, and N-carbamoylputrescine amidohydrolases, among others. These enzymes depend on a Glu-Lys-Cys catalytic triad, and work through a thiol acylenzyme intermediate. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. These oligomers include dimers, tetramers, hexamers, octamers, tetradecamers, octadecamers, as well as variable length helical arrangements and homo-oligomeric spirals. These proteins have roles in vitamin and co-enzyme metabolism, in detoxifying small molecules, in the synthesis of signaling molecules, and in the post-translational modification of proteins. They are used industrially, as biocatalysts in the fine chemical and pharmaceutical industry, in cyanide remediation, and in the treatment of toxic effluent. This superfamily has been classified previously in the literature, based on global and structure-based sequence analysis, into thirteen different enzyme classes (referred to as 1-13). This hierarchy includes those thirteen classes and a few additional subfamilies. A putative distant relative, the plasmid-borne TraB family, has not been included in the hierarchy.


Pssm-ID: 143587 [Multi-domain]  Cd Length: 253  Bit Score: 160.57  E-value: 2.20e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064   3 IALLQAAATPLDPEANLAALREAAATAQAAGAELILTPELFLSGYAPRELASWLTPERVTGIP--DAAAEIARDTGIAIA 80
Cdd:cd07197     1 IAAVQLAPKIGDVEANLAKALRLIKEAAEQGADLIVLPELFLTGYSFESAKEDLDLAEELDGPtlEALAELAKELGIYIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  81 ASFPLaRADGTFAIAAELWDASGASVLRYEKVHLWGDLEPLAFTPSTAAPaVAAWNGRSVGFQICYDIEFPEPARALAAG 160
Cdd:cd07197    81 AGIAE-KDGDKLYNTAVVIDPDGEIIGKYRKIHLFDFGERRYFSPGDEFP-VFDTPGGKIGLLICYDLRFPELARELALK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 161 GVDLLLVPTAIDGHSAYVPELLVRARAAENALVVAYADHAGQaepsaDPAADFTGLSTVAGREGRVLAVAGRTAELLCAE 240
Cdd:cd07197   159 GADIILVPAAWPTARREHWELLLRARAIENGVYVVAANRVGE-----EGGLEFAGGSMIVDPDGEVLAEASEEEGILVAE 233

                         250       260
                  ....*....|....*....|
gi 1198899064 241 L-PDVTPIAAGEANYLRDRR 259
Cdd:cd07197   234 LdLDELREARKRWSYLRDRR 253
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 35-260 1.24e-28

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143608  Cd Length: 258  Bit Score: 109.38  E-value: 1.24e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  35 ELILTPELFLSGYAPRELAS--WLTPERVTG-IPDAAAEIARDTGIAIAASFPLARAD-GTFAIAAELWDASGASVLRYE 110
Cdd:cd07584    34 DLICFPELATTGYRPDLLGPklWELSEPIDGpTVRLFSELAKELGVYIVCGFVEKGGVpGKVYNSAVVIDPEGESLGVYR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 111 KVHLWGdLEPLAFTPSTAAPAVAAWNGRsVGFQICYDIEFPEPARALAAGGVDLLLVPTAIDGHSAYVPELLVRARAAEN 190
Cdd:cd07584   114 KIHLWG-LEKQYFREGEQYPVFDTPFGK-IGVMICYDMGFPEVARILTLKGAEVIFCPSAWREQDADIWDINLPARALEN 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1198899064 191 ALVVAYADHAGQAEPSADPaadftGLSTVAGREGRVLAVAGRTAE-LLCAELpDVTPIA--AGEANYLRDRRP 260
Cdd:cd07584   192 TVFVAAVNRVGNEGDLVLF-----GKSKILNPRGQVLAEASEEAEeILYAEI-DLDAIAdyRMTLPYLKDRKP 258
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 3-241 3.98e-27

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143605  Cd Length: 255  Bit Score: 105.35  E-value: 3.98e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064   3 IALLQAAATPlDPEANLAALREAAATAQAAGAELILTPELFLS-----GYAPRELASWLTPERVTGIpdaaAEIARDTGI 77
Cdd:cd07581     1 VALAQFASSG-DKEENLEKVRRLLAEAAAAGADLVVFPEYTMArfgdgLDDYARVAEPLDGPFVSAL----ARLARELGI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  78 AIAASFPLARADGTFAIAAELWDASGASVLRYEKVHLW---GDLEPLAFTP-STAAPAVAAWNGRSVGFQICYDIEFPEP 153
Cdd:cd07581    76 TVVAGMFEPAGDGRVYNTLVVVGPDGEIIAVYRKIHLYdafGFRESDTVAPgDELPPVVFVVGGVKVGLATCYDLRFPEL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 154 ARALAAGGVDLLLVPTA-IDG-HSAYVPELLVRARAAENALVVAYADHAGqaepsadpaADFTGLSTVAGREGRVLAVAG 231
Cdd:cd07581   156 ARALALAGADVIVVPAAwVAGpGKEEHWETLLRARALENTVYVAAAGQAG---------PRGIGRSMVVDPLGVVLADLG 226

                         250
                  ....*....|
gi 1198899064 232 RTAELLCAEL 241
Cdd:cd07581   227 EREGLLVADI 236
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 35-263 1.10e-26

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143604  Cd Length: 268  Bit Score: 104.35  E-value: 1.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  35 ELILTPELFLSGY--APRELASWLTPERVTGIPDAA-AEIARDTGIAIAASFPlARADGTFAIAAELWDASGAsVLRYEK 111
Cdd:cd07580    34 NLVVLPELANTGYvfESRDEAFALAEEVPDGASTRAwAELAAELGLYIVAGFA-ERDGDRLYNSAVLVGPDGV-IGTYRK 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 112 VHLWGDlEPLAFTP-STAAPAVAAWNGRsVGFQICYDIEFPEPARALAAGGVDLLLVPT---AIDGHSAYVPEL---LVR 184
Cdd:cd07580   112 AHLWNE-EKLLFEPgDLGLPVFDTPFGR-IGVAICYDGWFPETFRLLALQGADIVCVPTnwvPMPRPPEGGPPManiLAM 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 185 ARAAENALVVAYADHAGQaepsaDPAADFTGLSTVAGREGRVLA-VAGRT-AELLCAELPDVTPIAAGEANY---LRDRR 259
Cdd:cd07580   190 AAAHSNGLFIACADRVGT-----ERGQPFIGQSLIVGPDGWPLAgPASGDeEEILLADIDLTAARRKRIWNSndvLRDRR 264


                  ....
gi 1198899064 260 PDVY 263
Cdd:cd07580   265 PDLY 268
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 2-259 4.71e-26

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143607  Cd Length: 253  Bit Score: 102.62  E-value: 4.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064   2 KIALLQAAATPLDPEANLAALREAAATAQAAGAELILTPELFLSGYAPRELasWLTPERVTG-IPDAAAEIARDTGIAIA 80
Cdd:cd07583     1 KIALIQLDIVWGDPEANIERVESLIEEAAAAGADLIVLPEMWNTGYFLDDL--YELADEDGGeTVSFLSELAKKHGVNIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  81 A-SFPLARADG----TFAIaaelwDASGASVLRYEKVHLWGDL-EPLAFTPSTaAPAVAAWNGRSVGFQICYDIEFPEPA 154
Cdd:cd07583    79 AgSVAEKEGGKlyntAYVI-----DPDGELIATYRKIHLFGLMgEDKYLTAGD-ELEVFELDGGKVGLFICYDLRFPELF 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 155 RALAAGGVDLLLVPtaidghsAYVPE-------LLVRARAAENALVVAYADHAGQaepsaDPAADFTGLSTVAGREGRVL 227
Cdd:cd07583   153 RKLALEGAEILFVP-------AEWPAariehwrTLLRARAIENQAFVVACNRVGT-----DGGNEFGGHSMVIDPWGEVL 220

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1198899064 228 AVAGRTAELLCAEL-PDVTPIAAGEANYLRDRR 259
Cdd:cd07583   221 AEAGEEEEILTAEIdLEEVAEVRKKIPVFKDRR 253
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
 35-263 3.98e-25

Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily (putative class 13 nitrilases); Uncharacterized subgroup of the nitrilase superfamily. This superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. Pyrococcus horikoshii Ph0642 is a hypothetical protein belonging to this subgroup. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). This subgroup was classified as belonging to class 13, which represents proteins that at the time were difficult to place in a distinct similarity group. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143601  Cd Length: 259  Bit Score: 100.07  E-value: 3.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  35 ELILTPELFLSGYA---PRELASwlTPErvtGIPDAAA-----EIARDTGIAIAASFPLARADGTFAIAAELWdaSGASV 106
Cdd:cd07577    31 DLIVLPELFNTGYAftsKEEVAS--LAE---SIPDGPTtrflqELARETGAYIVAGLPERDGDKFYNSAVVVG--PEGYI 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 107 LRYEKVHLWgDLEPLAFTPSTAAPAVAAWNGRSVGFQICYDIEFPEPARALAAGGVDLLLVPTAIdgHSAYVPELLVrAR 186
Cdd:cd07577   104 GIYRKTHLF-YEEKLFFEPGDTGFRVFDIGDIRIGVMICFDWYFPEAARTLALKGADIIAHPANL--VLPYCPKAMP-IR 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 187 AAENALVVAYADHAGQaEPSADPAADFTGLSTVAGREGRVLAVAGRTAELLcaELPDVTPIAA------GEANYLRDRRP 260
Cdd:cd07577   180 ALENRVFTITANRIGT-EERGGETLRFIGKSQITSPKGEVLARAPEDGEEV--LVAEIDPRLArdkrinEENDIFKDRRP 256


                  ...
gi 1198899064 261 DVY 263
Cdd:cd07577   257 EFY 259
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
 1-263 1.23e-23

N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known as N-carbamoylputrescine amidase and carbamoylputrescine hydrolase) converts N-carbamoylputrescine to putrescine, a step in polyamine biosynthesis in plants and bacteria. This subgroup includes Arabidopsis thaliana CPA, also known as nitrilase-like 1 (NLP1), and Pseudomonas aeruginosa AguB. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 11. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer; P. aeruginosa AugB is a homohexamer, Arabidopsis thaliana NLP1 is a homooctomer.


Pssm-ID: 143597  Cd Length: 284  Bit Score: 96.86  E-value: 1.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064   1 MKIALLQAAATPlDPEANLAALREAAATAQAAGAELILTPELFLSGYAPRE-------LASWLTPERVTgipDAAAEIAR 73
Cdd:cd07573     1 VTVALVQMACSE-DPEANLAKAEELVREAAAQGAQIVCLQELFETPYFCQEededyfdLAEPPIPGPTT---ARFQALAK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  74 DTGIAIAASFPLARADGTFAIAAELWDASGASVLRYEKVHLWGDL---EPLAFTPSTAAPAVaaWNGR--SVGFQICYDI 148
Cdd:cd07573    77 ELGVVIPVSLFEKRGNGLYYNSAVVIDADGSLLGVYRKMHIPDDPgyyEKFYFTPGDTGFKV--FDTRygRIGVLICWDQ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 149 EFPEPARALAAGGVDLLLVPTAIDGHSAYVPELL---------VRARAAENALVVAYADHAGqAEPSADPAADFTGLSTV 219
Cdd:cd07573   155 WFPEAARLMALQGAEILFYPTAIGSEPQEPPEGLdqrdawqrvQRGHAIANGVPVAAVNRVG-VEGDPGSGITFYGSSFI 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1198899064 220 AGREGRVLAVAGRTAE-LLCAELpDVTPIAAGEAN--YLRDRRPDVY 263
Cdd:cd07573   234 ADPFGEILAQASRDEEeILVAEF-DLDEIEEVRRAwpFFRDRRPDLY 279
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
 2-235 5.39e-22

Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. The family includes: Nitrilase EC:3.5.5.1, Aliphatic amidase EC:3.5.1.4, Biotidinase EC:3.5.1.12, Beta-ureidopropionase EC:3.5.1.6. Nitrilase-related proteins generally have a conserved E-K-C catalytic triad, and are multimeric alpha-beta-beta-alpha sandwich proteins.


Pssm-ID: 425873 [Multi-domain]  Cd Length: 257  Bit Score: 91.65  E-value: 5.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064   2 KIALLQAAATPLDPEANLAALREAAATAQAAGAELILTPELFLSGYA----PRELASWLTPERVTGIpdaaAEIARDTGI 77
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQKALELIEEAARYGADLIVLPELFITGYPcwahFLEAAEVGDGETLAGL----AALARKNGI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  78 AIAASFP-LARADGTFAIAAELWDASGASVLRYEKVHLW------GDLEPLAFTPSTAAPAVAAWNGRsVGFQICYDIEF 150
Cdd:pfam00795  77 AIVIGLIeRWLTGGRLYNTAVLLDPDGKLVGKYRKLHLFpeprppGFRERVLFEPGDGGTVFDTPLGK-IGAAICYEIRF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 151 PEPARALAAGGVDLLLVPTAIDGH----SAYVPELLVRARAAENALVVAYADHAGQAEpsadPAADFTGLSTVAGREGRV 226
Cdd:pfam00795 156 PELLRALALKGAEILINPSARAPFpgslGPPQWLLLARARALENGCFVIAANQVGGEE----DAPWPYGHSMIIDPDGRI 231


                  ....*....
gi 1198899064 227 LAVAGRTAE 235
Cdd:pfam00795 232 LAGAGEWEE 240
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 2-263 6.23e-21

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143609  Cd Length: 261  Bit Score: 88.91  E-value: 6.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064   2 KIALLQAAATPLDPEANLAALREAAATAQAAGAELILTPELFLSGYAPRElaswlTPERVTGIPD-----AAAEIARDTG 76
Cdd:cd07585     1 RIALVQFEARVGDKARNLAVIARWTRKAAAQGAELVCFPEMCITGYTHVR-----ALSREAEVPDgpstqALSDLARRYG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  77 IAIAASFpLARADGTFAIAAELWDASGaSVLRYEKVHLwGDLEPLAFTPSTAAPAVAAwNGRSVGFQICYDIEFPEPARA 156
Cdd:cd07585    76 LTILAGL-IEKAGDRPYNTYLVCLPDG-LVHRYRKLHL-FRREHPYIAAGDEYPVFAT-PGVRFGILICYDNHFPENVRA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 157 LAAGGVDLLLVPTAIDG-HSAYVPELLVR---ARAAENALVVAYADHAGQaepsaDPAADFTGLSTVAGREGRVLAVAGR 232
Cdd:cd07585   152 TALLGAEILFAPHATPGtTSPKGREWWMRwlpARAYDNGVFVAACNGVGR-----DGGEVFPGGAMILDPYGRVLAETTS 226

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1198899064 233 TAE-LLCAELPDVTPIAAGEANY---LRDRRPDVY 263
Cdd:cd07585   227 GGDgMVVADLDLDLINTVRGRRWisfLRARRPELY 261
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
 35-241 2.17e-19

Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); This subgroup includes mammalian Nit1 and Nit2, the Nit1-like domain of the invertebrate NitFhit, and various uncharacterized bacterial and archaeal Nit-like proteins. Nit1 and Nit2 are candidate tumor suppressor proteins. In NitFhit, the Nit1-like domain is encoded as a fusion protein with the non-homologous tumor suppressor, fragile histidine triad (Fhit). Mammalian Nit1 and Fhit may affect distinct signal pathways, and both may participate in DNA damage-induced apoptosis. Nit1 is a negative regulator in T cells. Overexpression of Nit2 in HeLa cells leads to a suppression of cell growth through cell cycle arrest in G2. These Nit proteins and the Nit1-like domain of NitFhit belong to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 10.


Pssm-ID: 143596  Cd Length: 265  Bit Score: 84.79  E-value: 2.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  35 ELILTPELFLSGYAPRELASWLTPERVTG-IPDAAAEIARDTGIAIAA-SFPL-ARADGTFAIAAELWDASGASVLRYEK 111
Cdd:cd07572    33 KLVVLPECFNYPGGTDAFKLALAEEEGDGpTLQALSELAKEHGIWLVGgSIPErDDDDGKVYNTSLVFDPDGELVARYRK 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 112 VHLWG-DL-------EPLAFTPSTAAPAVAAWNGRsVGFQICYDIEFPEPARALAAGGVDLLLVP---TAIDG--HSayv 178
Cdd:cd07572   113 IHLFDvDVpggisyrESDTLTPGDEVVVVDTPFGK-IGLGICYDLRFPELARALARQGADILTVPaafTMTTGpaHW--- 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1198899064 179 pELLVRARAAEN-ALVVAyadhAGQAEPSADPAADFtGLSTVAGREGRVLAVAGRTAELLCAEL 241
Cdd:cd07572   189 -ELLLRARAIENqCYVVA----AAQAGDHEAGRETY-GHSMIVDPWGEVLAEAGEGEGVVVAEI 246
PRK13981 PRK13981
NAD synthetase; Provisional
 35-197 9.60e-19

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 85.21  E-value: 9.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  35 ELILTPELFLSGYAPRELAswLTPERVTGIPDAAAEIARDT--GIAIAASFPLARADGTFAIAAELWDasGASVLRYEKV 112
Cdd:PRK13981   35 DLLLFPELFLSGYPPEDLL--LRPAFLAACEAALERLAAATagGPAVLVGHPWREGGKLYNAAALLDG--GEVLATYRKQ 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 113 HL--WG--DlEPLAFTPSTaAPAVAAWNGRSVGFQICYDIEFPEPARALAAGGVDLLLVPTAidghSAY------VPELL 182
Cdd:PRK13981  111 DLpnYGvfD-EKRYFAPGP-EPGVVELKGVRIGVPICEDIWNPEPAETLAEAGAELLLVPNA----SPYhrgkpdLREAV 184

                         170
                  ....*....|....*
gi 1198899064 183 VRARAAENALVVAYA 197
Cdd:PRK13981  185 LRARVRETGLPLVYL 199
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
 35-261 1.81e-16

Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an N-terminal RimI domain (class 12 nitrilases); Some members of this subgroup are implicated in post-translational modification, as they contain an N-terminal GCN5-related N-acetyltransferase (GNAT) protein RimI family domain. The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 12. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143598  Cd Length: 280  Bit Score: 76.86  E-value: 1.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  35 ELILTPELF---LSGYAPRE---LASWLT--PERVTGIPDAAAEIARDTGIAIAA-SFPLaRADGTFAIAAELWDASGaS 105
Cdd:cd07574    36 DLLVFPEYFtmeLLSLLPEAidgLDEAIRalAALTPDYVALFSELARKYGINIIAgSMPV-REDGRLYNRAYLFGPDG-T 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 106 VLRYEKVHL------WGDLEPlaftpsTAAPAVAAWNGRSVGFQICYDIEFPEPARALAAGGVDLLLVPTAIDGHSAYvp 179
Cdd:cd07574   114 IGHQDKLHMtpfereEWGISG------GDKLKVFDTDLGKIGILICYDSEFPELARALAEAGADLLLVPSCTDTRAGY-- 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 180 eLLVR----ARAAENALVVAYADHAGQAEPSadPAAD-FTGLSTVAG-------REGrVLAVA-GRTAELLCAELpDVTP 246
Cdd:cd07574   186 -WRVRigaqARALENQCYVVQSGTVGNAPWS--PAVDvNYGQAAVYTpcdfgfpEDG-ILAEGePNTEGWLIADL-DLEA 260

                         250
                  ....*....|....*....
gi 1198899064 247 IAA----GEANYLRDRRPD 261
Cdd:cd07574   261 LRRlreeGSVRNLRDWRED 279
PLN02747 PLN02747
N-carbamolyputrescine amidase
 36-263 4.12e-15

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 73.26  E-value: 4.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  36 LILTPELFLSGYAPR----ELASWLTPERVTGIPDAAAEIARDTGIAIAASFpLARADGTFAIAAELWDASGASVLRYEK 111
Cdd:PLN02747   41 IILIQELFEGYYFCQaqreDFFQRAKPYEGHPTIARMQKLAKELGVVIPVSF-FEEANNAHYNSIAIIDADGTDLGLYRK 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 112 VHL---WGDLEPLAFTPSTAAPAVAAWNGRSVGFQICYDIEFPEPARALAAGGVDLLLVPTAIdGHSAYVPEL------- 181
Cdd:PLN02747  120 SHIpdgPGYQEKFYFNPGDTGFKVFDTKFAKIGVAICWDQWFPEAARAMVLQGAEVLLYPTAI-GSEPQDPGLdsrdhwk 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 182 -LVRARAAENALVVAYADHAGQAE---PSADPAADFTGLSTVAGREGRVLAVAGRTAELLCAELPDVTPIAAGEANY--L 255
Cdd:PLN02747  199 rVMQGHAGANLVPLVASNRIGTEIletEHGPSKITFYGGSFIAGPTGEIVAEADDKAEAVLVAEFDLDQIKSKRASWgvF 278


                  ....*...
gi 1198899064 256 RDRRPDVY 263
Cdd:PLN02747  279 RDRRPDLY 286
nitrilase_4 cd07582
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 36-259 4.98e-14

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143606  Cd Length: 294  Bit Score: 70.45  E-value: 4.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  36 LILTPELFLSGY-APRELASWLTPERVTGIP----DAAAEIARDTGIAIAAS-------FPlaradGTFAIAAELWDASG 103
Cdd:cd07582    45 LVVLPEYALQGFpMGEPREVWQFDKAAIDIPgpetEALGEKAKELNVYIAANayerdpdFP-----GLYFNTAFIIDPSG 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 104 ASVLRYEKVHLWGD-------------LEPLAFTPSTAAPAVAAWNGRsVGFQICYDIEFPEPARALAAGGVDLLLVPTA 170
Cdd:cd07582   120 EIILRYRKMNSLAAegspsphdvwdeyIEVYGYGLDALFPVADTEIGN-LGCLACEEGLYPEVARGLAMNGAEVLLRSSS 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 171 IDGHSAYVP-ELLVRARAAENALVVAYADHAGQAePSADPAADFTGLSTVAGREGRVLAVAGRTAE--LLCAELpDVTP- 246
Cdd:cd07582   199 EVPSVELDPwEIANRARALENLAYVVSANSGGIY-GSPYPADSFGGGSMIVDYKGRVLAEAGYGPGsmVAGAEI-DIEAl 276

                         250
                  ....*....|....*..
gi 1198899064 247 ----IAAGEANYLRDRR 259
Cdd:cd07582   277 rrarARPGMHNWLKDLR 293
GAT_Gln-NAD-synth cd07570
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ...
 36-238 7.45e-14

Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases (class 7 and 8 nitrilases); Glutamine-dependent NAD synthetases are bifunctional enzymes, which have an N-terminal GAT domain and a C-terminal NAD+ synthetase domain. The GAT domain is a glutaminase (EC 3.5.1.2) which hydrolyses L-glutamine to L-glutamate and ammonia. The ammonia is used by the NAD+ synthetase domain in the ATP-dependent amidation of nicotinic acid adenine dinucleotide. Glutamine aminotransferases are categorized depending on their active site residues into different unrelated classes. This class of GAT domain belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to classes 7 and 8. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Mycobacterium tuberculosis glutamine-dependent NAD+ synthetase forms a homooctamer.


Pssm-ID: 143594 [Multi-domain]  Cd Length: 261  Bit Score: 69.42  E-value: 7.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  36 LILTPELFLSGYAPRELasWLTPERVTGIPDAAAEIARDT---GIAIAASFPLARADGTFAIAAELWDasGASVLRYEKV 112
Cdd:cd07570    35 LVVFPELSLTGYPPEDL--LLRPDFLEAAEEALEELAAATadlDIAVVVGLPLRHDGKLYNAAAVLQN--GKILGVVPKQ 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 113 HL----------WgdleplaFTPSTaAPAVAAWNGRSVGFQICYDIEFPE-PARALAAGGVDLLLVPTA---IDGHSAYV 178
Cdd:cd07570   111 LLpnygvfdekrY-------FTPGD-KPDVLFFKGLRIGVEICEDLWVPDpPSAELALAGADLILNLSAspfHLGKQDYR 182

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1198899064 179 pELLVRARAAENALVVAYADHAGqaepSADpaaD--FTGLSTVAGREGRVLAVAGRTAELLC 238
Cdd:cd07570   183 -RELVSSRSARTGLPYVYVNQVG----GQD---DlvFDGGSFIADNDGELLAEAPRFEEDLA 236
ML_beta-AS_like cd07568
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
 35-265 1.36e-13

mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This family includes mammalian-like beta-AS (EC 3.5.1.6, also known as beta-ureidopropionase or N-carbamoyl-beta-alanine amidohydrolase). This enzyme catalyzes the third and final step in the catabolic pyrimidine catabolic pathway responsible for the degradation of uracil and thymine, the hydrolysis of N-carbamyl-beta-alanine and N-carbamyl-beta-aminoisobutyrate to the beta-amino acids, beta-alanine and beta-aminoisobutyrate respectively. This family belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 5. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Beta-ASs from this subgroup are found in various oligomeric states, dimer (human), hexamer (calf liver), decamer (Arabidopsis and Zea mays), and in the case of Drosophila melanogaster beta-AS, as a homooctamer assembled as a left-handed helical turn, with the possibility of higher order oligomers formed by adding dimers at either end. Rat beta-AS changes its oligomeric state (hexamer, trimer, dodecamer) in response to allosteric effectors. Eukaryotic Saccharomyces kluyveri beta-AS belongs to a different superfamily.


Pssm-ID: 143592  Cd Length: 287  Bit Score: 69.06  E-value: 1.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  35 ELILTPELFLSGY-APRELASWLtpERVTGIPDAA-----AEIARDTGIAIAASFPLARADGTFAIAAELWDASGASVLR 108
Cdd:cd07568    45 QIVCLQEIFYGPYfCAEQDTKWY--EFAEEIPNGPttkrfAALAKEYNMVLILPIYEKEQGGTLYNTAAVIDADGTYLGK 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 109 YEKVHL------WgdlEPLAFTPSTAAPAVAAWNGRSVGFQICYDIEFPEPARALAAGGVDLLLVPTA-IDGHSAYVPEL 181
Cdd:cd07568   123 YRKNHIphvggfW---EKFYFRPGNLGYPVFDTAFGKIGVYICYDRHFPEGWRALGLNGAEIVFNPSAtVAGLSEYLWKL 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 182 LVRARAAENALVVAYADHAGQAEPSADpaADFTGLSTVAGREGRVLAVAGRTA-ELLCAELpDVTPIAAGEA--NYLRDR 258
Cdd:cd07568   200 EQPAAAVANGYFVGAINRVGTEAPWNI--GEFYGSSYFVDPRGQFVASASRDKdELLVAEL-DLDLIREVRDtwQFYRDR 276


                  ....*..
gi 1198899064 259 RPDVYAS 265
Cdd:cd07568   277 RPETYGE 283
aliphatic_amidase cd07565
aliphatic amidases (class 2 nitrilases); Aliphatic amidases catalyze the hydrolysis of ...
 35-241 3.90e-10

aliphatic amidases (class 2 nitrilases); Aliphatic amidases catalyze the hydrolysis of short-chain aliphatic amides to form ammonia and the corresponding organic acid. This group includes Pseudomonas aeruginosa (Pa) AmiE, the amidase from Geobacillus pallidus RAPc8 (RAPc8 amidase), and Helicobacter pylori (Hp) AmiE and AmiF. PaAimE and HpAmiE hydrolyze various very short aliphatic amides, including propionamide, acetamide and acrylamide. HpAmiF is a formamidase which specifically hydrolyzes formamide. These proteins belong to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 2. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. HpAmiE , HpAmiF, and RAPc8 amidase, and PaAimE appear to be homohexameric enzymes, trimer of dimers.


Pssm-ID: 143589  Cd Length: 291  Bit Score: 58.84  E-value: 3.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  35 ELILTPELFLSGYAPrelASWLTPERVTGIPDAAAEIARDTGIaiaasfpLARADGTFAI-------------AAELWDA 101
Cdd:cd07565    41 DLIVFPEYSTQGLMY---DKWTMDETACTVPGPETDIFAEACK-------EAKVWGVFSImernpdhgknpynTAIIIDD 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 102 SGASVLRYEKVHLWGDLEPLA----FTPSTAAPavaawNGRSVGFQICYDIEFPEPARALAAGGVDLLLVPTaidGHSAY 177
Cdd:cd07565   111 QGEIVLKYRKLHPWVPIEPWYpgdlGTPVCEGP-----KGSKIALIICHDGMYPEIARECAYKGAELIIRIQ---GYMYP 182

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1198899064 178 VPE---LLVRARAAENALVVAYADHAGqaepsADPAADFTGLSTVAGREGRVLAVAGRTA-ELLCAEL 241
Cdd:cd07565   183 AKDqwiITNKANAWCNLMYTASVNLAG-----FDGVFSYFGESMIVNFDGRTLGEGGREPdEIVTAEL 245
DCase cd07569
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ...
 35-263 3.72e-08

N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses N-carbamyl-D-amino acids to produce D-amino acids. It is an important biocatalyst in the pharmaceutical industry, producing useful D-amino acids for example in the preparation of beta-lactam antibiotics. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 6. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Agrobacterium radiobacter DCase forms a tetramer (dimer of dimers). Some DCases may form trimers.


Pssm-ID: 143593  Cd Length: 302  Bit Score: 53.08  E-value: 3.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  35 ELILTPELFLSGYAPR-------ELASWLTPERvtgiPDAAA----EIARDTGIAIAASFPLARADGTFAI---AAELWD 100
Cdd:cd07569    40 QLVVFPELALTTFFPRwyfpdeaELDSFFETEM----PNPETqplfDRAKELGIGFYLGYAELTEDGGVKRrfnTSILVD 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 101 ASGASVLRYEKVHLWGDLEPLAFTP------------STAAPAVAAWNGRsVGFQICYDIEFPEPARALAAGGVDLLLVP 168
Cdd:cd07569   116 KSGKIVGKYRKVHLPGHKEPEPYRPfqhlekryfepgDLGFPVFRVPGGI-MGMCICNDRRWPETWRVMGLQGVELVLLG 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 169 TAIDGHSAYVPE----------LLVRARAAENALVVAYADHAGQAEPSadpaaDFTGLSTVAGREGRVLAVA-GRTAELL 237
Cdd:cd07569   195 YNTPTHNPPAPEhdhlrlfhnlLSMQAGAYQNGTWVVAAAKAGMEDGC-----DLIGGSCIVAPTGEIVAQAtTLEDEVI 269

                         250       260
                  ....*....|....*....|....*...
gi 1198899064 238 CAE--LPDVTPIAAGEANYLRDRRPDVY 263
Cdd:cd07569   270 VADcdLDLCREGRETVFNFARHRRPEHY 297
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
 35-197 4.44e-08

apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the lgt/lsp/lnt system which is found broadly in bacteria but not in archaea. This model represents one component of the "lipoprotein lgt/lsp/lnt system" genome property. [Protein fate, Protein modification and repair]


Pssm-ID: 273129 [Multi-domain]  Cd Length: 391  Bit Score: 53.13  E-value: 4.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  35 ELILTPE---LFLSGYAPRELASWLtpervtgipdaaAEIARDTGIAIAASFPLARADGTFAI--AAELWDASGASVLRY 109
Cdd:TIGR00546 199 DLVVWPEtafPFDLENSPQKLADRL------------KLLVLSKGIPILIGAPDAVPGGPYHYynSAYLVDPGGEVVQRY 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 110 EKVHL------------WGDLEPLAFTPSTAAPA------VAAWNGRSVGFQICYDIEFPEPARALAAGGVDLLLVPTAi 171
Cdd:TIGR00546 267 DKVKLvpfgeyiplgflFKWLSKLFFLLSQEDFSrgpgpqVLKLPGGKIAPLICYESIFPDLVRASARQGAELLVNLTN- 345

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1198899064 172 DGHSAYVPELLV-----RARAAENALVVAYA 197
Cdd:TIGR00546 346 DAWFGDSSGPWQhfalaRFRAIENGRPLVRA 376
nitrilase_1_R2 cd07579
Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
 35-221 8.84e-08

Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); Members of this subgroup have two nitrilase domains. This is the second of those two domains. The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143603  Cd Length: 279  Bit Score: 52.17  E-value: 8.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  35 ELILTPELFLSG-YAPRELASWLTPERVtgipDAAAEIARDTGIAIAASFPLARADGtFAIAAELWDASGAsVLRYEKVH 113
Cdd:cd07579    33 ELVVFPELALTGlDDPASEAESDTGPAV----SALRRLARRLRLYLVAGFAEADGDG-LYNSAVLVGPEGL-VGTYRKTH 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 114 LWGDLEPLAfTPSTAAPAVAAWNGRsVGFQICYDIEFPEPARALAAGGVDLLLVPTAIDG------------HSAYVPE- 180
Cdd:cd07579   107 LIEPERSWA-TPGDTWPVYDLPLGR-VGLLIGHDALFPEAGRVLALRGCDLLACPAAIAIpfvgahagtsvpQPYPIPTg 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1198899064 181 ------LLVRARAAENALVVAYADhagqaepSADPAADFTGLSTVAG 221
Cdd:cd07579   185 adpthwHLARVRAGENNVYFAFAN-------VPDPARGYTGWSGVFG 224
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
 58-169 9.30e-08

Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an essential membrane-bound enzyme in gram-negative bacteria, which catalyzes the N-acylation of apolipoproteins, the final step in lipoprotein maturation. This is a reverse amidase (i.e. condensation) reaction. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 9.


Pssm-ID: 143595  Cd Length: 270  Bit Score: 51.83  E-value: 9.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  58 PERVTGIPDAAAEI---ARDTGIAIAASFP-LARADGTFAIAAELWDASGASVLRYEKVHL------------------W 115
Cdd:cd07571    51 PFDLQRDPDALARLaraARAVGAPLLTGAPrREPGGGRYYNSALLLDPGGGILGRYDKHHLvpfgeyvplrdllrflglL 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1198899064 116 GDLEPLAFTPSTAAPAVAAWNGRSVGFQICYDIEFPEPARALAAGGVDLLLVPT 169
Cdd:cd07571   131 FDLPMGDFSPGTGPQPLLLGGGVRVGPLICYESIFPELVRDAVRQGADLLVNIT 184
amiF PRK13287
formamidase; Provisional
 35-243 3.47e-07

formamidase; Provisional


Pssm-ID: 183950  Cd Length: 333  Bit Score: 50.46  E-value: 3.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  35 ELILTPELFLSGYAPrelASWLTPERVTGIP----DAAAEIARDTGIAIAASFPLARADGTFAI-AAELWDASGASVLRY 109
Cdd:PRK13287   54 DLIVFPEYSTQGLNT---KKWTTEEFLCTVDgpevDAFAQACKENKVWGVFSIMERNPDGNEPYnTAIIIDDQGEIILKY 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 110 EKVHLWGDLEPLAftPST-AAPAVAAWNGRSVGFQICYDIEFPEPARALAAGGVDLLLvptAIDGHSAYVPE---LLVRA 185
Cdd:PRK13287  131 RKLHPWVPVEPWE--PGDlGIPVCDGPGGSKLAVCICHDGMFPEMAREAAYKGANVMI---RISGYSTQVREqwiLTNRS 205

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 186 RAAENALVVAYADHAGqaepsADPAADFTGLSTVAGREGRVLAVAGRT-AELLCAEL-PD 243
Cdd:PRK13287  206 NAWQNLMYTASVNLAG-----YDGVFYYFGEGQVCNFDGTTLVQGHRNpWEIVTAEVrPD 260
PLN02798 PLN02798
nitrilase
 35-201 2.94e-06

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 47.43  E-value: 2.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  35 ELILTPELFlSGYAPRELASWLTPERVTG-IPDAAAEIARDTGIAIAA-SFPLARADGTFAIAAE-LWDASGASVLRYEK 111
Cdd:PLN02798   44 KLLFLPECF-SFIGDKDGESLAIAEPLDGpIMQRYRSLARESGLWLSLgGFQEKGPDDSHLYNTHvLIDDSGEIRSSYRK 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 112 VHLW-------GDLEPLAFT-PSTAAPAVAAWNGRsVGFQICYDIEFPEPARALA-AGGVDLLLVPTA---IDGHSAYvp 179
Cdd:PLN02798  123 IHLFdvdvpggPVLKESSFTaPGKTIVAVDSPVGR-LGLTVCYDLRFPELYQQLRfEHGAQVLLVPSAftkPTGEAHW-- 199

                         170       180
                  ....*....|....*....|..
gi 1198899064 180 ELLVRARAAENALVVAYADHAG 201
Cdd:PLN02798  200 EVLLRARAIETQCYVIAAAQAG 221
nitrilase_8 cd07586
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 2-241 7.71e-06

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143610  Cd Length: 269  Bit Score: 46.13  E-value: 7.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064   2 KIALLQAAATPLDPEANLAALREAAATAQAAGAELILTPELFLSGY----APRELASWLTPERVtgipDAAAEIARdtGI 77
Cdd:cd07586     1 RVAIAQIDPVLGDVEENLEKHLEIIETARERGADLVVFPELSLTGYnlgdLVYEVAMHADDPRL----QALAEASG--GI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  78 AIAASF-PLARADGTFAIAAELWDASGASVLRyeKVHL--WGDLEPLA-FTPSTAAPAVAAWNGRsVGFQICYDIEFPEP 153
Cdd:cd07586    75 CVVFGFvEEGRDGRFYNSAAYLEDGRVVHVHR--KVYLptYGLFEEGRyFAPGSHLRAFDTRFGR-AGVLICEDAWHPSL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 154 ARALAAGGVDLLLVPTA----IDGHSAYVPE---LLVRARAAENALVVAYADHAGQAEPSAdpaadFTGLSTVAGREGRV 226
Cdd:cd07586   152 PYLLALDGADVIFIPANsparGVGGDFDNEEnweTLLKFYAMMNGVYVVFANRVGVEDGVY-----FWGGSRVVDPDGEV 226

                         250
                  ....*....|....*.
gi 1198899064 227 LAVAGRTAE-LLCAEL 241
Cdd:cd07586   227 VAEAPLFEEdLLVAEL 242
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
58-169 7.75e-06

Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 46.76  E-value: 7.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  58 PERVTGIPDAAAEIARDTGIAIAASFPLAR-ADGTFAIAAELWDASGASVLRYEKVHL---------WGDLEPLA----- 122
Cdd:COG0815   248 LDEDPDALARLAAAAREAGAPLLTGAPRRDgGGGRYYNSALLLDPDGGILGRYDKHHLvpfgeyvplRDLLRPLIpfldl 327

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1198899064 123 ----FTPSTAAPAVAaWNGRSVGFQICYDIEFPEPARALAAGGVDLLLVPT 169
Cdd:COG0815   328 plgdFSPGTGPPVLD-LGGVRVGPLICYESIFPELVRDAVRAGADLLVNIT 377
lnt PRK00302
apolipoprotein N-acyltransferase; Reviewed
 56-166 1.63e-04

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 234721 [Multi-domain]  Cd Length: 505  Bit Score: 42.56  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  56 LTPERVTGIPDAAAEIARDTGIAI---AASFPLARADGTFAIAAELWDAsGASVLRYEKVHL--------WGD-LEPLA- 122
Cdd:PRK00302  271 LLEDLPQAFLKALDDLAREKGSALitgAPRAENKQGRYDYYNSIYVLGP-YGILNRYDKHHLvpfgeyvpLESlLRPLAp 349

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1198899064 123 --------FTPSTAAPAVAAWNGRSVGFQICYDIEFPEPARALAAGGVDLLL 166
Cdd:PRK00302  350 ffnlpmgdFSRGPYVQPPLLAKGLKLAPLICYEIIFPEEVRANVRQGADLLL 401
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
 1-190 1.74e-04

Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily (putative class 13 nitrilases); Uncharacterized subgroup belonging to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup either represents a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. XC1258 is a homotetramer.


Pssm-ID: 143599  Cd Length: 252  Bit Score: 41.76  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064   1 MKIALLQAAATPLDPEANLaALREAAATAQAAGAELILTPELFLSGYA--PRELA--------SWLtpervtgipdaaAE 70
Cdd:cd07575     1 LKIALIQTDLVWEDPEANL-AHFEEKIEQLKEKTDLIVLPEMFTTGFSmnAEALAepmngptlQWM------------KA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  71 IARDTGIAIAASFpLARADGTFAIAAeLWDASGASVLRYEKVHLW--GDlEPLAFTPSTaAPAVAAWNGRSVGFQICYDI 148
Cdd:cd07575    68 QAKKKGAAITGSL-IIKEGGKYYNRL-YFVTPDGEVYHYDKRHLFrmAG-EHKVYTAGN-ERVIVEYKGWKILLQVCYDL 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1198899064 149 EFPEPARalAAGGVDLLLvptaidghsaYV---PEL-------LVRARAAEN 190
Cdd:cd07575   144 RFPVWSR--NTNDYDLLL----------YVanwPAPrraawdtLLKARAIEN 183
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
 35-229 1.90e-04

First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); Members of this subgroup have two nitrilase domains. This is the first of those two domains. The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143602  Cd Length: 258  Bit Score: 41.75  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064  35 ELILTPELFLSGYA---PRELASWLTPervtgIPDAA----AEIARDTGIAIAASFP-LARADGTFAIAAELWDASGAsV 106
Cdd:cd07578    35 RLIVTPEMATTGYCwydRAEIAPFVEP-----IPGPTtarfAELAREHDCYIVVGLPeVDSRSGIYYNSAVLIGPSGV-I 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198899064 107 LRYEKVHlwgdlePLAFTPSTAAPAVAAWN------GRsVGFQICYDIEFPEPARALAAGGVDLLLVPTAIDGHSAYVPE 180
Cdd:cd07578   109 GRHRKTH------PYISEPKWAADGDLGHQvfdteiGR-IALLICMDIHFFETARLLALGGADVICHISNWLAERTPAPY 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1198899064 181 LLvrARAAENALVVAYADHAGqaepsADPAADFTGLSTVAGREGRVLAV 229
Cdd:cd07578   182 WI--NRAFENGCYLIESNRWG-----LERGVQFSGGSCIIEPDGTIQAS 223
biotinidase_like cd07567
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ...
 100-170 1.47e-03

biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin recycling. Biotinidase (EC 3.5.1.12) has both a hydrolase and a transferase activity. It hydrolyzes free biocytin or small biotinyl-peptides produced during the proteolytic degradation of biotin-dependent carboxylases, to release free biotin (vitamin H), and it can transfer biotin to acceptor molecules such as histones. Biotinidase deficiency in humans is an autosomal recessive disorder characterized by neurological and cutaneous symptoms. This subgroup includes the three human vanins, vanin1-3. Vanins are ectoenzymes, Vanin-1, and -2 are membrane associated, vanin-3 is secreted. They are pantotheinases (EC 3.5.1.92, pantetheine hydrolase), which convert pantetheine, to pantothenic acid (vitamin B5) and cysteamine (2-aminoethanethiol, a potent anti-oxidant). They are potential targets for therapeutic intervention in inflammatory disorders. Vanin-1 deficient mice lacking free cysteamine are less susceptible to intestinal inflammation, and expression of vanin-1 and -3 is induced as part of the inflammatory-regenerative differentiation program of human epidermis. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 4. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143591  Cd Length: 299  Bit Score: 39.15  E-value: 1.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1198899064 100 DASGASVLRYEKVHLWGdlEPlaFTPSTAAPAVAAWN---GRSVGFQICYDIEFPEPARALAA-GGVDLLLVPTA 170
Cdd:cd07567   136 DRDGTLIARYRKYNLFG--EP--GFDVPPEPEIVTFDtdfGVTFGIFTCFDILFKEPALELVKkLGVDDIVFPTA 206
 
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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