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Conserved domains on  [gi|974587522|ref|WP_059177817|]
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MULTISPECIES: amidohydrolase [Lelliottia]

Protein Classification

nitrilase family protein( domain architecture ID 10013522)

nitrilase family protein is a member of a large superfamily and predicted to act as a carbon-nitrogen hydrolase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
 1-256 0e+00

C-N hydrolase family amidase; Provisional


:

Pssm-ID: 182461  Cd Length: 256  Bit Score: 572.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522   1 MPGLKITLLQQPLVWMDGPANLRHFDRQLEEISGRDVIVLPEMFTTGFAMEAAKQSLPQDDVVAWMHTKAQQTNALVAGS 80
Cdd:PRK10438   1 MSGLKITLLQQPLVWMDGPANLRHFDRQLEGITGRDVIVLPEMFTTGFAMEAAASSLPQDDVVAWMTAKAQQTNALIAGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  81 AALQTDRGPVNRFLLVEPDGTLHFYDKRHLFRMADEHHHYEAGNERVIFEWRGWRILPLVCYDLRFPVWSRNRNDYDLAL 160
Cdd:PRK10438  81 VALQTESGAVNRFLLVEPGGTVHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNRNDYDLAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 161 YVANWPAPRSLHWQALLVARAIENQAYVVGCNRVGTDGNGHHYRGDSRVVNPQGEVLATAEAHQATRIDAELSLTALKEY 240
Cdd:PRK10438 161 YVANWPAPRSLHWQTLLTARAIENQAYVAGCNRVGSDGNGHHYRGDSRIINPQGEIIATAEPHQATRIDAELSLEALQEY 240

                        250
                 ....*....|....*.
gi 974587522 241 REKFPAWQDADPFIIG 256
Cdd:PRK10438 241 REKFPAWRDADEFTLR 256
 
Name Accession Description Interval E-value
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
 1-256 0e+00

C-N hydrolase family amidase; Provisional


Pssm-ID: 182461  Cd Length: 256  Bit Score: 572.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522   1 MPGLKITLLQQPLVWMDGPANLRHFDRQLEEISGRDVIVLPEMFTTGFAMEAAKQSLPQDDVVAWMHTKAQQTNALVAGS 80
Cdd:PRK10438   1 MSGLKITLLQQPLVWMDGPANLRHFDRQLEGITGRDVIVLPEMFTTGFAMEAAASSLPQDDVVAWMTAKAQQTNALIAGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  81 AALQTDRGPVNRFLLVEPDGTLHFYDKRHLFRMADEHHHYEAGNERVIFEWRGWRILPLVCYDLRFPVWSRNRNDYDLAL 160
Cdd:PRK10438  81 VALQTESGAVNRFLLVEPGGTVHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNRNDYDLAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 161 YVANWPAPRSLHWQALLVARAIENQAYVVGCNRVGTDGNGHHYRGDSRVVNPQGEVLATAEAHQATRIDAELSLTALKEY 240
Cdd:PRK10438 161 YVANWPAPRSLHWQTLLTARAIENQAYVAGCNRVGSDGNGHHYRGDSRIINPQGEIIATAEPHQATRIDAELSLEALQEY 240

                        250
                 ....*....|....*.
gi 974587522 241 REKFPAWQDADPFIIG 256
Cdd:PRK10438 241 REKFPAWRDADEFTLR 256
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
 4-254 4.20e-155

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: 431.19  E-value: 4.20e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522   4 LKITLLQQPLVWMDGPANLRHFDRQLEEISGR-DVIVLPEMFTTGFAMEAAKQSLP-QDDVVAWMHTKAQQTNALVAGSA 81
Cdd:cd07575    1 LKIALIQTDLVWEDPEANLAHFEEKIEQLKEKtDLIVLPEMFTTGFSMNAEALAEPmNGPTLQWMKAQAKKKGAAITGSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  82 ALQTDRGPVNRFLLVEPDGTLHFYDKRHLFRMADEHHHYEAGNERVIFEWRGWRILPLVCYDLRFPVWSRNRNDYDLALY 161
Cdd:cd07575   81 IIKEGGKYYNRLYFVTPDGEVYHYDKRHLFRMAGEHKVYTAGNERVIVEYKGWKILLQVCYDLRFPVWSRNTNDYDLLLY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 162 VANWPAPRSLHWQALLVARAIENQAYVVGCNRVGTDGNGHHYRGDSRVVNPQGEVLATAEAHQATRIdAELSLTALKEYR 241
Cdd:cd07575  161 VANWPAPRRAAWDTLLKARAIENQAYVIGVNRVGTDGNGLEYSGDSAVIDPLGEPLAEAEEDEGVLT-ATLDKEALQEFR 239

                        250
                 ....*....|...
gi 974587522 242 EKFPAWQDADPFI 254
Cdd:cd07575  240 EKFPFLKDADSFT 252
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
4-254 1.13e-76

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 232.83  E-value: 1.13e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522   4 LKITLLQQPLVWMDGPANLRHFDRQLEEISGR--DVIVLPEMFTTGFAMEAAKQSLPQDDV----VAWMHTKAQQTNALV 77
Cdd:COG0388    2 MRIALAQLNPTVGDIEANLAKIEELIREAAAQgaDLVVFPELFLTGYPPEDDDLLELAEPLdgpaLAALAELARELGIAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  78 AGSAALQTDRGPV-NRFLLVEPDGT-LHFYDKRHLFRM--ADEHHHYEAGNERVIFEWRGWRILPLVCYDLRFPVWSRN- 152
Cdd:COG0388   82 VVGLPERDEGGRLyNTALVIDPDGEiLGRYRKIHLPNYgvFDEKRYFTPGDELVVFDTDGGRIGVLICYDLWFPELARAl 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 153 -RNDYDLALYVANWPAPRSL-HWQALLVARAIENQAYVVGCNRVGTDGnGHHYRGDSRVVNPQGEVLATAEAHQATRIdA 230
Cdd:COG0388  162 aLAGADLLLVPSASPFGRGKdHWELLLRARAIENGCYVVAANQVGGED-GLVFDGGSMIVDPDGEVLAEAGDEEGLLV-A 239

                        250       260
                 ....*....|....*....|....
gi 974587522 231 ELSLTALKEYREKFPAWQDADPFI 254
Cdd:COG0388  240 DIDLDRLREARRRFPVLRDRRPDL 263
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
 5-241 2.74e-32

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: 118.61  E-value: 2.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522    5 KITLLQQPLVWMDGPANLRHFDRQLEEISGR--DVIVLPEMFTTGFAMEAAKQSLPQD---DVVAWMHTKAQQTNALVAG 79
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQKALELIEEAARYgaDLIVLPELFITGYPCWAHFLEAAEVgdgETLAGLAALARKNGIAIVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522   80 SAALQTDRGPV--NRFLLVEPDGTLHF-YDKRHLFRMAD-----EHHHYEAGNERVIFEWRGWRILPLVCYDLRFPVWSR 151
Cdd:pfam00795  81 GLIERWLTGGRlyNTAVLLDPDGKLVGkYRKLHLFPEPRppgfrERVLFEPGDGGTVFDTPLGKIGAAICYEIRFPELLR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  152 --NRNDYDLALYVAN----WPAPRSLHWQALLVARAIENQAYVVGCNRVGTDGNGHHYRGDSRVVNPQGEVLATAEAHQA 225
Cdd:pfam00795 161 alALKGAEILINPSArapfPGSLGPPQWLLLARARALENGCFVIAANQVGGEEDAPWPYGHSMIIDPDGRILAGAGEWEE 240

                         250
                  ....*....|....*.
gi 974587522  226 TRIDAELSLTALKEYR 241
Cdd:pfam00795 241 GVLIADIDLALVRAWR 256
de_GSH_amidase NF033621
deaminated glutathione amidase;
105-245 2.14e-13

deaminated glutathione amidase;


Pssm-ID: 468114  Cd Length: 260  Bit Score: 68.00  E-value: 2.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 105 YDKRHL---FRMaDEHHHYEAGNE-RVIFEWRGWRILPLVCYDLRFPVWSRNrndydLALYVAN---WPAP------RSL 171
Cdd:NF033621 107 YRKLHLydaFSM-QESRRVDAGNEiPPLVEVAGMKVGLMTCYDLRFPELARR-----LALDGADvlvLPAAwvrgplKEH 180

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 974587522 172 HWQALLVARAIENQAYVVGcnrVGTDGNghhyR--GDSRVVNPQGEVLATAeAHQATRIDAELSLTALKEYREKFP 245
Cdd:NF033621 181 HWETLLAARALENTCYMVA---VGECGN----RniGQSMVVDPLGVTIAAA-AEAPALIFAELDPERIAHAREQLP 248
 
Name Accession Description Interval E-value
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
 1-256 0e+00

C-N hydrolase family amidase; Provisional


Pssm-ID: 182461  Cd Length: 256  Bit Score: 572.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522   1 MPGLKITLLQQPLVWMDGPANLRHFDRQLEEISGRDVIVLPEMFTTGFAMEAAKQSLPQDDVVAWMHTKAQQTNALVAGS 80
Cdd:PRK10438   1 MSGLKITLLQQPLVWMDGPANLRHFDRQLEGITGRDVIVLPEMFTTGFAMEAAASSLPQDDVVAWMTAKAQQTNALIAGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  81 AALQTDRGPVNRFLLVEPDGTLHFYDKRHLFRMADEHHHYEAGNERVIFEWRGWRILPLVCYDLRFPVWSRNRNDYDLAL 160
Cdd:PRK10438  81 VALQTESGAVNRFLLVEPGGTVHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNRNDYDLAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 161 YVANWPAPRSLHWQALLVARAIENQAYVVGCNRVGTDGNGHHYRGDSRVVNPQGEVLATAEAHQATRIDAELSLTALKEY 240
Cdd:PRK10438 161 YVANWPAPRSLHWQTLLTARAIENQAYVAGCNRVGSDGNGHHYRGDSRIINPQGEIIATAEPHQATRIDAELSLEALQEY 240

                        250
                 ....*....|....*.
gi 974587522 241 REKFPAWQDADPFIIG 256
Cdd:PRK10438 241 REKFPAWRDADEFTLR 256
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
 4-254 4.20e-155

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: 431.19  E-value: 4.20e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522   4 LKITLLQQPLVWMDGPANLRHFDRQLEEISGR-DVIVLPEMFTTGFAMEAAKQSLP-QDDVVAWMHTKAQQTNALVAGSA 81
Cdd:cd07575    1 LKIALIQTDLVWEDPEANLAHFEEKIEQLKEKtDLIVLPEMFTTGFSMNAEALAEPmNGPTLQWMKAQAKKKGAAITGSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  82 ALQTDRGPVNRFLLVEPDGTLHFYDKRHLFRMADEHHHYEAGNERVIFEWRGWRILPLVCYDLRFPVWSRNRNDYDLALY 161
Cdd:cd07575   81 IIKEGGKYYNRLYFVTPDGEVYHYDKRHLFRMAGEHKVYTAGNERVIVEYKGWKILLQVCYDLRFPVWSRNTNDYDLLLY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 162 VANWPAPRSLHWQALLVARAIENQAYVVGCNRVGTDGNGHHYRGDSRVVNPQGEVLATAEAHQATRIdAELSLTALKEYR 241
Cdd:cd07575  161 VANWPAPRRAAWDTLLKARAIENQAYVIGVNRVGTDGNGLEYSGDSAVIDPLGEPLAEAEEDEGVLT-ATLDKEALQEFR 239

                        250
                 ....*....|...
gi 974587522 242 EKFPAWQDADPFI 254
Cdd:cd07575  240 EKFPFLKDADSFT 252
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 5-249 2.52e-80

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: 242.06  E-value: 2.52e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522   5 KITLLQQPLVWMDGPANLRHFDRQLEEISGR--DVIVLPEMFTTGFAMEAAKQS--LPQDDVVAWMHTKAQQTNA-LVAG 79
Cdd:cd07583    1 KIALIQLDIVWGDPEANIERVESLIEEAAAAgaDLIVLPEMWNTGYFLDDLYELadEDGGETVSFLSELAKKHGVnIVAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  80 SAALQTDRGPVNRFLLVEPDGTL-HFYDKRHLFRMADEHHHYEAGNERVIFEWRGWRILPLVCYDLRFPVWSRN--RNDY 156
Cdd:cd07583   81 SVAEKEGGKLYNTAYVIDPDGELiATYRKIHLFGLMGEDKYLTAGDELEVFELDGGKVGLFICYDLRFPELFRKlaLEGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 157 DLALYVANWPAPRSLHWQALLVARAIENQAYVVGCNRVGTDGNGhHYRGDSRVVNPQGEVLATAEAHQATrIDAELSLTA 236
Cdd:cd07583  161 EILFVPAEWPAARIEHWRTLLRARAIENQAFVVACNRVGTDGGN-EFGGHSMVIDPWGEVLAEAGEEEEI-LTAEIDLEE 238

                        250
                 ....*....|...
gi 974587522 237 LKEYREKFPAWQD 249
Cdd:cd07583  239 VAEVRKKIPVFKD 251
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
4-254 1.13e-76

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 232.83  E-value: 1.13e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522   4 LKITLLQQPLVWMDGPANLRHFDRQLEEISGR--DVIVLPEMFTTGFAMEAAKQSLPQDDV----VAWMHTKAQQTNALV 77
Cdd:COG0388    2 MRIALAQLNPTVGDIEANLAKIEELIREAAAQgaDLVVFPELFLTGYPPEDDDLLELAEPLdgpaLAALAELARELGIAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  78 AGSAALQTDRGPV-NRFLLVEPDGT-LHFYDKRHLFRM--ADEHHHYEAGNERVIFEWRGWRILPLVCYDLRFPVWSRN- 152
Cdd:COG0388   82 VVGLPERDEGGRLyNTALVIDPDGEiLGRYRKIHLPNYgvFDEKRYFTPGDELVVFDTDGGRIGVLICYDLWFPELARAl 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 153 -RNDYDLALYVANWPAPRSL-HWQALLVARAIENQAYVVGCNRVGTDGnGHHYRGDSRVVNPQGEVLATAEAHQATRIdA 230
Cdd:COG0388  162 aLAGADLLLVPSASPFGRGKdHWELLLRARAIENGCYVVAANQVGGED-GLVFDGGSMIVDPDGEVLAEAGDEEGLLV-A 239

                        250       260
                 ....*....|....*....|....
gi 974587522 231 ELSLTALKEYREKFPAWQDADPFI 254
Cdd:COG0388  240 DIDLDRLREARRRFPVLRDRRPDL 263
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
 6-249 3.11e-62

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: 195.62  E-value: 3.11e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522   6 ITLLQQPLVWMDGPANLRHFDRQLEEIS--GRDVIVLPEMFTTGF----AMEAAKQSLPQDD-VVAWMHTKAQQTNALVA 78
Cdd:cd07197    1 IAAVQLAPKIGDVEANLAKALRLIKEAAeqGADLIVLPELFLTGYsfesAKEDLDLAEELDGpTLEALAELAKELGIYIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  79 GSAALQTDRGPVNRFLLVEPDGT-LHFYDKRHLFRMaDEHHHYEAGNERVIFEWRGWRILPLVCYDLRFPVWSR--NRND 155
Cdd:cd07197   81 AGIAEKDGDKLYNTAVVIDPDGEiIGKYRKIHLFDF-GERRYFSPGDEFPVFDTPGGKIGLLICYDLRFPELARelALKG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 156 YDLALYVANWPAPRSLHWQALLVARAIENQAYVVGCNRVGTDGNGHHYrGDSRVVNPQGEVLATAEAHQATRIdAELSLT 235
Cdd:cd07197  160 ADIILVPAAWPTARREHWELLLRARAIENGVYVVAANRVGEEGGLEFA-GGSMIVDPDGEVLAEASEEEGILV-AELDLD 237

                        250
                 ....*....|....
gi 974587522 236 ALKEYREKFPAWQD 249
Cdd:cd07197  238 ELREARKRWSYLRD 251
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
 20-248 7.75e-39

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: 136.02  E-value: 7.75e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  20 ANLRHFDRQLEEIS--GRDVIVLPEMFT----TGFAMEAAKQSLPQDDVVAWMHTKAQQTN-ALVAGSAALQTDRG--PV 90
Cdd:cd07572   15 ANLARAKELIEEAAaqGAKLVVLPECFNypggTDAFKLALAEEEGDGPTLQALSELAKEHGiWLVGGSIPERDDDDgkVY 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  91 NRFLLVEPDGTL-HFYDKRHLF-------RMADEHHHYEAGNERVIFEWRGWRILPLVCYDLRFPVWSR--NRNDYDLAL 160
Cdd:cd07572   95 NTSLVFDPDGELvARYRKIHLFdvdvpggISYRESDTLTPGDEVVVVDTPFGKIGLGICYDLRFPELARalARQGADILT 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 161 YvanwPA-------PrsLHWQALLVARAIENQAYVVGCNRVGTDGNGHHYRGDSRVVNPQGEVLATAEAHQATrIDAELS 233
Cdd:cd07572  175 V----PAaftmttgP--AHWELLLRARAIENQCYVVAAAQAGDHEAGRETYGHSMIVDPWGEVLAEAGEGEGV-VVAEID 247

                        250
                 ....*....|....*
gi 974587522 234 LTALKEYREKFPAWQ 248
Cdd:cd07572  248 LDRLEEVRRQIPVLK 262
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
 5-249 3.73e-37

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: 131.16  E-value: 3.73e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522   5 KITLLQQPLVWMDGPANLRHFDRQLEEISGR--DVIVLPEMFTTGFAM--EAAKQSLPQD-DVVAWMHTKAQQTN-ALVA 78
Cdd:cd07576    1 RLALYQGPARDGDVAANLARLDEAAARAAAAgaDLLVFPELFLTGYNIgdAVARLAEPADgPALQALRAIARRHGiAIVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  79 GsAALQTDRGPVNRFLLVEPDGT-LHFYDKRHLFRmADEHHHYEAGNERVIFEWRGWRILPLVCYDLRFPVWSRnrndyD 157
Cdd:cd07576   81 G-YPERAGGAVYNAAVLIDEDGTvLANYRKTHLFG-DSERAAFTPGDRFPVVELRGLRVGLLICYDVEFPELVR-----A 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 158 LALYVANW---PAPRSLHW----QALLVARAIENQAYVVGCNRVGTDGnGHHYRGDSRVVNPQGEVLATAEAHqATRIDA 230
Cdd:cd07576  154 LALAGADLvlvPTALMEPYgfvaRTLVPARAFENQIFVAYANRCGAED-GLTYVGLSSIAGPDGTVLARAGRG-EALLVA 231

                        250
                 ....*....|....*....
gi 974587522 231 ELSLTALKEYREKFPAWQD 249
Cdd:cd07576  232 DLDPAALAAARRENPYLAD 250
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
 5-241 2.74e-32

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: 118.61  E-value: 2.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522    5 KITLLQQPLVWMDGPANLRHFDRQLEEISGR--DVIVLPEMFTTGFAMEAAKQSLPQD---DVVAWMHTKAQQTNALVAG 79
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQKALELIEEAARYgaDLIVLPELFITGYPCWAHFLEAAEVgdgETLAGLAALARKNGIAIVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522   80 SAALQTDRGPV--NRFLLVEPDGTLHF-YDKRHLFRMAD-----EHHHYEAGNERVIFEWRGWRILPLVCYDLRFPVWSR 151
Cdd:pfam00795  81 GLIERWLTGGRlyNTAVLLDPDGKLVGkYRKLHLFPEPRppgfrERVLFEPGDGGTVFDTPLGKIGAAICYEIRFPELLR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  152 --NRNDYDLALYVAN----WPAPRSLHWQALLVARAIENQAYVVGCNRVGTDGNGHHYRGDSRVVNPQGEVLATAEAHQA 225
Cdd:pfam00795 161 alALKGAEILINPSArapfPGSLGPPQWLLLARARALENGCFVIAANQVGGEEDAPWPYGHSMIIDPDGRILAGAGEWEE 240

                         250
                  ....*....|....*.
gi 974587522  226 TRIDAELSLTALKEYR 241
Cdd:pfam00795 241 GVLIADIDLALVRAWR 256
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
 36-234 1.05e-30

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: 114.70  E-value: 1.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  36 DVIVLPEMFTTGFAMEAAKQ------SLPQDDVVAWMHTKAQQTNALVAGSAALQTDRGPVNRFLLVEPDGTLHFYDKRH 109
Cdd:cd07577   31 DLIVLPELFNTGYAFTSKEEvaslaeSIPDGPTTRFLQELARETGAYIVAGLPERDGDKFYNSAVVVGPEGYIGIYRKTH 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 110 LFRmaDEHHHYEAGNER-VIFEWRGWRILPLVCYDLRFPVWSRNrndydLAL-------YVANWPAPrslHWQALLVARA 181
Cdd:cd07577  111 LFY--EEKLFFEPGDTGfRVFDIGDIRIGVMICFDWYFPEAART-----LALkgadiiaHPANLVLP---YCPKAMPIRA 180

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 182 IENQAYVVGCNRVGTDGNGH---HYRGDSRVVNPQGEVLA----TAEAHQATRIDAELSL 234
Cdd:cd07577  181 LENRVFTITANRIGTEERGGetlRFIGKSQITSPKGEVLArapeDGEEVLVAEIDPRLAR 240
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 16-245 1.77e-29

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: 111.13  E-value: 1.77e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  16 MDGPANLRHFDRQLEEISGR--DVIVLPEM----------------------FTTGFAMEAAKQSLpqdDVVAWMHTKAQ 71
Cdd:cd07581   10 GDKEENLEKVRRLLAEAAAAgaDLVVFPEYtmarfgdglddyarvaepldgpFVSALARLARELGI---TVVAGMFEPAG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  72 qtnalvagsaalqtDRGPVNRFLLVEPDGTLH-FYDKRHLFrmaD-----EHHHYEAGNE--RVIFEWRGWRILPLVCYD 143
Cdd:cd07581   87 --------------DGRVYNTLVVVGPDGEIIaVYRKIHLY---DafgfrESDTVAPGDElpPVVFVVGGVKVGLATCYD 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 144 LRFPVWSRN--RNDYDLALYVANW-PAPRSL-HWQALLVARAIENQAYVVGCNRVgtdgnGHHYRGDSRVVNPQGEVLAT 219
Cdd:cd07581  150 LRFPELARAlaLAGADVIVVPAAWvAGPGKEeHWETLLRARALENTVYVAAAGQA-----GPRGIGRSMVVDPLGVVLAD 224

                        250       260
                 ....*....|....*....|....*.
gi 974587522 220 AEAHQATRIdAELSLTALKEYREKFP 245
Cdd:cd07581  225 LGEREGLLV-ADIDPERVEEAREALP 249
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 5-252 2.52e-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: 143608  Cd Length: 258  Bit Score: 103.22  E-value: 2.52e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522   5 KITLLQQPLVWMDGPANLR---HFDRQLEEiSGRDVIVLPEMFTTGFAMEAAKQSL------PQDDVVAWMHTKAQQTNA 75
Cdd:cd07584    1 KVALIQMDSVLGDVKANLKkaaELCKEAAA-EGADLICFPELATTGYRPDLLGPKLwelsepIDGPTVRLFSELAKELGV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  76 -LVAGSAALQTDRGPV-NRFLLVEPDG-TLHFYDKRHLFrmADEHHHYEAGNERVIFEWRGWRILPLVCYDLRFPVWSRn 152
Cdd:cd07584   80 yIVCGFVEKGGVPGKVyNSAVVIDPEGeSLGVYRKIHLW--GLEKQYFREGEQYPVFDTPFGKIGVMICYDMGFPEVAR- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 153 rndyDLALYVAN-------WPAPRSLHWQALLVARAIENQAYVVGCNRVGTDGNGHHYrGDSRVVNPQGEVLATAEAHQA 225
Cdd:cd07584  157 ----ILTLKGAEvifcpsaWREQDADIWDINLPARALENTVFVAAVNRVGNEGDLVLF-GKSKILNPRGQVLAEASEEAE 231

                        250       260
                 ....*....|....*....|....*..
gi 974587522 226 TRIDAELSLTALKEYREKFPAWQDADP 252
Cdd:cd07584  232 EILYAEIDLDAIADYRMTLPYLKDRKP 258
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 26-234 1.13e-25

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: 101.24  E-value: 1.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  26 DRQLEEIS---------GRDVIVLPEMFTTGFAMEAA--KQSLPQD-DVVAWMHTKAQQTN-ALVAGSAALQTDRgPVNR 92
Cdd:cd07585   15 ARNLAVIArwtrkaaaqGAELVCFPEMCITGYTHVRAlsREAEVPDgPSTQALSDLARRYGlTILAGLIEKAGDR-PYNT 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  93 FLLVEPDGTLHFYDKRHLFRMadEHHHYEAGNERVIFEWRGWRILPLVCYDLRFPVWSRNrndydLALYVA--------- 163
Cdd:cd07585   94 YLVCLPDGLVHRYRKLHLFRR--EHPYIAAGDEYPVFATPGVRFGILICYDNHFPENVRA-----TALLGAeilfaphat 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 974587522 164 --NWPAPRSLHWQALLVARAIENQAYVVGCNRVGTDGnGHHYRGDSRVVNPQGEVLATAEAHQATRIDAELSL 234
Cdd:cd07585  167 pgTTSPKGREWWMRWLPARAYDNGVFVAACNGVGRDG-GEVFPGGAMILDPYGRVLAETTSGGDGMVVADLDL 238
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
 4-251 5.56e-23

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: 94.58  E-value: 5.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522   4 LKITLLQQPlvwMDGPANLRHFDRQLEEI------SGRDVIVLPEMFTTGFA------MEAAKQSLP-----QDDVVAWM 66
Cdd:cd07574    1 VRVAAAQYP---LRRYASFEEFAAKVEYWvaeaagYGADLLVFPEYFTMELLsllpeaIDGLDEAIRalaalTPDYVALF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  67 HTKAQQTNA-LVAGSAALQTDRGPVNRFLLVEPDGTLHFYDKRHLFRMADEHHHYEAGNERVIFEWRGWRILPLVCYDLR 145
Cdd:cd07574   78 SELARKYGInIIAGSMPVREDGRLYNRAYLFGPDGTIGHQDKLHMTPFEREEWGISGGDKLKVFDTDLGKIGILICYDSE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 146 FPVWSRNrndydLA------LYVANWPAPRSLHWQALL--VARAIENQAYVVGCNRVG---TDGNGHHYRGDSRVVNP-- 212
Cdd:cd07574  158 FPELARA-----LAeagadlLLVPSCTDTRAGYWRVRIgaQARALENQCYVVQSGTVGnapWSPAVDVNYGQAAVYTPcd 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 974587522 213 -----QGeVLATAEAHQATRIDAELSLTALKEYREKFPAWQDAD 251
Cdd:cd07574  233 fgfpeDG-ILAEGEPNTEGWLIADLDLEALRRLREEGSVRNLRD 275
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 20-241 2.69e-20

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: 87.02  E-value: 2.69e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  20 ANLRHFDRQLEEI--SGRDVIVLPEMFTTGF-------AMEAAKQSLPQDDVVAWMHTKAQQTNALVAGSAALQTDRgPV 90
Cdd:cd07580   16 ANLARSIELIREAadAGANLVVLPELANTGYvfesrdeAFALAEEVPDGASTRAWAELAAELGLYIVAGFAERDGDR-LY 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  91 NRFLLVEPDGTLHFYDKRHLFrmADEHHHYEAGNERV-IFEWRGWRILPLVCYDLRFPVWSRNrndydLALYVA------ 163
Cdd:cd07580   95 NSAVLVGPDGVIGTYRKAHLW--NEEKLLFEPGDLGLpVFDTPFGRIGVAICYDGWFPETFRL-----LALQGAdivcvp 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 164 -NW-PAPRSLHWQA-----LLVARAIENQAYVVGCNRVGTDgNGHHYRGDSRVVNPQGEVLAT-AEAHQATRIDAELSLT 235
Cdd:cd07580  168 tNWvPMPRPPEGGPpmaniLAMAAAHSNGLFIACADRVGTE-RGQPFIGQSLIVGPDGWPLAGpASGDEEEILLADIDLT 246


                 ....*.
gi 974587522 236 ALKEYR 241
Cdd:cd07580  247 AARRKR 252
nitrilase_8 cd07586
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 22-251 3.45e-20

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: 86.96  E-value: 3.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  22 LRHFDRQLEEisGRDVIVLPEMFTTGFAMeaakqslpQDDV--VAwMHTKAQQTNAL---------VAGSAALQTDRGPV 90
Cdd:cd07586   22 LEIIETARER--GADLVVFPELSLTGYNL--------GDLVyeVA-MHADDPRLQALaeasggicvVFGFVEEGRDGRFY 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  91 NRFLLVEPDGTLHFYDKRHL--FRMADEHHHYEAGNERVIFEWRGWRILPLVCYDLrfpvW--------SRNRNDYDLAL 160
Cdd:cd07586   91 NSAAYLEDGRVVHVHRKVYLptYGLFEEGRYFAPGSHLRAFDTRFGRAGVLICEDA----WhpslpyllALDGADVIFIP 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 161 yvANWPAPRSLH-------WQALLVARAIENQAYVVGCNRVGTDGnGHHYRGDSRVVNPQGEVLATAEAHQATRIDAELS 233
Cdd:cd07586  167 --ANSPARGVGGdfdneenWETLLKFYAMMNGVYVVFANRVGVED-GVYFWGGSRVVDPDGEVVAEAPLFEEDLLVAELD 243

                        250
                 ....*....|....*...
gi 974587522 234 LTALKEYREKFPAWQDAD 251
Cdd:cd07586  244 RSAIRRARFFSPTFRDED 261
PLN02798 PLN02798
nitrilase
 91-245 6.26e-15

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 72.47  E-value: 6.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  91 NRFLLVEPDGTLH-FYDKRHLF-------RMADEHHHYEAGNERVIFEWRGWRILPLVCYDLRFP-VWSRNRNDYDL-AL 160
Cdd:PLN02798 105 NTHVLIDDSGEIRsSYRKIHLFdvdvpggPVLKESSFTAPGKTIVAVDSPVGRLGLTVCYDLRFPeLYQQLRFEHGAqVL 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 161 YVanwPAPRSL-----HWQALLVARAIENQAYVVGCNRVGTDGNGHHYRGDSRVVNPQGEVLATAEAHQATRID-AELSL 234
Cdd:PLN02798 185 LV---PSAFTKptgeaHWEVLLRARAIETQCYVIAAAQAGKHNEKRESYGHALIIDPWGTVVARLPDRLSTGIAvADIDL 261

                        170
                 ....*....|.
gi 974587522 235 TALKEYREKFP 245
Cdd:PLN02798 262 SLLDSVRTKMP 272
de_GSH_amidase NF033621
deaminated glutathione amidase;
105-245 2.14e-13

deaminated glutathione amidase;


Pssm-ID: 468114  Cd Length: 260  Bit Score: 68.00  E-value: 2.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 105 YDKRHL---FRMaDEHHHYEAGNE-RVIFEWRGWRILPLVCYDLRFPVWSRNrndydLALYVAN---WPAP------RSL 171
Cdd:NF033621 107 YRKLHLydaFSM-QESRRVDAGNEiPPLVEVAGMKVGLMTCYDLRFPELARR-----LALDGADvlvLPAAwvrgplKEH 180

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 974587522 172 HWQALLVARAIENQAYVVGcnrVGTDGNghhyR--GDSRVVNPQGEVLATAeAHQATRIDAELSLTALKEYREKFP 245
Cdd:NF033621 181 HWETLLAARALENTCYMVA---VGECGN----RniGQSMVVDPLGVTIAAA-AEAPALIFAELDPERIAHAREQLP 248
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
2-235 4.56e-13

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


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 68.33  E-value: 4.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522   2 PGLKITLLQ----QPLVWMdgPANLR-HFDRQLEEI-----SGRDVIVLPEmftTGFAMeaakqSLPQD-DVVAWMHTKA 70
Cdd:COG0815  193 EPLRVALVQgnipQDLKWD--PEQRReILDRYLDLTreladDGPDLVVWPE---TALPF-----LLDEDpDALARLAAAA 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  71 QQTNA-LVAGSAALQTDRGPV-NRFLLVEPDG-TLHFYDKRHLF-----------------RMADEHHHYEAGNERVIFE 130
Cdd:COG0815  263 REAGApLLTGAPRRDGGGGRYyNSALLLDPDGgILGRYDKHHLVpfgeyvplrdllrplipFLDLPLGDFSPGTGPPVLD 342

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 131 WRGWRILPLVCYDLRFP--VWSRNRNDYDLALYVAN--W----PAPRSLHWQAllVARAIENQAYVVgcnRVGTDGnghh 202
Cdd:COG0815  343 LGGVRVGPLICYESIFPelVRDAVRAGADLLVNITNdaWfgdsIGPYQHLAIA--RLRAIETGRPVV---RATNTG---- 413

                        250       260       270
                 ....*....|....*....|....*....|...
gi 974587522 203 yrgDSRVVNPQGEVLATAEAHQATRIDAELSLT 235
Cdd:COG0815  414 ---ISAVIDPDGRVLARLPLFTRGVLVAEVPLR 443
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
 4-234 3.77e-10

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: 58.76  E-value: 3.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522   4 LKITLLQQ---PLVWMDGPANLRHFDRQLEEI-----SGRDVIVLPEmfttgfameaakQSLP-----QDDVVAWMHTKA 70
Cdd:cd07571    1 LRVALVQGnipQDEKWDPEQRQATLDRYLDLTreladEKPDLVVWPE------------TALPfdlqrDPDALARLARAA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  71 QQTNA-LVAGSAALQTDRGPV-NRFLLVEPDG-TLHFYDKRHL-----------------FRMADEHHHYEAGNERVIFE 130
Cdd:cd07571   69 RAVGApLLTGAPRREPGGGRYyNSALLLDPGGgILGRYDKHHLvpfgeyvplrdllrflgLLFDLPMGDFSPGTGPQPLL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 131 WRG-WRILPLVCYDLRFP--VWSRNRNDYDLALYVAN--WPAPRSLHWQ--ALLVARAIENQAYVVgcnRVGTDGnghhy 203
Cdd:cd07571  149 LGGgVRVGPLICYESIFPelVRDAVRQGADLLVNITNdaWFGDSAGPYQhlAMARLRAIETGRPLV---RAANTG----- 220

                        250       260       270
                 ....*....|....*....|....*....|.
gi 974587522 204 rgDSRVVNPQGEVLATAEAHQATRIDAELSL 234
Cdd:cd07571  221 --ISAVIDPDGRIVARLPLFEAGVLVAEVPL 249
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
 4-249 9.44e-10

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: 57.57  E-value: 9.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522   4 LKITLLQQplVWMDGPAnlRHFDRQLEEI-----SGRDVIVLPEMFTTG-FAMEaakqslpQD-DVVAWMHTKAqqTNAL 76
Cdd:cd07573    1 VTVALVQM--ACSEDPE--ANLAKAEELVreaaaQGAQIVCLQELFETPyFCQE-------EDeDYFDLAEPPI--PGPT 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  77 VAGSAALQTDRGPV---------------NRFLLVEPDGTLH-FYDKRHLfrmADEHHHYE-----AGNE--RViFEWRG 133
Cdd:cd07573   68 TARFQALAKELGVVipvslfekrgnglyyNSAVVIDADGSLLgVYRKMHI---PDDPGYYEkfyftPGDTgfKV-FDTRY 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 134 WRILPLVCYDLRFPVWSRNrndydLALYVAN---------W------PAPRSL-HWQALLVARAIENQAYVVGCNRVGT- 196
Cdd:cd07573  144 GRIGVLICWDQWFPEAARL-----MALQGAEilfyptaigSepqeppEGLDQRdAWQRVQRGHAIANGVPVAAVNRVGVe 218

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 974587522 197 --DGNGHHYRGDSRVVNPQGEVLATAEAHQATRIDAELSLTALKEYREKFPAWQD 249
Cdd:cd07573  219 gdPGSGITFYGSSFIADPFGEILAQASRDEEEILVAEFDLDEIEEVRRAWPFFRD 273
lnt PRK00302
apolipoprotein N-acyltransferase; Reviewed
 2-235 7.85e-09

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 234721 [Multi-domain]  Cd Length: 505  Bit Score: 55.66  E-value: 7.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522   2 PGLKITLLQ----QPLVWmdGPANL-----RHFDRQLEEISGRDVIVLPEmfttgFAMEAAKQSLPQDdVVAWMHTKAQQ 72
Cdd:PRK00302 218 PALKVALVQgnipQSLKW--DPAGLeatlqKYLDLSRPALGPADLIIWPE-----TAIPFLLEDLPQA-FLKALDDLARE 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  73 TN-ALVAGSAALQTDRGPV---NRFLLVEPDGTLHFYDKRHL------------FR-----MADEHHHYEAGNER-VIFE 130
Cdd:PRK00302 290 KGsALITGAPRAENKQGRYdyyNSIYVLGPYGILNRYDKHHLvpfgeyvpleslLRplapfFNLPMGDFSRGPYVqPPLL 369

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 131 WRGWRILPLVCYDLRFP--VWSRNRNDYDLALYVAN--W----PAPrslhWQALLVA--RAIENQAYVV-GCNrvgtdgN 199
Cdd:PRK00302 370 AKGLKLAPLICYEIIFPeeVRANVRQGADLLLNISNdaWfgdsIGP----YQHFQMArmRALELGRPLIrATN------T 439

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 974587522 200 GHhyrgdSRVVNPQGEVLATAEAHQATRIDAELSLT 235
Cdd:PRK00302 440 GI-----TAVIDPLGRIIAQLPQFTEGVLDGTVPPT 470
PRK13981 PRK13981
NAD synthetase; Provisional
 34-222 1.55e-08

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 54.78  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  34 GRDVIVLPEMFTTGF-------------AMEAAKQSLPQDdvvawmhtkaqqtnaLVAGSAAL-----QTDRGPVNRFLL 95
Cdd:PRK13981  33 GADLLLFPELFLSGYppedlllrpaflaACEAALERLAAA---------------TAGGPAVLvghpwREGGKLYNAAAL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  96 VEPDGTLHFYDKRHL-----FrmaDEHHHYEAGNERVIFEWRGWRILPLVCYDLRFP-VWSR-----------------N 152
Cdd:PRK13981  98 LDGGEVLATYRKQDLpnygvF---DEKRYFAPGPEPGVVELKGVRIGVPICEDIWNPePAETlaeagaelllvpnaspyH 174

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 974587522 153 RNDYDLALyvanwpaprslhwqALLVARAIENQAYVVGCNRVGT------DGNghhyrgdSRVVNPQGEVLATAEA 222
Cdd:PRK13981 175 RGKPDLRE--------------AVLRARVRETGLPLVYLNQVGGqdelvfDGA-------SFVLNADGELAARLPA 229
nitrilase_4 cd07582
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 38-243 1.65e-08

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: 54.27  E-value: 1.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  38 IVLPEMFTTGFAMEA-------AKQSLPQDDV-VAWMHTKAQQTNALVAGSAALQTDRGPVNRF---LLVEPDGTLhFYD 106
Cdd:cd07582   46 VVLPEYALQGFPMGEprevwqfDKAAIDIPGPeTEALGEKAKELNVYIAANAYERDPDFPGLYFntaFIIDPSGEI-ILR 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 107 KRHLFRMA-----------DEHHHYEAGNERVIF---EWRGWRILPLVCYDLRFPVWSRNrndydLALY--------VAN 164
Cdd:cd07582  125 YRKMNSLAaegspsphdvwDEYIEVYGYGLDALFpvaDTEIGNLGCLACEEGLYPEVARG-----LAMNgaevllrsSSE 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 165 WPAPRSLHWQALLVARAIENQAYVVGCNR---VGTDGNGHHYRGDSRVVNPQGEVLATAE-AHQATRIDAELSLTALKEY 240
Cdd:cd07582  200 VPSVELDPWEIANRARALENLAYVVSANSggiYGSPYPADSFGGGSMIVDYKGRVLAEAGyGPGSMVAGAEIDIEALRRA 279


                 ...
gi 974587522 241 REK 243
Cdd:cd07582  280 RAR 282
DCase cd07569
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ...
 34-243 9.35e-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: 51.93  E-value: 9.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  34 GRDVIVLPEM-FTTGFAM-----EAA-----KQSLPQDDVVAWMHTKAQQTNALVAGSAALQTDRGPVNRF---LLVEPD 99
Cdd:cd07569   38 GAQLVVFPELaLTTFFPRwyfpdEAEldsffETEMPNPETQPLFDRAKELGIGFYLGYAELTEDGGVKRRFntsILVDKS 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 100 GTLHF-YDKRHL-----FRMADEHHH-----YEAGNerviFEWRGWRILP-----LVCYDLRFPVWSRN---------RN 154
Cdd:cd07569  118 GKIVGkYRKVHLpghkePEPYRPFQHlekryFEPGD----LGFPVFRVPGgimgmCICNDRRWPETWRVmglqgvelvLL 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 155 DYDLALYVANWPAP---RSLHWQALLVARAIENQAYVVGCNRVGTDgNGHHYRGDSRVVNPQGEVLATAEAHQATRIDAE 231
Cdd:cd07569  194 GYNTPTHNPPAPEHdhlRLFHNLLSMQAGAYQNGTWVVAAAKAGME-DGCDLIGGSCIVAPTGEIVAQATTLEDEVIVAD 272

                        250
                 ....*....|..
gi 974587522 232 LSLTALKEYREK 243
Cdd:cd07569  273 CDLDLCREGRET 284
GAT_Gln-NAD-synth cd07570
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ...
 5-254 1.55e-07

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: 50.93  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522   5 KITLLQQPLVWMDGPANLrhfDRQLEEIS-----GRDVIVLPEMFTTGFA----------MEAAKQSLpqDDVVAwmHTK 69
Cdd:cd07570    1 RIALAQLNPTVGDLEGNA---EKILEAIReakaqGADLVVFPELSLTGYPpedlllrpdfLEAAEEAL--EELAA--ATA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  70 AQQTNALVaGsAALQTDRGPVNRFLLVEpDGT-LHFYDKRHL-----FrmaDEHHHYEAGNERVIFEWRGWRILPLVCYD 143
Cdd:cd07570   74 DLDIAVVV-G-LPLRHDGKLYNAAAVLQ-NGKiLGVVPKQLLpnygvF---DEKRYFTPGDKPDVLFFKGLRIGVEICED 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 144 LRFPV---------------------WSRNRNDYdlalyvanwpapRslhwQALLVARAIENQAYVVGCNRVGtdGNGH- 201
Cdd:cd07570  148 LWVPDppsaelalagadlilnlsaspFHLGKQDY------------R----RELVSSRSARTGLPYVYVNQVG--GQDDl 209

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 974587522 202 HYRGDSRVVNPQGEVLatAEAHQATRIDAELSLTALKEYREKFPAWQDADPFI 254
Cdd:cd07570  210 VFDGGSFIADNDGELL--AEAPRFEEDLADVDLDRLRSERRRNSSFLDEEAEI 260
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
 33-219 2.21e-07

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: 50.61  E-value: 2.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  33 SGRDVIVLPEMFTTGFAMEAAKQSLPQDDVV-----AWMHTKAQQTNA-LVAGSAALQTDRGPV-NRFLLVEPDGTLHFY 105
Cdd:cd07578   32 AGARLIVTPEMATTGYCWYDRAEIAPFVEPIpgpttARFAELAREHDCyIVVGLPEVDSRSGIYyNSAVLIGPSGVIGRH 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 106 DKRHLF-------RMADEHHHyeagnervIFEWRGWRILPLVCYDLRFPVWSR--NRNDYDLALYVANW-----PAPrsl 171
Cdd:cd07578  112 RKTHPYisepkwaADGDLGHQ--------VFDTEIGRIALLICMDIHFFETARllALGGADVICHISNWlaertPAP--- 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 974587522 172 HWqallVARAIENQAYVVGCNRVGTDgNGHHYRGDSRVVNPQGEVLAT 219
Cdd:cd07578  181 YW----INRAFENGCYLIESNRWGLE-RGVQFSGGSCIIEPDGTIQAS 223
ML_beta-AS_like cd07568
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
 91-252 8.79e-07

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: 49.03  E-value: 8.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  91 NRFLLVEPDGT-LHFYDKRHLFRMAD--EHHHYEAGNE-RVIFEWRGWRILPLVCYDLRFPVWSR--NRNDYDLALYVAN 164
Cdd:cd07568  108 NTAAVIDADGTyLGKYRKNHIPHVGGfwEKFYFRPGNLgYPVFDTAFGKIGVYICYDRHFPEGWRalGLNGAEIVFNPSA 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 165 WPAPRSLH-WQALLVARAIENQAYVVGCNRVGTD--GNGHHYRGDSRVVNPQGEVLATAEAHQATRIDAELSLTALKEYR 241
Cdd:cd07568  188 TVAGLSEYlWKLEQPAAAVANGYFVGAINRVGTEapWNIGEFYGSSYFVDPRGQFVASASRDKDELLVAELDLDLIREVR 267

                        170
                 ....*....|.
gi 974587522 242 EKFPAWQDADP 252
Cdd:cd07568  268 DTWQFYRDRRP 278
nitrilases_CHs cd07564
Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases ...
 160-252 6.61e-05

Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases (nitrile aminohydrolases, EC:3.5.5.1) hydrolyze nitriles (RCN) to ammonia and the corresponding carboxylic acid. Most nitrilases prefer aromatic nitriles, some prefer arylacetonitriles and others aliphatic nitriles. This group includes the nitrilase cyanide dihydratase (CDH), which hydrolyzes inorganic cyanide (HCN) to produce formate. It also includes cyanide hydratase (CH), which hydrolyzes HCN to formamide. This group includes four Arabidopsis thaliana nitrilases (Ath)NIT1-4. AthNIT1-3 have a strong substrate preference for phenylpropionitrile (PPN) and other nitriles which may originate from the breakdown of glucosinolates. The product of PPN hydrolysis, phenylacetic acid has auxin activity. AthNIT1-3 can also convert indoacetonitrile to indole-3-acetic acid (IAA, auxin), but with a lower affinity and velocity. From their expression patterns, it has been speculated that NIT3 may produce IAA during the early stages of germination, and that NIT3 may produce IAA during embryo development and maturation. AthNIT4 has a strong substrate specificity for the nitrile, beta-cyano-L-alanine (Ala(CN)), an intermediate of cyanide detoxification. AthNIT4 has both a nitrilase activity and a nitrile hydratase (NHase) activity, which generate aspartic acid and asparagine respectively from Ala(CN). NHase catalyzes the hydration of nitriles to their corresponding amides. This subgroup belongs to a larger nitrilase superfamily comprised of 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 1.


Pssm-ID: 143588  Cd Length: 297  Bit Score: 43.25  E-value: 6.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 160 LYVANWPAPRSLH-----WQALLVARAIENQAYVVGCNRV----------GTDGNGHHY----RGDSRVVNPQGEVLATA 220
Cdd:cd07564  176 IHVAPWPDFSPYYlsreaWLAASRHYALEGRCFVLSACQVvteedipadcEDDEEADPLevlgGGGSAIVGPDGEVLAGP 255

                         90       100       110
                 ....*....|....*....|....*....|..
gi 974587522 221 EAHQATRIDAELSLTALkeYREKfpawQDADP 252
Cdd:cd07564  256 LPDEEGILYADIDLDDI--VEAK----LDFDP 281
PLN02747 PLN02747
N-carbamolyputrescine amidase
 172-252 9.40e-05

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 42.83  E-value: 9.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 172 HWQALLVARAIENQAYVVGCNRVGTD-------GNGHHYRGDSRVVNPQGEVLATAEAHQATRIDAELSLTALKEYREKF 244
Cdd:PLN02747 196 HWKRVMQGHAGANLVPLVASNRIGTEiletehgPSKITFYGGSFIAGPTGEIVAEADDKAEAVLVAEFDLDQIKSKRASW 275


                 ....*...
gi 974587522 245 PAWQDADP 252
Cdd:PLN02747 276 GVFRDRRP 283
aliphatic_amidase cd07565
aliphatic amidases (class 2 nitrilases); Aliphatic amidases catalyze the hydrolysis of ...
 34-242 1.50e-04

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: 42.27  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  34 GRDVIVLPEMFTTGFA-----MEAAKQSLPQDDVVAWmhtKAQQTNALVAGSAAL-----QTDRGPVNRFLLVEPDGTL- 102
Cdd:cd07565   39 GMDLIVFPEYSTQGLMydkwtMDETACTVPGPETDIF---AEACKEAKVWGVFSImernpDHGKNPYNTAIIIDDQGEIv 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522 103 HFYDKRHLFRMADEHhhyEAGNER--VIFEWRGWRILPLVCYDLRFPVWSRN--RNDYDLALYVANWPAPRSLHWQALLV 178
Cdd:cd07565  116 LKYRKLHPWVPIEPW---YPGDLGtpVCEGPKGSKIALIICHDGMYPEIAREcaYKGAELIIRIQGYMYPAKDQWIITNK 192

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 974587522 179 ARAIENQAYVVGCNRVGTDGNgHHYRGDSRVVNPQGEVLATAEAHQATRIDAELSLTALKEYRE 242
Cdd:cd07565  193 ANAWCNLMYTASVNLAGFDGV-FSYFGESMIVNFDGRTLGEGGREPDEIVTAELSPSLVRDARK 255
nitrilase_1_R2 cd07579
Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
 20-212 4.65e-04

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: 40.62  E-value: 4.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  20 ANLRHFDRQLEEI--SGRDVIVLPEMFTTGF---AMEAAKQSLPQDDVVAWMHTKAQQtnALVAGSAALQTDrGPVNRFL 94
Cdd:cd07579   15 GNLATIDRLAAEAkaTGAELVVFPELALTGLddpASEAESDTGPAVSALRRLARRLRL--YLVAGFAEADGD-GLYNSAV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974587522  95 LVEPDGTLHFYDKRHLfrMADEHHHYEAGNERVIFEWRGWRILPLVCYDLRFPVWSRNrndydLAL----YVA------- 163
Cdd:cd07579   92 LVGPEGLVGTYRKTHL--IEPERSWATPGDTWPVYDLPLGRVGLLIGHDALFPEAGRV-----LALrgcdLLAcpaaiai 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 974587522 164 -------------NWPAPRS---LHWQALLVaRAIENQAYVVGCNRVGTDGNghhYRGDSRVVNP 212
Cdd:cd07579  165 pfvgahagtsvpqPYPIPTGadpTHWHLARV-RAGENNVYFAFANVPDPARG---YTGWSGVFGP 225
 
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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