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Conserved domains on  [gi|490366861|ref|WP_004246525|]
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MULTISPECIES: nitrilase family protein [Proteus]

Protein Classification

nitrilase family protein( domain architecture ID 10166106)

nitrilase family protein is a member of a large superfamily and predicted to act as a carbon-nitrogen hydrolase; it depends on Glu-Lys-Cys catalytic triad

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
8-301 1.57e-125

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: 359.71  E-value: 1.57e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   8 RVASVQLQHKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGYWHVPKLPaqqvyaLSEKLADSASLKSIKQKAQQY 87
Cdd:cd07585    1 RIALVQFEARVGDKARNLAVIARWTRKAAAQGAELVCFPEMCITGYTHVRALS------REAEVPDGPSTQALSDLARRY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  88 AMAIGVGLIERDNNNnLYNTWVVCMPDGSLQKHRKLHAF--EHPVICSGDQYTVFDTPwGIKMGILICWDNNLVENARAT 165
Cdd:cd07585   75 GLTILAGLIEKAGDR-PYNTYLVCLPDGLVHRYRKLHLFrrEHPYIAAGDEYPVFATP-GVRFGILICYDNHFPENVRAT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 166 ALLGADILLAPHQTGGTHSrsphsmkpipmalwenrqqdpqalqaafqgEHGKGWLMRWLPARAHDNGMFIIFSNGVGRD 245
Cdd:cd07585  153 ALLGAEILFAPHATPGTTS------------------------------PKGREWWMRWLPARAYDNGVFVAACNGVGRD 202
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490366861 246 EEEVRTGNAMVIDPYGRIVKESCAIEDDMVVTDIDLTLLPESTGRRW---LTGRRPELY 301
Cdd:cd07585  203 GGEVFPGGAMILDPYGRVLAETTSGGDGMVVADLDLDLINTVRGRRWisfLRARRPELY 261
 
Name Accession Description Interval E-value
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
8-301 1.57e-125

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: 359.71  E-value: 1.57e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   8 RVASVQLQHKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGYWHVPKLPaqqvyaLSEKLADSASLKSIKQKAQQY 87
Cdd:cd07585    1 RIALVQFEARVGDKARNLAVIARWTRKAAAQGAELVCFPEMCITGYTHVRALS------REAEVPDGPSTQALSDLARRY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  88 AMAIGVGLIERDNNNnLYNTWVVCMPDGSLQKHRKLHAF--EHPVICSGDQYTVFDTPwGIKMGILICWDNNLVENARAT 165
Cdd:cd07585   75 GLTILAGLIEKAGDR-PYNTYLVCLPDGLVHRYRKLHLFrrEHPYIAAGDEYPVFATP-GVRFGILICYDNHFPENVRAT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 166 ALLGADILLAPHQTGGTHSrsphsmkpipmalwenrqqdpqalqaafqgEHGKGWLMRWLPARAHDNGMFIIFSNGVGRD 245
Cdd:cd07585  153 ALLGAEILFAPHATPGTTS------------------------------PKGREWWMRWLPARAYDNGVFVAACNGVGRD 202
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490366861 246 EEEVRTGNAMVIDPYGRIVKESCAIEDDMVVTDIDLTLLPESTGRRW---LTGRRPELY 301
Cdd:cd07585  203 GGEVFPGGAMILDPYGRVLAETTSGGDGMVVADLDLDLINTVRGRRWisfLRARRPELY 261
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
6-301 4.09e-73

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 226.28  E-value: 4.09e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   6 TLRVASVQLQHKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGYwhvpkLPAQQVYALSEKLADSASLKSIKQKAQ 85
Cdd:COG0388    1 TMRIALAQLNPTVGDIEANLAKIEELIREAAAQGADLVVFPELFLTGY-----PPEDDDLLELAEPLDGPALAALAELAR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  86 QYAMAIGVGLIERDNNNNLYNTWVVCMPDGSLQ-KHRKLHAF------EHPVICSGDQYTVFDTPWGiKMGILICWDNNL 158
Cdd:COG0388   76 ELGIAVVVGLPERDEGGRLYNTALVIDPDGEILgRYRKIHLPnygvfdEKRYFTPGDELVVFDTDGG-RIGVLICYDLWF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 159 VENARATALLGADILLAPHQTGGTHSRsphsmkpipmALWEnrqqdpqalqaafqgehgkgwlmRWLPARAHDNGMFIIF 238
Cdd:COG0388  155 PELARALALAGADLLLVPSASPFGRGK----------DHWE-----------------------LLLRARAIENGCYVVA 201
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490366861 239 SNGVGRDEEEVRTGNAMVIDPYGRIVKEsCAIEDDMVVTDIDLTLLPESTGRR-WLTGRRPELY 301
Cdd:COG0388  202 ANQVGGEDGLVFDGGSMIVDPDGEVLAE-AGDEEGLLVADIDLDRLREARRRFpVLRDRRPDLY 264
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
8-281 5.09e-49

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: 164.45  E-value: 5.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861    8 RVASVQLQHKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGYWHVPKlpaqqVYALSEKLaDSASLKSIKQKAQQY 87
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQKALELIEEAARYGADLIVLPELFITGYPCWAH-----FLEAAEVG-DGETLAGLAALARKN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   88 AMAIGVGLIER-DNNNNLYNTWVVCMPDGSL-QKHRKLHAF---------EHPVICSGDQYTVFDTPwGIKMGILICWDN 156
Cdd:pfam00795  75 GIAIVIGLIERwLTGGRLYNTAVLLDPDGKLvGKYRKLHLFpeprppgfrERVLFEPGDGGTVFDTP-LGKIGAAICYEI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  157 NLVENARATALLGADILLAphqtggthsrsPHSMKPIPMALWENRQQdpqalqaafqgehgkgWLMRwlpARAHDNGMFI 236
Cdd:pfam00795 154 RFPELLRALALKGAEILIN-----------PSARAPFPGSLGPPQWL----------------LLAR---ARALENGCFV 203
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 490366861  237 IFSNGVGRDEEEVRT-GNAMVIDPYGRIVKESCAIEDDMVVTDIDL 281
Cdd:pfam00795 204 IAANQVGGEEDAPWPyGHSMIIDPDGRILAGAGEWEEGVLIADIDL 249
PLN02747 PLN02747
N-carbamolyputrescine amidase
1-310 2.12e-25

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 102.92  E-value: 2.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   1 MNPLTTLRVASVQLQhKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGYWhvPKLPAQQVYALSEKLADSASLKSI 80
Cdd:PLN02747   1 MGMGRKVVVAALQFA-CSDDRAANVDKAERLVREAHAKGANIILIQELFEGYYF--CQAQREDFFQRAKPYEGHPTIARM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  81 KQKAQQYAMAIGVGLIERdNNNNLYNTWVVCMPDGS-LQKHRKLHAFEHP------VICSGDQ-YTVFDTPWGiKMGILI 152
Cdd:PLN02747  78 QKLAKELGVVIPVSFFEE-ANNAHYNSIAIIDADGTdLGLYRKSHIPDGPgyqekfYFNPGDTgFKVFDTKFA-KIGVAI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 153 CWDNNLVENARATALLGADILLAPHQTGgthsrsphsmkpipmalweNRQQDPqALQAAfqgEHgkgWlMRWLPARAHDN 232
Cdd:PLN02747 156 CWDQWFPEAARAMVLQGAEVLLYPTAIG-------------------SEPQDP-GLDSR---DH---W-KRVMQGHAGAN 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 233 GMFIIFSNGVGRDEEEVRT--------GNAMVIDPYGRIVKESCAIEDDMVVTDIDLTLLpESTGRRW--LTGRRPELYQ 302
Cdd:PLN02747 209 LVPLVASNRIGTEILETEHgpskitfyGGSFIAGPTGEIVAEADDKAEAVLVAEFDLDQI-KSKRASWgvFRDRRPDLYK 287

                 ....*...
gi 490366861 303 ILTTRQGN 310
Cdd:PLN02747 288 VLLTLDGN 295
 
Name Accession Description Interval E-value
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
8-301 1.57e-125

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: 359.71  E-value: 1.57e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   8 RVASVQLQHKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGYWHVPKLPaqqvyaLSEKLADSASLKSIKQKAQQY 87
Cdd:cd07585    1 RIALVQFEARVGDKARNLAVIARWTRKAAAQGAELVCFPEMCITGYTHVRALS------REAEVPDGPSTQALSDLARRY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  88 AMAIGVGLIERDNNNnLYNTWVVCMPDGSLQKHRKLHAF--EHPVICSGDQYTVFDTPwGIKMGILICWDNNLVENARAT 165
Cdd:cd07585   75 GLTILAGLIEKAGDR-PYNTYLVCLPDGLVHRYRKLHLFrrEHPYIAAGDEYPVFATP-GVRFGILICYDNHFPENVRAT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 166 ALLGADILLAPHQTGGTHSrsphsmkpipmalwenrqqdpqalqaafqgEHGKGWLMRWLPARAHDNGMFIIFSNGVGRD 245
Cdd:cd07585  153 ALLGAEILFAPHATPGTTS------------------------------PKGREWWMRWLPARAYDNGVFVAACNGVGRD 202
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490366861 246 EEEVRTGNAMVIDPYGRIVKESCAIEDDMVVTDIDLTLLPESTGRRW---LTGRRPELY 301
Cdd:cd07585  203 GGEVFPGGAMILDPYGRVLAETTSGGDGMVVADLDLDLINTVRGRRWisfLRARRPELY 261
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
6-301 4.09e-73

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 226.28  E-value: 4.09e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   6 TLRVASVQLQHKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGYwhvpkLPAQQVYALSEKLADSASLKSIKQKAQ 85
Cdd:COG0388    1 TMRIALAQLNPTVGDIEANLAKIEELIREAAAQGADLVVFPELFLTGY-----PPEDDDLLELAEPLDGPALAALAELAR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  86 QYAMAIGVGLIERDNNNNLYNTWVVCMPDGSLQ-KHRKLHAF------EHPVICSGDQYTVFDTPWGiKMGILICWDNNL 158
Cdd:COG0388   76 ELGIAVVVGLPERDEGGRLYNTALVIDPDGEILgRYRKIHLPnygvfdEKRYFTPGDELVVFDTDGG-RIGVLICYDLWF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 159 VENARATALLGADILLAPHQTGGTHSRsphsmkpipmALWEnrqqdpqalqaafqgehgkgwlmRWLPARAHDNGMFIIF 238
Cdd:COG0388  155 PELARALALAGADLLLVPSASPFGRGK----------DHWE-----------------------LLLRARAIENGCYVVA 201
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490366861 239 SNGVGRDEEEVRTGNAMVIDPYGRIVKEsCAIEDDMVVTDIDLTLLPESTGRR-WLTGRRPELY 301
Cdd:COG0388  202 ANQVGGEDGLVFDGGSMIVDPDGEVLAE-AGDEEGLLVADIDLDRLREARRRFpVLRDRRPDLY 264
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
9-292 1.37e-63

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: 201.78  E-value: 1.37e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   9 VASVQLQHKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGYWhvPKLPAQQVYALSEklADSASLKSIKQKAQQYA 88
Cdd:cd07197    1 IAAVQLAPKIGDVEANLAKALRLIKEAAEQGADLIVLPELFLTGYS--FESAKEDLDLAEE--LDGPTLEALAELAKELG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  89 MAIGVGLIERDnNNNLYNTWVVCMPDGS-LQKHRKLHAF---EHPVICSGDQYTVFDTPWGiKMGILICWDNNLVENARA 164
Cdd:cd07197   77 IYIVAGIAEKD-GDKLYNTAVVIDPDGEiIGKYRKIHLFdfgERRYFSPGDEFPVFDTPGG-KIGLLICYDLRFPELARE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 165 TALLGADILLAPHQTGGthSRSPHsmkpipmalWEnrqqdpqalqaafqgehgkgwlmRWLPARAHDNGMFIIFSNGVGR 244
Cdd:cd07197  155 LALKGADIILVPAAWPT--ARREH---------WE-----------------------LLLRARAIENGVYVVAANRVGE 200
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 490366861 245 DEEEVRTGNAMVIDPYGRIVKEsCAIEDDMVVTDIDLTLLPESTGRRW 292
Cdd:cd07197  201 EGGLEFAGGSMIVDPDGEVLAE-ASEEEGILVAELDLDELREARKRWS 247
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
8-281 5.09e-49

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: 164.45  E-value: 5.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861    8 RVASVQLQHKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGYWHVPKlpaqqVYALSEKLaDSASLKSIKQKAQQY 87
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQKALELIEEAARYGADLIVLPELFITGYPCWAH-----FLEAAEVG-DGETLAGLAALARKN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   88 AMAIGVGLIER-DNNNNLYNTWVVCMPDGSL-QKHRKLHAF---------EHPVICSGDQYTVFDTPwGIKMGILICWDN 156
Cdd:pfam00795  75 GIAIVIGLIERwLTGGRLYNTAVLLDPDGKLvGKYRKLHLFpeprppgfrERVLFEPGDGGTVFDTP-LGKIGAAICYEI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  157 NLVENARATALLGADILLAphqtggthsrsPHSMKPIPMALWENRQQdpqalqaafqgehgkgWLMRwlpARAHDNGMFI 236
Cdd:pfam00795 154 RFPELLRALALKGAEILIN-----------PSARAPFPGSLGPPQWL----------------LLAR---ARALENGCFV 203
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 490366861  237 IFSNGVGRDEEEVRT-GNAMVIDPYGRIVKESCAIEDDMVVTDIDL 281
Cdd:pfam00795 204 IAANQVGGEEDAPWPyGHSMIIDPDGRILAGAGEWEEGVLIADIDL 249
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
8-299 5.48e-42

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: 145.80  E-value: 5.48e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   8 RVASVQLQHKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGYwhvpkLPAQQVYALSEkLADSASLKSIKQKAQQY 87
Cdd:cd07576    1 RLALYQGPARDGDVAANLARLDEAAARAAAAGADLLVFPELFLTGY-----NIGDAVARLAE-PADGPALQALRAIARRH 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  88 AMAIGVGLIERDnNNNLYNTWVVCMPDG-SLQKHRKLHAF---EHPVICSGDQYTVFDTpWGIKMGILICWDNNLVENAR 163
Cdd:cd07576   75 GIAIVVGYPERA-GGAVYNAAVLIDEDGtVLANYRKTHLFgdsERAAFTPGDRFPVVEL-RGLRVGLLICYDVEFPELVR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 164 ATALLGADILLAPhqTGgthsrsphSMKPipmalWENrqqDPQALqaafqgehgkgwlmrwLPARAHDNGMFIIFSNGVG 243
Cdd:cd07576  153 ALALAGADLVLVP--TA--------LMEP-----YGF---VARTL----------------VPARAFENQIFVAYANRCG 198
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490366861 244 RDEEEVRTGNAMVIDPYGRIVKEsCAIEDDMVVTDIDLTLLPESTGR-RWLTGRRPE 299
Cdd:cd07576  199 AEDGLTYVGLSSIAGPDGTVLAR-AGRGEALLVADLDPAALAAARREnPYLADRRPE 254
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
8-286 2.51e-38

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: 136.79  E-value: 2.51e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   8 RVASVQLqHKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGYWHvpklPAQQVYALSEKLaDSASLKSIKQKAQQY 87
Cdd:cd07572    1 RVALIQM-TSTADKEANLARAKELIEEAAAQGAKLVVLPECFNYPGGT----DAFKLALAEEEG-DGPTLQALSELAKEH 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  88 AMAI-GVGLIERDNNNN-LYNTWVVCMPDGSL-QKHRKLHAF-----------EHPVICSGDQYTVFDTPWGiKMGILIC 153
Cdd:cd07572   75 GIWLvGGSIPERDDDDGkVYNTSLVFDPDGELvARYRKIHLFdvdvpggisyrESDTLTPGDEVVVVDTPFG-KIGLGIC 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 154 WDNNLVENARATALLGADILLAP----HQTGGTHsrsphsmkpipmalWEnrqqdpqaLqaafqgehgkgwLMRwlpARA 229
Cdd:cd07572  154 YDLRFPELARALARQGADILTVPaaftMTTGPAH--------------WE--------L------------LLR---ARA 196
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490366861 230 HDNGMFIIFSNGVGRDEEEVRT-GNAMVIDPYGRIVKEsCAIEDDMVVTDIDLTLLPE 286
Cdd:cd07572  197 IENQCYVVAAAQAGDHEAGRETyGHSMIVDPWGEVLAE-AGEGEGVVVAEIDLDRLEE 253
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
8-301 3.08e-38

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: 136.71  E-value: 3.08e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   8 RVASVQLQHKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGYWHVPKlpaQQVYALSEKLADSASLKSIKQKAQQY 87
Cdd:cd07580    1 RVACVQFDPRVGDLDANLARSIELIREAADAGANLVVLPELANTGYVFESR---DEAFALAEEVPDGASTRAWAELAAEL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  88 AMAIGVGLIERDnNNNLYNTWVVCMPDGSLQKHRKLH--AFEHPVICSGDQ-YTVFDTPWGiKMGILICWDNNLVENARA 164
Cdd:cd07580   78 GLYIVAGFAERD-GDRLYNSAVLVGPDGVIGTYRKAHlwNEEKLLFEPGDLgLPVFDTPFG-RIGVAICYDGWFPETFRL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 165 TALLGADILLAPhqTGGthsrsphsmkpIPMAlwenRQQDPQALQAAFQGEhgkgwlmrwlpARAHDNGMFIIFSNGVGR 244
Cdd:cd07580  156 LALQGADIVCVP--TNW-----------VPMP----RPPEGGPPMANILAM-----------AAAHSNGLFIACADRVGT 207
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490366861 245 DEEEVRTGNAMVIDPYGRIVKE-SCAIEDDMVVTDIDLTllpESTGRR-W-----LTGRRPELY 301
Cdd:cd07580  208 ERGQPFIGQSLIVGPDGWPLAGpASGDEEEILLADIDLT---AARRKRiWnsndvLRDRRPDLY 268
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
7-306 4.61e-38

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: 136.54  E-value: 4.61e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   7 LRVASVQlQHKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGYWhvPKLPAQQVYALSEKLADSASLKSIKQKAQQ 86
Cdd:cd07573    1 VTVALVQ-MACSEDPEANLAKAEELVREAAAQGAQIVCLQELFETPYF--CQEEDEDYFDLAEPPIPGPTTARFQALAKE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  87 YAMAIGVGLIERDNNNNLYNTWVVCMPDGS-LQKHRKLH-----AFEH-----PvicsGDQ-YTVFDTPWGiKMGILICW 154
Cdd:cd07573   78 LGVVIPVSLFEKRGNGLYYNSAVVIDADGSlLGVYRKMHipddpGYYEkfyftP----GDTgFKVFDTRYG-RIGVLICW 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 155 DNNLVENARATALLGADILLAPHQTGgthsrsphsmkpipmalWEnrQQDPQAlqaafqgehGKGWLMRWLPA-RAHD-- 231
Cdd:cd07573  153 DQWFPEAARLMALQGAEILFYPTAIG-----------------SE--PQEPPE---------GLDQRDAWQRVqRGHAia 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 232 NGMFIIFSNGVGRDEEEVRT----GNAMVIDPYGRIVKESCAIEDDMVVTDIDLTLLpESTGRRW--LTGRRPELYQILT 305
Cdd:cd07573  205 NGVPVAAVNRVGVEGDPGSGitfyGSSFIADPFGEILAQASRDEEEILVAEFDLDEI-EEVRRAWpfFRDRRPDLYGALT 283

                 .
gi 490366861 306 T 306
Cdd:cd07573  284 K 284
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
8-301 1.22e-37

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: 134.73  E-value: 1.22e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   8 RVASVQLQHKANDKDYNLAKIHQFIEmaaSEKVNLLVFPEMCITGYWHVPKlpaQQVYALSEKLADSASLKSIKQKAQQY 87
Cdd:cd07577    1 KVGYVQFNPKFGEVEKNLKKVESLIK---GVEADLIVLPELFNTGYAFTSK---EEVASLAESIPDGPTTRFLQELARET 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  88 AMAIGVGLIERDNNNnLYNTWVVCMPDGSLQKHRKLHAF--EHPVICSGDQ-YTVFDTPwGIKMGILICWDNNLVENARA 164
Cdd:cd07577   75 GAYIVAGLPERDGDK-FYNSAVVVGPEGYIGIYRKTHLFyeEKLFFEPGDTgFRVFDIG-DIRIGVMICFDWYFPEAART 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 165 TALLGADILLAPHQtggthsrsphsmkpIPMALWenrqqdPQAlqaafqgehgkgwlmrwLPARAHDNGMFIIFSNGVG- 243
Cdd:cd07577  153 LALKGADIIAHPAN--------------LVLPYC------PKA-----------------MPIRALENRVFTITANRIGt 195
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490366861 244 --RDEEEVR-TGNAMVIDPYGRIVKESCAIEDDMVVTDIDltllPESTGRRWLTG-------RRPELY 301
Cdd:cd07577  196 eeRGGETLRfIGKSQITSPKGEVLARAPEDGEEVLVAEID----PRLARDKRINEendifkdRRPEFY 259
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
8-284 2.07e-36

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: 131.34  E-value: 2.07e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   8 RVASVQLQHKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGYwhVPKLPAQQVYALSEKLaDSASLKSIKQKAQQY 87
Cdd:cd07584    1 KVALIQMDSVLGDVKANLKKAAELCKEAAAEGADLICFPELATTGY--RPDLLGPKLWELSEPI-DGPTVRLFSELAKEL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  88 AMAIGVGLIERDN-NNNLYNTWVVCMPDG-SLQKHRKLHAF--EHPVICSGDQYTVFDTPWGiKMGILICWDNNLVENAR 163
Cdd:cd07584   78 GVYIVCGFVEKGGvPGKVYNSAVVIDPEGeSLGVYRKIHLWglEKQYFREGEQYPVFDTPFG-KIGVMICYDMGFPEVAR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 164 ATALLGADILLAPhqtggthsrsphsmkpipmALWENRQQDpqalqaafqgehgkgwlmRW---LPARAHDNGMFIIFSN 240
Cdd:cd07584  157 ILTLKGAEVIFCP-------------------SAWREQDAD------------------IWdinLPARALENTVFVAAVN 199
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 490366861 241 GVGRDEEEVRTGNAMVIDPYGRIVKESCAIEDDMVVTDIDLTLL 284
Cdd:cd07584  200 RVGNEGDLVLFGKSKILNPRGQVLAEASEEAEEILYAEIDLDAI 243
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
8-286 1.58e-35

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: 129.20  E-value: 1.58e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   8 RVASVQLQHKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGYwhvpklPAQQVYALSEKLaDSASLKSIKQKAQQY 87
Cdd:cd07583    1 KIALIQLDIVWGDPEANIERVESLIEEAAAAGADLIVLPEMWNTGY------FLDDLYELADED-GGETVSFLSELAKKH 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  88 AMAIGVGLIERDNNNNLYNTWVVCMPDGSLQ-KHRKLHAF----EHPVICSGDQYTVFDTPwGIKMGILICWDNNLVENA 162
Cdd:cd07583   74 GVNIVAGSVAEKEGGKLYNTAYVIDPDGELIaTYRKIHLFglmgEDKYLTAGDELEVFELD-GGKVGLFICYDLRFPELF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 163 RATALLGADILLAPhqtggthsrsphsmkpipmALWenrqqdPQAlqaafQGEHgkgwlmrW---LPARAHDNGMFIIFS 239
Cdd:cd07583  153 RKLALEGAEILFVP-------------------AEW------PAA-----RIEH-------WrtlLRARAIENQAFVVAC 195
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 490366861 240 NGVGRDEEEVRTGNAMVIDPYGRIVKESCAiEDDMVVTDIDLTLLPE 286
Cdd:cd07583  196 NRVGTDGGNEFGGHSMVIDPWGEVLAEAGE-EEEILTAEIDLEEVAE 241
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
9-284 1.11e-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: 113.44  E-value: 1.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   9 VASVQLqHKANDKDYNLAKIHQFIEMAASEKVNLLVFPE--MCITGywhvpkLPAQQVYALSEKLaDSASLKSIKQKAQQ 86
Cdd:cd07581    1 VALAQF-ASSGDKEENLEKVRRLLAEAAAAGADLVVFPEytMARFG------DGLDDYARVAEPL-DGPFVSALARLARE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  87 YAMAIGVGLIERDNNNNLYNTWVVCMPDGSLQKH-RKLH---AF---EHPVICSGDQYTVFDTPW-GIKMGILICWDNNL 158
Cdd:cd07581   73 LGITVVAGMFEPAGDGRVYNTLVVVGPDGEIIAVyRKIHlydAFgfrESDTVAPGDELPPVVFVVgGVKVGLATCYDLRF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 159 VENARATALLGADILLAPhqtggthsrsphsmkpipmALWenrqqdpqalqaaFQGEhGKgwLMRW---LPARAHDNGMF 235
Cdd:cd07581  153 PELARALALAGADVIVVP-------------------AAW-------------VAGP-GK--EEHWetlLRARALENTVY 197
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 490366861 236 IIFSNGVGRDeeevRTGNAMVIDPYGRIVKEScAIEDDMVVTDIDLTLL 284
Cdd:cd07581  198 VAAAGQAGPR----GIGRSMVVDPLGVVLADL-GEREGLLVADIDPERV 241
nitrilase_8 cd07586
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
8-287 1.06e-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: 143610  Cd Length: 269  Bit Score: 108.53  E-value: 1.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   8 RVASVQLQHKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGYwHVPKLpAQQVYalseKLADSASLKSIKQKAQQy 87
Cdd:cd07586    1 RVAIAQIDPVLGDVEENLEKHLEIIETARERGADLVVFPELSLTGY-NLGDL-VYEVA----MHADDPRLQALAEASGG- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  88 aMAIGVGLIERDNNNNLYNTwVVCMPDGSLQ-KHRKLH-----AFE-----HPvicsGDQYTVFDTPWGiKMGILIC--- 153
Cdd:cd07586   74 -ICVVFGFVEEGRDGRFYNS-AAYLEDGRVVhVHRKVYlptygLFEegryfAP----GSHLRAFDTRFG-RAGVLICeda 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 154 WDNNLVEnarATALLGADILLAPhqtggthSRSPhsmkpipmalWENRQQDPQALQaafqgehgkGWLMRwLPARAHDNG 233
Cdd:cd07586  147 WHPSLPY---LLALDGADVIFIP-------ANSP----------ARGVGGDFDNEE---------NWETL-LKFYAMMNG 196
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490366861 234 MFIIFSNGVGRDEEEVRTGNAMVIDPYGRIVKESCAIEDDMVVTDIDLTLLPES 287
Cdd:cd07586  197 VYVVFANRVGVEDGVYFWGGSRVVDPDGEVVAEAPLFEEDLLVAELDRSAIRRA 250
PLN02747 PLN02747
N-carbamolyputrescine amidase
1-310 2.12e-25

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 102.92  E-value: 2.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   1 MNPLTTLRVASVQLQhKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGYWhvPKLPAQQVYALSEKLADSASLKSI 80
Cdd:PLN02747   1 MGMGRKVVVAALQFA-CSDDRAANVDKAERLVREAHAKGANIILIQELFEGYYF--CQAQREDFFQRAKPYEGHPTIARM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  81 KQKAQQYAMAIGVGLIERdNNNNLYNTWVVCMPDGS-LQKHRKLHAFEHP------VICSGDQ-YTVFDTPWGiKMGILI 152
Cdd:PLN02747  78 QKLAKELGVVIPVSFFEE-ANNAHYNSIAIIDADGTdLGLYRKSHIPDGPgyqekfYFNPGDTgFKVFDTKFA-KIGVAI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 153 CWDNNLVENARATALLGADILLAPHQTGgthsrsphsmkpipmalweNRQQDPqALQAAfqgEHgkgWlMRWLPARAHDN 232
Cdd:PLN02747 156 CWDQWFPEAARAMVLQGAEVLLYPTAIG-------------------SEPQDP-GLDSR---DH---W-KRVMQGHAGAN 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 233 GMFIIFSNGVGRDEEEVRT--------GNAMVIDPYGRIVKESCAIEDDMVVTDIDLTLLpESTGRRW--LTGRRPELYQ 302
Cdd:PLN02747 209 LVPLVASNRIGTEILETEHgpskitfyGGSFIAGPTGEIVAEADDKAEAVLVAEFDLDQI-KSKRASWgvFRDRRPDLYK 287

                 ....*...
gi 490366861 303 ILTTRQGN 310
Cdd:PLN02747 288 VLLTLDGN 295
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
7-179 2.87e-25

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: 102.28  E-value: 2.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   7 LRVASVQLQ-HKANDKDYNLAKIHQFIEMAASEKVNLLVFPEM----CITGYWHVPKLPAQQVYALSEKLADSASLKSik 81
Cdd:cd07574    1 VRVAAAQYPlRRYASFEEFAAKVEYWVAEAAGYGADLLVFPEYftmeLLSLLPEAIDGLDEAIRALAALTPDYVALFS-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  82 QKAQQYAMAI--GVGLIERDNNnnLYNTWVVCMPDGSLQKHRKLHAF----EHPVICSGDQYTVFDTPWGiKMGILICWD 155
Cdd:cd07574   79 ELARKYGINIiaGSMPVREDGR--LYNRAYLFGPDGTIGHQDKLHMTpferEEWGISGGDKLKVFDTDLG-KIGILICYD 155
                        170       180
                 ....*....|....*....|....
gi 490366861 156 NNLVENARATALLGADILLAPHQT 179
Cdd:cd07574  156 SEFPELARALAEAGADLLLVPSCT 179
GAT_Gln-NAD-synth cd07570
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ...
8-282 2.67e-24

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: 99.47  E-value: 2.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   8 RVASVQLQHKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGYwhvpklPAQQVYaLSEKLADSA--SLKSIKQKAQ 85
Cdd:cd07570    1 RIALAQLNPTVGDLEGNAEKILEAIREAKAQGADLVVFPELSLTGY------PPEDLL-LRPDFLEAAeeALEELAAATA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  86 QYAMAIGVGLIERdNNNNLYNTWVVCMpDGSLQKHR-KLHafehpvICSgdqYTVFD-----TPW---------GIKMGI 150
Cdd:cd07570   74 DLDIAVVVGLPLR-HDGKLYNAAAVLQ-NGKILGVVpKQL------LPN---YGVFDekryfTPGdkpdvlffkGLRIGV 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 151 LIC---WDNNLVenARATALLGADILLAPhqtggthSRSPHSM-KPipmalwENRQQdpqalqaafqgehgkgwLMRwlp 226
Cdd:cd07570  143 EICedlWVPDPP--SAELALAGADLILNL-------SASPFHLgKQ------DYRRE-----------------LVS--- 187
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490366861 227 ARAHDNGMFIIFSNGVGRDEEEVRTGNAMVIDPYGRIVKESCAIEDDMVVTDIDLT 282
Cdd:cd07570  188 SRSARTGLPYVYVNQVGGQDDLVFDGGSFIADNDGELLAEAPRFEEDLADVDLDRL 243
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
7-300 4.78e-24

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: 98.76  E-value: 4.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   7 LRVASVQLQHKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGY-W--------HVPKLPAqqvyALSEKLAdsasl 77
Cdd:cd07578    1 YKAAAIQFEPEMGEKERNIERLLALCEEAARAGARLIVTPEMATTGYcWydraeiapFVEPIPG----PTTARFA----- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  78 ksikQKAQQYAMAIGVGLIERDNNNNL-YNTWVVCMPDGSLQKHRKLHAF--EHPVICSGDQ-YTVFDTPWGiKMGILIC 153
Cdd:cd07578   72 ----ELAREHDCYIVVGLPEVDSRSGIyYNSAVLIGPSGVIGRHRKTHPYisEPKWAADGDLgHQVFDTEIG-RIALLIC 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 154 WDNNLVENARATALLGADILLapHQTGGTHSRSPhsmkpipmalwenrqqdpqalqaafqgehGKGWLmrwlpARAHDNG 233
Cdd:cd07578  147 MDIHFFETARLLALGGADVIC--HISNWLAERTP-----------------------------APYWI-----NRAFENG 190
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490366861 234 MFIIFSNGVGRDEEEVRTGNAMVIDPYGRIVKeSCAIEDDMVVTDIDLTLL--PESTGRRWLTGRRPEL 300
Cdd:cd07578  191 CYLIESNRWGLERGVQFSGGSCIIEPDGTIQA-SIDSGDGVALGEIDLDRArhRQFPGELVFTARRPEL 258
ML_beta-AS_like cd07568
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
20-305 2.43e-23

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: 97.18  E-value: 2.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  20 DKDYNLAKIHQFIEMAASEKVNLLVFPEMcitgyWHVPKLPAQQV---YALSEKLADSASLKSIKQKAQQYAMAIGVGLI 96
Cdd:cd07568   24 QKEAMIQKHVTMIREAAEAGAQIVCLQEI-----FYGPYFCAEQDtkwYEFAEEIPNGPTTKRFAALAKEYNMVLILPIY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  97 ERDNNNNLYNTWVVCMPDGS-LQKHRKLHA------FEHPVICSGDQ-YTVFDTPWGiKMGILICWDNNLVENARATALL 168
Cdd:cd07568   99 EKEQGGTLYNTAAVIDADGTyLGKYRKNHIphvggfWEKFYFRPGNLgYPVFDTAFG-KIGVYICYDRHFPEGWRALGLN 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 169 GADILLAPHQTGGTHSRSphsmkpipmaLWENRQqdpqalqaafqgehgkgwlmrwlPARAHDNGMFIIFSNGVGrdEEE 248
Cdd:cd07568  178 GAEIVFNPSATVAGLSEY----------LWKLEQ-----------------------PAAAVANGYFVGAINRVG--TEA 222
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490366861 249 VRT-----GNAMVIDPYGRIVKESCAIEDDMVVTDIDLTLLPEsTGRRW--LTGRRPELYQILT 305
Cdd:cd07568  223 PWNigefyGSSYFVDPRGQFVASASRDKDELLVAELDLDLIRE-VRDTWqfYRDRRPETYGELT 285
nitrilases_CHs cd07564
Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases ...
7-287 1.78e-21

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: 92.17  E-value: 1.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   7 LRVASVQLQHKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGY-WHVPKLPAQQVYALSEKLADSA------SLKS 79
Cdd:cd07564    1 VKVAAVQAAPVFLDLAATVEKACRLIEEAAANGAQLVVFPEAFIPGYpYWIWFGAPAEGRELFARYYENSvevdgpELER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  80 IKQKAQQYAMAIGVGLIERDnNNNLYNTWVVCMPDGS-LQKHRKLH--AFEHPVICSGDQYT--VFDTPWGiKMGILICW 154
Cdd:cd07564   81 LAEAARENGIYVVLGVSERD-GGTLYNTQLLIDPDGElLGKHRKLKptHAERLVWGQGDGSGlrVVDTPIG-RLGALICW 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 155 dnnlvEN----ARaTALL--GADILLAPhqtggTHSRSPHSMKPipmALWENRqqdpqalqaafqgehgkgwlMRwlpAR 228
Cdd:cd07564  159 -----ENymplAR-YALYaqGEQIHVAP-----WPDFSPYYLSR---EAWLAA--------------------SR---HY 201
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490366861 229 AHDNGMFIIFSNGVGRDE---------------EEVRTGNAMVIDPYGRIVKESCAIEDDMVVTDIDLTLLPES 287
Cdd:cd07564  202 ALEGRCFVLSACQVVTEEdipadceddeeadplEVLGGGGSAIVGPDGEVLAGPLPDEEGILYADIDLDDIVEA 275
DCase cd07569
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ...
6-305 9.29e-18

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: 81.97  E-value: 9.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   6 TLRVASVQLQ--HKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGY---WHVPKlpAQQVYALSEKLADSASLKSI 80
Cdd:cd07569    3 QVILAAAQMGpiARAETRESVVARLIALLEEAASRGAQLVVFPELALTTFfprWYFPD--EAELDSFFETEMPNPETQPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  81 KQKAQQYAMAIGVG---LIERDNNNNLYNTWVVCMPDGS-LQKHRKLH-----------AFEH-------PvicsGDQ-Y 137
Cdd:cd07569   81 FDRAKELGIGFYLGyaeLTEDGGVKRRFNTSILVDKSGKiVGKYRKVHlpghkepepyrPFQHlekryfeP----GDLgF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 138 TVFDTPWGIkMGILICWDNNLVENARATALLGADILLAPHQTGgthSRSPHSMKPIPMALWENRQqdpqALQAAfqgehg 217
Cdd:cd07569  157 PVFRVPGGI-MGMCICNDRRWPETWRVMGLQGVELVLLGYNTP---THNPPAPEHDHLRLFHNLL----SMQAG------ 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 218 kgwlmrwlparAHDNGMFIIFSNGVGRDEEEVRTGNAMVIDPYGRIVKESCAIEDDMVVTDIDLTLlpestGRRWLTG-- 295
Cdd:cd07569  223 -----------AYQNGTWVVAAAKAGMEDGCDLIGGSCIVAPTGEIVAQATTLEDEVIVADCDLDL-----CREGRETvf 286
                        330
                 ....*....|....*
gi 490366861 296 -----RRPELYQILT 305
Cdd:cd07569  287 nfarhRRPEHYGLIA 301
nitrilase_1_R2 cd07579
Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
8-240 2.93e-17

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: 80.29  E-value: 2.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   8 RVASVQLQHKANDKDyNLAKIHQFIEMAASEKVNLLVFPEMCITGYWHvpklPAQQVYALseklaDSASLKSIKQKAQQY 87
Cdd:cd07579    1 RIAVAQFAPTPDIAG-NLATIDRLAAEAKATGAELVVFPELALTGLDD----PASEAESD-----TGPAVSALRRLARRL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  88 AMAIGVGLIERDnNNNLYNTWVVCMPDGSLQKHRKLH--AFEHPVICSGDQYTVFDTPWGiKMGILICWDNNLVENARAT 165
Cdd:cd07579   71 RLYLVAGFAEAD-GDGLYNSAVLVGPEGLVGTYRKTHliEPERSWATPGDTWPVYDLPLG-RVGLLIGHDALFPEAGRVL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 166 ALLGADILLAPHQTGG--THSRSPHSMK---PIPMAlwenrqQDPqalqaaFQGEHGKgwlmrwlpARAHDNGMFIIFSN 240
Cdd:cd07579  149 ALRGCDLLACPAAIAIpfVGAHAGTSVPqpyPIPTG------ADP------THWHLAR--------VRAGENNVYFAFAN 208
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
7-280 3.71e-15

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: 73.73  E-value: 3.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   7 LRVASVQLQHKANDKDYNLAKIHQFIEmAASEKVNLLVFPEMCITGYwhvpklpAQQVYALSEKlADSASLKSIKQKAQQ 86
Cdd:cd07575    1 LKIALIQTDLVWEDPEANLAHFEEKIE-QLKEKTDLIVLPEMFTTGF-------SMNAEALAEP-MNGPTLQWMKAQAKK 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  87 YAMAIGVGLIERDnNNNLYNTWVVCMPDGSLQKHRKLHAF----EHPVICSGDQYTVFDtpW-GIKMGILIC-------W 154
Cdd:cd07575   72 KGAAITGSLIIKE-GGKYYNRLYFVTPDGEVYHYDKRHLFrmagEHKVYTAGNERVIVE--YkGWKILLQVCydlrfpvW 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 155 DNNLVEnaratallgADILLAphqtggthsrsphsmkpipMALWenrqqdPQALQAAfqgehgkgwlmrW---LPARAHD 231
Cdd:cd07575  149 SRNTND---------YDLLLY-------------------VANW------PAPRRAA------------WdtlLKARAIE 182
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 490366861 232 NGMFIIFSNGVGRDEEEVR-TGNAMVIDPYGRIVKEsCAIEDDMVVTDID 280
Cdd:cd07575  183 NQAYVIGVNRVGTDGNGLEySGDSAVIDPLGEPLAE-AEEDEGVLTATLD 231
PRK13981 PRK13981
NAD synthetase; Provisional
7-282 1.42e-14

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 74.04  E-value: 1.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   7 LRVASVQLQHKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGY--------WHVPKLPAQQVYALSEKLADSAslk 78
Cdd:PRK13981   1 LRIALAQLNPTVGDIAGNAAKILAAAAEAADAGADLLLFPELFLSGYppedlllrPAFLAACEAALERLAAATAGGP--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  79 sikqkaqqyamAIGVGLIERDnNNNLYNTWVVCMPDGSLQKHRKLH-----AF-EHPVICSGDQYTVFDTPwGIKMGILI 152
Cdd:PRK13981  78 -----------AVLVGHPWRE-GGKLYNAAALLDGGEVLATYRKQDlpnygVFdEKRYFAPGPEPGVVELK-GVRIGVPI 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 153 CWDNNLVENARATALLGADILLAPhqtggthSRSPHSM-KPipmalwENRQQdpqalqaafqgehgkgwLMRwlpARAHD 231
Cdd:PRK13981 145 CEDIWNPEPAETLAEAGAELLLVP-------NASPYHRgKP------DLREA-----------------VLR---ARVRE 191
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490366861 232 NGMFIIFSNGVGRDEEEVRTGNAMVIDPYGRIVKESCAIEDDMVVTDIDLT 282
Cdd:PRK13981 192 TGLPLVYLNQVGGQDELVFDGASFVLNADGELAARLPAFEEQIAVVDFDRG 242
nitrilase_4 cd07582
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
40-294 3.07e-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: 71.99  E-value: 3.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  40 VNLLVFPEMCITGywhvPKLPAQQVYALSEKLA---DSASLKSIKQKAQQYAMAIGVGLIERDNN--NNLYNTWVVCMPD 114
Cdd:cd07582   43 VRLVVLPEYALQG----FPMGEPREVWQFDKAAidiPGPETEALGEKAKELNVYIAANAYERDPDfpGLYFNTAFIIDPS 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 115 GS-LQKHRKLHA------------FEHPVICSGDQ----YTVFDTPWGiKMGILICWDNNLVENARATALLGADILLaph 177
Cdd:cd07582  119 GEiILRYRKMNSlaaegspsphdvWDEYIEVYGYGldalFPVADTEIG-NLGCLACEEGLYPEVARGLAMNGAEVLL--- 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 178 qtggtHSRSPhsMKPIPMALWE--NRqqdpqalqaafqgehgkgwlmrwlpARAHDNGMFIIFSNGVGRDEE----EVRT 251
Cdd:cd07582  195 -----RSSSE--VPSVELDPWEiaNR-------------------------ARALENLAYVVSANSGGIYGSpypaDSFG 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 490366861 252 GNAMVIDPYGRIVKESCAIEDDMVV-TDIDLTLLPESTGRRWLT 294
Cdd:cd07582  243 GGSMIVDYKGRVLAEAGYGPGSMVAgAEIDIEALRRARARPGMH 286
PLN02798 PLN02798
nitrilase
6-284 1.11e-13

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 70.16  E-value: 1.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   6 TLRVASVQLQhKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCItgywHVPKLPAQQVyALSEKLaDSASLKSIKQKAQ 85
Cdd:PLN02798  10 SVRVAVAQMT-STNDLAANFATCSRLAKEAAAAGAKLLFLPECFS----FIGDKDGESL-AIAEPL-DGPIMQRYRSLAR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  86 QYAMAIGVGLI-ERD-NNNNLYNTWVVCMPDGSLQ-KHRKLHAF-----------EHPVICSGDQYTVFDTPWGiKMGIL 151
Cdd:PLN02798  83 ESGLWLSLGGFqEKGpDDSHLYNTHVLIDDSGEIRsSYRKIHLFdvdvpggpvlkESSFTAPGKTIVAVDSPVG-RLGLT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 152 ICWDNNLVE-NARATALLGADILLAP----HQTGGTHsrsphsmkpipmalWENrqqdpqalqaafqgehgkgwLMRwlp 226
Cdd:PLN02798 162 VCYDLRFPElYQQLRFEHGAQVLLVPsaftKPTGEAH--------------WEV--------------------LLR--- 204
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 227 ARAHDNGMFIIFSNGVGRDEEEVRT-GNAMVIDPYGRIV-KESCAIEDDMVVTDIDLTLL 284
Cdd:PLN02798 205 ARAIETQCYVIAAAQAGKHNEKRESyGHALIIDPWGTVVaRLPDRLSTGIAVADIDLSLL 264
PLN02504 PLN02504
nitrilase
5-158 6.23e-13

nitrilase


Pssm-ID: 178120  Cd Length: 346  Bit Score: 68.63  E-value: 6.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   5 TTLRVASVQLQHKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGYWHVPKLpAQQVYALSEKLADS-----AS--- 76
Cdd:PLN02504  23 STVRATVVQASTVFYDTPATLDKAERLIAEAAAYGSQLVVFPEAFIGGYPRGSTF-GLAIGDRSPKGREDfrkyhASaid 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  77 -----LKSIKQKAQQYAMAIGVGLIERDNNNnLYNTWVVCMPDGS-LQKHRKL--HAFEHPVICSGDQYT--VFDTPWGi 146
Cdd:PLN02504 102 vpgpeVDRLAAMAGKYKVYLVMGVIERDGYT-LYCTVLFFDPQGQyLGKHRKLmpTALERLIWGFGDGSTipVYDTPIG- 179
                        170
                 ....*....|..
gi 490366861 147 KMGILICWDNNL 158
Cdd:PLN02504 180 KIGAVICWENRM 191
ML_beta-AS cd07587
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
10-193 2.85e-11

mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This subgroup 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 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 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: 143611 [Multi-domain]  Cd Length: 363  Bit Score: 63.54  E-value: 2.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  10 ASVQLQHKANDKdynlaKIHQFIEMAASEKVNLLVFPEMcitgyWHVP-------KLPAQQvyaLSEKLADSASLKSIKQ 82
Cdd:cd07587   79 APIAEQREAIHD-----RIKKIIEAAAMAGVNIICFQEA-----WTMPfafctreKLPWCE---FAESAEDGPTTKFCQE 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  83 KAQQYAMAIGVGLIERD--NNNNLYNTWVVCMPDGS-LQKHRKLH-----AFE-----------HPvicsgdqytVFDTP 143
Cdd:cd07587  146 LAKKYNMVIVSPILERDeeHGDTIWNTAVVISNSGNvLGKSRKNHiprvgDFNestyymegntgHP---------VFETQ 216
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 490366861 144 WGiKMGILICWDNNLVENARATALLGADILLAPHQTGGTHSRsphSMKPI 193
Cdd:cd07587  217 FG-KIAVNICYGRHHPLNWLMYGLNGAEIVFNPSATVGALSE---PMWPI 262
aliphatic_amidase cd07565
aliphatic amidases (class 2 nitrilases); Aliphatic amidases catalyze the hydrolysis of ...
9-277 2.48e-09

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: 57.30  E-value: 2.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   9 VASVQLQ----HKANDKDYNLAKIHQFIEMAAS--EKVNLLVFPEMCITGY----WHVPK----LPAQQVYALSE--KLA 72
Cdd:cd07565    3 VAVVQYKvpvlHTKEEVLENAERIADMVEGTKRglPGMDLIVFPEYSTQGLmydkWTMDEtactVPGPETDIFAEacKEA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  73 DSASLKSIKQKaqqyamaigvgliERDNNNNLYNTWVVCMPDGSL-QKHRKLHAFEhPVIC--SGDQYT-VFDTPWGIKM 148
Cdd:cd07565   83 KVWGVFSIMER-------------NPDHGKNPYNTAIIIDDQGEIvLKYRKLHPWV-PIEPwyPGDLGTpVCEGPKGSKI 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 149 GILICWDNNLVENARATALLGADILLaphqtggthsRSPHSMKPIpmalweNRQQDPQALQAAFQgehgkgwlmrwlpar 228
Cdd:cd07565  149 ALIICHDGMYPEIARECAYKGAELII----------RIQGYMYPA------KDQWIITNKANAWC--------------- 197
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 490366861 229 ahdNGMFIIFSNGVGRDEEEVRTGNAMVIDPYGRIVKEsCAIEDDMVVT 277
Cdd:cd07565  198 ---NLMYTASVNLAGFDGVFSYFGESMIVNFDGRTLGE-GGREPDEIVT 242
PLN00202 PLN00202
beta-ureidopropionase
27-193 4.36e-09

beta-ureidopropionase


Pssm-ID: 177792  Cd Length: 405  Bit Score: 57.16  E-value: 4.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  27 KIHQFIEMAASEKVNLLvfpemCITGYWHVPK--LPAQQVYALSEKLADSASLKSIKQKAQQYAMAIGVGLIERDNNNN- 103
Cdd:PLN00202 114 KVKPMIDAAGAAGVNIL-----CLQEAWTMPFafCTREKRWCEFAEPVDGESTKFLQELARKYNMVIVSPILERDVNHGe 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 104 -LYNTWVVCMPDGS-LQKHRKLHA-----F-EHPVICSGDQ-YTVFDTPWGiKMGILICWDNNLVENARATALLGADILL 174
Cdd:PLN00202 189 tLWNTAVVIGNNGNiIGKHRKNHIprvgdFnESTYYMEGNTgHPVFETAFG-KIAVNICYGRHHPLNWLAFGLNGAEIVF 267
                        170
                 ....*....|....*....
gi 490366861 175 APHQTGGTHSrspHSMKPI 193
Cdd:PLN00202 268 NPSATVGDLS---EPMWPI 283
biotinidase_like cd07567
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ...
24-155 1.48e-07

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: 51.86  E-value: 1.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  24 NLAKIHQFIEMAASEKVNLLVFPEMCITGY---WHVPKLPAQQVYALS---------EKLADSASLKSIKQKAQQYAMAI 91
Cdd:cd07567   25 NLDIYEEIIKSAAKQGADIIVFPEDGLTGFiftRFVIYPFLEDVPDPEvnwnpcldpDRFDYTEVLQRLSCAARENSIYV 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  92 GVGLIER---DNNNN--------LYNTWVVCMPDGSL-QKHRKLH-----AFEHPVICsgdQYTVFDTPWGIKMGILICW 154
Cdd:cd07567  105 VANLGEKqpcDSSDPhcppdgryQYNTNVVFDRDGTLiARYRKYNlfgepGFDVPPEP---EIVTFDTDFGVTFGIFTCF 181

                 .
gi 490366861 155 D 155
Cdd:cd07567  182 D 182
nadE PRK02628
NAD synthetase; Reviewed
8-110 3.23e-06

NAD synthetase; Reviewed


Pssm-ID: 235057 [Multi-domain]  Cd Length: 679  Bit Score: 48.71  E-value: 3.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   8 RVASVQLQHKANDKDYNLAKIHQFIEMAASEKVNLLVFPEMCITGYwHVPKLPAQQvyALSEKLADsaSLKSIKQKAQQY 87
Cdd:PRK02628  14 RVAAATPKVRVADPAFNAARILALARRAADDGVALAVFPELSLSGY-SCDDLFLQD--TLLDAVED--ALATLVEASADL 88
                         90       100
                 ....*....|....*....|...
gi 490366861  88 AMAIGVGLIERDnNNNLYNTWVV 110
Cdd:PRK02628  89 DPLLVVGAPLRV-RHRLYNCAVV 110
ScNTA1_like cd07566
Saccharomyces cerevisiae N-terminal amidase NTA1, and related proteins (class 3 nitrilases); ...
8-301 3.40e-05

Saccharomyces cerevisiae N-terminal amidase NTA1, and related proteins (class 3 nitrilases); Saccharomyces cerevisiae NTA1 functions in the N-end rule protein degradation pathway. It specifically deaminates the N-terminal asparagine and glutamine residues of substrates of this pathway, to aspartate and glutamate respectively, these latter are the destabilizing residues. 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 3.


Pssm-ID: 143590  Cd Length: 295  Bit Score: 44.64  E-value: 3.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   8 RVASVQLQHKANDKDYNLAKIHQFIE----MAASEKVNLLVFPEMCITGY-WHVPklpaQQVYALSEKLADSASLKSIKQ 82
Cdd:cd07566    1 RIACLQLNPQIGQVEENLSRAWELLDktkkRAKLKKPDILVLPELALTGYnFHSL----EHIKPYLEPTTSGPSFEWARE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  83 KAQQYAMAIGVGLIERDNNNN--LYNTWVVCMPDGSLQKH-RKLH------------------AFEHPVICSGDQYTVFD 141
Cdd:cd07566   77 VAKKFNCHVVIGYPEKVDESSpkLYNSALVVDPEGEVVFNyRKSFlyytdeewgceenpggfqTFPLPFAKDDDFDGGSV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 142 TPwGIKMGILICWDNN---------LVENARATALLGADILLAPhqTGGTHSRSPHSMKPIPmalwenrqQDPQALQAAF 212
Cdd:cd07566  157 DV-TLKTSIGICMDLNpykfeapftDFEFATHVLDNGTELIICP--MAWLHSLSPTELTVLP--------QEPDTETVSY 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 213 qgehgkgWLMRWLPARAH-DNGMFIIFSNGVGRDEEEVRTGNAMVidpygrivkesCAIEDDMVVTDIdltllpeSTGRR 291
Cdd:cd07566  226 -------WLQRFEPLRAEpLEGTQVVFCNRIGTENDTLYAGSSAV-----------IGIYDGLDSPDG-------SNGNY 280
                        330
                 ....*....|
gi 490366861 292 WLTGRRPELY 301
Cdd:cd07566  281 WKLRFDPFLD 290
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
7-267 6.69e-05

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: 43.74  E-value: 6.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861   7 LRVASVQLQHKANDKDYN------LAKIHQFIEMAASEKVNLLVFPEMCITGYWHVPKLPAQQVyalsekladsaslksi 80
Cdd:cd07571    1 LRVALVQGNIPQDEKWDPeqrqatLDRYLDLTRELADEKPDLVVWPETALPFDLQRDPDALARL---------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  81 kqkaQQYAMAIGVGLI-----ERDNNNNLYNTWVVCMPDGS-LQKHRKLH------------------AFEHPVICS--- 133
Cdd:cd07571   65 ----ARAARAVGAPLLtgaprREPGGGRYYNSALLLDPGGGiLGRYDKHHlvpfgeyvplrdllrflgLLFDLPMGDfsp 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 134 GDQYTVFDTPWGIKMGILICWDN---NLVenaRATALLGADILL------------APHQtggthsrsphsmkpipmalw 198
Cdd:cd07571  141 GTGPQPLLLGGGVRVGPLICYESifpELV---RDAVRQGADLLVnitndawfgdsaGPYQ-------------------- 197
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861 199 enrqqdpQALQAAFQG-EHGkgwlmRWLpARAhdngmfiifSNgvgrdeeevrTGNAMVIDPYGRIVKES 267
Cdd:cd07571  198 -------HLAMARLRAiETG-----RPL-VRA---------AN----------TGISAVIDPDGRIVARL 235
amiF PRK13287
formamidase; Provisional
26-174 3.64e-03

formamidase; Provisional


Pssm-ID: 183950  Cd Length: 333  Bit Score: 38.52  E-value: 3.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  26 AKIHQFIEMAASEK-----VNLLVFPEMCITG----YWHVPKL------PAQQVYALSEKLADSASLKSIkqkaqqyama 90
Cdd:PRK13287  34 KQIEQIIKTVHKTKagypgLDLIVFPEYSTQGlntkKWTTEEFlctvdgPEVDAFAQACKENKVWGVFSI---------- 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366861  91 igvglIERDNNNNL-YNTWVVCMPDGSLQ-KHRKLHAFEhPV--ICSGD-QYTVFDTPWGIKMGILICWDNNLVENARAT 165
Cdd:PRK13287 104 -----MERNPDGNEpYNTAIIIDDQGEIIlKYRKLHPWV-PVepWEPGDlGIPVCDGPGGSKLAVCICHDGMFPEMAREA 177

                 ....*....
gi 490366861 166 ALLGADILL 174
Cdd:PRK13287 178 AYKGANVMI 186
 
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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