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Conserved domains on  [gi|57116738|ref|NP_214994|]
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amidohydrolase [Mycobacterium tuberculosis H37Rv]

Protein Classification

carbon-nitrogen hydrolase family protein( domain architecture ID 10166099)

carbon-nitrogen hydrolase family protein such as Escherichia coli deaminated glutathione amidase, which hydrolyzes deaminated glutathione (dGSH) to 2-oxoglutarate and L-cysteinylglycine and may function as a metabolite repair enzyme

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
3-267 7.75e-114

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: 328.00  E-value: 7.75e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   3 IALAQIRSGTDPAANLQLVGKYAGEAATAGAQLVVFPEATMCRLGVPL---RQVAEPVDGPWANGVRRIATEAGITVIAG 79
Cdd:cd07581   1 VALAQFASSGDKEENLEKVRRLLAEAAAAGADLVVFPEYTMARFGDGLddyARVAEPLDGPFVSALARLARELGITVVAG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  80 MFTPTGDGRVTNTLIAAGPgtPNQPDAHYHKIHLYDAFGFTESRTVAPGRE--PVVVVVDGVRVGLTVCYDIRFPALYTE 157
Cdd:cd07581  81 MFEPAGDGRVYNTLVVVGP--DGEIIAVYRKIHLYDAFGFRESDTVAPGDElpPVVFVVGGVKVGLATCYDLRFPELARA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 158 LARRGAQLIAVCASWGSGPGKLEQWTLLARARALDSMSYVAAAGQADpgdartgvgassaaPTGVGGSLVASPLGEVVVS 237
Cdd:cd07581 159 LALAGADVIVVPAAWVAGPGKEEHWETLLRARALENTVYVAAAGQAG--------------PRGIGRSMVVDPLGVVLAD 224
                       250       260       270
                ....*....|....*....|....*....|
gi 57116738 238 AGTQPQLLVADIDVDNVAAARDRIAVLRNQ 267
Cdd:cd07581 225 LGEREGLLVADIDPERVEEAREALPVLENR 254
 
Name Accession Description Interval E-value
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
3-267 7.75e-114

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: 328.00  E-value: 7.75e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   3 IALAQIRSGTDPAANLQLVGKYAGEAATAGAQLVVFPEATMCRLGVPL---RQVAEPVDGPWANGVRRIATEAGITVIAG 79
Cdd:cd07581   1 VALAQFASSGDKEENLEKVRRLLAEAAAAGADLVVFPEYTMARFGDGLddyARVAEPLDGPFVSALARLARELGITVVAG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  80 MFTPTGDGRVTNTLIAAGPgtPNQPDAHYHKIHLYDAFGFTESRTVAPGRE--PVVVVVDGVRVGLTVCYDIRFPALYTE 157
Cdd:cd07581  81 MFEPAGDGRVYNTLVVVGP--DGEIIAVYRKIHLYDAFGFRESDTVAPGDElpPVVFVVGGVKVGLATCYDLRFPELARA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 158 LARRGAQLIAVCASWGSGPGKLEQWTLLARARALDSMSYVAAAGQADpgdartgvgassaaPTGVGGSLVASPLGEVVVS 237
Cdd:cd07581 159 LALAGADVIVVPAAWVAGPGKEEHWETLLRARALENTVYVAAAGQAG--------------PRGIGRSMVVDPLGVVLAD 224
                       250       260       270
                ....*....|....*....|....*....|
gi 57116738 238 AGTQPQLLVADIDVDNVAAARDRIAVLRNQ 267
Cdd:cd07581 225 LGEREGLLVADIDPERVEEAREALPVLENR 254
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
1-266 1.62e-71

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 220.89  E-value: 1.62e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   1 MRIALAQIR-SGTDPAANLQLVGKYAGEAATAGAQLVVFPEATMCRLGV---PLRQVAEPVDGPWANGVRRIATEAGITV 76
Cdd:COG0388   2 MRIALAQLNpTVGDIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPeddDLLELAEPLDGPALAALAELARELGIAV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  77 IAGMFTPTGDGRVTNTLIAAGP-GtpnQPDAHYHKIHLYDAFGFTESRTVAPGREPVVVVVDGVRVGLTVCYDIRFPALY 155
Cdd:COG0388  82 VVGLPERDEGGRLYNTALVIDPdG---EILGRYRKIHLPNYGVFDEKRYFTPGDELVVFDTDGGRIGVLICYDLWFPELA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 156 TELARRGAQLIAVCASWGSGPGKlEQWTLLARARALDSMSYVAAAGQADPGDARtgvgassaapTGVGGSLVASPLGEVV 235
Cdd:COG0388 159 RALALAGADLLLVPSASPFGRGK-DHWELLLRARAIENGCYVVAANQVGGEDGL----------VFDGGSMIVDPDGEVL 227
                       250       260       270
                ....*....|....*....|....*....|.
gi 57116738 236 VSAGTQPQLLVADIDVDNVAAARDRIAVLRN 266
Cdd:COG0388 228 AEAGDEEGLLVADIDLDRLREARRRFPVLRD 258
de_GSH_amidase NF033621
deaminated glutathione amidase;
2-266 6.90e-56

deaminated glutathione amidase;


Pssm-ID: 468114  Cd Length: 260  Bit Score: 180.48  E-value: 6.90e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738    2 RIALAQIRSGTDPAANLQLVGKYAGEAATAGAQLVVFPEATMCR------LGVplrQVAEPVDGPWANGVRRIATEAGIT 75
Cdd:NF033621   1 KVALGQFAVTPDWQENAQTCVDLMAQAAEAGADLLVLPEAVLARddtdpdLSV---KSAQPLDGPFLTQLLAESRGNDLT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   76 VIAGMFTPTGDGRVTNTLIAAGPGtpnQPDAHYHKIHLYDAFGFTESRTVAPGRE-PVVVVVDGVRVGLTVCYDIRFPAL 154
Cdd:NF033621  78 TVLTVHVPSGDGRAWNTLVALRDG---EIIAQYRKLHLYDAFSMQESRRVDAGNEiPPLVEVAGMKVGLMTCYDLRFPEL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  155 YTELARRGAQLIAVCASWGSGPGKLEQWTLLARARALDSMSYVAAAGQadpgdartgvgassAAPTGVGGSLVASPLGEV 234
Cdd:NF033621 155 ARRLALDGADVLVLPAAWVRGPLKEHHWETLLAARALENTCYMVAVGE--------------CGNRNIGQSMVVDPLGVT 220
                        250       260       270
                 ....*....|....*....|....*....|..
gi 57116738  235 VVSAGTQPQLLVADIDVDNVAAARDRIAVLRN 266
Cdd:NF033621 221 IAAAAEAPALIFAELDPERIAHAREQLPVLEN 252
PLN02798 PLN02798
nitrilase
1-263 2.58e-39

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 138.72  E-value: 2.58e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738    1 MRIALAQIRSGTDPAANLQLVGKYAGEAATAGAQLVVFPEAtMCRLGVPLRQ---VAEPVDGPWANGVRRIATEAGITVI 77
Cdd:PLN02798  11 VRVAVAQMTSTNDLAANFATCSRLAKEAAAAGAKLLFLPEC-FSFIGDKDGEslaIAEPLDGPIMQRYRSLARESGLWLS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   78 AGMFTPTG--DGRVTNT-LIAAGPGTPNqpdAHYHKIHLYD-----AFGFTESRTVAPGREPVVVVVDGVRVGLTVCYDI 149
Cdd:PLN02798  90 LGGFQEKGpdDSHLYNThVLIDDSGEIR---SSYRKIHLFDvdvpgGPVLKESSFTAPGKTIVAVDSPVGRLGLTVCYDL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  150 RFPALYTELA-RRGAQLIAVCASWGSGPGKlEQWTLLARARALDSMSYVAAAGQAdpgdartgvGASSAAPTGVGGSLVA 228
Cdd:PLN02798 167 RFPELYQQLRfEHGAQVLLVPSAFTKPTGE-AHWEVLLRARAIETQCYVIAAAQA---------GKHNEKRESYGHALII 236
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 57116738  229 SPLGEVV--VSAGTQPQLLVADIDVDNVAAARDRIAV 263
Cdd:PLN02798 237 DPWGTVVarLPDRLSTGIAVADIDLSLLDSVRTKMPI 273
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
2-258 1.03e-36

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: 130.94  E-value: 1.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738     2 RIALAQIRSG-TDPAANLQLVGKYAGEAATAGAQLVVFPEA--TMCRLGVPLRQVAEPVDGPWANGVRRIATEAGITVIA 78
Cdd:pfam00795   1 RVALVQLPQGfWDLEANLQKALELIEEAARYGADLIVLPELfiTGYPCWAHFLEAAEVGDGETLAGLAALARKNGIAIVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738    79 GMF-TPTGDGRVTNTLIAAGPGtpNQPDAHYHKIHLYDAF---GFTESRTVAPGREPVVVVVDGVRVGLTVCYDIRFPAL 154
Cdd:pfam00795  81 GLIeRWLTGGRLYNTAVLLDPD--GKLVGKYRKLHLFPEPrppGFRERVLFEPGDGGTVFDTPLGKIGAAICYEIRFPEL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   155 YTELARRGAQLIAVCASWGSGPGKL--EQWTLLARARALDSMSYVAAAGQadpgdartgVGASSAAPTGVGGSLVASPLG 232
Cdd:pfam00795 159 LRALALKGAEILINPSARAPFPGSLgpPQWLLLARARALENGCFVIAANQ---------VGGEEDAPWPYGHSMIIDPDG 229
                         250       260
                  ....*....|....*....|....*..
gi 57116738   233 EVVVSAG-TQPQLLVADIDVDNVAAAR 258
Cdd:pfam00795 230 RILAGAGeWEEGVLIADIDLALVRAWR 256
 
Name Accession Description Interval E-value
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
3-267 7.75e-114

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: 328.00  E-value: 7.75e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   3 IALAQIRSGTDPAANLQLVGKYAGEAATAGAQLVVFPEATMCRLGVPL---RQVAEPVDGPWANGVRRIATEAGITVIAG 79
Cdd:cd07581   1 VALAQFASSGDKEENLEKVRRLLAEAAAAGADLVVFPEYTMARFGDGLddyARVAEPLDGPFVSALARLARELGITVVAG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  80 MFTPTGDGRVTNTLIAAGPgtPNQPDAHYHKIHLYDAFGFTESRTVAPGRE--PVVVVVDGVRVGLTVCYDIRFPALYTE 157
Cdd:cd07581  81 MFEPAGDGRVYNTLVVVGP--DGEIIAVYRKIHLYDAFGFRESDTVAPGDElpPVVFVVGGVKVGLATCYDLRFPELARA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 158 LARRGAQLIAVCASWGSGPGKLEQWTLLARARALDSMSYVAAAGQADpgdartgvgassaaPTGVGGSLVASPLGEVVVS 237
Cdd:cd07581 159 LALAGADVIVVPAAWVAGPGKEEHWETLLRARALENTVYVAAAGQAG--------------PRGIGRSMVVDPLGVVLAD 224
                       250       260       270
                ....*....|....*....|....*....|
gi 57116738 238 AGTQPQLLVADIDVDNVAAARDRIAVLRNQ 267
Cdd:cd07581 225 LGEREGLLVADIDPERVEEAREALPVLENR 254
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
1-266 1.62e-71

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 220.89  E-value: 1.62e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   1 MRIALAQIR-SGTDPAANLQLVGKYAGEAATAGAQLVVFPEATMCRLGV---PLRQVAEPVDGPWANGVRRIATEAGITV 76
Cdd:COG0388   2 MRIALAQLNpTVGDIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPeddDLLELAEPLDGPALAALAELARELGIAV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  77 IAGMFTPTGDGRVTNTLIAAGP-GtpnQPDAHYHKIHLYDAFGFTESRTVAPGREPVVVVVDGVRVGLTVCYDIRFPALY 155
Cdd:COG0388  82 VVGLPERDEGGRLYNTALVIDPdG---EILGRYRKIHLPNYGVFDEKRYFTPGDELVVFDTDGGRIGVLICYDLWFPELA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 156 TELARRGAQLIAVCASWGSGPGKlEQWTLLARARALDSMSYVAAAGQADPGDARtgvgassaapTGVGGSLVASPLGEVV 235
Cdd:COG0388 159 RALALAGADLLLVPSASPFGRGK-DHWELLLRARAIENGCYVVAANQVGGEDGL----------VFDGGSMIVDPDGEVL 227
                       250       260       270
                ....*....|....*....|....*....|.
gi 57116738 236 VSAGTQPQLLVADIDVDNVAAARDRIAVLRN 266
Cdd:COG0388 228 AEAGDEEGLLVADIDLDRLREARRRFPVLRD 258
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
2-266 6.21e-57

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: 183.40  E-value: 6.21e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   2 RIALAQIRSGTDPAANLQLVGKYAGEAATAGAQLVVFPEATMC---RLGVPLRQVAEPVDGPWANGVRRIATEAGITVIA 78
Cdd:cd07572   1 RVALIQMTSTADKEANLARAKELIEEAAAQGAKLVVLPECFNYpggTDAFKLALAEEEGDGPTLQALSELAKEHGIWLVG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  79 GMF--TPTGDGRVTNTLIAAGPgtpnqpD----AHYHKIHLYDAF-----GFTESRTVAPGREPVVVVVDGVRVGLTVCY 147
Cdd:cd07572  81 GSIpeRDDDDGKVYNTSLVFDP------DgelvARYRKIHLFDVDvpggiSYRESDTLTPGDEVVVVDTPFGKIGLGICY 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 148 DIRFPALYTELARRGAQLIAVCASWGSGPGKLeQWTLLARARALDSMSYVAAAGQA-DPGDARtgvgassaapTGVGGSL 226
Cdd:cd07572 155 DLRFPELARALARQGADILTVPAAFTMTTGPA-HWELLLRARAIENQCYVVAAAQAgDHEAGR----------ETYGHSM 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 57116738 227 VASPLGEVVVSAGTQPQLLVADIDVDNVAAARDRIAVLRN 266
Cdd:cd07572 224 IVDPWGEVLAEAGEGEGVVVAEIDLDRLEEVRRQIPVLKH 263
de_GSH_amidase NF033621
deaminated glutathione amidase;
2-266 6.90e-56

deaminated glutathione amidase;


Pssm-ID: 468114  Cd Length: 260  Bit Score: 180.48  E-value: 6.90e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738    2 RIALAQIRSGTDPAANLQLVGKYAGEAATAGAQLVVFPEATMCR------LGVplrQVAEPVDGPWANGVRRIATEAGIT 75
Cdd:NF033621   1 KVALGQFAVTPDWQENAQTCVDLMAQAAEAGADLLVLPEAVLARddtdpdLSV---KSAQPLDGPFLTQLLAESRGNDLT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   76 VIAGMFTPTGDGRVTNTLIAAGPGtpnQPDAHYHKIHLYDAFGFTESRTVAPGRE-PVVVVVDGVRVGLTVCYDIRFPAL 154
Cdd:NF033621  78 TVLTVHVPSGDGRAWNTLVALRDG---EIIAQYRKLHLYDAFSMQESRRVDAGNEiPPLVEVAGMKVGLMTCYDLRFPEL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  155 YTELARRGAQLIAVCASWGSGPGKLEQWTLLARARALDSMSYVAAAGQadpgdartgvgassAAPTGVGGSLVASPLGEV 234
Cdd:NF033621 155 ARRLALDGADVLVLPAAWVRGPLKEHHWETLLAARALENTCYMVAVGE--------------CGNRNIGQSMVVDPLGVT 220
                        250       260       270
                 ....*....|....*....|....*....|..
gi 57116738  235 VVSAGTQPQLLVADIDVDNVAAARDRIAVLRN 266
Cdd:NF033621 221 IAAAAEAPALIFAELDPERIAHAREQLPVLEN 252
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
2-265 2.86e-51

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: 168.49  E-value: 2.86e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   2 RIALAQIRSGT-DPAANLQLVGKYAGEAATAGAQLVVFPEatMCRLGVPLRQ---VAEPVDGPWANGVRRIATEAGITVI 77
Cdd:cd07583   1 KIALIQLDIVWgDPEANIERVESLIEEAAAAGADLIVLPE--MWNTGYFLDDlyeLADEDGGETVSFLSELAKKHGVNIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  78 AGMFTPTGDGRVTNTLIAAGPGtpNQPDAHYHKIHLydaFGFT-ESRTVAPGREPVVVVVDGVRVGLTVCYDIRFPALYT 156
Cdd:cd07583  79 AGSVAEKEGGKLYNTAYVIDPD--GELIATYRKIHL---FGLMgEDKYLTAGDELEVFELDGGKVGLFICYDLRFPELFR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 157 ELARRGAQLIAVCASWgsgPGK-LEQWTLLARARALDSMSYVAAAGqadpgdaRTGVGASSAAPtgvGGSLVASPLGEVV 235
Cdd:cd07583 154 KLALEGAEILFVPAEW---PAArIEHWRTLLRARAIENQAFVVACN-------RVGTDGGNEFG---GHSMVIDPWGEVL 220
                       250       260       270
                ....*....|....*....|....*....|
gi 57116738 236 VSAGTQPQLLVADIDVDNVAAARDRIAVLR 265
Cdd:cd07583 221 AEAGEEEEILTAEIDLEEVAEVRKKIPVFK 250
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
3-265 7.86e-51

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: 167.50  E-value: 7.86e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   3 IALAQIRSG-TDPAANLQLVGKYAGEAATAGAQLVVFPEAT----MCRLGVPLRQVAEPVDGPWANGVRRIATEAGITVI 77
Cdd:cd07197   1 IAAVQLAPKiGDVEANLAKALRLIKEAAEQGADLIVLPELFltgySFESAKEDLDLAEELDGPTLEALAELAKELGIYIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  78 AGMFTPtGDGRVTNTLIAAGPGtpNQPDAHYHKIHLydaFGFTESRTVAPGREPVVVVVDGVRVGLTVCYDIRFPALYTE 157
Cdd:cd07197  81 AGIAEK-DGDKLYNTAVVIDPD--GEIIGKYRKIHL---FDFGERRYFSPGDEFPVFDTPGGKIGLLICYDLRFPELARE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 158 LARRGAQLIAVCASWGSGPgkLEQWTLLARARALDSMSYVAAAGQAdpGDARTGVGAssaaptgvGGSLVASPLGEVVVS 237
Cdd:cd07197 155 LALKGADIILVPAAWPTAR--REHWELLLRARAIENGVYVVAANRV--GEEGGLEFA--------GGSMIVDPDGEVLAE 222
                       250       260
                ....*....|....*....|....*...
gi 57116738 238 AGTQPQLLVADIDVDNVAAARDRIAVLR 265
Cdd:cd07197 223 ASEEEGILVAELDLDELREARKRWSYLR 250
PLN02798 PLN02798
nitrilase
1-263 2.58e-39

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 138.72  E-value: 2.58e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738    1 MRIALAQIRSGTDPAANLQLVGKYAGEAATAGAQLVVFPEAtMCRLGVPLRQ---VAEPVDGPWANGVRRIATEAGITVI 77
Cdd:PLN02798  11 VRVAVAQMTSTNDLAANFATCSRLAKEAAAAGAKLLFLPEC-FSFIGDKDGEslaIAEPLDGPIMQRYRSLARESGLWLS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   78 AGMFTPTG--DGRVTNT-LIAAGPGTPNqpdAHYHKIHLYD-----AFGFTESRTVAPGREPVVVVVDGVRVGLTVCYDI 149
Cdd:PLN02798  90 LGGFQEKGpdDSHLYNThVLIDDSGEIR---SSYRKIHLFDvdvpgGPVLKESSFTAPGKTIVAVDSPVGRLGLTVCYDL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  150 RFPALYTELA-RRGAQLIAVCASWGSGPGKlEQWTLLARARALDSMSYVAAAGQAdpgdartgvGASSAAPTGVGGSLVA 228
Cdd:PLN02798 167 RFPELYQQLRfEHGAQVLLVPSAFTKPTGE-AHWEVLLRARAIETQCYVIAAAQA---------GKHNEKRESYGHALII 236
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 57116738  229 SPLGEVV--VSAGTQPQLLVADIDVDNVAAARDRIAV 263
Cdd:PLN02798 237 DPWGTVVarLPDRLSTGIAVADIDLSLLDSVRTKMPI 273
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
2-260 9.64e-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: 9.64e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   2 RIALAQIRSGT-DPAANLQLVGKYAGEAATAGAQLVVFPEATMC--RLGVPLRQVAEPVDGPWANGVRRIATEAGITVIA 78
Cdd:cd07576   1 RLALYQGPARDgDVAANLARLDEAAARAAAAGADLLVFPELFLTgyNIGDAVARLAEPADGPALQALRAIARRHGIAIVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  79 GmFTPTGDGRVTNTLIAAGPGtpNQPDAHYHKIHLydaFGFTESRTVAPGREPVVVVVDGVRVGLTVCYDIRFPALYTEL 158
Cdd:cd07576  81 G-YPERAGGAVYNAAVLIDED--GTVLANYRKTHL---FGDSERAAFTPGDRFPVVELRGLRVGLLICYDVEFPELVRAL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 159 ARRGAQLIAVcaswgsgPGKLEQW-----TLLARARALDSMSYVAAAGQADPGDARtgvgassaapTGVGGSLVASPLGE 233
Cdd:cd07576 155 ALAGADLVLV-------PTALMEPygfvaRTLVPARAFENQIFVAYANRCGAEDGL----------TYVGLSSIAGPDGT 217
                       250       260
                ....*....|....*....|....*..
gi 57116738 234 VVVSAGTQPQLLVADIDVDNVAAARDR 260
Cdd:cd07576 218 VLARAGRGEALLVADLDPAALAAARRE 244
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
2-258 1.03e-36

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: 130.94  E-value: 1.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738     2 RIALAQIRSG-TDPAANLQLVGKYAGEAATAGAQLVVFPEA--TMCRLGVPLRQVAEPVDGPWANGVRRIATEAGITVIA 78
Cdd:pfam00795   1 RVALVQLPQGfWDLEANLQKALELIEEAARYGADLIVLPELfiTGYPCWAHFLEAAEVGDGETLAGLAALARKNGIAIVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738    79 GMF-TPTGDGRVTNTLIAAGPGtpNQPDAHYHKIHLYDAF---GFTESRTVAPGREPVVVVVDGVRVGLTVCYDIRFPAL 154
Cdd:pfam00795  81 GLIeRWLTGGRLYNTAVLLDPD--GKLVGKYRKLHLFPEPrppGFRERVLFEPGDGGTVFDTPLGKIGAAICYEIRFPEL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   155 YTELARRGAQLIAVCASWGSGPGKL--EQWTLLARARALDSMSYVAAAGQadpgdartgVGASSAAPTGVGGSLVASPLG 232
Cdd:pfam00795 159 LRALALKGAEILINPSARAPFPGSLgpPQWLLLARARALENGCFVIAANQ---------VGGEEDAPWPYGHSMIIDPDG 229
                         250       260
                  ....*....|....*....|....*..
gi 57116738   233 EVVVSAG-TQPQLLVADIDVDNVAAAR 258
Cdd:pfam00795 230 RILAGAGeWEEGVLIADIDLALVRAWR 256
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
2-260 2.18e-31

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: 117.03  E-value: 2.18e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   2 RIALAQI--RSGtDPAANLQLVGKYAGEAATAGAQLVVFPEATMC--RLGVPLRQVAEPVDGPWANGVRRIATEAGITVI 77
Cdd:cd07585   1 RIALVQFeaRVG-DKARNLAVIARWTRKAAAQGAELVCFPEMCITgyTHVRALSREAEVPDGPSTQALSDLARRYGLTIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  78 AGMFTpTGDGRVTNTLIAAgpgTPNQPDAHYHKIHLydafGFTESRTVAPGREPVVVVVDGVRVGLTVCYDIRFPALYTE 157
Cdd:cd07585  80 AGLIE-KAGDRPYNTYLVC---LPDGLVHRYRKLHL----FRREHPYIAAGDEYPVFATPGVRFGILICYDNHFPENVRA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 158 LARRGAQLI-AVCASWGSGPGKLEQWTLL-ARARALDSMSYVAAAGQA--DPGDARTgvgassaaptgvGGSLVASPLGE 233
Cdd:cd07585 152 TALLGAEILfAPHATPGTTSPKGREWWMRwLPARAYDNGVFVAACNGVgrDGGEVFP------------GGAMILDPYGR 219
                       250       260
                ....*....|....*....|....*...
gi 57116738 234 VVV-SAGTQPQLLVADIDVDNVAAARDR 260
Cdd:cd07585 220 VLAeTTSGGDGMVVADLDLDLINTVRGR 247
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
2-266 3.95e-28

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


Pssm-ID: 143608  Cd Length: 258  Bit Score: 108.61  E-value: 3.95e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   2 RIALAQIRSGT-DPAANLQLVGKYAGEAATAGAQLVVFPE-AT----MCRLGVPLRQVAEPVDGPWANGVRRIATEAGIT 75
Cdd:cd07584   1 KVALIQMDSVLgDVKANLKKAAELCKEAAAEGADLICFPElATtgyrPDLLGPKLWELSEPIDGPTVRLFSELAKELGVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  76 VIAGMFTPTGD-GRVTNTLIAAGPGtpNQPDAHYHKIHLYDafgfTESRTVAPGREPVVVVVDGVRVGLTVCYDIRFPAL 154
Cdd:cd07584  81 IVCGFVEKGGVpGKVYNSAVVIDPE--GESLGVYRKIHLWG----LEKQYFREGEQYPVFDTPFGKIGVMICYDMGFPEV 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 155 YTELARRGAQLIAVCASWGSgpGKLEQWTLLARARALDSMSYVAAAGqadpgdaRTGVGASSAAPtgvGGSLVASPLGEV 234
Cdd:cd07584 155 ARILTLKGAEVIFCPSAWRE--QDADIWDINLPARALENTVFVAAVN-------RVGNEGDLVLF---GKSKILNPRGQV 222
                       250       260       270
                ....*....|....*....|....*....|...
gi 57116738 235 VVSAGTQP-QLLVADIDVDNVAAARDRIAVLRN 266
Cdd:cd07584 223 LAEASEEAeEILYAEIDLDAIADYRMTLPYLKD 255
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
1-271 5.01e-21

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: 89.13  E-value: 5.01e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   1 MRIALAQIR-SGTDPAANLQLVGKYAgEAATAGAQLVVFPEA-----TMcrlgvPLRQVAEPVDGPWANGVRRIATEAGi 74
Cdd:cd07575   1 LKIALIQTDlVWEDPEANLAHFEEKI-EQLKEKTDLIVLPEMfttgfSM-----NAEALAEPMNGPTLQWMKAQAKKKG- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  75 TVIAGMFTPTGDGRVTNTLIAAgpgTPNQPDAHYHKIHLydaFGFT-ESRTVAPGREPVVVVVDGVRVGLTVCYDIRFPA 153
Cdd:cd07575  74 AAITGSLIIKEGGKYYNRLYFV---TPDGEVYHYDKRHL---FRMAgEHKVYTAGNERVIVEYKGWKILLQVCYDLRFPV 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 154 lyteLARRGAQ---LIAVcASWgsgPGK-LEQWTLLARARALDSMSYVAAAGqadpgdaRTGVGassaaPTGV---GGSL 226
Cdd:cd07575 148 ----WSRNTNDydlLLYV-ANW---PAPrRAAWDTLLKARAIENQAYVIGVN-------RVGTD-----GNGLeysGDSA 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 57116738 227 VASPLGEVVVSAGTQPQLLVADIDVDNVAAARDRIAVLRNQTDFV 271
Cdd:cd07575 208 VIDPLGEPLAEAEEDEGVLTATLDKEALQEFREKFPFLKDADSFT 252
nitrilase_8 cd07586
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
2-258 2.63e-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: 87.73  E-value: 2.63e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   2 RIALAQIRSG-TDPAANLQLVGKYAGEAATAGAQLVVFPEATMC--RLGVPLRQVAEPVDGPWANGVRRIAteAGITVIA 78
Cdd:cd07586   1 RVAIAQIDPVlGDVEENLEKHLEIIETARERGADLVVFPELSLTgyNLGDLVYEVAMHADDPRLQALAEAS--GGICVVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  79 GMFTPTGDGRVTNTLIAAGPGTPnqpdAHYH-KIHLYDAFGFTESRTVAPGREPVVVVVDGVRVGLTVCYDIRFPALYTE 157
Cdd:cd07586  79 GFVEEGRDGRFYNSAAYLEDGRV----VHVHrKVYLPTYGLFEEGRYFAPGSHLRAFDTRFGRAGVLICEDAWHPSLPYL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 158 LARRGAQLIAVCAS--WGSGPGKL---EQWTLLARARALDSMSYVAAAGqadpgdaRTGVGASSaapTGVGGSLVASPLG 232
Cdd:cd07586 155 LALDGADVIFIPANspARGVGGDFdneENWETLLKFYAMMNGVYVVFAN-------RVGVEDGV---YFWGGSRVVDPDG 224
                       250       260
                ....*....|....*....|....*..
gi 57116738 233 EVVVSAGT-QPQLLVADIDVDNVAAAR 258
Cdd:cd07586 225 EVVAEAPLfEEDLLVAELDRSAIRRAR 251
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
2-261 4.18e-19

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: 84.32  E-value: 4.18e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   2 RIALAQ--IRSGtDPAANLQLVGKYAGEAATAGAQLVVFPEATMCRLGVPLRQ-----VAEPVDGPWANGVRRIATEAGI 74
Cdd:cd07580   1 RVACVQfdPRVG-DLDANLARSIELIREAADAGANLVVLPELANTGYVFESRDeafalAEEVPDGASTRAWAELAAELGL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  75 TVIAGmFTPTGDGRVTNTLIAAGPgtpNQPDAHYHKIHLYDAfgftESRTVAPGREPVVVVVDGVR-VGLTVCYDIRFPA 153
Cdd:cd07580  80 YIVAG-FAERDGDRLYNSAVLVGP---DGVIGTYRKAHLWNE----EKLLFEPGDLGLPVFDTPFGrIGVAICYDGWFPE 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 154 LYTELARRGAQLIAVCASWGSGPGKLE----QWTLLARARALDSMSYVAAAGQAdpGDARtGVGAssaaptgVGGSLVAS 229
Cdd:cd07580 152 TFRLLALQGADIVCVPTNWVPMPRPPEggppMANILAMAAAHSNGLFIACADRV--GTER-GQPF-------IGQSLIVG 221
                       250       260       270
                ....*....|....*....|....*....|....
gi 57116738 230 PLGEVV--VSAGTQPQLLVADIDVDnvAAARDRI 261
Cdd:cd07580 222 PDGWPLagPASGDEEEILLADIDLT--AARRKRI 253
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
1-266 4.92e-19

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: 84.54  E-value: 4.92e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   1 MRIALAQIRSGTDPAANLQLVGKYAGEAATAGAQLVVFPEAT----MC-RLGVPLRQVAEPV-DGPWANGVRRIATEAGI 74
Cdd:cd07573   1 VTVALVQMACSEDPEANLAKAEELVREAAAQGAQIVCLQELFetpyFCqEEDEDYFDLAEPPiPGPTTARFQALAKELGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  75 TVIAGMFTPTGDGRVTNTLIAAGpgtpnqPD----AHYHKIHLYDAFGFTESRTVAPGREP-VVVVVDGVRVGLTVCYDI 149
Cdd:cd07573  81 VIPVSLFEKRGNGLYYNSAVVID------ADgsllGVYRKMHIPDDPGYYEKFYFTPGDTGfKVFDTRYGRIGVLICWDQ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 150 RFPalytELAR----RGAQLIAVCASWGSGPGKLEQ-------WTLLARARALDSMSYVAAAGqadpgdaRTGVGASSAA 218
Cdd:cd07573 155 WFP----EAARlmalQGAEILFYPTAIGSEPQEPPEgldqrdaWQRVQRGHAIANGVPVAAVN-------RVGVEGDPGS 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 57116738 219 P-TGVGGSLVASPLGEVVVSAG-TQPQLLVADIDVDNVAAARDRIAVLRN 266
Cdd:cd07573 224 GiTFYGSSFIADPFGEILAQASrDEEEILVAEFDLDEIEEVRRAWPFFRD 273
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
1-270 2.19e-18

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: 82.63  E-value: 2.19e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   1 MRIALAQ--IRSGTDPAANLQLVGKYAGEAATAGAQLVVFPE-ATMCRLG-------VPLRQVAE--PVDGPWANGVRRI 68
Cdd:cd07574   1 VRVAAAQypLRRYASFEEFAAKVEYWVAEAAGYGADLLVFPEyFTMELLSllpeaidGLDEAIRAlaALTPDYVALFSEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  69 ATEAGITVIAGMFTPTGDGRVTNTliaAGPGTPNQPDAHYHKIHLydaFGFTESR-TVAPGREPVVVVVDGVRVGLTVCY 147
Cdd:cd07574  81 ARKYGINIIAGSMPVREDGRLYNR---AYLFGPDGTIGHQDKLHM---TPFEREEwGISGGDKLKVFDTDLGKIGILICY 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 148 DIRFPALYTELARRGAQLIaVCASWGSGP-GKLEQWtLLARARALDSMSYVAAAGQAdpGDARTgvgaSSAAPTGVGGSL 226
Cdd:cd07574 155 DSEFPELARALAEAGADLL-LVPSCTDTRaGYWRVR-IGAQARALENQCYVVQSGTV--GNAPW----SPAVDVNYGQAA 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 57116738 227 VASPL-------GEVVVSAGTQPQLLVADIDVDNVAAARDRIAVlRNQTDF 270
Cdd:cd07574 227 VYTPCdfgfpedGILAEGEPNTEGWLIADLDLEALRRLREEGSV-RNLRDW 276
GAT_Gln-NAD-synth cd07570
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ...
2-262 2.50e-15

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: 73.66  E-value: 2.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   2 RIALAQIRS--GtDPAANLQLVGKYAGEAATAGAQLVVFPEatMCRLGVP----------LRQVAEpvdgpwanGVRRIA 69
Cdd:cd07570   1 RIALAQLNPtvG-DLEGNAEKILEAIREAKAQGADLVVFPE--LSLTGYPpedlllrpdfLEAAEE--------ALEELA 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  70 TE---AGITVIAGMFTPTgDGRVTNT--LIAAGpgtpnQPDAHYHKIHL--YDAfgFTESRTVAPGREPVVVVVDGVRVG 142
Cdd:cd07570  70 AAtadLDIAVVVGLPLRH-DGKLYNAaaVLQNG-----KILGVVPKQLLpnYGV--FDEKRYFTPGDKPDVLFFKGLRIG 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 143 LTVCYDIRFPALY-TELARRGAQLIAVC-ASwgsgP---GKLEQWTLLARARALDSMSYVAAAGQadpgdartgVGASSA 217
Cdd:cd07570 142 VEICEDLWVPDPPsAELALAGADLILNLsAS----PfhlGKQDYRRELVSSRSARTGLPYVYVNQ---------VGGQDD 208
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 57116738 218 AptgV--GGSLVASPLGEVVVSaGTQPQLLVADIDVDNVAAARDRIA 262
Cdd:cd07570 209 L---VfdGGSFIADNDGELLAE-APRFEEDLADVDLDRLRSERRRNS 251
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
13-260 9.64e-14

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: 69.25  E-value: 9.64e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  13 DPAANLQLVGKYAGEAAtagAQLVVFPEatMCRLGV------PLRQVAEPV-DGPWANGVRRIATEAGITVIAGmFTPTG 85
Cdd:cd07577  13 EVEKNLKKVESLIKGVE---ADLIVLPE--LFNTGYaftskeEVASLAESIpDGPTTRFLQELARETGAYIVAG-LPERD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  86 DGRVTNTLIAAGPGTPNqpdAHYHKIHLYDAfgftESRTVAPG-REPVVVVVDGVRVGLTVCYDIRFPALYTELARRGAQ 164
Cdd:cd07577  87 GDKFYNSAVVVGPEGYI---GIYRKTHLFYE----EKLFFEPGdTGFRVFDIGDIRIGVMICFDWYFPEAARTLALKGAD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 165 LIAVCASWgsgpgKLEQWTLLARARALDSMSYVAAAGqadpgdaRTGVGASSAAP-TGVGGSLVASPLGEVVVSAG-TQP 242
Cdd:cd07577 160 IIAHPANL-----VLPYCPKAMPIRALENRVFTITAN-------RIGTEERGGETlRFIGKSQITSPKGEVLARAPeDGE 227
                       250
                ....*....|....*...
gi 57116738 243 QLLVADIDVDnvaAARDR 260
Cdd:cd07577 228 EVLVAEIDPR---LARDK 242
nitrilase_1_R2 cd07579
Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
2-256 2.86e-13

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: 68.35  E-value: 2.86e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   2 RIALAQIRSGTDPAANLQLVGKYAGEAATAGAQLVVFPEATMCRLGVPLRQvAEPVDGPWANGVRRIATEAGITVIAGMF 81
Cdd:cd07579   1 RIAVAQFAPTPDIAGNLATIDRLAAEAKATGAELVVFPELALTGLDDPASE-AESDTGPAVSALRRLARRLRLYLVAGFA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  82 TPTGDGRVTNTLIAAGPGTPnqpdAHYHKIHLydafGFTESRTVAPGREPVVVVVDGVRVGLTVCYDIRFPALYTELARR 161
Cdd:cd07579  80 EADGDGLYNSAVLVGPEGLV----GTYRKTHL----IEPERSWATPGDTWPVYDLPLGRVGLLIGHDALFPEAGRVLALR 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 162 GAQLIAVCASWGS------GPGKLEQ------------WTlLARARALDSMSYVAAAGQADPgdARTGVGASSAaptgVG 223
Cdd:cd07579 152 GCDLLACPAAIAIpfvgahAGTSVPQpypiptgadpthWH-LARVRAGENNVYFAFANVPDP--ARGYTGWSGV----FG 224
                       250       260       270
                ....*....|....*....|....*....|...
gi 57116738 224 GSLVASPLGEVVVsaGTQPQLLVADIDVDNVAA 256
Cdd:cd07579 225 PDTFAFPRQEAAI--GDEEGIAWALIDTSNLDS 255
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
27-249 9.80e-13

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: 66.47  E-value: 9.80e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  27 EAATAGAQLVVFPEATmcrlgVPLRQVAEPvdgPWANGVRRIATEAGITVIAGMFTPTGDG-RVTNTLIAAGPGTPnqPD 105
Cdd:cd07571  34 ELADEKPDLVVWPETA-----LPFDLQRDP---DALARLARAARAVGAPLLTGAPRREPGGgRYYNSALLLDPGGG--IL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 106 AHYHKIHL-----Y----DAFGFTESRTVA------PGREPVVVVVDGVRVGLT-VCYDIRFPALYTELARRGAQLIAVC 169
Cdd:cd07571 104 GRYDKHHLvpfgeYvplrDLLRFLGLLFDLpmgdfsPGTGPQPLLLGGGVRVGPlICYESIFPELVRDAVRQGADLLVNI 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 170 ---ASWGSGPGKLEQWTlLARARALDsmsyvaaagqadpgdarTGVGASSAAPTGVggSLVASPLGEVVVSAG-TQPQLL 245
Cdd:cd07571 184 tndAWFGDSAGPYQHLA-MARLRAIE-----------------TGRPLVRAANTGI--SAVIDPDGRIVARLPlFEAGVL 243

                ....
gi 57116738 246 VADI 249
Cdd:cd07571 244 VAEV 247
PRK13981 PRK13981
NAD synthetase; Provisional
1-193 1.88e-11

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 64.02  E-value: 1.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738    1 MRIALAQIRS--GtDPAANLQLVGKYAGEAATAGAQLVVFPEATMCrlGVP----------LRQVAEPVDgpwangvrRI 68
Cdd:PRK13981   1 LRIALAQLNPtvG-DIAGNAAKILAAAAEAADAGADLLLFPELFLS--GYPpedlllrpafLAACEAALE--------RL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   69 A--TEAGITVIAGmfTPT-GDGRVTN--TLIAAGpgtpnQPDAHYHKIHL--YDAFgfTESRTVAPGREPVVVVVDGVRV 141
Cdd:PRK13981  70 AaaTAGGPAVLVG--HPWrEGGKLYNaaALLDGG-----EVLATYRKQDLpnYGVF--DEKRYFAPGPEPGVVELKGVRI 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 57116738  142 GLTVCYDIRFPALYTELARRGAQLIAVC-ASwgsgP---GKLEQWTLLARARALDS 193
Cdd:PRK13981 141 GVPICEDIWNPEPAETLAEAGAELLLVPnAS----PyhrGKPDLREAVLRARVRET 192
nitrilase_4 cd07582
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
33-260 1.66e-10

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: 60.43  E-value: 1.66e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  33 AQLVVFPEATMCrlGVPLRQVAE---------PVDGPWANGVRRIATEAGITVIAGMFT-----------------PTGD 86
Cdd:cd07582  43 VRLVVLPEYALQ--GFPMGEPREvwqfdkaaiDIPGPETEALGEKAKELNVYIAANAYErdpdfpglyfntafiidPSGE 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  87 ----GRVTNTLIAAGPGTPNQPDAHYHKIHLY--DAFgFTESRTvAPGRepvvvvvdgvrVGLTVCYDIRFPALYTELAR 160
Cdd:cd07582 121 iilrYRKMNSLAAEGSPSPHDVWDEYIEVYGYglDAL-FPVADT-EIGN-----------LGCLACEEGLYPEVARGLAM 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 161 RGAQLI----AVCASWGSGPgkleqWTLLARARALDSMSYVAAAGQAdpgdarTGVGASSAAPTGVGGSLVASPLGEVVV 236
Cdd:cd07582 188 NGAEVLlrssSEVPSVELDP-----WEIANRARALENLAYVVSANSG------GIYGSPYPADSFGGGSMIVDYKGRVLA 256
                       250       260
                ....*....|....*....|....*.
gi 57116738 237 SA--GTQPQLLVADIDVDNVAAARDR 260
Cdd:cd07582 257 EAgyGPGSMVAGAEIDIEALRRARAR 282
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
27-191 8.81e-10

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


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 58.70  E-value: 8.81e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  27 EAATAGAQLVVFPEAtmcrlGVPLRQVAEPvdgPWANGVRRIATEAGITVIAGMFTPTGD-GRVTNTLIAAGPGTpnQPD 105
Cdd:COG0815 228 ELADDGPDLVVWPET-----ALPFLLDEDP---DALARLAAAAREAGAPLLTGAPRRDGGgGRYYNSALLLDPDG--GIL 297
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 106 AHYHKIHL-----Y----DAFGFTESRTV------APGREPVVVVVDGVRVGLTVCYDIRFPALYTELARRGAQLIAVC- 169
Cdd:COG0815 298 GRYDKHHLvpfgeYvplrDLLRPLIPFLDlplgdfSPGTGPPVLDLGGVRVGPLICYESIFPELVRDAVRAGADLLVNIt 377
                       170       180
                ....*....|....*....|....
gi 57116738 170 --ASWGSGPGKLEQWTlLARARAL 191
Cdd:COG0815 378 ndAWFGDSIGPYQHLA-IARLRAI 400
PLN02747 PLN02747
N-carbamolyputrescine amidase
3-267 1.68e-07

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 51.31  E-value: 1.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738    3 IALAQIRSGTDPAANLQLVGKYAGEAATAGAQLVVFPE----ATMCRLGVP-LRQVAEPVDG-PWANGVRRIATEAGITV 76
Cdd:PLN02747   9 VAALQFACSDDRAANVDKAERLVREAHAKGANIILIQElfegYYFCQAQREdFFQRAKPYEGhPTIARMQKLAKELGVVI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   77 IAGMFTPTGDGRVTNTLIAAGPGTPNqpdAHYHKIHLYDAFGFTESRTVAPGREPVVV-VVDGVRVGLTVCYDIRFPALY 155
Cdd:PLN02747  89 PVSFFEEANNAHYNSIAIIDADGTDL---GLYRKSHIPDGPGYQEKFYFNPGDTGFKVfDTKFAKIGVAICWDQWFPEAA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  156 TELARRGAQLIAVCASWGSGP-----GKLEQWTLLARARALDSMSYVAAAGQADPGDARTGVGASSAapTGVGGSLVASP 230
Cdd:PLN02747 166 RAMVLQGAEVLLYPTAIGSEPqdpglDSRDHWKRVMQGHAGANLVPLVASNRIGTEILETEHGPSKI--TFYGGSFIAGP 243
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 57116738  231 LGEVVVSAGTQPQ-LLVADIDVDNVAAARDRIAVLRNQ 267
Cdd:PLN02747 244 TGEIVAEADDKAEaVLVAEFDLDQIKSKRASWGVFRDR 281
nitrilases_CHs cd07564
Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases ...
1-258 2.53e-07

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: 50.95  E-value: 2.53e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   1 MRIALAQIRSG-TDPAANLQLVGKYAGEAATAGAQLVVFPEATM------CRLGVPLRQVAE---------PVDGPWANG 64
Cdd:cd07564   1 VKVAAVQAAPVfLDLAATVEKACRLIEEAAANGAQLVVFPEAFIpgypywIWFGAPAEGRELfaryyensvEVDGPELER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  65 VRRIATEAGITVIAGM---------------------------FTPT---------GDG---RVTNTliAAGP-GTPN-- 102
Cdd:cd07564  81 LAEAARENGIYVVLGVserdggtlyntqllidpdgellgkhrkLKPThaerlvwgqGDGsglRVVDT--PIGRlGALIcw 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 103 ---QPDAHYhkihlydafgftesrtvapgrepvvvvvdgvrvgltvcydirfpALYtelarrgAQLIAV-CASW-GSGPG 177
Cdd:cd07564 159 enyMPLARY--------------------------------------------ALY-------AQGEQIhVAPWpDFSPY 187
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 178 KL--EQWTLLARARALDSMSYVAAAGQ-----ADPGDARTGVGASSAAPTGVGGSLVASPLGEVVVS-AGTQPQLLVADI 249
Cdd:cd07564 188 YLsrEAWLAASRHYALEGRCFVLSACQvvteeDIPADCEDDEEADPLEVLGGGGSAIVGPDGEVLAGpLPDEEGILYADI 267

                ....*....
gi 57116738 250 DVDNVAAAR 258
Cdd:cd07564 268 DLDDIVEAK 276
ML_beta-AS_like cd07568
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
16-267 8.74e-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: 8.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  16 ANLQLVGKYAGEAATAGAQLVVFPEA----TMC-RLGVPLRQVAEPV-DGPWANGVRRIATEAGITVIAGMFTPTGDGRV 89
Cdd:cd07568  27 AMIQKHVTMIREAAEAGAQIVCLQEIfygpYFCaEQDTKWYEFAEEIpNGPTTKRFAALAKEYNMVLILPIYEKEQGGTL 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  90 TNTliAAGPGTPNQPDAHYHKIHLYDAFGFTESRTVAPGREPVVV-VVDGVRVGLTVCYDIRFPALYTELARRGAQLI-A 167
Cdd:cd07568 107 YNT--AAVIDADGTYLGKYRKNHIPHVGGFWEKFYFRPGNLGYPVfDTAFGKIGVYICYDRHFPEGWRALGLNGAEIVfN 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 168 VCASWGSGPGKLeqWTLLARARALDSMSYVAAAGqadpgdaRTGVGASSAAPTGVGGSLVASPLGEVVVSAGT-QPQLLV 246
Cdd:cd07568 185 PSATVAGLSEYL--WKLEQPAAAVANGYFVGAIN-------RVGTEAPWNIGEFYGSSYFVDPRGQFVASASRdKDELLV 255
                       250       260
                ....*....|....*....|.
gi 57116738 247 ADIDVDNVAAARDRIAVLRNQ 267
Cdd:cd07568 256 AELDLDLIREVRDTWQFYRDR 276
DCase cd07569
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ...
1-261 2.16e-05

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: 44.99  E-value: 2.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   1 MRIALAQI----RSGTDPAANLQLVgKYAGEAATAGAQLVVFPEATMC----RLGVPLRQVAE-----PVDGPWANGVRR 67
Cdd:cd07569   4 VILAAAQMgpiaRAETRESVVARLI-ALLEEAASRGAQLVVFPELALTtffpRWYFPDEAELDsffetEMPNPETQPLFD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  68 IATEAGITVIAGMFTPTGDGRVT---NTLIAAGPGtpNQPDAHYHKIHL--------YDAFGFTESRTVAPG-------R 129
Cdd:cd07569  83 RAKELGIGFYLGYAELTEDGGVKrrfNTSILVDKS--GKIVGKYRKVHLpghkepepYRPFQHLEKRYFEPGdlgfpvfR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 130 EPVVVVVdgvrvgLTVCYDIRFPALYTELARRGAQLIAV---CASWGSGPG-----KLEQWTLLARARALDSMSYVAAAG 201
Cdd:cd07569 161 VPGGIMG------MCICNDRRWPETWRVMGLQGVELVLLgynTPTHNPPAPehdhlRLFHNLLSMQAGAYQNGTWVVAAA 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57116738 202 QA--DPGDARtgvgassaaptgVGGSLVASPLGEVVVSAGT-QPQLLVADIDVDNVAAARDRI 261
Cdd:cd07569 235 KAgmEDGCDL------------IGGSCIVAPTGEIVAQATTlEDEVIVADCDLDLCREGRETV 285
aliphatic_amidase cd07565
aliphatic amidases (class 2 nitrilases); Aliphatic amidases catalyze the hydrolysis of ...
143-258 9.58e-05

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: 43.04  E-value: 9.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738 143 LTVCYDIRFPALYTELARRGAQLIAVCASWgSGPGKlEQWTLLARARALDSMSYVAAAGQAdpgdartgvgASSAAPTGV 222
Cdd:cd07565 150 LIICHDGMYPEIARECAYKGAELIIRIQGY-MYPAK-DQWIITNKANAWCNLMYTASVNLA----------GFDGVFSYF 217
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 57116738 223 GGSLVASPLGEVVVSAGTQPQLLV-ADIDVDNVAAAR 258
Cdd:cd07565 218 GESMIVNFDGRTLGEGGREPDEIVtAELSPSLVRDAR 254
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
145-270 2.42e-04

C-N hydrolase family amidase; Provisional


Pssm-ID: 182461  Cd Length: 256  Bit Score: 41.65  E-value: 2.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  145 VCYDIRFP-----------ALYTelarrgaqliavcASWgSGPGKLEQWTLLArARALDSMSYVAAAGQadpgdartgVG 213
Cdd:PRK10438 140 VCYDLRFPvwsrnrndydlALYV-------------ANW-PAPRSLHWQTLLT-ARAIENQAYVAGCNR---------VG 195
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 57116738  214 ASSAAPTGVGGSLVASPLGEVVVSAGT-QPQLLVADIDVDNVAAARDRIAVLRNQTDF 270
Cdd:PRK10438 196 SDGNGHHYRGDSRIINPQGEIIATAEPhQATRIDAELSLEALQEYREKFPAWRDADEF 253
lnt PRK00302
apolipoprotein N-acyltransferase; Reviewed
27-166 3.58e-04

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 234721 [Multi-domain]  Cd Length: 505  Bit Score: 41.79  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738   27 EAATAGAQLVVFPEATmcrlgVPLrqVAEPVDGPWANGVRRIATEAGITVIAGMF---TPTGDGRVTNTLIAAGPGtpnQ 103
Cdd:PRK00302 252 RPALGPADLIIWPETA-----IPF--LLEDLPQAFLKALDDLAREKGSALITGAPraeNKQGRYDYYNSIYVLGPY---G 321
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  104 PDAHYHKIHL---------YDAFG--------FTESRTVAPGREPVVVVVDGVRVGLtVCYDIRFPALYTELARRGAQLI 166
Cdd:PRK00302 322 ILNRYDKHHLvpfgeyvplESLLRplapffnlPMGDFSRGPYVQPPLLAKGLKLAPL-ICYEIIFPEEVRANVRQGADLL 400
amiE PRK13286
aliphatic amidase;
143-203 7.16e-03

aliphatic amidase;


Pssm-ID: 237335  Cd Length: 345  Bit Score: 37.41  E-value: 7.16e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57116738  143 LTVCYDIRFPALYTELARRGAQLIAVCASWGSgPGKlEQWTLLARARALDSMSYVAAAGQA 203
Cdd:PRK13286 163 LIICDDGNYPEIWRDCAMKGAELIVRCQGYMY-PAK-EQQVLVAKAMAWANNCYVAVANAA 221
PLN02504 PLN02504
nitrilase
145-258 7.65e-03

nitrilase


Pssm-ID: 178120  Cd Length: 346  Bit Score: 37.43  E-value: 7.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116738  145 VCYDIRFPALYTELARRGAQLiaVCASWGSGPgklEQWTLLARARALDSMSYVAAAGQ-------ADPGDARTGVGASSA 217
Cdd:PLN02504 185 ICWENRMPLLRTAMYAKGIEI--YCAPTADSR---ETWQASMRHIALEGGCFVLSANQfcrrkdyPPPPEYLFSGTEEDL 259
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 57116738  218 APTGV---GGSLVASPLGEVVvsAGTQPQ---LLVADIDVDNVAAAR 258
Cdd:PLN02504 260 TPDSIvcaGGSVIISPSGTVL--AGPNYEgegLITADLDLGEIARAK 304
 
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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