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Conserved domains on  [gi|495539913|ref|WP_008264492|]
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amidohydrolase [Stenotrophomonas sp. SKA14]

Protein Classification

nitrilase family protein( domain architecture ID 10166093)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
4-262 7.53e-152

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: 423.49  E-value: 7.53e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   4 LRISLVQGDTRWHDPAANRAYYGALLAPLAGTTDLVILPETFTSGFSNEAIAQAEGMDGPTVAWVREQARALDAAVIGSV 83
Cdd:cd07575    1 LKIALIQTDLVWEDPEANLAHFEEKIEQLKEKTDLIVLPEMFTTGFSMNAEALAEPMNGPTLQWMKAQAKKKGAAITGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  84 QLREGEGVYNRLLFATPDGALQYYDKRHLFRYGGEHERYAAGRERLSVEWKGWRINPQVCYDLRFPVFCRNRynverpgq 163
Cdd:cd07575   81 IIKEGGKYYNRLYFVTPDGEVYHYDKRHLFRMAGEHKVYTAGNERVIVEYKGWKILLQVCYDLRFPVWSRNT-------- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 164 LDFDLQIFVANWPSARAYAWKTLLRARAIENLCFVAAVNRIGVDGNQLHYAGDSAVIDFLGQPQVEIREREQVVTTTISA 243
Cdd:cd07575  153 NDYDLLLYVANWPAPRRAAWDTLLKARAIENQAYVIGVNRVGTDGNGLEYSGDSAVIDPLGEPLAEAEEDEGVLTATLDK 232
                        250
                 ....*....|....*....
gi 495539913 244 EALAAHRARFPAMLDADAF 262
Cdd:cd07575  233 EALQEFREKFPFLKDADSF 251
 
Name Accession Description Interval E-value
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
4-262 7.53e-152

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: 423.49  E-value: 7.53e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   4 LRISLVQGDTRWHDPAANRAYYGALLAPLAGTTDLVILPETFTSGFSNEAIAQAEGMDGPTVAWVREQARALDAAVIGSV 83
Cdd:cd07575    1 LKIALIQTDLVWEDPEANLAHFEEKIEQLKEKTDLIVLPEMFTTGFSMNAEALAEPMNGPTLQWMKAQAKKKGAAITGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  84 QLREGEGVYNRLLFATPDGALQYYDKRHLFRYGGEHERYAAGRERLSVEWKGWRINPQVCYDLRFPVFCRNRynverpgq 163
Cdd:cd07575   81 IIKEGGKYYNRLYFVTPDGEVYHYDKRHLFRMAGEHKVYTAGNERVIVEYKGWKILLQVCYDLRFPVWSRNT-------- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 164 LDFDLQIFVANWPSARAYAWKTLLRARAIENLCFVAAVNRIGVDGNQLHYAGDSAVIDFLGQPQVEIREREQVVTTTISA 243
Cdd:cd07575  153 NDYDLLLYVANWPAPRRAAWDTLLKARAIENQAYVIGVNRVGTDGNGLEYSGDSAVIDPLGEPLAEAEEDEGVLTATLDK 232
                        250
                 ....*....|....*....
gi 495539913 244 EALAAHRARFPAMLDADAF 262
Cdd:cd07575  233 EALQEFREKFPFLKDADSF 251
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
1-264 5.29e-93

C-N hydrolase family amidase; Provisional


Pssm-ID: 182461  Cd Length: 256  Bit Score: 274.70  E-value: 5.29e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   1 MQDLRISLVQGDTRWHDPAANRAYYGALLAPLAGTtDLVILPETFTSGFSNEAIAQAEGMDgPTVAWVREQARALDAAVI 80
Cdd:PRK10438   1 MSGLKITLLQQPLVWMDGPANLRHFDRQLEGITGR-DVIVLPEMFTTGFAMEAAASSLPQD-DVVAWMTAKAQQTNALIA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  81 GSVQLREGEGVYNRLLFATPDGALQYYDKRHLFRYGGEHERYAAGRERLSVEWKGWRINPQVCYDLRFPVFCRNRYnver 160
Cdd:PRK10438  79 GSVALQTESGAVNRFLLVEPGGTVHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNRN---- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 161 pgqlDFDLQIFVANWPSARAYAWKTLLRARAIENLCFVAAVNRIGVDGNQLHYAGDSAVIDflgqPQVEI---REREQV- 236
Cdd:PRK10438 155 ----DYDLALYVANWPAPRSLHWQTLLTARAIENQAYVAGCNRVGSDGNGHHYRGDSRIIN----PQGEIiatAEPHQAt 226
                        250       260
                 ....*....|....*....|....*....
gi 495539913 237 -VTTTISAEALAAHRARFPAMLDADAFHL 264
Cdd:PRK10438 227 rIDAELSLEALQEYREKFPAWRDADEFTL 255
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
4-264 6.05e-66

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 206.25  E-value: 6.05e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   4 LRISLVQGDTRWHDPAANRAYYGALLAPLAGT-TDLVILPETFTSGFSNEAI---AQAEGMDGPTVAWVREQARALDAAV 79
Cdd:COG0388    2 MRIALAQLNPTVGDIEANLAKIEELIREAAAQgADLVVFPELFLTGYPPEDDdllELAEPLDGPALAALAELARELGIAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  80 IGSVQLR-EGEGVYNRLLFATPDGALQ-YYDKRHLFRYGGEHER--YAAGRERLSVEWKGWRINPQVCYDLRFPVFCRNR 155
Cdd:COG0388   82 VVGLPERdEGGRLYNTALVIDPDGEILgRYRKIHLPNYGVFDEKryFTPGDELVVFDTDGGRIGVLICYDLWFPELARAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 156 YnverpgQLDFDLQIFVANWPSARAYA-WKTLLRARAIENLCFVAAVNRIGVDGNqLHYAGDSAVIDFLGQPQVEIRERE 234
Cdd:COG0388  162 A------LAGADLLLVPSASPFGRGKDhWELLLRARAIENGCYVVAANQVGGEDG-LVFDGGSMIVDPDGEVLAEAGDEE 234
                        250       260       270
                 ....*....|....*....|....*....|
gi 495539913 235 QVVTTTISAEALAAHRARFPAMLDADAFHL 264
Cdd:COG0388  235 GLLVADIDLDRLREARRRFPVLRDRRPDLY 264
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
5-251 1.22e-31

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: 117.46  E-value: 1.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913    5 RISLVQGDTRWHDPAANRAYYGALLA-PLAGTTDLVILPETFTSGFSNEA--IAQAEGMDGPTVAWVREQARALDAAVIG 81
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQKALELIEeAARYGADLIVLPELFITGYPCWAhfLEAAEVGDGETLAGLAALARKNGIAIVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   82 SVQLREGEG--VYNRLLFATPDGAL-QYYDKRHLFRYGG-----EHERYAAGRERLSVEWKGWRINPQVCYDLRFPVFCR 153
Cdd:pfam00795  81 GLIERWLTGgrLYNTAVLLDPDGKLvGKYRKLHLFPEPRppgfrERVLFEPGDGGTVFDTPLGKIGAAICYEIRFPELLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  154 nrynveRPGQLDFDLQIFVAN----WPSARAYAWKTLLRARAIENLCFVAAVNRIGVDGNQLHYAGDSAVIDFLGQPQVE 229
Cdd:pfam00795 161 ------ALALKGAEILINPSArapfPGSLGPPQWLLLARARALENGCFVIAANQVGGEEDAPWPYGHSMIIDPDGRILAG 234
                         250       260
                  ....*....|....*....|...
gi 495539913  230 I-REREQVVTTTISAEALAAHRA 251
Cdd:pfam00795 235 AgEWEEGVLIADIDLALVRAWRY 257
de_GSH_amidase NF033621
deaminated glutathione amidase;
57-254 1.58e-14

deaminated glutathione amidase;


Pssm-ID: 468114  Cd Length: 260  Bit Score: 71.47  E-value: 1.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  57 AEGMDGPTVAWVREQARALDAAVIGSVQLREGEG-VYNrLLFATPDGA-LQYYDKRHLfrYGG----EHERYAAGRErLS 130
Cdd:NF033621  56 AQPLDGPFLTQLLAESRGNDLTTVLTVHVPSGDGrAWN-TLVALRDGEiIAQYRKLHL--YDAfsmqESRRVDAGNE-IP 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 131 --VEWKGWRINPQVCYDLRFPVFCRNRynverpgQLD-FDLQIFVANW---PSARAYaWKTLLRARAIENLCFVAAVNRI 204
Cdd:NF033621 132 plVEVAGMKVGLMTCYDLRFPELARRL-------ALDgADVLVLPAAWvrgPLKEHH-WETLLAARALENTCYMVAVGEC 203
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 495539913 205 GVDGnqlhyAGDSAVIDFLGQPQVEIREREQVVTTTISAEALAAHRARFP 254
Cdd:NF033621 204 GNRN-----IGQSMVVDPLGVTIAAAAEAPALIFAELDPERIAHAREQLP 248
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
3-224 5.74e-09

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


Pssm-ID: 273129 [Multi-domain]  Cd Length: 391  Bit Score: 55.83  E-value: 5.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913    3 DLRISLVQGDT----RWHDPAANRAY--YGALLAPLAGTTDLVILPET-FTSGFSNEAIAQAegmdgptvAWVREQARAL 75
Cdd:TIGR00546 159 TLNVALVQPNIpqdlKFDSEGLEAILeiLTSLTKQAVEKPDLVVWPETaFPFDLENSPQKLA--------DRLKLLVLSK 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   76 DAAVIGSVQLREGEGV---YNRLLFATPDGA-LQYYDKRHLFRYG------------------GEHERYAAGRERLSVEW 133
Cdd:TIGR00546 231 GIPILIGAPDAVPGGPyhyYNSAYLVDPGGEvVQRYDKVKLVPFGeyiplgflfkwlsklfflLSQEDFSRGPGPQVLKL 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  134 KGWRINPQVCYDLRFPVFCRNryNVERPGqldfDLQIFVAN--W--PSARAYAWKTLLRARAIEN-LCFVAAVNrigvdg 208
Cdd:TIGR00546 311 PGGKIAPLICYESIFPDLVRA--SARQGA----ELLVNLTNdaWfgDSSGPWQHFALARFRAIENgRPLVRATN------ 378
                         250
                  ....*....|....*.
gi 495539913  209 nqlhyAGDSAVIDFLG 224
Cdd:TIGR00546 379 -----TGISAVIDPRG 389
 
Name Accession Description Interval E-value
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
4-262 7.53e-152

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: 423.49  E-value: 7.53e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   4 LRISLVQGDTRWHDPAANRAYYGALLAPLAGTTDLVILPETFTSGFSNEAIAQAEGMDGPTVAWVREQARALDAAVIGSV 83
Cdd:cd07575    1 LKIALIQTDLVWEDPEANLAHFEEKIEQLKEKTDLIVLPEMFTTGFSMNAEALAEPMNGPTLQWMKAQAKKKGAAITGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  84 QLREGEGVYNRLLFATPDGALQYYDKRHLFRYGGEHERYAAGRERLSVEWKGWRINPQVCYDLRFPVFCRNRynverpgq 163
Cdd:cd07575   81 IIKEGGKYYNRLYFVTPDGEVYHYDKRHLFRMAGEHKVYTAGNERVIVEYKGWKILLQVCYDLRFPVWSRNT-------- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 164 LDFDLQIFVANWPSARAYAWKTLLRARAIENLCFVAAVNRIGVDGNQLHYAGDSAVIDFLGQPQVEIREREQVVTTTISA 243
Cdd:cd07575  153 NDYDLLLYVANWPAPRRAAWDTLLKARAIENQAYVIGVNRVGTDGNGLEYSGDSAVIDPLGEPLAEAEEDEGVLTATLDK 232
                        250
                 ....*....|....*....
gi 495539913 244 EALAAHRARFPAMLDADAF 262
Cdd:cd07575  233 EALQEFREKFPFLKDADSF 251
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
1-264 5.29e-93

C-N hydrolase family amidase; Provisional


Pssm-ID: 182461  Cd Length: 256  Bit Score: 274.70  E-value: 5.29e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   1 MQDLRISLVQGDTRWHDPAANRAYYGALLAPLAGTtDLVILPETFTSGFSNEAIAQAEGMDgPTVAWVREQARALDAAVI 80
Cdd:PRK10438   1 MSGLKITLLQQPLVWMDGPANLRHFDRQLEGITGR-DVIVLPEMFTTGFAMEAAASSLPQD-DVVAWMTAKAQQTNALIA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  81 GSVQLREGEGVYNRLLFATPDGALQYYDKRHLFRYGGEHERYAAGRERLSVEWKGWRINPQVCYDLRFPVFCRNRYnver 160
Cdd:PRK10438  79 GSVALQTESGAVNRFLLVEPGGTVHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNRN---- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 161 pgqlDFDLQIFVANWPSARAYAWKTLLRARAIENLCFVAAVNRIGVDGNQLHYAGDSAVIDflgqPQVEI---REREQV- 236
Cdd:PRK10438 155 ----DYDLALYVANWPAPRSLHWQTLLTARAIENQAYVAGCNRVGSDGNGHHYRGDSRIIN----PQGEIiatAEPHQAt 226
                        250       260
                 ....*....|....*....|....*....
gi 495539913 237 -VTTTISAEALAAHRARFPAMLDADAFHL 264
Cdd:PRK10438 227 rIDAELSLEALQEYREKFPAWRDADEFTL 255
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
5-258 6.92e-76

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: 230.89  E-value: 6.92e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   5 RISLVQGDTRWHDPAANRAYYGALLAPLAG-TTDLVILPETFTSGFSNEAIAQ-AEGMDGPTVAWVREQARALDAAVI-G 81
Cdd:cd07583    1 KIALIQLDIVWGDPEANIERVESLIEEAAAaGADLIVLPEMWNTGYFLDDLYElADEDGGETVSFLSELAKKHGVNIVaG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  82 SVQLREGEGVYNRLLFATPDGALQY-YDKRHLFRYGGEHERYAAGRERLSVEWKGWRINPQVCYDLRFPVFCRnrynveR 160
Cdd:cd07583   81 SVAEKEGGKLYNTAYVIDPDGELIAtYRKIHLFGLMGEDKYLTAGDELEVFELDGGKVGLFICYDLRFPELFR------K 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 161 PGQLDFDLQIFVANWPSARAYAWKTLLRARAIENLCFVAAVNRIGVDGNqLHYAGDSAVIDFLGQPQVEIREREQVVTTT 240
Cdd:cd07583  155 LALEGAEILFVPAEWPAARIEHWRTLLRARAIENQAFVVACNRVGTDGG-NEFGGHSMVIDPWGEVLAEAGEEEEILTAE 233
                        250
                 ....*....|....*...
gi 495539913 241 ISAEALAAHRARFPAMLD 258
Cdd:cd07583  234 IDLEEVAEVRKKIPVFKD 251
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
4-264 6.05e-66

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 206.25  E-value: 6.05e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   4 LRISLVQGDTRWHDPAANRAYYGALLAPLAGT-TDLVILPETFTSGFSNEAI---AQAEGMDGPTVAWVREQARALDAAV 79
Cdd:COG0388    2 MRIALAQLNPTVGDIEANLAKIEELIREAAAQgADLVVFPELFLTGYPPEDDdllELAEPLDGPALAALAELARELGIAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  80 IGSVQLR-EGEGVYNRLLFATPDGALQ-YYDKRHLFRYGGEHER--YAAGRERLSVEWKGWRINPQVCYDLRFPVFCRNR 155
Cdd:COG0388   82 VVGLPERdEGGRLYNTALVIDPDGEILgRYRKIHLPNYGVFDEKryFTPGDELVVFDTDGGRIGVLICYDLWFPELARAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 156 YnverpgQLDFDLQIFVANWPSARAYA-WKTLLRARAIENLCFVAAVNRIGVDGNqLHYAGDSAVIDFLGQPQVEIRERE 234
Cdd:COG0388  162 A------LAGADLLLVPSASPFGRGKDhWELLLRARAIENGCYVVAANQVGGEDG-LVFDGGSMIVDPDGEVLAEAGDEE 234
                        250       260       270
                 ....*....|....*....|....*....|
gi 495539913 235 QVVTTTISAEALAAHRARFPAMLDADAFHL 264
Cdd:COG0388  235 GLLVADIDLDRLREARRRFPVLRDRRPDLY 264
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
6-258 7.41e-64

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: 200.24  E-value: 7.41e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   6 ISLVQGDTRWHDPAANRAYYGALLAPLAGT-TDLVILPETFTSGFSNEAIA----QAEGMDGPTVAWVREQARALDAAVI 80
Cdd:cd07197    1 IAAVQLAPKIGDVEANLAKALRLIKEAAEQgADLIVLPELFLTGYSFESAKedldLAEELDGPTLEALAELAKELGIYIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  81 GSVQLREGEGVYNRLLFATPDG-ALQYYDKRHLFRyGGEHERYAAGRERLSVEWKGWRINPQVCYDLRFPVFCRnRYNVE 159
Cdd:cd07197   81 AGIAEKDGDKLYNTAVVIDPDGeIIGKYRKIHLFD-FGERRYFSPGDEFPVFDTPGGKIGLLICYDLRFPELAR-ELALK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 160 rpgqlDFDLQIFVANWPSARAYAWKTLLRARAIENLCFVAAVNRIGVDGNqLHYAGDSAVIDFLGQPQVEIREREQVVTT 239
Cdd:cd07197  159 -----GADIILVPAAWPTARREHWELLLRARAIENGVYVVAANRVGEEGG-LEFAGGSMIVDPDGEVLAEASEEEGILVA 232
                        250
                 ....*....|....*....
gi 495539913 240 TISAEALAAHRARFPAMLD 258
Cdd:cd07197  233 ELDLDELREARKRWSYLRD 251
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
17-256 1.64e-33

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: 122.30  E-value: 1.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  17 DPAANRAYYGALLAPLAGT-TDLVILPET--FTSGFSNEAIA-QAEGMDGPTVAWVREQARALDAAVIGSVQLREGEG-V 91
Cdd:cd07581   11 DKEENLEKVRRLLAEAAAAgADLVVFPEYtmARFGDGLDDYArVAEPLDGPFVSALARLARELGITVVAGMFEPAGDGrV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  92 YNRLLFATPDGALQ-YYDKRHLFRYGG--EHERYAAGRE--RLSVEWKGWRINPQVCYDLRFP-VFcrnRYNVERPGQLd 165
Cdd:cd07581   91 YNTLVVVGPDGEIIaVYRKIHLYDAFGfrESDTVAPGDElpPVVFVVGGVKVGLATCYDLRFPeLA---RALALAGADV- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 166 fdlqIFV-ANWPS--ARAYAWKTLLRARAIENLCFVAAVNRIGVdgnqlHYAGDSAVIDFLGQPQVEIREREQVVTTTIS 242
Cdd:cd07581  167 ----IVVpAAWVAgpGKEEHWETLLRARALENTVYVAAAGQAGP-----RGIGRSMVVDPLGVVLADLGEREGLLVADID 237
                        250
                 ....*....|....
gi 495539913 243 AEALAAHRARFPAM 256
Cdd:cd07581  238 PERVEEAREALPVL 251
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
5-256 2.58e-33

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: 121.77  E-value: 2.58e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   5 RISLVQGDTRwHDPAANRAYYGALLAPLAGT-TDLVILPETFTSGFSNEA--IAQAEGM-DGPTVAWVREQARALDAA-V 79
Cdd:cd07572    1 RVALIQMTST-ADKEANLARAKELIEEAAAQgAKLVVLPECFNYPGGTDAfkLALAEEEgDGPTLQALSELAKEHGIWlV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  80 IGSVQLREGEG--VYNRLLFATPDGAL-QYYDKRHLFRY---GG----EHERYAAGRERLSVEWKGWRINPQVCYDLRFP 149
Cdd:cd07572   80 GGSIPERDDDDgkVYNTSLVFDPDGELvARYRKIHLFDVdvpGGisyrESDTLTPGDEVVVVDTPFGKIGLGICYDLRFP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 150 VFCRnRYnverpGQLDFDLqIFVanwPSA------RAYaWKTLLRARAIENLCFVAAVNRIGVDGNQLHYAGDSAVIDFL 223
Cdd:cd07572  160 ELAR-AL-----ARQGADI-LTV---PAAftmttgPAH-WELLLRARAIENQCYVVAAAQAGDHEAGRETYGHSMIVDPW 228
                        250       260       270
                 ....*....|....*....|....*....|...
gi 495539913 224 GQPQVEIREREQVVTTTISAEALAAHRARFPAM 256
Cdd:cd07572  229 GEVLAEAGEGEGVVVAEIDLDRLEEVRRQIPVL 261
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
5-268 3.31e-33

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: 121.53  E-value: 3.31e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   5 RISLVQGDTRWHDPAAN-RAYYGALLAPLAGTTDLVILPETFTSGF--SNEAIAQAEGMDGPTVAWVREQARALDAAVIG 81
Cdd:cd07576    1 RLALYQGPARDGDVAANlARLDEAAARAAAAGADLLVFPELFLTGYniGDAVARLAEPADGPALQALRAIARRHGIAIVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  82 SVQLREGEGVYNRLLFATPDGA-LQYYDKRHLFrygGEHER--YAAGRERLSVEWKGWRINPQVCYDLRFPVFCRnrynv 158
Cdd:cd07576   81 GYPERAGGAVYNAAVLIDEDGTvLANYRKTHLF---GDSERaaFTPGDRFPVVELRGLRVGLLICYDVEFPELVR----- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 159 eRPGQLDFDLqIFVanwPSARAYAW----KTLLRARAIENLCFVAAVNRIGVDGnQLHYAGDSAVIDFLGQPQVEIRERE 234
Cdd:cd07576  153 -ALALAGADL-VLV---PTALMEPYgfvaRTLVPARAFENQIFVAYANRCGAED-GLTYVGLSSIAGPDGTVLARAGRGE 226
                        250       260       270
                 ....*....|....*....|....*....|....
gi 495539913 235 QVVTTTISAEALAAHRARFPamldadafHLDERA 268
Cdd:cd07576  227 ALLVADLDPAALAAARRENP--------YLADRR 252
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
5-251 1.22e-31

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: 117.46  E-value: 1.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913    5 RISLVQGDTRWHDPAANRAYYGALLA-PLAGTTDLVILPETFTSGFSNEA--IAQAEGMDGPTVAWVREQARALDAAVIG 81
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQKALELIEeAARYGADLIVLPELFITGYPCWAhfLEAAEVGDGETLAGLAALARKNGIAIVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   82 SVQLREGEG--VYNRLLFATPDGAL-QYYDKRHLFRYGG-----EHERYAAGRERLSVEWKGWRINPQVCYDLRFPVFCR 153
Cdd:pfam00795  81 GLIERWLTGgrLYNTAVLLDPDGKLvGKYRKLHLFPEPRppgfrERVLFEPGDGGTVFDTPLGKIGAAICYEIRFPELLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  154 nrynveRPGQLDFDLQIFVAN----WPSARAYAWKTLLRARAIENLCFVAAVNRIGVDGNQLHYAGDSAVIDFLGQPQVE 229
Cdd:pfam00795 161 ------ALALKGAEILINPSArapfPGSLGPPQWLLLARARALENGCFVIAANQVGGEEDAPWPYGHSMIIDPDGRILAG 234
                         250       260
                  ....*....|....*....|...
gi 495539913  230 I-REREQVVTTTISAEALAAHRA 251
Cdd:pfam00795 235 AgEWEEGVLIADIDLALVRAWRY 257
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
5-241 1.99e-24

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: 98.14  E-value: 1.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   5 RISLVQGDTRWHDPAANRAYYGALLAPLAgtTDLVILPETFTSG--FSN--EAIAQAEGM-DGPTVAWVREQARALDAAV 79
Cdd:cd07577    1 KVGYVQFNPKFGEVEKNLKKVESLIKGVE--ADLIVLPELFNTGyaFTSkeEVASLAESIpDGPTTRFLQELARETGAYI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  80 IGSVQLREGEGVYNRLLFATPDGALQYYDKRHLFryggEHER--YAAGRERLSV-EWKGWRINPQVCYDLRFPVFCRNRy 156
Cdd:cd07577   79 VAGLPERDGDKFYNSAVVVGPEGYIGIYRKTHLF----YEEKlfFEPGDTGFRVfDIGDIRIGVMICFDWYFPEAARTL- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 157 nverpGQLDFDLQIFVANW--PsarayAWKTLLRARAIENLCFVAAVNRIGVDGNQ---LHYAGDSAVIDflgqPQVEI- 230
Cdd:cd07577  154 -----ALKGADIIAHPANLvlP-----YCPKAMPIRALENRVFTITANRIGTEERGgetLRFIGKSQITS----PKGEVl 219
                        250
                 ....*....|....*
gi 495539913 231 ----REREQVVTTTI 241
Cdd:cd07577  220 arapEDGEEVLVAEI 234
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
5-258 4.17e-24

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: 97.44  E-value: 4.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   5 RISLVQGDTRWHDPAANRAYyGALLAPLAGT--TDLVILPETFTSGF-----SNEAIAQAEGMDGPTVAWVREQARALDA 77
Cdd:cd07584    1 KVALIQMDSVLGDVKANLKK-AAELCKEAAAegADLICFPELATTGYrpdllGPKLWELSEPIDGPTVRLFSELAKELGV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  78 AVIGSVQLREGEG--VYNRLLFATPDGALQ-YYDKRHLFrygGEHERYAAGRERLSV-EWKGWRINPQVCYDLRFPvfcr 153
Cdd:cd07584   80 YIVCGFVEKGGVPgkVYNSAVVIDPEGESLgVYRKIHLW---GLEKQYFREGEQYPVfDTPFGKIGVMICYDMGFP---- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 154 nryNVERPGQLDFDLQIFV-ANWPSARAYAWKTLLRARAIENLCFVAAVNRIGVDGNqLHYAGDSAVIDFLGQPQVEI-R 231
Cdd:cd07584  153 ---EVARILTLKGAEVIFCpSAWREQDADIWDINLPARALENTVFVAAVNRVGNEGD-LVLFGKSKILNPRGQVLAEAsE 228
                        250       260
                 ....*....|....*....|....*..
gi 495539913 232 EREQVVTTTISAEALAAHRARFPAMLD 258
Cdd:cd07584  229 EAEEILYAEIDLDAIADYRMTLPYLKD 255
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
5-252 2.16e-23

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: 95.46  E-value: 2.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   5 RISLVQGDTRWHDPAANRAYYGALL--APLAGTtDLVILPETFTSGFSNEAI--AQAEGMDGPTVAWVREQARALDAAVI 80
Cdd:cd07585    1 RIALVQFEARVGDKARNLAVIARWTrkAAAQGA-ELVCFPEMCITGYTHVRAlsREAEVPDGPSTQALSDLARRYGLTIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  81 GSVQLREGEGVYNRLLFATPDGALQYYDKRHLFRYggEHERYAAGRERLSVEWKGWRINPQVCYDLRFPvfcrnrYNVER 160
Cdd:cd07585   80 AGLIEKAGDRPYNTYLVCLPDGLVHRYRKLHLFRR--EHPYIAAGDEYPVFATPGVRFGILICYDNHFP------ENVRA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 161 PGQLDFDLQIF-----VANWPSARAYaWKTLLRARAIENLCFVAAVNRIGVDGNQLhYAGDSAVIDFLGQPQVEIRE-RE 234
Cdd:cd07585  152 TALLGAEILFAphatpGTTSPKGREW-WMRWLPARAYDNGVFVAACNGVGRDGGEV-FPGGAMILDPYGRVLAETTSgGD 229
                        250
                 ....*....|....*...
gi 495539913 235 QVVTTTISAEALAAHRAR 252
Cdd:cd07585  230 GMVVADLDLDLINTVRGR 247
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
5-242 3.20e-20

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


Pssm-ID: 143604  Cd Length: 268  Bit Score: 87.02  E-value: 3.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   5 RISLVQGDTRWHDPAANRAY-YGALLAPLAGTTDLVILPETFTSGFSNEAIAQAEGM-----DGPTVAWVREQARALDAA 78
Cdd:cd07580    1 RVACVQFDPRVGDLDANLARsIELIREAADAGANLVVLPELANTGYVFESRDEAFALaeevpDGASTRAWAELAAELGLY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  79 VIGSVQLREGEGVYNRLLFATPDGALQYYDKRHLfrYGGEHERYAAGRERLSV-EWKGWRINPQVCYDLRFPVFCRnryn 157
Cdd:cd07580   81 IVAGFAERDGDRLYNSAVLVGPDGVIGTYRKAHL--WNEEKLLFEPGDLGLPVfDTPFGRIGVAICYDGWFPETFR---- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 158 veRPGQLDFDLQIFVANW---PSARAYAW---KTLLRARAIENLCFVAAVNRIGVDGNQlHYAGDSAVIDFLGQP--QVE 229
Cdd:cd07580  155 --LLALQGADIVCVPTNWvpmPRPPEGGPpmaNILAMAAAHSNGLFIACADRVGTERGQ-PFIGQSLIVGPDGWPlaGPA 231
                        250
                 ....*....|...
gi 495539913 230 IREREQVVTTTIS 242
Cdd:cd07580  232 SGDEEEILLADID 244
PLN02798 PLN02798
nitrilase
38-221 1.99e-16

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 77.09  E-value: 1.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  38 LVILPETFtsGF----SNEAIAQAEGMDGPTVAWVREQARALDAAV-IGSVQLREGEG--VYNRLLFATPDGALQ-YYDK 109
Cdd:PLN02798  45 LLFLPECF--SFigdkDGESLAIAEPLDGPIMQRYRSLARESGLWLsLGGFQEKGPDDshLYNTHVLIDDSGEIRsSYRK 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 110 RHLFRY---GG----EHERYAAGRERLSVEWKGWRINPQVCYDLRFPvfcrnrynvERPGQLDFDLQIFVANWPSAR--- 179
Cdd:PLN02798 123 IHLFDVdvpGGpvlkESSFTAPGKTIVAVDSPVGRLGLTVCYDLRFP---------ELYQQLRFEHGAQVLLVPSAFtkp 193
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 495539913 180 --AYAWKTLLRARAIENLCFVAAVNRIGVDGNQLHYAGDSAVID 221
Cdd:PLN02798 194 tgEAHWEVLLRARAIETQCYVIAAAQAGKHNEKRESYGHALIID 237
de_GSH_amidase NF033621
deaminated glutathione amidase;
57-254 1.58e-14

deaminated glutathione amidase;


Pssm-ID: 468114  Cd Length: 260  Bit Score: 71.47  E-value: 1.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  57 AEGMDGPTVAWVREQARALDAAVIGSVQLREGEG-VYNrLLFATPDGA-LQYYDKRHLfrYGG----EHERYAAGRErLS 130
Cdd:NF033621  56 AQPLDGPFLTQLLAESRGNDLTTVLTVHVPSGDGrAWN-TLVALRDGEiIAQYRKLHL--YDAfsmqESRRVDAGNE-IP 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 131 --VEWKGWRINPQVCYDLRFPVFCRNRynverpgQLD-FDLQIFVANW---PSARAYaWKTLLRARAIENLCFVAAVNRI 204
Cdd:NF033621 132 plVEVAGMKVGLMTCYDLRFPELARRL-------ALDgADVLVLPAAWvrgPLKEHH-WETLLAARALENTCYMVAVGEC 203
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 495539913 205 GVDGnqlhyAGDSAVIDFLGQPQVEIREREQVVTTTISAEALAAHRARFP 254
Cdd:NF033621 204 GNRN-----IGQSMVVDPLGVTIAAAAEAPALIFAELDPERIAHAREQLP 248
nitrilase_8 cd07586
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
37-260 7.27e-13

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: 66.54  E-value: 7.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  37 DLVILPETFTSGFSNEAIAQAEGM--DGPTVAWVREQARALDAaVIGSVQLREGEGVYNRLLFATpDGALQ-YYDKRHLF 113
Cdd:cd07586   34 DLVVFPELSLTGYNLGDLVYEVAMhaDDPRLQALAEASGGICV-VFGFVEEGRDGRFYNSAAYLE-DGRVVhVHRKVYLP 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 114 RYGGEHER--YAAGRERLSVEWKGWRINPQVCYDLRFP-------------VFCRNRyNVERPGQLDFDLQIfvanwpsa 178
Cdd:cd07586  112 TYGLFEEGryFAPGSHLRAFDTRFGRAGVLICEDAWHPslpyllaldgadvIFIPAN-SPARGVGGDFDNEE-------- 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 179 rayAWKTLLRARAIENLCFVAAVNRIGVDGNqLHYAGDSAVIDFLGQPQVEIREREQ-VVTTTISAEALAahRARF--PA 255
Cdd:cd07586  183 ---NWETLLKFYAMMNGVYVVFANRVGVEDG-VYFWGGSRVVDPDGEVVAEAPLFEEdLLVAELDRSAIR--RARFfsPT 256

                 ....*
gi 495539913 256 MLDAD 260
Cdd:cd07586  257 FRDED 261
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
4-251 8.50e-13

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: 66.46  E-value: 8.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   4 LRISLVQGDTR----WHDPAANRAYYGALLAplAGTTDLVILPETFT---SGFSNEAIAQAEG--MDGPTVA--WV---R 69
Cdd:cd07574    1 VRVAAAQYPLRryasFEEFAAKVEYWVAEAA--GYGADLLVFPEYFTmelLSLLPEAIDGLDEaiRALAALTpdYValfS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  70 EQARALDAAVI-GSVQLREGEGVYNRLLFATPDGALQYYDKRHLFRYGGEHERYAAGrERLSV-EWKGWRINPQVCYDLR 147
Cdd:cd07574   79 ELARKYGINIIaGSMPVREDGRLYNRAYLFGPDGTIGHQDKLHMTPFEREEWGISGG-DKLKVfDTDLGKIGILICYDSE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 148 FPVFcrNRYNVERPGQLdfdlqIFVANWPSARAYAWKTLL--RARAIENLCFVAAVNRIG----VDGNQLHYAGdSAVI- 220
Cdd:cd07574  158 FPEL--ARALAEAGADL-----LLVPSCTDTRAGYWRVRIgaQARALENQCYVVQSGTVGnapwSPAVDVNYGQ-AAVYt 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 495539913 221 --DF---------LGQPQVeirerEQVVTTTISAEALAAHRA 251
Cdd:cd07574  230 pcDFgfpedgilaEGEPNT-----EGWLIADLDLEALRRLRE 266
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
2-149 1.95e-11

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


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 63.71  E-value: 1.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   2 QDLRISLVQG----DTRW---HDPAANRAYYGALLAPLAGTTDLVILPETftsgfsneAIAQAEGMDGPTVAWVREQARA 74
Cdd:COG0815  193 EPLRVALVQGnipqDLKWdpeQRREILDRYLDLTRELADDGPDLVVWPET--------ALPFLLDEDPDALARLAAAARE 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  75 LDAAVI-GSVQLREGEG-VYNRLLFATPDG-ALQYYDKRHL--FrygGEH------------------ERYAAGRERLSV 131
Cdd:COG0815  265 AGAPLLtGAPRRDGGGGrYYNSALLLDPDGgILGRYDKHHLvpF---GEYvplrdllrplipfldlplGDFSPGTGPPVL 341
                        170
                 ....*....|....*...
gi 495539913 132 EWKGWRINPQVCYDLRFP 149
Cdd:COG0815  342 DLGGVRVGPLICYESIFP 359
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
4-149 1.96e-10

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


Pssm-ID: 143595  Cd Length: 270  Bit Score: 59.53  E-value: 1.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   4 LRISLVQG----DTRWhDPAANRA----YYGALLAPLAGTTDLVILPETftsgfsneAIAQAEGMDGPTVAWVREQARAL 75
Cdd:cd07571    1 LRVALVQGnipqDEKW-DPEQRQAtldrYLDLTRELADEKPDLVVWPET--------ALPFDLQRDPDALARLARAARAV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  76 DAAVIGSVQLREGEG--VYNRLLFATPDGA-LQYYDKRHL------------FRYGGEHER-----YAAGRERLSVEWKG 135
Cdd:cd07571   72 GAPLLTGAPRREPGGgrYYNSALLLDPGGGiLGRYDKHHLvpfgeyvplrdlLRFLGLLFDlpmgdFSPGTGPQPLLLGG 151
                        170
                 ....*....|....*
gi 495539913 136 -WRINPQVCYDLRFP 149
Cdd:cd07571  152 gVRVGPLICYESIFP 166
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
4-254 5.48e-09

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: 55.65  E-value: 5.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   4 LRISLVQgdTRWH-DPAANRAYYGALLAPLAGT-TDLVILPETFTSGF----SNEAIAQ-AEGM-DGPTVAWVREQARAL 75
Cdd:cd07573    1 VTVALVQ--MACSeDPEANLAKAEELVREAAAQgAQIVCLQELFETPYfcqeEDEDYFDlAEPPiPGPTTARFQALAKEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  76 DAAVIGSVQLREGEGVY-NRLLFATPDGA-LQYYDKRHLFRYGGEHERY--AAGRERLSV-EWKGWRINPQVCYDLRFPV 150
Cdd:cd07573   79 GVVIPVSLFEKRGNGLYyNSAVVIDADGSlLGVYRKMHIPDDPGYYEKFyfTPGDTGFKVfDTRYGRIGVLICWDQWFPE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 151 FCRNrynverpgqldFDLQ----IFvanWPSA-------------RAYAWKTLLRARAIENLCFVAAVNRIG---VDGNQ 210
Cdd:cd07573  159 AARL-----------MALQgaeiLF---YPTAigsepqeppegldQRDAWQRVQRGHAIANGVPVAAVNRVGvegDPGSG 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 495539913 211 LHYAGDSAVIDFLGQPQVEI-REREQVVTTTISAEALAAHRARFP 254
Cdd:cd07573  225 ITFYGSSFIADPFGEILAQAsRDEEEILVAEFDLDEIEEVRRAWP 269
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
3-224 5.74e-09

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


Pssm-ID: 273129 [Multi-domain]  Cd Length: 391  Bit Score: 55.83  E-value: 5.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913    3 DLRISLVQGDT----RWHDPAANRAY--YGALLAPLAGTTDLVILPET-FTSGFSNEAIAQAegmdgptvAWVREQARAL 75
Cdd:TIGR00546 159 TLNVALVQPNIpqdlKFDSEGLEAILeiLTSLTKQAVEKPDLVVWPETaFPFDLENSPQKLA--------DRLKLLVLSK 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   76 DAAVIGSVQLREGEGV---YNRLLFATPDGA-LQYYDKRHLFRYG------------------GEHERYAAGRERLSVEW 133
Cdd:TIGR00546 231 GIPILIGAPDAVPGGPyhyYNSAYLVDPGGEvVQRYDKVKLVPFGeyiplgflfkwlsklfflLSQEDFSRGPGPQVLKL 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  134 KGWRINPQVCYDLRFPVFCRNryNVERPGqldfDLQIFVAN--W--PSARAYAWKTLLRARAIEN-LCFVAAVNrigvdg 208
Cdd:TIGR00546 311 PGGKIAPLICYESIFPDLVRA--SARQGA----ELLVNLTNdaWfgDSSGPWQHFALARFRAIENgRPLVRATN------ 378
                         250
                  ....*....|....*.
gi 495539913  209 nqlhyAGDSAVIDFLG 224
Cdd:TIGR00546 379 -----TGISAVIDPRG 389
lnt PRK00302
apolipoprotein N-acyltransferase; Reviewed
4-164 1.67e-08

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 234721 [Multi-domain]  Cd Length: 505  Bit Score: 54.89  E-value: 1.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   4 LRISLVQG----DTRWhDPA---ANRAYYGALLAPLAGTTDLVILPETftsgfsneAI-AQAEGMDGPTVAWVREQARAL 75
Cdd:PRK00302 220 LKVALVQGnipqSLKW-DPAgleATLQKYLDLSRPALGPADLIIWPET--------AIpFLLEDLPQAFLKALDDLAREK 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  76 DAAVI-GSV---QLREGEGVYNRLLFATPDGALQYYDKRHL--FrygGE-----------HER-------YAAGRERLSV 131
Cdd:PRK00302 291 GSALItGAPraeNKQGRYDYYNSIYVLGPYGILNRYDKHHLvpF---GEyvplesllrplAPFfnlpmgdFSRGPYVQPP 367
                        170       180       190
                 ....*....|....*....|....*....|....
gi 495539913 132 -EWKGWRINPQVCYDLRFPVFCRNryNVERPGQL 164
Cdd:PRK00302 368 lLAKGLKLAPLICYEIIFPEEVRA--NVRQGADL 399
aliphatic_amidase cd07565
aliphatic amidases (class 2 nitrilases); Aliphatic amidases catalyze the hydrolysis of ...
37-239 4.10e-08

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: 53.06  E-value: 4.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  37 DLVILPETFTSGFSN---EAIAQAEGMDGPTVAWVREQARalDAAVIG--SVQLR--EGEGV-YNRLLFATPDGAL-QYY 107
Cdd:cd07565   41 DLIVFPEYSTQGLMYdkwTMDETACTVPGPETDIFAEACK--EAKVWGvfSIMERnpDHGKNpYNTAIIIDDQGEIvLKY 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 108 DKRHLFRyggEHERYAAGRERLSVEW--KGWRINPQVCYDLRFPVFCRN-RYNverpGQldfDLQIFVANWPSARAYAWK 184
Cdd:cd07565  119 RKLHPWV---PIEPWYPGDLGTPVCEgpKGSKIALIICHDGMYPEIAREcAYK----GA---ELIIRIQGYMYPAKDQWI 188
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495539913 185 TLLRARAIENLCFVAAVNRIGVDGNqLHYAGDSAVIDFLGQPQVEIREREQVVTT 239
Cdd:cd07565  189 ITNKANAWCNLMYTASVNLAGFDGV-FSYFGESMIVNFDGRTLGEGGREPDEIVT 242
PRK13981 PRK13981
NAD synthetase; Provisional
4-261 8.73e-08

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 52.47  E-value: 8.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   4 LRISLVQGDTRWHDPAAN--RAYYGALLAPLAGTtDLVILPETFTSGFSNEA-------IAQAEgmdgptvAWVREQARA 74
Cdd:PRK13981   1 LRIALAQLNPTVGDIAGNaaKILAAAAEAADAGA-DLLLFPELFLSGYPPEDlllrpafLAACE-------AALERLAAA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  75 LD---AAVIGSVQLREGEgVYNRLLFATpDGA-LQYYDKRHLFRYG--GEHERYAAGRERLSVEWKGWRINPQVCYDLRF 148
Cdd:PRK13981  73 TAggpAVLVGHPWREGGK-LYNAAALLD-GGEvLATYRKQDLPNYGvfDEKRYFAPGPEPGVVELKGVRIGVPICEDIWN 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 149 PVFCrnRYNVERPGQLdfdlqIFVanwPSARAYAW------KTLLRARAIENLCFVAAVNRIGvdGN-QLHYAGDSAVID 221
Cdd:PRK13981 151 PEPA--ETLAEAGAEL-----LLV---PNASPYHRgkpdlrEAVLRARVRETGLPLVYLNQVG--GQdELVFDGASFVLN 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 495539913 222 FLGQ-----PQVEirEREQVVTTTISAEALAAHRARFPAMLDADA 261
Cdd:PRK13981 219 ADGElaarlPAFE--EQIAVVDFDRGEDGWRPLPGPIAPPPEGEA 261
nitrilase_1_R2 cd07579
Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
17-121 4.87e-07

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: 49.86  E-value: 4.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  17 DPAANRAYYGALLAPL-AGTTDLVILPETFTSGFSNEAiAQAEGMDGPTVAWVREQARALDAAVIGSVQLREGEGVYNRL 95
Cdd:cd07579   12 DIAGNLATIDRLAAEAkATGAELVVFPELALTGLDDPA-SEAESDTGPAVSALRRLARRLRLYLVAGFAEADGDGLYNSA 90
                         90       100
                 ....*....|....*....|....*.
gi 495539913  96 LFATPDGALQYYDKRHLfrygGEHER 121
Cdd:cd07579   91 VLVGPEGLVGTYRKTHL----IEPER 112
ML_beta-AS_like cd07568
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
61-225 7.81e-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: 7.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  61 DGPTVAWVREQARALDAAVIGSVQLREGEGV-YNRLLFATPDGA-LQYYDKRHLFRYGGEHERYAAGRERLsvewkGW-- 136
Cdd:cd07568   75 NGPTTKRFAALAKEYNMVLILPIYEKEQGGTlYNTAAVIDADGTyLGKYRKNHIPHVGGFWEKFYFRPGNL-----GYpv 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913 137 ------RINPQVCYDLRFPVFCRnrynverpgQLDFDLQIFVANwPSARA-----YAWKTLLRARAIENLCFVAAVNRIG 205
Cdd:cd07568  150 fdtafgKIGVYICYDRHFPEGWR---------ALGLNGAEIVFN-PSATVaglseYLWKLEQPAAAVANGYFVGAINRVG 219
                        170       180
                 ....*....|....*....|..
gi 495539913 206 VD--GNQLHYAGDSAVIDFLGQ 225
Cdd:cd07568  220 TEapWNIGEFYGSSYFVDPRGQ 241
nitrilase_4 cd07582
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
183-252 4.57e-06

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


Pssm-ID: 143606  Cd Length: 294  Bit Score: 46.95  E-value: 4.57e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495539913 183 WKTLL-RARAIENLCFVAAVNRIGVDGNQLHYA---GDSAVIDFLGQPQVEIR--EREQVVTTTISAEALAAHRAR 252
Cdd:cd07582  207 PWEIAnRARALENLAYVVSANSGGIYGSPYPADsfgGGSMIVDYKGRVLAEAGygPGSMVAGAEIDIEALRRARAR 282
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
4-230 1.80e-05

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: 44.83  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   4 LRISLVQGDTRWHDPAANRAYYGALLAPLA-GTTDLVILPETFTSG---FSNEAIAQ-AEGMDGPTVAWVREQARALDA- 77
Cdd:cd07578    1 YKAAAIQFEPEMGEKERNIERLLALCEEAArAGARLIVTPEMATTGycwYDRAEIAPfVEPIPGPTTARFAELAREHDCy 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913  78 AVIGSVQLREGEGV-YNRLLFATPDGALQYYDKRHlfRYGGEHERYAAGRERLSV-EWKGWRINPQVCYDLRFpvfcrnr 155
Cdd:cd07578   81 IVVGLPEVDSRSGIyYNSAVLIGPSGVIGRHRKTH--PYISEPKWAADGDLGHQVfDTEIGRIALLICMDIHF------- 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495539913 156 YNVERPGQLD-FDLQIFVANWPSARAYA--WKtllrARAIENLCFVAAVNRIGVDgNQLHYAGDSAVIDFLGQPQVEI 230
Cdd:cd07578  152 FETARLLALGgADVICHISNWLAERTPApyWI----NRAFENGCYLIESNRWGLE-RGVQFSGGSCIIEPDGTIQASI 224
ScNTA1_like cd07566
Saccharomyces cerevisiae N-terminal amidase NTA1, and related proteins (class 3 nitrilases); ...
5-113 2.68e-03

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: 38.47  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495539913   5 RISLVQ-----GDTrwhDPAANRAYygALLA---PLAGTT--DLVILPETFTSGFSNEAIAQA-----EGMDGPTVAWVR 69
Cdd:cd07566    1 RIACLQlnpqiGQV---EENLSRAW--ELLDktkKRAKLKkpDILVLPELALTGYNFHSLEHIkpylePTTSGPSFEWAR 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 495539913  70 EQARALDA-AVIGSVQlREGEG---VYNRLLFATPDGALQY-YDKRHLF 113
Cdd:cd07566   76 EVAKKFNChVVIGYPE-KVDESspkLYNSALVVDPEGEVVFnYRKSFLY 123
 
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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