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Conserved domains on  [gi|1101469631|gb|APB81809|]
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carbon-nitrogen hydrolase [Bacillus amyloliquefaciens]

Protein Classification

carbon-nitrogen family hydrolase( domain architecture ID 10166103)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
4-255 1.02e-141

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: 397.68  E-value: 1.02e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   4 TVSCLQFDISYGNPSENFKKAESLIEQE-SRHADVIVLPELWTTGYDLTRLDQLADENGKVSEQWLKETAKTYNVHLVAG 82
Cdd:cd07583     1 KIALIQLDIVWGDPEANIERVESLIEEAaAAGADLIVLPEMWNTGYFLDDLYELADEDGGETVSFLSELAKKHGVNIVAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  83 SFAVKEGENVYNTMYIADNSGQIVKRYQKAHLFQLMDEHLYLSAGNSDGSFELDGVKCAGLICYDIRFPEWIRKHTSQGA 162
Cdd:cd07583    81 SVAEKEGGKLYNTAYVIDPDGELIATYRKIHLFGLMGEDKYLTAGDELEVFELDGGKVGLFICYDLRFPELFRKLALEGA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 163 NVLFISAEWPLPRLDHWRSLLIARAIENQCFVAASNCTGSNPDNEFAGHSLIIDPWGRILAEGDRTEGAVRAEIDVSESA 242
Cdd:cd07583   161 EILFVPAEWPAARIEHWRTLLRARAIENQAFVVACNRVGTDGGNEFGGHSMVIDPWGEVLAEAGEEEEILTAEIDLEEVA 240
                         250
                  ....*....|...
gi 1101469631 243 AVRGTIPVFQDLR 255
Cdd:cd07583   241 EVRKKIPVFKDRR 253
 
Name Accession Description Interval E-value
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
4-255 1.02e-141

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: 397.68  E-value: 1.02e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   4 TVSCLQFDISYGNPSENFKKAESLIEQE-SRHADVIVLPELWTTGYDLTRLDQLADENGKVSEQWLKETAKTYNVHLVAG 82
Cdd:cd07583     1 KIALIQLDIVWGDPEANIERVESLIEEAaAAGADLIVLPEMWNTGYFLDDLYELADEDGGETVSFLSELAKKHGVNIVAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  83 SFAVKEGENVYNTMYIADNSGQIVKRYQKAHLFQLMDEHLYLSAGNSDGSFELDGVKCAGLICYDIRFPEWIRKHTSQGA 162
Cdd:cd07583    81 SVAEKEGGKLYNTAYVIDPDGELIATYRKIHLFGLMGEDKYLTAGDELEVFELDGGKVGLFICYDLRFPELFRKLALEGA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 163 NVLFISAEWPLPRLDHWRSLLIARAIENQCFVAASNCTGSNPDNEFAGHSLIIDPWGRILAEGDRTEGAVRAEIDVSESA 242
Cdd:cd07583   161 EILFVPAEWPAARIEHWRTLLRARAIENQAFVVACNRVGTDGGNEFGGHSMVIDPWGEVLAEAGEEEEILTAEIDLEEVA 240
                         250
                  ....*....|...
gi 1101469631 243 AVRGTIPVFQDLR 255
Cdd:cd07583   241 EVRKKIPVFKDRR 253
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
4-259 1.01e-98

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 289.07  E-value: 1.01e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   4 TVSCLQFDISYGNPSENFKKAESLIEQ-ESRHADVIVLPELWTTGY--DLTRLDQLADENGKVSEQWLKETAKTYNVHLV 80
Cdd:COG0388     3 RIALAQLNPTVGDIEANLAKIEELIREaAAQGADLVVFPELFLTGYppEDDDLLELAEPLDGPALAALAELARELGIAVV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  81 AGSFAVKEGENVYNTMYIADNSGQIVKRYQKAHLF--QLMDEHLYLSAGNSDGSFELDGVKCAGLICYDIRFPEWIRKHT 158
Cdd:COG0388    83 VGLPERDEGGRLYNTALVIDPDGEILGRYRKIHLPnyGVFDEKRYFTPGDELVVFDTDGGRIGVLICYDLWFPELARALA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 159 SQGANVLFISAEWPLPR-LDHWRSLLIARAIENQCFVAASNCTGSNPDNEFAGHSLIIDPWGRILAEGDRTEGAVRAEID 237
Cdd:COG0388   163 LAGADLLLVPSASPFGRgKDHWELLLRARAIENGCYVVAANQVGGEDGLVFDGGSMIVDPDGEVLAEAGDEEGLLVADID 242
                         250       260
                  ....*....|....*....|..
gi 1101469631 238 VSESAAVRGTIPVFQDLRRDLY 259
Cdd:COG0388   243 LDRLREARRRFPVLRDRRPDLY 264
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
4-245 6.33e-54

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: 174.85  E-value: 6.33e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   4 TVSCLQFDISYGNPSENFKKAESLIEQESRH-ADVIVLPELWTTGYDLTRLDQLADENGKVSE-QWLKETAKTYNVHLVA 81
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQKALELIEEAARYgADLIVLPELFITGYPCWAHFLEAAEVGDGETlAGLAALARKNGIAIVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  82 GSF-AVKEGENVYNTMYIADNSGQIVKRYQKAHLFQL-----MDEHLYLSAGNSDGSFELDGVKCAGLICYDIRFPEWIR 155
Cdd:pfam00795  81 GLIeRWLTGGRLYNTAVLLDPDGKLVGKYRKLHLFPEprppgFRERVLFEPGDGGTVFDTPLGKIGAAICYEIRFPELLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 156 KHTSQGANVLFISAE----WPLPRLDHWRSLLIARAIENQCFVAASNCTG-SNPDNEFAGHSLIIDPWGRILAEGDR-TE 229
Cdd:pfam00795 161 ALALKGAEILINPSArapfPGSLGPPQWLLLARARALENGCFVIAANQVGgEEDAPWPYGHSMIIDPDGRILAGAGEwEE 240
                         250
                  ....*....|....*.
gi 1101469631 230 GAVRAEIDVSESAAVR 245
Cdd:pfam00795 241 GVLIADIDLALVRAWR 256
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
5-253 3.75e-46

C-N hydrolase family amidase; Provisional


Pssm-ID: 182461  Cd Length: 256  Bit Score: 154.90  E-value: 3.75e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   5 VSCLQFDISYGNPSENFKKAESLIEQESRHaDVIVLPELWTTGYDLTRLDQLADENgkVSEQWLKETAKTYNVhLVAGSF 84
Cdd:PRK10438    6 ITLLQQPLVWMDGPANLRHFDRQLEGITGR-DVIVLPEMFTTGFAMEAAASSLPQD--DVVAWMTAKAQQTNA-LIAGSV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  85 AVKEGENVYNTMYIADNSGQiVKRYQKAHLFQLMDEHLYLSAGNSDGSFELDGVKCAGLICYDIRFPEWIRkhTSQGANV 164
Cdd:PRK10438   82 ALQTESGAVNRFLLVEPGGT-VHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSR--NRNDYDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 165 LFISAEWPLPRLDHWRSLLIARAIENQCFVAASNCTGSNPDN-EFAGHSLIIDPWGRILAEGDRTEGA-VRAEIDVSESA 242
Cdd:PRK10438  159 ALYVANWPAPRSLHWQTLLTARAIENQAYVAGCNRVGSDGNGhHYRGDSRIINPQGEIIATAEPHQATrIDAELSLEALQ 238
                         250
                  ....*....|.
gi 1101469631 243 AVRGTIPVFQD 253
Cdd:PRK10438  239 EYREKFPAWRD 249
de_GSH_amidase NF033621
deaminated glutathione amidase;
18-256 1.64e-29

deaminated glutathione amidase;


Pssm-ID: 468114  Cd Length: 260  Bit Score: 111.53  E-value: 1.64e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  18 SENFKKAESLIEQ-ESRHADVIVLPE--LWT--TGYDLTR-----LDqladenGKVSEQWLKETAktYNVHLVAGSFAVK 87
Cdd:NF033621   14 QENAQTCVDLMAQaAEAGADLLVLPEavLARddTDPDLSVksaqpLD------GPFLTQLLAESR--GNDLTTVLTVHVP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  88 EGEN-VYNTMyIADNSGQIVKRYQKAHLFQL--MDEHLYLSAGNSDGSF-ELDGVKCAGLICYDIRFPEWIRKHTSQGAN 163
Cdd:NF033621   86 SGDGrAWNTL-VALRDGEIIAQYRKLHLYDAfsMQESRRVDAGNEIPPLvEVAGMKVGLMTCYDLRFPELARRLALDGAD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 164 VLFISAEW---PLPRLdHWRSLLIARAIENQCF-VAASNCTGSNpdnefAGHSLIIDPWGRILAEGDRTEGAVRAEIDVS 239
Cdd:NF033621  165 VLVLPAAWvrgPLKEH-HWETLLAARALENTCYmVAVGECGNRN-----IGQSMVVDPLGVTIAAAAEAPALIFAELDPE 238
                         250
                  ....*....|....*..
gi 1101469631 240 ESAAVRGTIPVFQDlRR 256
Cdd:NF033621  239 RIAHAREQLPVLEN-RR 254
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
14-221 2.55e-16

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: 77.40  E-value: 2.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  14 YGNPSENFKKAESLIEQESRHADVIVLPElwttgydlTRLDQLADENGKVSEQWLKETAKTYNVHLVAGSFAVKEGENV- 92
Cdd:TIGR00546 177 SEGLEAILEILTSLTKQAVEKPDLVVWPE--------TAFPFDLENSPQKLADRLKLLVLSKGIPILIGAPDAVPGGPYh 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  93 -YNTMYIADNSGQIVKRYQKAHL------------------FQLMDEHLYLSAGNSDGSFELDGVKCAGLICYDIRFPEW 153
Cdd:TIGR00546 249 yYNSAYLVDPGGEVVQRYDKVKLvpfgeyiplgflfkwlskLFFLLSQEDFSRGPGPQVLKLPGGKIAPLICYESIFPDL 328
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1101469631 154 IRKHTSQGANVLFISAE--W----PLPRLDHWRSLLiaRAIENQCFVAASNCTGSnpdnefaghSLIIDPWGRI 221
Cdd:TIGR00546 329 VRASARQGAELLVNLTNdaWfgdsSGPWQHFALARF--RAIENGRPLVRATNTGI---------SAVIDPRGRT 391
 
Name Accession Description Interval E-value
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
4-255 1.02e-141

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: 397.68  E-value: 1.02e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   4 TVSCLQFDISYGNPSENFKKAESLIEQE-SRHADVIVLPELWTTGYDLTRLDQLADENGKVSEQWLKETAKTYNVHLVAG 82
Cdd:cd07583     1 KIALIQLDIVWGDPEANIERVESLIEEAaAAGADLIVLPEMWNTGYFLDDLYELADEDGGETVSFLSELAKKHGVNIVAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  83 SFAVKEGENVYNTMYIADNSGQIVKRYQKAHLFQLMDEHLYLSAGNSDGSFELDGVKCAGLICYDIRFPEWIRKHTSQGA 162
Cdd:cd07583    81 SVAEKEGGKLYNTAYVIDPDGELIATYRKIHLFGLMGEDKYLTAGDELEVFELDGGKVGLFICYDLRFPELFRKLALEGA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 163 NVLFISAEWPLPRLDHWRSLLIARAIENQCFVAASNCTGSNPDNEFAGHSLIIDPWGRILAEGDRTEGAVRAEIDVSESA 242
Cdd:cd07583   161 EILFVPAEWPAARIEHWRTLLRARAIENQAFVVACNRVGTDGGNEFGGHSMVIDPWGEVLAEAGEEEEILTAEIDLEEVA 240
                         250
                  ....*....|...
gi 1101469631 243 AVRGTIPVFQDLR 255
Cdd:cd07583   241 EVRKKIPVFKDRR 253
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
4-259 1.01e-98

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 289.07  E-value: 1.01e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   4 TVSCLQFDISYGNPSENFKKAESLIEQ-ESRHADVIVLPELWTTGY--DLTRLDQLADENGKVSEQWLKETAKTYNVHLV 80
Cdd:COG0388     3 RIALAQLNPTVGDIEANLAKIEELIREaAAQGADLVVFPELFLTGYppEDDDLLELAEPLDGPALAALAELARELGIAVV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  81 AGSFAVKEGENVYNTMYIADNSGQIVKRYQKAHLF--QLMDEHLYLSAGNSDGSFELDGVKCAGLICYDIRFPEWIRKHT 158
Cdd:COG0388    83 VGLPERDEGGRLYNTALVIDPDGEILGRYRKIHLPnyGVFDEKRYFTPGDELVVFDTDGGRIGVLICYDLWFPELARALA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 159 SQGANVLFISAEWPLPR-LDHWRSLLIARAIENQCFVAASNCTGSNPDNEFAGHSLIIDPWGRILAEGDRTEGAVRAEID 237
Cdd:COG0388   163 LAGADLLLVPSASPFGRgKDHWELLLRARAIENGCYVVAANQVGGEDGLVFDGGSMIVDPDGEVLAEAGDEEGLLVADID 242
                         250       260
                  ....*....|....*....|..
gi 1101469631 238 VSESAAVRGTIPVFQDLRRDLY 259
Cdd:COG0388   243 LDRLREARRRFPVLRDRRPDLY 264
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
5-255 2.89e-89

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: 264.57  E-value: 2.89e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   5 VSCLQFDISYGNPSENFKKAESLIEQESR-HADVIVLPELWTTGYDLTRLD---QLADENGKVSEQWLKETAKTYNVHLV 80
Cdd:cd07197     1 IAAVQLAPKIGDVEANLAKALRLIKEAAEqGADLIVLPELFLTGYSFESAKedlDLAEELDGPTLEALAELAKELGIYIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  81 AGsFAVKEGENVYNTMYIADNSGQIVKRYQKAHLFQlMDEHLYLSAGNSDGSFELDGVKCAGLICYDIRFPEWIRKHTSQ 160
Cdd:cd07197    81 AG-IAEKDGDKLYNTAVVIDPDGEIIGKYRKIHLFD-FGERRYFSPGDEFPVFDTPGGKIGLLICYDLRFPELARELALK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 161 GANVLFISAEWPLPRLDHWRSLLIARAIENQCFVAASNCTGSNPDNEFAGHSLIIDPWGRILAEGDRTEGAVRAEIDVSE 240
Cdd:cd07197   159 GADIILVPAAWPTARREHWELLLRARAIENGVYVVAANRVGEEGGLEFAGGSMIVDPDGEVLAEASEEEGILVAELDLDE 238
                         250
                  ....*....|....*
gi 1101469631 241 SAAVRGTIPVFQDLR 255
Cdd:cd07197   239 LREARKRWSYLRDRR 253
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
4-253 3.47e-72

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: 221.26  E-value: 3.47e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   4 TVSCLQFDISYGNPSENFKKAESLIEQESRHADVIVLPELWTTGYDLtRLDQLADENGKVSEQWLKETAKTYNVhLVAGS 83
Cdd:cd07575     2 KIALIQTDLVWEDPEANLAHFEEKIEQLKEKTDLIVLPEMFTTGFSM-NAEALAEPMNGPTLQWMKAQAKKKGA-AITGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  84 FAVKEGENVYNTMYIADNSGQIVKrYQKAHLFQLMDEHLYLSAGNSDGSFELDGVKCAGLICYDIRFPEWIRkhtsqgaN 163
Cdd:cd07575    80 LIIKEGGKYYNRLYFVTPDGEVYH-YDKRHLFRMAGEHKVYTAGNERVIVEYKGWKILLQVCYDLRFPVWSR-------N 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 164 -----VLFISAEWPLPRLDHWRSLLIARAIENQCFVAASNCTGSNPDN-EFAGHSLIIDPWGRILAEGDRTEGAVRAEID 237
Cdd:cd07575   152 tndydLLLYVANWPAPRRAAWDTLLKARAIENQAYVIGVNRVGTDGNGlEYSGDSAVIDPLGEPLAEAEEDEGVLTATLD 231
                         250
                  ....*....|....*.
gi 1101469631 238 VSESAAVRGTIPVFQD 253
Cdd:cd07575   232 KEALQEFREKFPFLKD 247
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
4-252 8.44e-71

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: 218.07  E-value: 8.44e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   4 TVSCLQFDISyGNPSENFKKAESLIEQ-ESRHADVIVLPELWTTGY--DLTRLDQLADENGKVSEQWLKETAKTYNVHLV 80
Cdd:cd07572     1 RVALIQMTST-ADKEANLARAKELIEEaAAQGAKLVVLPECFNYPGgtDAFKLALAEEEGDGPTLQALSELAKEHGIWLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  81 AGSFAVKEGEN--VYNTMYIADNSGQIVKRYQKAHLF-------QLMDEHLYLSAGNSDGSFELDGVKCaGL-ICYDIRF 150
Cdd:cd07572    80 GGSIPERDDDDgkVYNTSLVFDPDGELVARYRKIHLFdvdvpggISYRESDTLTPGDEVVVVDTPFGKI-GLgICYDLRF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 151 PEWIRKHTSQGANVLFISA-------EwplprlDHWRSLLIARAIENQCFVAASNCTGSNPDNEFA-GHSLIIDPWGRIL 222
Cdd:cd07572   159 PELARALARQGADILTVPAaftmttgP------AHWELLLRARAIENQCYVVAAAQAGDHEAGRETyGHSMIVDPWGEVL 232
                         250       260       270
                  ....*....|....*....|....*....|
gi 1101469631 223 AEGDRTEGAVRAEIDVSESAAVRGTIPVFQ 252
Cdd:cd07572   233 AEAGEGEGVVVAEIDLDRLEEVRRQIPVLK 262
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
5-256 3.60e-58

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: 185.47  E-value: 3.60e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   5 VSCLQFDISyGNPSENFKKAESLIEQ-ESRHADVIVLPE--LWTTGYDLTRLDQLAD-ENGK-VSEqwLKETAKTYNVHL 79
Cdd:cd07581     1 VALAQFASS-GDKEENLEKVRRLLAEaAAAGADLVVFPEytMARFGDGLDDYARVAEpLDGPfVSA--LARLARELGITV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  80 VAGSFAVKEGENVYNTMYIADNSGQIVKRYQKAHLFqlmD-----EHLYLSAGNSD--GSFELDGVKCAGLICYDIRFPE 152
Cdd:cd07581    78 VAGMFEPAGDGRVYNTLVVVGPDGEIIAVYRKIHLY---DafgfrESDTVAPGDELppVVFVVGGVKVGLATCYDLRFPE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 153 WIRKHTSQGANVLFISAEW---PLpRLDHWRSLLIARAIENQCFVAASNCTGSNpdneFAGHSLIIDPWGRILAEGDRTE 229
Cdd:cd07581   155 LARALALAGADVIVVPAAWvagPG-KEEHWETLLRARALENTVYVAAAGQAGPR----GIGRSMVVDPLGVVLADLGERE 229
                         250       260
                  ....*....|....*....|....*..
gi 1101469631 230 GAVRAEIDVSESAAVRGTIPVFQdLRR 256
Cdd:cd07581   230 GLLVADIDPERVEEAREALPVLE-NRR 255
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
4-255 2.64e-56

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: 180.85  E-value: 2.64e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   4 TVSCLQFDISYGNPSENFKKAESLIEQES-RHADVIVLPELWTTGY----DLTRLDQLADENgkvSEQWLKETAKTYNVH 78
Cdd:cd07576     1 RLALYQGPARDGDVAANLARLDEAAARAAaAGADLLVFPELFLTGYnigdAVARLAEPADGP---ALQALRAIARRHGIA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  79 LVAGsFAVKEGENVYNTMYIADNSGQIVKRYQKAHLFqLMDEHLYLSAGNSDGSFELDGVKCAGLICYDIRFPEWIRKHT 158
Cdd:cd07576    78 IVVG-YPERAGGAVYNAAVLIDEDGTVLANYRKTHLF-GDSERAAFTPGDRFPVVELRGLRVGLLICYDVEFPELVRALA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 159 SQGANVLFISAEWPLPRLDHWRSLLIARAIENQCFVAASNCTGSNPDNEFAGHSLIIDPWGRILAEGDRTEGAVRAEIDV 238
Cdd:cd07576   156 LAGADLVLVPTALMEPYGFVARTLVPARAFENQIFVAYANRCGAEDGLTYVGLSSIAGPDGTVLARAGRGEALLVADLDP 235
                         250
                  ....*....|....*..
gi 1101469631 239 SESAAVRGTIPVFQDLR 255
Cdd:cd07576   236 AALAAARRENPYLADRR 252
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
4-255 1.62e-55

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: 178.72  E-value: 1.62e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   4 TVSCLQFDISYGNPSENFKKAESLIEQESRH-ADVIVLPELWTTGYDLTRLD----QLADENGKVSEQWLKETAKTYNVH 78
Cdd:cd07584     1 KVALIQMDSVLGDVKANLKKAAELCKEAAAEgADLICFPELATTGYRPDLLGpklwELSEPIDGPTVRLFSELAKELGVY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  79 LVAGsFAVKEGEN--VYNTMYIADNSGQIVKRYQKAHLFQLmdEHLYLSAGNSDGSFELDGVKCAGLICYDIRFPEWIRK 156
Cdd:cd07584    81 IVCG-FVEKGGVPgkVYNSAVVIDPEGESLGVYRKIHLWGL--EKQYFREGEQYPVFDTPFGKIGVMICYDMGFPEVARI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 157 HTSQGANVLFISAEWPLPRLDHWRSLLIARAIENQCFVAASNCTGSNPDNEFAGHSLIIDPWGRILAE-GDRTEGAVRAE 235
Cdd:cd07584   158 LTLKGAEVIFCPSAWREQDADIWDINLPARALENTVFVAAVNRVGNEGDLVLFGKSKILNPRGQVLAEaSEEAEEILYAE 237
                         250       260
                  ....*....|....*....|
gi 1101469631 236 IDVSESAAVRGTIPVFQDLR 255
Cdd:cd07584   238 IDLDAIADYRMTLPYLKDRK 257
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
4-245 6.33e-54

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: 174.85  E-value: 6.33e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   4 TVSCLQFDISYGNPSENFKKAESLIEQESRH-ADVIVLPELWTTGYDLTRLDQLADENGKVSE-QWLKETAKTYNVHLVA 81
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQKALELIEEAARYgADLIVLPELFITGYPCWAHFLEAAEVGDGETlAGLAALARKNGIAIVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  82 GSF-AVKEGENVYNTMYIADNSGQIVKRYQKAHLFQL-----MDEHLYLSAGNSDGSFELDGVKCAGLICYDIRFPEWIR 155
Cdd:pfam00795  81 GLIeRWLTGGRLYNTAVLLDPDGKLVGKYRKLHLFPEprppgFRERVLFEPGDGGTVFDTPLGKIGAAICYEIRFPELLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 156 KHTSQGANVLFISAE----WPLPRLDHWRSLLIARAIENQCFVAASNCTG-SNPDNEFAGHSLIIDPWGRILAEGDR-TE 229
Cdd:pfam00795 161 ALALKGAEILINPSArapfPGSLGPPQWLLLARARALENGCFVIAANQVGgEEDAPWPYGHSMIIDPDGRILAGAGEwEE 240
                         250
                  ....*....|....*.
gi 1101469631 230 GAVRAEIDVSESAAVR 245
Cdd:pfam00795 241 GVLIADIDLALVRAWR 256
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
5-253 3.75e-46

C-N hydrolase family amidase; Provisional


Pssm-ID: 182461  Cd Length: 256  Bit Score: 154.90  E-value: 3.75e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   5 VSCLQFDISYGNPSENFKKAESLIEQESRHaDVIVLPELWTTGYDLTRLDQLADENgkVSEQWLKETAKTYNVhLVAGSF 84
Cdd:PRK10438    6 ITLLQQPLVWMDGPANLRHFDRQLEGITGR-DVIVLPEMFTTGFAMEAAASSLPQD--DVVAWMTAKAQQTNA-LIAGSV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  85 AVKEGENVYNTMYIADNSGQiVKRYQKAHLFQLMDEHLYLSAGNSDGSFELDGVKCAGLICYDIRFPEWIRkhTSQGANV 164
Cdd:PRK10438   82 ALQTESGAVNRFLLVEPGGT-VHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSR--NRNDYDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 165 LFISAEWPLPRLDHWRSLLIARAIENQCFVAASNCTGSNPDN-EFAGHSLIIDPWGRILAEGDRTEGA-VRAEIDVSESA 242
Cdd:PRK10438  159 ALYVANWPAPRSLHWQTLLTARAIENQAYVAGCNRVGSDGNGhHYRGDSRIINPQGEIIATAEPHQATrIDAELSLEALQ 238
                         250
                  ....*....|.
gi 1101469631 243 AVRGTIPVFQD 253
Cdd:PRK10438  239 EYREKFPAWRD 249
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
4-259 2.43e-44

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: 150.14  E-value: 2.43e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   4 TVSCLQFDISYGNPSENFKKAESLIEqeSRHADVIVLPELWTTGYDLTRLDQLAD-----ENGKvSEQWLKETAKTYNVH 78
Cdd:cd07577     1 KVGYVQFNPKFGEVEKNLKKVESLIK--GVEADLIVLPELFNTGYAFTSKEEVASlaesiPDGP-TTRFLQELARETGAY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  79 LVAGsFAVKEGENVYNTMYIADNSGQIvKRYQKAHLFQlmDEHLYLSAGNSDGS-FELDGVKCAGLICYDIRFPEWIRKH 157
Cdd:cd07577    78 IVAG-LPERDGDKFYNSAVVVGPEGYI-GIYRKTHLFY--EEKLFFEPGDTGFRvFDIGDIRIGVMICFDWYFPEAARTL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 158 TSQGANVLFISAEWPLPrldHWRSLLIARAIENQCFVAASNCTGSNPDNE----FAGHSLIIDPWGRILAE-GDRTEGAV 232
Cdd:cd07577   154 ALKGADIIAHPANLVLP---YCPKAMPIRALENRVFTITANRIGTEERGGetlrFIGKSQITSPKGEVLARaPEDGEEVL 230
                         250       260
                  ....*....|....*....|....*....
gi 1101469631 233 RAEIDVSESAAVRGTI--PVFQDLRRDLY 259
Cdd:cd07577   231 VAEIDPRLARDKRINEenDIFKDRRPEFY 259
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
4-259 7.22e-41

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: 141.93  E-value: 7.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   4 TVSCLQFDISyGNPSENFKKAESLIEQ-ESRHADVIVLPELWTTGYDLTRLD----QLAD--ENGKVSEQWlKETAKTYN 76
Cdd:cd07573     2 TVALVQMACS-EDPEANLAKAEELVREaAAQGAQIVCLQELFETPYFCQEEDedyfDLAEppIPGPTTARF-QALAKELG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  77 VHLVAgSFAVKEGENVY-NTMYIADNSGQIVKRYQKAH-----LFQlmdEHLYLSAGNS-----DGSFELDGVkcagLIC 145
Cdd:cd07573    80 VVIPV-SLFEKRGNGLYyNSAVVIDADGSLLGVYRKMHipddpGYY---EKFYFTPGDTgfkvfDTRYGRIGV----LIC 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 146 YDIRFPEWIRKHTSQGANVLF---------ISAEWPLPRLDHWRSLLIARAIENQCFVAASNCTG----SNPDNEFAGHS 212
Cdd:cd07573   152 WDQWFPEAARLMALQGAEILFyptaigsepQEPPEGLDQRDAWQRVQRGHAIANGVPVAAVNRVGvegdPGSGITFYGSS 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1101469631 213 LIIDPWGRILAEGDRT-EGAVRAEIDVSESAAVRGTIPVFQDLRRDLY 259
Cdd:cd07573   232 FIADPFGEILAQASRDeEEILVAEFDLDEIEEVRRAWPFFRDRRPDLY 279
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
4-258 4.16e-40

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: 139.64  E-value: 4.16e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   4 TVSCLQFDI-SYGNPSENFKKAESLIEQESR-HADVIVLPE------LWTTGYDLTRLDQLADENGKVSEQW---LKETA 72
Cdd:cd07574     2 RVAAAQYPLrRYASFEEFAAKVEYWVAEAAGyGADLLVFPEyftmelLSLLPEAIDGLDEAIRALAALTPDYvalFSELA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  73 KTYNVHLVAGSFAVKEGENVYNTMYIADNSGQIVKRYqKAHLFQLMDEHLYLSAGNSDGSFELDGVKCAGLICYDIRFPE 152
Cdd:cd07574    82 RKYGINIIAGSMPVREDGRLYNRAYLFGPDGTIGHQD-KLHMTPFEREEWGISGGDKLKVFDTDLGKIGILICYDSEFPE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 153 WIRKHTSQGANVLFIsaewplP-----RLDHWRSLL--IARAIENQCFVAASNCTGSNP----DNEFAGHSLIIDP---- 217
Cdd:cd07574   161 LARALAEAGADLLLV------PsctdtRAGYWRVRIgaQARALENQCYVVQSGTVGNAPwspaVDVNYGQAAVYTPcdfg 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1101469631 218 WGR--ILAEGD-RTEGAVRAEIDVSESAAVR--GTIPVFQDLRRDL 258
Cdd:cd07574   235 FPEdgILAEGEpNTEGWLIADLDLEALRRLReeGSVRNLRDWREDL 280
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
9-259 4.64e-39

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: 136.68  E-value: 4.64e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   9 QFDISYGNPSENFKKAESLIEQ-ESRHADVIVLPELWTTGYDLTR-LDQLADENGKVSEQWLKETAKTYNVHLVAGsFAV 86
Cdd:cd07585     6 QFEARVGDKARNLAVIARWTRKaAAQGAELVCFPEMCITGYTHVRaLSREAEVPDGPSTQALSDLARRYGLTILAG-LIE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  87 KEGENVYNTMYIADNSGQiVKRYQKAHLFQLmdEHLYLSAGNSDGSFELDGVKCAGLICYDIRFPEWIRKHTSQGANVLF 166
Cdd:cd07585    85 KAGDRPYNTYLVCLPDGL-VHRYRKLHLFRR--EHPYIAAGDEYPVFATPGVRFGILICYDNHFPENVRATALLGAEILF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 167 ISAEWP----LPRLDHWRSLLIARAIENQCFVAASNCTGSNPDNEFAGHSLIIDPWGRILAEGDR-TEGAVRAEIDVSES 241
Cdd:cd07585   162 APHATPgttsPKGREWWMRWLPARAYDNGVFVAACNGVGRDGGEVFPGGAMILDPYGRVLAETTSgGDGMVVADLDLDLI 241
                         250       260
                  ....*....|....*....|
gi 1101469631 242 AAVRGT--IPVFQDLRRDLY 259
Cdd:cd07585   242 NTVRGRrwISFLRARRPELY 261
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
4-259 2.49e-38

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


Pssm-ID: 143604  Cd Length: 268  Bit Score: 134.78  E-value: 2.49e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   4 TVSCLQFDISYGNPSENFKKAESLIEQ-ESRHADVIVLPELWTTGYDLTRLDQLADENGKV----SEQWLKETAKTYNVH 78
Cdd:cd07580     1 RVACVQFDPRVGDLDANLARSIELIREaADAGANLVVLPELANTGYVFESRDEAFALAEEVpdgaSTRAWAELAAELGLY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  79 LVAGsFAVKEGENVYNTMYIADNSGQIVKrYQKAHLFQlmDEHLYLSAGNS-----DGSFELDGVkcagLICYDIRFPEW 153
Cdd:cd07580    81 IVAG-FAERDGDRLYNSAVLVGPDGVIGT-YRKAHLWN--EEKLLFEPGDLglpvfDTPFGRIGV----AICYDGWFPET 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 154 IRKHTSQGANVLFISAEWPL---PRLDHW---RSLLIARAIENQCFVAASNCTGSNPDNEFAGHSLIIDPWGRIL---AE 224
Cdd:cd07580   153 FRLLALQGADIVCVPTNWVPmprPPEGGPpmaNILAMAAAHSNGLFIACADRVGTERGQPFIGQSLIVGPDGWPLagpAS 232
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1101469631 225 GDRtEGAVRAEIDVSESAAVRGT--IPVFQDLRRDLY 259
Cdd:cd07580   233 GDE-EEILLADIDLTAARRKRIWnsNDVLRDRRPDLY 268
nitrilase_8 cd07586
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
4-258 4.34e-36

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


Pssm-ID: 143610  Cd Length: 269  Bit Score: 128.94  E-value: 4.34e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   4 TVSCLQFDISYGNPSENFKKAESLIEQESRH-ADVIVLPELWTTGYDLTRLDQ-LADEngkVSEQWLKETA-KTYNVHLV 80
Cdd:cd07586     1 RVAIAQIDPVLGDVEENLEKHLEIIETARERgADLVVFPELSLTGYNLGDLVYeVAMH---ADDPRLQALAeASGGICVV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  81 AGSFAVKEGENVYNTMYIADNsGQIVKRYQKAHL--FQLMDEHLYLSAGNSDGSFELDGVKCAGLICYDIRFPEWIRKHT 158
Cdd:cd07586    78 FGFVEEGRDGRFYNSAAYLED-GRVVHVHRKVYLptYGLFEEGRYFAPGSHLRAFDTRFGRAGVLICEDAWHPSLPYLLA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 159 SQGANVLFISAEWPLPRLDH-------WRSLLIARAIENQCFVAASNCTGSNPDNEFAGHSLIIDPWGRILAEGDRTEGA 231
Cdd:cd07586   157 LDGADVIFIPANSPARGVGGdfdneenWETLLKFYAMMNGVYVVFANRVGVEDGVYFWGGSRVVDPDGEVVAEAPLFEED 236
                         250       260
                  ....*....|....*....|....*...
gi 1101469631 232 -VRAEIDVSESAAVRGTIPVFQDLRRDL 258
Cdd:cd07586   237 lLVAELDRSAIRRARFFSPTFRDEDIRL 264
PLN02798 PLN02798
nitrilase
72-257 4.46e-33

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 121.78  E-value: 4.46e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  72 AKTYNVHLVAGSFAVK--EGENVYNTMYIADNSGQIVKRYQKAHLFQ-------LMDEHLYLSAGNSDGSFElDGVKCAG 142
Cdd:PLN02798   81 ARESGLWLSLGGFQEKgpDDSHLYNTHVLIDDSGEIRSSYRKIHLFDvdvpggpVLKESSFTAPGKTIVAVD-SPVGRLG 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 143 L-ICYDIRFPEWIRKHT-SQGANVLFISAEWPLPRLD-HWRSLLIARAIENQCFV-AASNCTGSNPDNEFAGHSLIIDPW 218
Cdd:PLN02798  160 LtVCYDLRFPELYQQLRfEHGAQVLLVPSAFTKPTGEaHWEVLLRARAIETQCYViAAAQAGKHNEKRESYGHALIIDPW 239
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1101469631 219 GRILAE-GDRTE-GAVRAEIDVSESAAVRGTIPVFQDLRRD 257
Cdd:PLN02798  240 GTVVARlPDRLStGIAVADIDLSLLDSVRTKMPIAEHRRSL 280
GAT_Gln-NAD-synth cd07570
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ...
4-259 1.43e-29

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: 111.79  E-value: 1.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   4 TVSCLQFDISYGNPSENFKKAESLIEQ-ESRHADVIVLPELWTTGY---DLTRLDQLADENGKVSEQWLKETAkTYNVHL 79
Cdd:cd07570     1 RIALAQLNPTVGDLEGNAEKILEAIREaKAQGADLVVFPELSLTGYppeDLLLRPDFLEAAEEALEELAAATA-DLDIAV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  80 VAGsFAVKEGENVYNTMYIADNsGQIVKRYQKAHL-----FqlmDEHLYLSAGNSDGSFELDGVKCAGLICYDIRFPE-W 153
Cdd:cd07570    80 VVG-LPLRHDGKLYNAAAVLQN-GKILGVVPKQLLpnygvF---DEKRYFTPGDKPDVLFFKGLRIGVEICEDLWVPDpP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 154 IRKHTSQGANVLF-ISAEwplP----RLDHWRSLLIARAIENQCFVAASNCTGSNPDNEFAGHSLIIDPWGRILAEGDRT 228
Cdd:cd07570   155 SAELALAGADLILnLSAS---PfhlgKQDYRRELVSSRSARTGLPYVYVNQVGGQDDLVFDGGSFIADNDGELLAEAPRF 231
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1101469631 229 EGAVrAEIDVSESAAVRGTIPVFQDLRRDLY 259
Cdd:cd07570   232 EEDL-ADVDLDRLRSERRRNSSFLDEEAEIY 261
de_GSH_amidase NF033621
deaminated glutathione amidase;
18-256 1.64e-29

deaminated glutathione amidase;


Pssm-ID: 468114  Cd Length: 260  Bit Score: 111.53  E-value: 1.64e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  18 SENFKKAESLIEQ-ESRHADVIVLPE--LWT--TGYDLTR-----LDqladenGKVSEQWLKETAktYNVHLVAGSFAVK 87
Cdd:NF033621   14 QENAQTCVDLMAQaAEAGADLLVLPEavLARddTDPDLSVksaqpLD------GPFLTQLLAESR--GNDLTTVLTVHVP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  88 EGEN-VYNTMyIADNSGQIVKRYQKAHLFQL--MDEHLYLSAGNSDGSF-ELDGVKCAGLICYDIRFPEWIRKHTSQGAN 163
Cdd:NF033621   86 SGDGrAWNTL-VALRDGEIIAQYRKLHLYDAfsMQESRRVDAGNEIPPLvEVAGMKVGLMTCYDLRFPELARRLALDGAD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 164 VLFISAEW---PLPRLdHWRSLLIARAIENQCF-VAASNCTGSNpdnefAGHSLIIDPWGRILAEGDRTEGAVRAEIDVS 239
Cdd:NF033621  165 VLVLPAAWvrgPLKEH-HWETLLAARALENTCYmVAVGECGNRN-----IGQSMVVDPLGVTIAAAAEAPALIFAELDPE 238
                         250
                  ....*....|....*..
gi 1101469631 240 ESAAVRGTIPVFQDlRR 256
Cdd:NF033621  239 RIAHAREQLPVLEN-RR 254
PLN02747 PLN02747
N-carbamolyputrescine amidase
5-259 4.81e-25

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 100.61  E-value: 4.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   5 VSCLQFDISyGNPSENFKKAESLIEQESRH-ADVIVLPELWTTGY--DLTRLD--QLADE-NGKVSEQWLKETAKTYNVH 78
Cdd:PLN02747    9 VAALQFACS-DDRAANVDKAERLVREAHAKgANIILIQELFEGYYfcQAQREDffQRAKPyEGHPTIARMQKLAKELGVV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  79 LVAGSFavKEGENV-YNTMYIADNSGQIVKRYQKAHL-----FQlmdEHLYLSAGnsDGSFELDGVKCAGL---ICYDIR 149
Cdd:PLN02747   88 IPVSFF--EEANNAhYNSIAIIDADGTDLGLYRKSHIpdgpgYQ---EKFYFNPG--DTGFKVFDTKFAKIgvaICWDQW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 150 FPEWIRKHTSQGANVLF----ISAEWPLPRLD---HWRSLLIARAIENQCFVAASNCTGS--------NPDNEFAGHSLI 214
Cdd:PLN02747  161 FPEAARAMVLQGAEVLLyptaIGSEPQDPGLDsrdHWKRVMQGHAGANLVPLVASNRIGTeiletehgPSKITFYGGSFI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1101469631 215 IDPWGRILAE-GDRTEGAVRAEIDVSESAAVRGTIPVFQDLRRDLY 259
Cdd:PLN02747  241 AGPTGEIVAEaDDKAEAVLVAEFDLDQIKSKRASWGVFRDRRPDLY 286
nitrilase_4 cd07582
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
38-256 5.47e-25

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


Pssm-ID: 143606  Cd Length: 294  Bit Score: 100.50  E-value: 5.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  38 IVLPELWTTG--YDLTR----LDQLA-DENGKVSEQwLKETAKTYNVHLVAGSFAVKEG--ENVYNTMYIADNSGQIVKR 108
Cdd:cd07582    46 VVLPEYALQGfpMGEPRevwqFDKAAiDIPGPETEA-LGEKAKELNVYIAANAYERDPDfpGLYFNTAFIIDPSGEIILR 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 109 YQKAHLF---------QLMDEHLYLSAGNSDGSF-----ELDGVKCagLICYDIRFPEWIRKHTSQGANVLF-ISAEWPL 173
Cdd:cd07582   125 YRKMNSLaaegspsphDVWDEYIEVYGYGLDALFpvadtEIGNLGC--LACEEGLYPEVARGLAMNGAEVLLrSSSEVPS 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 174 PRLDHWRSLLIARAIENQCFVAASNCTGSN----PDNEFAGHSLIIDPWGRILAEGDRTEG--AVRAEIDVS---ESAAV 244
Cdd:cd07582   203 VELDPWEIANRARALENLAYVVSANSGGIYgspyPADSFGGGSMIVDYKGRVLAEAGYGPGsmVAGAEIDIEalrRARAR 282
                         250
                  ....*....|..
gi 1101469631 245 RGTIPVFQDLRR 256
Cdd:cd07582   283 PGMHNWLKDLRT 294
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
33-236 6.38e-23

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


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 96.84  E-value: 6.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  33 RHADVIVLPElwtTG--YDLTRLDQLADEngkvseqwLKETAKTYNVHLVAGSFAVKEGEN-VYNTMYIADNSGQIVKRY 109
Cdd:COG0815   232 DGPDLVVWPE---TAlpFLLDEDPDALAR--------LAAAAREAGAPLLTGAPRRDGGGGrYYNSALLLDPDGGILGRY 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 110 QKAHL------------FQLMDEHL-----YLSAGNSDGSFELDGVKCAGLICYDIRFPEWIRKHTSQGANVLFI----- 167
Cdd:COG0815   301 DKHHLvpfgeyvplrdlLRPLIPFLdlplgDFSPGTGPPVLDLGGVRVGPLICYESIFPELVRDAVRAGADLLVNitnda 380
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1101469631 168 ----SAEwplprldHWRSLLIA--RAIENQCFVA-ASNcTgsnpdnefaGHSLIIDPWGRILAEGDR-TEGAVRAEI 236
Cdd:COG0815   381 wfgdSIG-------PYQHLAIArlRAIETGRPVVrATN-T---------GISAVIDPDGRVLARLPLfTRGVLVAEV 440
ML_beta-AS_like cd07568
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
23-259 1.35e-22

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: 93.71  E-value: 1.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  23 KAESLIEQESRH-ADVIVLPELWTTGYDLTRLD----QLADE--NGKVSEQwLKETAKTYNVHLVAGSFAVKEGENVYNT 95
Cdd:cd07568    31 KHVTMIREAAEAgAQIVCLQEIFYGPYFCAEQDtkwyEFAEEipNGPTTKR-FAALAKEYNMVLILPIYEKEQGGTLYNT 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  96 MYIADNSGQIVKRYQKAHLFQLMD--EHLYLSAGNSDGS-FELDGVKCAGLICYDIRFPEWIRKHTSQGANVLF-ISAEw 171
Cdd:cd07568   110 AAVIDADGTYLGKYRKNHIPHVGGfwEKFYFRPGNLGYPvFDTAFGKIGVYICYDRHFPEGWRALGLNGAEIVFnPSAT- 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 172 pLPRLDH--WRSLLIARAIENQCFVAASNCTGSN---PDNEFAGHSLIIDPWGRILAEGDRTE-GAVRAEIDVSESAAVR 245
Cdd:cd07568   189 -VAGLSEylWKLEQPAAAVANGYFVGAINRVGTEapwNIGEFYGSSYFVDPRGQFVASASRDKdELLVAELDLDLIREVR 267
                         250
                  ....*....|....
gi 1101469631 246 GTIPVFQDLRRDLY 259
Cdd:cd07568   268 DTWQFYRDRRPETY 281
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
14-236 1.77e-20

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: 87.65  E-value: 1.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  14 YGNPSENFKKAESLIEQE-SRHADVIVLPElwttgydlTRLDQLADENGKVSEQwLKETAKTYNVHLVAGSF-AVKEGEN 91
Cdd:cd07571    18 PEQRQATLDRYLDLTRELaDEKPDLVVWPE--------TALPFDLQRDPDALAR-LARAARAVGAPLLTGAPrREPGGGR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  92 VYNTMYIADNSGQIVKRYQKAHL--------FQLMDEHLYL---------SAGNSDGSFELDG-VKCAGLICYDIRFPEW 153
Cdd:cd07571    89 YYNSALLLDPGGGILGRYDKHHLvpfgeyvpLRDLLRFLGLlfdlpmgdfSPGTGPQPLLLGGgVRVGPLICYESIFPEL 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 154 IRKHTSQGANVLFISA------EWPLPRLdHwrsLLIA--RAIENQCFVA-ASNctgsnpdnefAGHSLIIDPWGRILAE 224
Cdd:cd07571   169 VRDAVRQGADLLVNITndawfgDSAGPYQ-H---LAMArlRAIETGRPLVrAAN----------TGISAVIDPDGRIVAR 234
                         250
                  ....*....|...
gi 1101469631 225 GD-RTEGAVRAEI 236
Cdd:cd07571   235 LPlFEAGVLVAEV 247
aliphatic_amidase cd07565
aliphatic amidases (class 2 nitrilases); Aliphatic amidases catalyze the hydrolysis of ...
36-239 1.41e-19

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: 85.42  E-value: 1.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  36 DVIVLPELWTTG--YDL-TRLDQLADENGKVSEQwLKETAKTYNVHlvaGSFAVKE-----GENVYNTMYIADNSGQIVK 107
Cdd:cd07565    41 DLIVFPEYSTQGlmYDKwTMDETACTVPGPETDI-FAEACKEAKVW---GVFSIMErnpdhGKNPYNTAIIIDDQGEIVL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 108 RYQKAHLFQLMDEHlylSAGN-----SDGSfelDGVKCAGLICYDIRFPEWIRKHTSQGANVLFISAEWPLPRLDHWRSL 182
Cdd:cd07565   117 KYRKLHPWVPIEPW---YPGDlgtpvCEGP---KGSKIALIICHDGMYPEIARECAYKGAELIIRIQGYMYPAKDQWIIT 190
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1101469631 183 LIARAIENQCFVAASNCTGSNPDNEFAGHSLIIDPWGRILAEGDRTE-GAVRAEIDVS 239
Cdd:cd07565   191 NKANAWCNLMYTASVNLAGFDGVFSYFGESMIVNFDGRTLGEGGREPdEIVTAELSPS 248
PRK13981 PRK13981
NAD synthetase; Provisional
9-224 2.94e-19

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 86.75  E-value: 2.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   9 QFDISYGNPSENFKKA-ESLIEQESRHADVIVLPELWTTGY---DLTRLDQLADENGKVSEQWLKETAKtyNVHLVAGsF 84
Cdd:PRK13981    7 QLNPTVGDIAGNAAKIlAAAAEAADAGADLLLFPELFLSGYppeDLLLRPAFLAACEAALERLAAATAG--GPAVLVG-H 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  85 AVKEGENVYNTMYIADNsGQIVKRYQKAHL--FQLMDEHLYLSAGNSDGSFELDGVKCAGLICYDIRFPEWIRKHTSQGA 162
Cdd:PRK13981   84 PWREGGKLYNAAALLDG-GEVLATYRKQDLpnYGVFDEKRYFAPGPEPGVVELKGVRIGVPICEDIWNPEPAETLAEAGA 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1101469631 163 NVLFISAEWPLPRLDHWR--SLLIARAIENQCFVAASNCTGSNPDNEFAGHSLIIDPWGRILAE 224
Cdd:PRK13981  163 ELLLVPNASPYHRGKPDLreAVLRARVRETGLPLVYLNQVGGQDELVFDGASFVLNADGELAAR 226
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
3-258 6.57e-19

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: 83.35  E-value: 6.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   3 WTVSCLQFDISYGNPSENFKKAESLIEQESRH-ADVIVLPELWTTGY---DLTRLDQLADENGKVSEQWLKETAKTYNVH 78
Cdd:cd07578     1 YKAAAIQFEPEMGEKERNIERLLALCEEAARAgARLIVTPEMATTGYcwyDRAEIAPFVEPIPGPTTARFAELAREHDCY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  79 LVAGSFAVKEGENV-YNTMYIADNSGqIVKRYQKAHLFqlMDEHLYLSAGN-SDGSFELDGVKCAGLICYDIRFPEWIRK 156
Cdd:cd07578    81 IVVGLPEVDSRSGIyYNSAVLIGPSG-VIGRHRKTHPY--ISEPKWAADGDlGHQVFDTEIGRIALLICMDIHFFETARL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 157 HTSQGANVLFISAEWPLPRLD--HWrsllIARAIENQCFVAASNCTGSNPDNEFAGHSLIIDPWGRILAEGDRTEGAVRA 234
Cdd:cd07578   158 LALGGADVICHISNWLAERTPapYW----INRAFENGCYLIESNRWGLERGVQFSGGSCIIEPDGTIQASIDSGDGVALG 233
                         250       260
                  ....*....|....*....|....*
gi 1101469631 235 EIDVSESAAVR-GTIPVFQDLRRDL 258
Cdd:cd07578   234 EIDLDRARHRQfPGELVFTARRPEL 258
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
14-221 2.55e-16

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: 77.40  E-value: 2.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  14 YGNPSENFKKAESLIEQESRHADVIVLPElwttgydlTRLDQLADENGKVSEQWLKETAKTYNVHLVAGSFAVKEGENV- 92
Cdd:TIGR00546 177 SEGLEAILEILTSLTKQAVEKPDLVVWPE--------TAFPFDLENSPQKLADRLKLLVLSKGIPILIGAPDAVPGGPYh 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  93 -YNTMYIADNSGQIVKRYQKAHL------------------FQLMDEHLYLSAGNSDGSFELDGVKCAGLICYDIRFPEW 153
Cdd:TIGR00546 249 yYNSAYLVDPGGEVVQRYDKVKLvpfgeyiplgflfkwlskLFFLLSQEDFSRGPGPQVLKLPGGKIAPLICYESIFPDL 328
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1101469631 154 IRKHTSQGANVLFISAE--W----PLPRLDHWRSLLiaRAIENQCFVAASNCTGSnpdnefaghSLIIDPWGRI 221
Cdd:TIGR00546 329 VRASARQGAELLVNLTNdaWfgdsSGPWQHFALARF--RAIENGRPLVRATNTGI---------SAVIDPRGRT 391
ScNTA1_like cd07566
Saccharomyces cerevisiae N-terminal amidase NTA1, and related proteins (class 3 nitrilases); ...
5-148 1.19e-15

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: 74.68  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   5 VSCLQFDISYGNPSENFKKAESLI-----EQESRHADVIVLPELWTTGYDLTRLDQ----LADENGKVSEQWLKETAKTY 75
Cdd:cd07566     2 IACLQLNPQIGQVEENLSRAWELLdktkkRAKLKKPDILVLPELALTGYNFHSLEHikpyLEPTTSGPSFEWAREVAKKF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  76 NVHLVAGsFAVKEGEN---VYNTMYIADNSGQIVKRYQKAHLFQlMDEHLYLSaGNSDGSFELD---------------- 136
Cdd:cd07566    82 NCHVVIG-YPEKVDESspkLYNSALVVDPEGEVVFNYRKSFLYY-TDEEWGCE-ENPGGFQTFPlpfakdddfdggsvdv 158
                         170
                  ....*....|..
gi 1101469631 137 GVKCAGLICYDI 148
Cdd:cd07566   159 TLKTSIGICMDL 170
nitrilases_CHs cd07564
Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases ...
22-245 4.35e-15

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: 73.29  E-value: 4.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  22 KKAESLIEQESR-HADVIVLPELWTTGY---------DLTR------LDQLADENGKVSEQwLKETAKTYNVHLVAGsFA 85
Cdd:cd07564    20 EKACRLIEEAAAnGAQLVVFPEAFIPGYpywiwfgapAEGRelfaryYENSVEVDGPELER-LAEAARENGIYVVLG-VS 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  86 VKEGENVYNTMYIADNSGQIVKRYQKahlfqLMDEHL-YLSAGNSDGS----FELDGVKCAGLICydirfpeWirKHT-- 158
Cdd:cd07564    98 ERDGGTLYNTQLLIDPDGELLGKHRK-----LKPTHAeRLVWGQGDGSglrvVDTPIGRLGALIC-------W--ENYmp 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 159 -------SQGANVlFISAeWP---LPRLDH--WRSLLIARAIENQCFVAASN--CTGS-------------NPDNEFAGH 211
Cdd:cd07564   164 laryalyAQGEQI-HVAP-WPdfsPYYLSReaWLAASRHYALEGRCFVLSACqvVTEEdipadceddeeadPLEVLGGGG 241
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1101469631 212 SLIIDPWGRILAE-GDRTEGAVRAEIDVSESAAVR 245
Cdd:cd07564   242 SAIVGPDGEVLAGpLPDEEGILYADIDLDDIVEAK 276
lnt PRK00302
apolipoprotein N-acyltransferase; Reviewed
1-236 1.40e-13

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 234721 [Multi-domain]  Cd Length: 505  Bit Score: 69.91  E-value: 1.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631   1 MKWtvsclqfdiSYGNPSENFKKAESLIEQESRHADVIVLPE-----LWTTGYD--LTRLDQLADENGkvseqwlketak 73
Cdd:PRK00302  233 LKW---------DPAGLEATLQKYLDLSRPALGPADLIIWPEtaipfLLEDLPQafLKALDDLAREKG------------ 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  74 tynVHLVAGSFAV---KEGENVYNTMYIADNsGQIVKRYQKAHL----------------FQLMDEHLY-LSAGNSDGS- 132
Cdd:PRK00302  292 ---SALITGAPRAenkQGRYDYYNSIYVLGP-YGILNRYDKHHLvpfgeyvplesllrplAPFFNLPMGdFSRGPYVQPp 367
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 133 FELDGVKCAGLICYDIRFPEWIRKHTSQGANVLF-IS--AeW----PLPrldhWRSLLIA--RAIENQCFV--AASNctg 201
Cdd:PRK00302  368 LLAKGLKLAPLICYEIIFPEEVRANVRQGADLLLnISndA-WfgdsIGP----YQHFQMArmRALELGRPLirATNT--- 439
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1101469631 202 snpdnefaGHSLIIDPWGRILAEGD-RTEGAVRAEI 236
Cdd:PRK00302  440 --------GITAVIDPLGRIIAQLPqFTEGVLDGTV 467
DCase cd07569
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ...
26-256 6.40e-13

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: 66.95  E-value: 6.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  26 SLIEQ-ESRHADVIVLPELWTTGY-------DLTRLDQLADENGKVSE-QWLKETAKTYNVHLVAGsFA--VKEGENV-- 92
Cdd:cd07569    29 ALLEEaASRGAQLVVFPELALTTFfprwyfpDEAELDSFFETEMPNPEtQPLFDRAKELGIGFYLG-YAelTEDGGVKrr 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  93 YNTMYIADNSGQIVKRYQKAHL-----------FQlmdeHL---YLSAGNSD-GSFELDGVKCAGLICYDIRFPEWIRKH 157
Cdd:cd07569   108 FNTSILVDKSGKIVGKYRKVHLpghkepepyrpFQ----HLekrYFEPGDLGfPVFRVPGGIMGMCICNDRRWPETWRVM 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 158 TSQGANVLFI-------SAEWPLP---RLDHWRSLLIARAIENQCFVAASNCTGSNPDNEFAGHSLIIDPWGRILAEGDr 227
Cdd:cd07569   184 GLQGVELVLLgyntpthNPPAPEHdhlRLFHNLLSMQAGAYQNGTWVVAAAKAGMEDGCDLIGGSCIVAPTGEIVAQAT- 262
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1101469631 228 TEG--AVRAEIDVSESAAVRGTIPVFQDLRR 256
Cdd:cd07569   263 TLEdeVIVADCDLDLCREGRETVFNFARHRR 293
amiE PRK13286
aliphatic amidase;
36-239 9.34e-10

aliphatic amidase;


Pssm-ID: 237335  Cd Length: 345  Bit Score: 58.21  E-value: 9.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  36 DVIVLPELWTTG--YDLTRLDQLA-----DENGKVSEQWLKetAKTYNVHLVAGSFAVKEGE-NVYNTMYIADNSGQIVK 107
Cdd:PRK13286   53 DLVIFPEYSTHGimYDRQEMYETAstipgEETAIFAEACRK--AKVWGVFSLTGERHEEHPRkAPYNTLILINDKGEIVQ 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 108 RYQKahlfqLMD----EHLYlsAGN----SDGSfelDGVKCAGLICYDIRFPEWIRKHTSQGANVLFISAEWPLPRLDhw 179
Cdd:PRK13286  131 KYRK-----IMPwcpiEGWY--PGDctyvSEGP---KGLKISLIICDDGNYPEIWRDCAMKGAELIVRCQGYMYPAKE-- 198
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1101469631 180 RSLLIARAIE--NQCFVAASNCTGSNPDNEFAGHSLIIDPWGRILAE-GDRTEGAVRAEIDVS 239
Cdd:PRK13286  199 QQVLVAKAMAwaNNCYVAVANAAGFDGVYSYFGHSAIIGFDGRTLGEcGEEEMGIQYAQLSVS 261
PLN02504 PLN02504
nitrilase
23-242 1.19e-09

nitrilase


Pssm-ID: 178120  Cd Length: 346  Bit Score: 57.85  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  23 KAESLI-EQESRHADVIVLPELWTTGY------DLTrldqLADENGKVSEQWLK-----------------ETAKTYNVH 78
Cdd:PLN02504   45 KAERLIaEAAAYGSQLVVFPEAFIGGYprgstfGLA----IGDRSPKGREDFRKyhasaidvpgpevdrlaAMAGKYKVY 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  79 LVAGSFaVKEGENVYNTMYIADNSGQIVKRYQKahLFQLMDEHLYLSAGnsDGS----FELDGVKCAGLICYDIRFPEWI 154
Cdd:PLN02504  121 LVMGVI-ERDGYTLYCTVLFFDPQGQYLGKHRK--LMPTALERLIWGFG--DGStipvYDTPIGKIGAVICWENRMPLLR 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 155 RKHTSQGANVlfisaeWPLPRLDH---WRSLLIARAIENQCFVAASN--CTGSN----PDNEF--------------AGH 211
Cdd:PLN02504  196 TAMYAKGIEI------YCAPTADSretWQASMRHIALEGGCFVLSANqfCRRKDypppPEYLFsgteedltpdsivcAGG 269
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1101469631 212 SLIIDPWGRILA----EGdrtEGAVRAEIDVSESA 242
Cdd:PLN02504  270 SVIISPSGTVLAgpnyEG---EGLITADLDLGEIA 301
amiF PRK13287
formamidase; Provisional
36-240 1.76e-09

formamidase; Provisional


Pssm-ID: 183950  Cd Length: 333  Bit Score: 57.39  E-value: 1.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  36 DVIVLPELWTTGYDL---TRLDQLADENGKVSEQwLKETAKTYNVHlvaGSFAVKE----GENVYNTMYIADNSGQIVKR 108
Cdd:PRK13287   54 DLIVFPEYSTQGLNTkkwTTEEFLCTVDGPEVDA-FAQACKENKVW---GVFSIMErnpdGNEPYNTAIIIDDQGEIILK 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631 109 YQKAHLFQLMDEhlyLSAGN-----SDGSfelDGVKCAGLICYDIRFPEWIRKHTSQGANVLFISAEWPLPRLDHWRSLL 183
Cdd:PRK13287  130 YRKLHPWVPVEP---WEPGDlgipvCDGP---GGSKLAVCICHDGMFPEMAREAAYKGANVMIRISGYSTQVREQWILTN 203
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1101469631 184 IARAIENQCFVAASNCTGSnpDNEF--AGHSLIIDPWGRILAEGDRTegavRAEIDVSE 240
Cdd:PRK13287  204 RSNAWQNLMYTASVNLAGY--DGVFyyFGEGQVCNFDGTTLVQGHRN----PWEIVTAE 256
PLN00202 PLN00202
beta-ureidopropionase
21-202 2.55e-06

beta-ureidopropionase


Pssm-ID: 177792  Cd Length: 405  Bit Score: 47.91  E-value: 2.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  21 FKKAESLIEQESRHA-DVIVLPELWTTGYDL----TRLDQLADENGKVSEQWLKETAKTYNVHLVAGSFA--VKEGENVY 93
Cdd:PLN00202  112 MDKVKPMIDAAGAAGvNILCLQEAWTMPFAFctreKRWCEFAEPVDGESTKFLQELARKYNMVIVSPILErdVNHGETLW 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  94 NTMYIADNSGQIVKRYQKAHLFQLMD--EHLYLSAGNSDGS-FELDGVKCAGLICYDIRFPEWIRKHTSQGANVLFISAE 170
Cdd:PLN00202  192 NTAVVIGNNGNIIGKHRKNHIPRVGDfnESTYYMEGNTGHPvFETAFGKIAVNICYGRHHPLNWLAFGLNGAEIVFNPSA 271
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1101469631 171 ---------WPLPrldhwrslliAR--AIENQCFVAASNCTGS 202
Cdd:PLN00202  272 tvgdlsepmWPIE----------ARnaAIANSYFVGSINRVGT 304
PRK12291 PRK12291
apolipoprotein N-acyltransferase; Reviewed
18-146 9.70e-06

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 237042 [Multi-domain]  Cd Length: 418  Bit Score: 46.12  E-value: 9.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  18 SENFKKAESLIEQesrHADVIVLPElwtTGY--DLTRLDQLADEngkvseqwLKEtaKTYNVHLVAGSFAVkEGENVYNT 95
Cdd:PRK12291  220 NENLKEIDKAIDE---KKDLIVLPE---TAFplALNNSPILLDK--------LKE--LSHKITIITGALRV-EDGHIYNS 282
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1101469631  96 MYIADNSGqiVKRYQKAHL------------FQLMDEHL------YLSAGNSDGSFELDGVKCAGLICY 146
Cdd:PRK12291  283 TYIFSKGN--VQIADKVILvpfgeeiplpkfFKKPINKLffggasDFSKASKFSDFTLDGVKFRNAICY 349
ML_beta-AS cd07587
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
21-208 4.92e-04

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


Pssm-ID: 143611 [Multi-domain]  Cd Length: 363  Bit Score: 40.81  E-value: 4.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  21 FKKAESLIEQESRH-ADVIVLPELWTTGYDL-TRLD----QLAD--ENGKvSEQWLKETAKTYNVHLVAGSFAVKE--GE 90
Cdd:cd07587    89 HDRIKKIIEAAAMAgVNIICFQEAWTMPFAFcTREKlpwcEFAEsaEDGP-TTKFCQELAKKYNMVIVSPILERDEehGD 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101469631  91 NVYNTMYIADNSGQIVKRYQKAHLFQLMD--EHLYLSAGNSdGS--FELDGVKCAGLICYDIRFP-EWIrKHTSQGANVL 165
Cdd:cd07587   168 TIWNTAVVISNSGNVLGKSRKNHIPRVGDfnESTYYMEGNT-GHpvFETQFGKIAVNICYGRHHPlNWL-MYGLNGAEIV 245
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1101469631 166 F-ISAE--------WPLPrldhwrslliAR--AIENQCFVAASNCTGSN--PdNEF 208
Cdd:cd07587   246 FnPSATvgalsepmWPIE----------ARnaAIANSYFTVGINRVGTEvfP-NEF 290
 
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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