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Conserved domains on  [gi|42573345|ref|NP_974769|]
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Nitrilase/cyanide hydratase and apolipoprotein N-acyltransferase family protein [Arabidopsis thaliana]

Protein Classification

carbon-nitrogen hydrolase family protein( domain architecture ID 10166075)

carbon-nitrogen hydrolase family protein 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

CATH:  3.60.110.10
EC:  3.5.-.-
Gene Ontology:  GO:0016787
PubMed:  12504683|11380987

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
90-290 3.57e-119

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: 342.48  E-value: 3.57e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  90 IGLCQLSVTSDKKRNISHAKKAIEEAASKGAKLVLLPEIWNSPYSNDSFPVYAEEIDAGGdasPSTAMLSEVSKRLKITI 169
Cdd:cd07572   2 VALIQMTSTADKEANLARAKELIEEAAAQGAKLVVLPECFNYPGGTDAFKLALAEEEGDG---PTLQALSELAKEHGIWL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 170 IGGSIPERVG--DRLYNTCCVFGSDGELKAKHRKIHLFDIDIPGKITFMESKTLTAGETPTIVDTDVGRIGIGICYDIRF 247
Cdd:cd07572  79 VGGSIPERDDddGKVYNTSLVFDPDGELVARYRKIHLFDVDVPGGISYRESDTLTPGDEVVVVDTPFGKIGLGICYDLRF 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 42573345 248 QELAMIYAARGAHLLCYPGAFNMTTGPLHWELLQRARATDNQV 290
Cdd:cd07572 159 PELARALARQGADILTVPAAFTMTTGPAHWELLLRARAIENQC 201
 
Name Accession Description Interval E-value
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
90-290 3.57e-119

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: 342.48  E-value: 3.57e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  90 IGLCQLSVTSDKKRNISHAKKAIEEAASKGAKLVLLPEIWNSPYSNDSFPVYAEEIDAGGdasPSTAMLSEVSKRLKITI 169
Cdd:cd07572   2 VALIQMTSTADKEANLARAKELIEEAAAQGAKLVVLPECFNYPGGTDAFKLALAEEEGDG---PTLQALSELAKEHGIWL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 170 IGGSIPERVG--DRLYNTCCVFGSDGELKAKHRKIHLFDIDIPGKITFMESKTLTAGETPTIVDTDVGRIGIGICYDIRF 247
Cdd:cd07572  79 VGGSIPERDDddGKVYNTSLVFDPDGELVARYRKIHLFDVDVPGGISYRESDTLTPGDEVVVVDTPFGKIGLGICYDLRF 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 42573345 248 QELAMIYAARGAHLLCYPGAFNMTTGPLHWELLQRARATDNQV 290
Cdd:cd07572 159 PELARALARQGADILTVPAAFTMTTGPAHWELLLRARAIENQC 201
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
87-290 2.25e-69

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 215.88  E-value: 2.25e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  87 KFNIGLCQLSVTS-DKKRNISHAKKAIEEAASKGAKLVLLPEIWNSPYSNDSFPVYAEEIDAGGdasPSTAMLSEVSKRL 165
Cdd:COG0388   1 TMRIALAQLNPTVgDIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDG---PALAALAELAREL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 166 KITIIGGsIPERV-GDRLYNTCCVFGSDGELKAKHRKIHLFDIDipgkiTFMESKTLTAGETPTIVDTDVGRIGIGICYD 244
Cdd:COG0388  78 GIAVVVG-LPERDeGGRLYNTALVIDPDGEILGRYRKIHLPNYG-----VFDEKRYFTPGDELVVFDTDGGRIGVLICYD 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 42573345 245 IRFQELAMIYAARGAHLLCYPGAFNMTTGPLHWELLQRARATDNQV 290
Cdd:COG0388 152 LWFPELARALALAGADLLLVPSASPFGRGKDHWELLLRARAIENGC 197
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
90-290 3.03e-57

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: 184.48  E-value: 3.03e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345    90 IGLCQL-SVTSDKKRNISHAKKAIEEAASKGAKLVLLPEIWNSPY-SNDSFPVYAEEIDaggdaSPSTAMLSEVSKRLKI 167
Cdd:pfam00795   2 VALVQLpQGFWDLEANLQKALELIEEAARYGADLIVLPELFITGYpCWAHFLEAAEVGD-----GETLAGLAALARKNGI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345   168 TIIGGSIPERV-GDRLYNTCCVFGSDGELKAKHRKIHLFDIdiPGKITFMESKTLTAGETPTIVDTDVGRIGIGICYDIR 246
Cdd:pfam00795  77 AIVIGLIERWLtGGRLYNTAVLLDPDGKLVGKYRKLHLFPE--PRPPGFRERVLFEPGDGGTVFDTPLGKIGAAICYEIR 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 42573345   247 FQELAMIYAARGAHLLCYPGA---FNMTTGPLHWELLQRARATDNQV 290
Cdd:pfam00795 155 FPELLRALALKGAEILINPSArapFPGSLGPPQWLLLARARALENGC 201
PLN02798 PLN02798
nitrilase
90-289 2.49e-45

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 154.90  E-value: 2.49e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345   90 IGLCQLSVTSDKKRNISHAKKAIEEAASKGAKLVLLPEIWNSPYSNDSFPV-YAEEIDAggdasPSTAMLSEVSKRLKIT 168
Cdd:PLN02798  13 VAVAQMTSTNDLAANFATCSRLAKEAAAAGAKLLFLPECFSFIGDKDGESLaIAEPLDG-----PIMQRYRSLARESGLW 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  169 IIGGSIPERVGD--RLYNTCCVFGSDGELKAKHRKIHLFDIDIPGKITFMESKTLTAGETPTIVDTDVGRIGIGICYDIR 246
Cdd:PLN02798  88 LSLGGFQEKGPDdsHLYNTHVLIDDSGEIRSSYRKIHLFDVDVPGGPVLKESSFTAPGKTIVAVDSPVGRLGLTVCYDLR 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 42573345  247 FQELamiYAA----RGAHLLCYPGAFNMTTGPLHWELLQRARATDNQ 289
Cdd:PLN02798 168 FPEL---YQQlrfeHGAQVLLVPSAFTKPTGEAHWEVLLRARAIETQ 211
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
86-288 7.47e-10

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: 58.91  E-value: 7.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345    86 TKFNIGLCQLSVTSDKKRNISHAK-------KAIEEAASKgAKLVLLPEiwnspysnDSFPVYAEEidaggdaSPSTAM- 157
Cdd:TIGR00546 158 PTLNVALVQPNIPQDLKFDSEGLEaileiltSLTKQAVEK-PDLVVWPE--------TAFPFDLEN-------SPQKLAd 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345   158 -LSEVSKRLKITIIGGsIPERVGDR---LYNTCCVFGSDGELKAKHRKIHL--FDIDIP--------GKITFMESKTL-T 222
Cdd:TIGR00546 222 rLKLLVLSKGIPILIG-APDAVPGGpyhYYNSAYLVDPGGEVVQRYDKVKLvpFGEYIPlgflfkwlSKLFFLLSQEDfS 300
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42573345   223 AGETPTIVDTDVGRIGIGICYDIRFQELAMIYAARGAHLLCYP---GAFNMTTGPLHWELLQRARATDN 288
Cdd:TIGR00546 301 RGPGPQVLKLPGGKIAPLICYESIFPDLVRASARQGAELLVNLtndAWFGDSSGPWQHFALARFRAIEN 369
 
Name Accession Description Interval E-value
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
90-290 3.57e-119

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: 342.48  E-value: 3.57e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  90 IGLCQLSVTSDKKRNISHAKKAIEEAASKGAKLVLLPEIWNSPYSNDSFPVYAEEIDAGGdasPSTAMLSEVSKRLKITI 169
Cdd:cd07572   2 VALIQMTSTADKEANLARAKELIEEAAAQGAKLVVLPECFNYPGGTDAFKLALAEEEGDG---PTLQALSELAKEHGIWL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 170 IGGSIPERVG--DRLYNTCCVFGSDGELKAKHRKIHLFDIDIPGKITFMESKTLTAGETPTIVDTDVGRIGIGICYDIRF 247
Cdd:cd07572  79 VGGSIPERDDddGKVYNTSLVFDPDGELVARYRKIHLFDVDVPGGISYRESDTLTPGDEVVVVDTPFGKIGLGICYDLRF 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 42573345 248 QELAMIYAARGAHLLCYPGAFNMTTGPLHWELLQRARATDNQV 290
Cdd:cd07572 159 PELARALARQGADILTVPAAFTMTTGPAHWELLLRARAIENQC 201
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
87-290 2.25e-69

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 215.88  E-value: 2.25e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  87 KFNIGLCQLSVTS-DKKRNISHAKKAIEEAASKGAKLVLLPEIWNSPYSNDSFPVYAEEIDAGGdasPSTAMLSEVSKRL 165
Cdd:COG0388   1 TMRIALAQLNPTVgDIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDG---PALAALAELAREL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 166 KITIIGGsIPERV-GDRLYNTCCVFGSDGELKAKHRKIHLFDIDipgkiTFMESKTLTAGETPTIVDTDVGRIGIGICYD 244
Cdd:COG0388  78 GIAVVVG-LPERDeGGRLYNTALVIDPDGEILGRYRKIHLPNYG-----VFDEKRYFTPGDELVVFDTDGGRIGVLICYD 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 42573345 245 IRFQELAMIYAARGAHLLCYPGAFNMTTGPLHWELLQRARATDNQV 290
Cdd:COG0388 152 LWFPELARALALAGADLLLVPSASPFGRGKDHWELLLRARAIENGC 197
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
90-290 2.31e-62

Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes; This superfamily (also known as the C-N hydrolase superfamily) contains hydrolases that break carbon-nitrogen bonds; it includes nitrilases, cyanide dihydratases, aliphatic amidases, N-terminal amidases, beta-ureidopropionases, biotinidases, pantotheinase, N-carbamyl-D-amino acid amidohydrolases, the glutaminase domain of glutamine-dependent NAD+ synthetase, apolipoprotein N-acyltransferases, and N-carbamoylputrescine amidohydrolases, among others. These enzymes depend on a Glu-Lys-Cys catalytic triad, and work through a thiol acylenzyme intermediate. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. These oligomers include dimers, tetramers, hexamers, octamers, tetradecamers, octadecamers, as well as variable length helical arrangements and homo-oligomeric spirals. These proteins have roles in vitamin and co-enzyme metabolism, in detoxifying small molecules, in the synthesis of signaling molecules, and in the post-translational modification of proteins. They are used industrially, as biocatalysts in the fine chemical and pharmaceutical industry, in cyanide remediation, and in the treatment of toxic effluent. This superfamily has been classified previously in the literature, based on global and structure-based sequence analysis, into thirteen different enzyme classes (referred to as 1-13). This hierarchy includes those thirteen classes and a few additional subfamilies. A putative distant relative, the plasmid-borne TraB family, has not been included in the hierarchy.


Pssm-ID: 143587 [Multi-domain]  Cd Length: 253  Bit Score: 197.55  E-value: 2.31e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  90 IGLCQLSVT-SDKKRNISHAKKAIEEAASKGAKLVLLPEIWNSPYSNDSF---PVYAEEIDaggdaSPSTAMLSEVSKRL 165
Cdd:cd07197   1 IAAVQLAPKiGDVEANLAKALRLIKEAAEQGADLIVLPELFLTGYSFESAkedLDLAEELD-----GPTLEALAELAKEL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 166 KITIIGGsIPERVGDRLYNTCCVFGSDGELKAKHRKIHLFDidipgkitFMESKTLTAGETPTIVDTDVGRIGIGICYDI 245
Cdd:cd07197  76 GIYIVAG-IAEKDGDKLYNTAVVIDPDGEIIGKYRKIHLFD--------FGERRYFSPGDEFPVFDTPGGKIGLLICYDL 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 42573345 246 RFQELAMIYAARGAHLLCYPGAFnMTTGPLHWELLQRARATDNQV 290
Cdd:cd07197 147 RFPELARELALKGADIILVPAAW-PTARREHWELLLRARAIENGV 190
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
89-290 4.63e-61

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: 194.29  E-value: 4.63e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  89 NIGLCQLSVTS-DKKRNISHAKKAIEEAASKGAKLVLLPEIWNSPYSNDSFPVYAEEidaggDASPSTAMLSEVSKRLKI 167
Cdd:cd07583   1 KIALIQLDIVWgDPEANIERVESLIEEAAAAGADLIVLPEMWNTGYFLDDLYELADE-----DGGETVSFLSELAKKHGV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 168 TIIGGSIPERVGDRLYNTCCVFGSDGELKAKHRKIHLFdidipgkiTFM-ESKTLTAGETPTIVDTDVGRIGIGICYDIR 246
Cdd:cd07583  76 NIVAGSVAEKEGGKLYNTAYVIDPDGELIATYRKIHLF--------GLMgEDKYLTAGDELEVFELDGGKVGLFICYDLR 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 42573345 247 FQELAMIYAARGAHLLCYPGAFnmttgPL----HWELLQRARATDNQV 290
Cdd:cd07583 148 FPELFRKLALEGAEILFVPAEW-----PAarieHWRTLLRARAIENQA 190
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
90-290 3.03e-57

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: 184.48  E-value: 3.03e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345    90 IGLCQL-SVTSDKKRNISHAKKAIEEAASKGAKLVLLPEIWNSPY-SNDSFPVYAEEIDaggdaSPSTAMLSEVSKRLKI 167
Cdd:pfam00795   2 VALVQLpQGFWDLEANLQKALELIEEAARYGADLIVLPELFITGYpCWAHFLEAAEVGD-----GETLAGLAALARKNGI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345   168 TIIGGSIPERV-GDRLYNTCCVFGSDGELKAKHRKIHLFDIdiPGKITFMESKTLTAGETPTIVDTDVGRIGIGICYDIR 246
Cdd:pfam00795  77 AIVIGLIERWLtGGRLYNTAVLLDPDGKLVGKYRKLHLFPE--PRPPGFRERVLFEPGDGGTVFDTPLGKIGAAICYEIR 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 42573345   247 FQELAMIYAARGAHLLCYPGA---FNMTTGPLHWELLQRARATDNQV 290
Cdd:pfam00795 155 FPELLRALALKGAEILINPSArapFPGSLGPPQWLLLARARALENGC 201
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
90-290 1.66e-47

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: 159.28  E-value: 1.66e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  90 IGLCQLSVTSDKKRNISHAKKAIEEAASKGAKLVLLPE--IWNSPYSNDSFPVYAEEIDaggdaSPSTAMLSEVSKRLKI 167
Cdd:cd07581   1 VALAQFASSGDKEENLEKVRRLLAEAAAAGADLVVFPEytMARFGDGLDDYARVAEPLD-----GPFVSALARLARELGI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 168 TIIGGsIPERVGD-RLYNTCCVFGSDGELKAKHRKIHLFDidipgKITFMESKTLTAGET--PTIVDTDVGRIGIGICYD 244
Cdd:cd07581  76 TVVAG-MFEPAGDgRVYNTLVVVGPDGEIIAVYRKIHLYD-----AFGFRESDTVAPGDElpPVVFVVGGVKVGLATCYD 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 42573345 245 IRFQELAMIYAARGAHLLCYPGAFNmtTGPL---HWELLQRARATDNQV 290
Cdd:cd07581 150 LRFPELARALALAGADVIVVPAAWV--AGPGkeeHWETLLRARALENTV 196
PLN02798 PLN02798
nitrilase
90-289 2.49e-45

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 154.90  E-value: 2.49e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345   90 IGLCQLSVTSDKKRNISHAKKAIEEAASKGAKLVLLPEIWNSPYSNDSFPV-YAEEIDAggdasPSTAMLSEVSKRLKIT 168
Cdd:PLN02798  13 VAVAQMTSTNDLAANFATCSRLAKEAAAAGAKLLFLPECFSFIGDKDGESLaIAEPLDG-----PIMQRYRSLARESGLW 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  169 IIGGSIPERVGD--RLYNTCCVFGSDGELKAKHRKIHLFDIDIPGKITFMESKTLTAGETPTIVDTDVGRIGIGICYDIR 246
Cdd:PLN02798  88 LSLGGFQEKGPDdsHLYNTHVLIDDSGEIRSSYRKIHLFDVDVPGGPVLKESSFTAPGKTIVAVDSPVGRLGLTVCYDLR 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 42573345  247 FQELamiYAA----RGAHLLCYPGAFNMTTGPLHWELLQRARATDNQ 289
Cdd:PLN02798 168 FPEL---YQQlrfeHGAQVLLVPSAFTKPTGEAHWEVLLRARAIETQ 211
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
88-291 3.11e-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: 143.86  E-value: 3.11e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  88 FNIGLCQLSVTSDKKRNISHAKKAIEEAASKGAKLVLLPEIWNSPY----SNDSFPVYAEEIDAGgdasPSTAMLSEVSK 163
Cdd:cd07573   1 VTVALVQMACSEDPEANLAKAEELVREAAAQGAQIVCLQELFETPYfcqeEDEDYFDLAEPPIPG----PTTARFQALAK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 164 RLKITIIgGSIPERVGDRLY-NTCCVFGSDGELKAKHRKIHlfdidIPGKITFMESKTLTAGETP-TIVDTDVGRIGIGI 241
Cdd:cd07573  77 ELGVVIP-VSLFEKRGNGLYyNSAVVIDADGSLLGVYRKMH-----IPDDPGYYEKFYFTPGDTGfKVFDTRYGRIGVLI 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42573345 242 CYDIRFQELAMIYAARGAHLLCYPGAF-NMTTGP-------LHWELLQRARATDNQVH 291
Cdd:cd07573 151 CWDQWFPEAARLMALQGAEILFYPTAIgSEPQEPpegldqrDAWQRVQRGHAIANGVP 208
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
90-265 8.52e-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: 134.40  E-value: 8.52e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  90 IGLCQLS-VTSDKKRNISHAKKAIEEAASKGAKLVLLPEIWNSPY---SNDSFPVYAEEIDAGgdasPSTAMLSEVSKRL 165
Cdd:cd07580   2 VACVQFDpRVGDLDANLARSIELIREAADAGANLVVLPELANTGYvfeSRDEAFALAEEVPDG----ASTRAWAELAAEL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 166 KITIIGGsIPERVGDRLYNTCCVFGSDGELkAKHRKIHLFDIdipgkitfmESKTLTAG-ETPTIVDTDVGRIGIGICYD 244
Cdd:cd07580  78 GLYIVAG-FAERDGDRLYNSAVLVGPDGVI-GTYRKAHLWNE---------EKLLFEPGdLGLPVFDTPFGRIGVAICYD 146
                       170       180
                ....*....|....*....|.
gi 42573345 245 IRFQELAMIYAARGAHLLCYP 265
Cdd:cd07580 147 GWFPETFRLLALQGADIVCVP 167
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
90-291 3.34e-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: 143608  Cd Length: 258  Bit Score: 130.18  E-value: 3.34e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  90 IGLCQL-SVTSDKKRNISHAKKAIEEAASKGAKLVLLPEIWNSPYSNDSF-PVY---AEEIDaggdaSPSTAMLSEVSKR 164
Cdd:cd07584   2 VALIQMdSVLGDVKANLKKAAELCKEAAAEGADLICFPELATTGYRPDLLgPKLwelSEPID-----GPTVRLFSELAKE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 165 LKITIIGGsIPER--VGDRLYNTCCVFGSDGELKAKHRKIHLFDIdipgkitfmESKTLTAGETPTIVDTDVGRIGIGIC 242
Cdd:cd07584  77 LGVYIVCG-FVEKggVPGKVYNSAVVIDPEGESLGVYRKIHLWGL---------EKQYFREGEQYPVFDTPFGKIGVMIC 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 42573345 243 YDIRFQELAMIYAARGAHLLCYPGAFNMTTGPLhWELLQRARATDNQVH 291
Cdd:cd07584 147 YDMGFPEVARILTLKGAEVIFCPSAWREQDADI-WDINLPARALENTVF 194
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
100-290 2.69e-32

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: 120.11  E-value: 2.69e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 100 DKKRNISHAKKAIEEAASKGAKLVLLPEIWNSPYSNDSFPVYAEEIDAGgdasPSTAMLSEVSKRLKITIIGGSIpERVG 179
Cdd:cd07585  13 DKARNLAVIARWTRKAAAQGAELVCFPEMCITGYTHVRALSREAEVPDG----PSTQALSDLARRYGLTILAGLI-EKAG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 180 DRLYNT-CCVFGsdGELKAKHRKIHLFDIdipgkitfmESKTLTAGETPTIVDTDVGRIGIGICYDIRFQELAMIYAARG 258
Cdd:cd07585  88 DRPYNTyLVCLP--DGLVHRYRKLHLFRR---------EHPYIAAGDEYPVFATPGVRFGILICYDNHFPENVRATALLG 156
                       170       180       190
                ....*....|....*....|....*....|....*
gi 42573345 259 AHLLCYPGAFNMTTGPLHWELLQR---ARATDNQV 290
Cdd:cd07585 157 AEILFAPHATPGTTSPKGREWWMRwlpARAYDNGV 191
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
89-291 4.75e-30

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: 113.83  E-value: 4.75e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  89 NIGLCQLS-VTSDKKRNISHAKKAIEEAASKGAKLVLLPEIWNSPYSNDSFPVYAEEIDAGgdasPSTAMLSEVSKRLKI 167
Cdd:cd07576   1 RLALYQGPaRDGDVAANLARLDEAAARAAAAGADLLVFPELFLTGYNIGDAVARLAEPADG----PALQALRAIARRHGI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 168 TIIGGsIPERVGDRLYNTCCVFGSDGELKAKHRKIHLFdidipGKitfMESKTLTAGETPTIVDTDVGRIGIGICYDIRF 247
Cdd:cd07576  77 AIVVG-YPERAGGAVYNAAVLIDEDGTVLANYRKTHLF-----GD---SERAAFTPGDRFPVVELRGLRVGLLICYDVEF 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 42573345 248 QELAMIYAARGAHLLCYPGAfNMT-TGPLHwELLQRARATDNQVH 291
Cdd:cd07576 148 PELVRALALAGADLVLVPTA-LMEpYGFVA-RTLVPARAFENQIF 190
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
112-290 5.06e-29

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: 111.91  E-value: 5.06e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 112 IEEAASKGAKLVLLPEIWNSP---YSNDSFPVYAEEIDAGGD-ASPSTAMLSEVSKRLKITIIGGSIPERVGDRLYNTCC 187
Cdd:cd07574  27 VAEAAGYGADLLVFPEYFTMEllsLLPEAIDGLDEAIRALAAlTPDYVALFSELARKYGINIIAGSMPVREDGRLYNRAY 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 188 VFGSDGELkAKHRKIHLFdidiPgkitFMESK-TLTAGETPTIVDTDVGRIGIGICYDIRFQELAMIYAARGAHLLCYPG 266
Cdd:cd07574 107 LFGPDGTI-GHQDKLHMT----P----FEREEwGISGGDKLKVFDTDLGKIGILICYDSEFPELARALAEAGADLLLVPS 177
                       170       180
                ....*....|....*....|....*...
gi 42573345 267 AfnmtTGPLHWELLQR----ARATDNQV 290
Cdd:cd07574 178 C----TDTRAGYWRVRigaqARALENQC 201
ML_beta-AS_like cd07568
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
96-288 1.14e-26

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: 105.66  E-value: 1.14e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  96 SVTSDKKRNISHAKKAIEEAASKGAKLVLLPEIWNSPY--SNDSFPVY--AEEIDAGgdasPSTAMLSEVSKRLKITIIG 171
Cdd:cd07568  20 PIEKQKEAMIQKHVTMIREAAEAGAQIVCLQEIFYGPYfcAEQDTKWYefAEEIPNG----PTTKRFAALAKEYNMVLIL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 172 GSIPERVGDRLYNTCCVFGSDGELKAKHRKIHlfdidIPGKITFMESKTLTAGET--PtIVDTDVGRIGIGICYDIRFQE 249
Cdd:cd07568  96 PIYEKEQGGTLYNTAAVIDADGTYLGKYRKNH-----IPHVGGFWEKFYFRPGNLgyP-VFDTAFGKIGVYICYDRHFPE 169
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 42573345 250 LAMIYAARGAHLLCYPGAfnmTTGPLH---WELLQRARATDN 288
Cdd:cd07568 170 GWRALGLNGAEIVFNPSA---TVAGLSeylWKLEQPAAAVAN 208
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
90-265 1.05e-25

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: 102.38  E-value: 1.05e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  90 IGLCQLS-VTSDKKRNISHAKKAIEEAAskgAKLVLLPEIWNSPYS----NDSFPVyAEEIDAGgdasPSTAMLSEVSKR 164
Cdd:cd07577   2 VGYVQFNpKFGEVEKNLKKVESLIKGVE---ADLIVLPELFNTGYAftskEEVASL-AESIPDG----PTTRFLQELARE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 165 LKITIIGGsIPERVGDRLYNTCCVFGSDGELkAKHRKIHLFDIDipgKITFMESKTLtagetPTIVDTDVGRIGIGICYD 244
Cdd:cd07577  74 TGAYIVAG-LPERDGDKFYNSAVVVGPEGYI-GIYRKTHLFYEE---KLFFEPGDTG-----FRVFDIGDIRIGVMICFD 143
                       170       180
                ....*....|....*....|.
gi 42573345 245 IRFQELAMIYAARGAHLLCYP 265
Cdd:cd07577 144 WYFPEAARTLALKGADIIAHP 164
PLN02747 PLN02747
N-carbamolyputrescine amidase
94-290 1.67e-22

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 94.45  E-value: 1.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345   94 QLSVTSDKKRNISHAKKAIEEAASKGAKLVLLPEIWNSPYsndsFPVYAEEI----DAGGDASPSTAMLSEVSKRLKItI 169
Cdd:PLN02747  13 QFACSDDRAANVDKAERLVREAHAKGANIILIQELFEGYY----FCQAQREDffqrAKPYEGHPTIARMQKLAKELGV-V 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  170 IGGSIPERVGDRLYNTCCVFGSDGELKAKHRKIHlfdidIPGKITFMESKTLTAGETPTIV-DTDVGRIGIGICYDIRFQ 248
Cdd:PLN02747  88 IPVSFFEEANNAHYNSIAIIDADGTDLGLYRKSH-----IPDGPGYQEKFYFNPGDTGFKVfDTKFAKIGVAICWDQWFP 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 42573345  249 ELAMIYAARGAHLLCYPGAF-------NMTTGPlHWELLQRARATDNQV 290
Cdd:PLN02747 163 EAARAMVLQGAEVLLYPTAIgsepqdpGLDSRD-HWKRVMQGHAGANLV 210
nitrilase_1_R2 cd07579
Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
90-290 1.52e-19

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


Pssm-ID: 143603  Cd Length: 279  Bit Score: 86.07  E-value: 1.52e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  90 IGLCQLSVTSDKKRNISHAKKAIEEAASKGAKLVLLPEiwnspYSNDSFPVYAEEidAGGDASPSTAMLSEVSKRLKITI 169
Cdd:cd07579   2 IAVAQFAPTPDIAGNLATIDRLAAEAKATGAELVVFPE-----LALTGLDDPASE--AESDTGPAVSALRRLARRLRLYL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 170 IGGsIPERVGDRLYNTCCVFGSDGeLKAKHRKIHLfdidipgkiTFMESKTLTAGETPTIVDTDVGRIGIGICYDIRFQE 249
Cdd:cd07579  75 VAG-FAEADGDGLYNSAVLVGPEG-LVGTYRKTHL---------IEPERSWATPGDTWPVYDLPLGRVGLLIGHDALFPE 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 250 LAMIYAARGAHLLCYPGA-----------------FNMTTG--PLHWELLqRARATDNQV 290
Cdd:cd07579 144 AGRVLALRGCDLLACPAAiaipfvgahagtsvpqpYPIPTGadPTHWHLA-RVRAGENNV 202
nitrilases_CHs cd07564
Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases ...
88-243 2.19e-19

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: 86.00  E-value: 2.19e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  88 FNIGLCQLS-VTSDKKRNISHAKKAIEEAASKGAKLVLLPEIW-----------NSPYSNDSFPVYAEE-IDAGGdasPS 154
Cdd:cd07564   1 VKVAAVQAApVFLDLAATVEKACRLIEEAAANGAQLVVFPEAFipgypywiwfgAPAEGRELFARYYENsVEVDG---PE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 155 TAMLSEVSKRLKITI-IGGSipERVGDRLYNTCCVFGSDGELKAKHRKIhlfdidipgKITFMEsKTLTA---GETPTIV 230
Cdd:cd07564  78 LERLAEAARENGIYVvLGVS--ERDGGTLYNTQLLIDPDGELLGKHRKL---------KPTHAE-RLVWGqgdGSGLRVV 145
                       170
                ....*....|...
gi 42573345 231 DTDVGRIGIGICY 243
Cdd:cd07564 146 DTPIGRLGALICW 158
PLN02504 PLN02504
nitrilase
96-267 5.27e-16

nitrilase


Pssm-ID: 178120  Cd Length: 346  Bit Score: 77.11  E-value: 5.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345   96 SVTSDKKRNISHAKKAIEEAASKGAKLVLLPEIW----------------NSPYSNDSFPVY-AEEIDAGGdasPSTAML 158
Cdd:PLN02504  34 TVFYDTPATLDKAERLIAEAAAYGSQLVVFPEAFiggyprgstfglaigdRSPKGREDFRKYhASAIDVPG---PEVDRL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  159 SEVSKRLKITIIGGSIpERVGDRLYNTCCVFGSDGELKAKHRKIhlfdidIPgkiTFMESKTLTAGE--TPTIVDTDVGR 236
Cdd:PLN02504 111 AAMAGKYKVYLVMGVI-ERDGYTLYCTVLFFDPQGQYLGKHRKL------MP---TALERLIWGFGDgsTIPVYDTPIGK 180
                        170       180       190
                 ....*....|....*....|....*....|.
gi 42573345  237 IGIGICYDIRFQELAMIYAARGAHLLCYPGA 267
Cdd:PLN02504 181 IGAVICWENRMPLLRTAMYAKGIEIYCAPTA 211
nitrilase_8 cd07586
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
89-290 7.86e-16

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: 75.40  E-value: 7.86e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  89 NIGLCQL-SVTSDKKRNISHAKKAIEEAASKGAKLVLLPEIWNSPY--SNDSFPVYAEEIDaggdasPSTAMLSEVSKRl 165
Cdd:cd07586   1 RVAIAQIdPVLGDVEENLEKHLEIIETARERGADLVVFPELSLTGYnlGDLVYEVAMHADD------PRLQALAEASGG- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 166 kITIIGGSIpERVGD-RLYNTCCVFgSDGELKAKHRKIHLfdidiPGKITFMESKTLTAGETPTIVDTDVGRIGIGICYD 244
Cdd:cd07586  74 -ICVVFGFV-EEGRDgRFYNSAAYL-EDGRVVHVHRKVYL-----PTYGLFEEGRYFAPGSHLRAFDTRFGRAGVLICED 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42573345 245 IRFQELAMIYAARGAHLLCYP---------GAFNMTTGplhWELLQRARATDNQV 290
Cdd:cd07586 146 AWHPSLPYLLALDGADVIFIPanspargvgGDFDNEEN---WETLLKFYAMMNGV 197
ML_beta-AS cd07587
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
109-275 7.99e-16

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: 76.64  E-value: 7.99e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 109 KKAIEEAASKGAKLVLLPEIWNSPY---SNDSFP--VYAEEIDAGgdasPSTAMLSEVSKRLKITIIGgSIPER---VGD 180
Cdd:cd07587  93 KKIIEAAAMAGVNIICFQEAWTMPFafcTREKLPwcEFAESAEDG----PTTKFCQELAKKYNMVIVS-PILERdeeHGD 167
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 181 RLYNTCCVFGSDGELKAKHRKIHlfdidIPGKITFMESKTLTAGETPTIV-DTDVGRIGIGICYDiRFQELA-MIYAARG 258
Cdd:cd07587 168 TIWNTAVVISNSGNVLGKSRKNH-----IPRVGDFNESTYYMEGNTGHPVfETQFGKIAVNICYG-RHHPLNwLMYGLNG 241
                       170
                ....*....|....*..
gi 42573345 259 AHLLCYPGAfnmTTGPL 275
Cdd:cd07587 242 AEIVFNPSA---TVGAL 255
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
97-274 1.71e-15

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: 74.49  E-value: 1.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  97 VTSDKKRNISHAKKAIEEAASKGAKLVLLPEIWNSPY---SNDSFPVYAEEIdaggdASPSTAMLSEVSKRLKITIIGGs 173
Cdd:cd07578  11 EMGEKERNIERLLALCEEAARAGARLIVTPEMATTGYcwyDRAEIAPFVEPI-----PGPTTARFAELAREHDCYIVVG- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 174 IPErVGDR---LYNTCCVFGSDGeLKAKHRKIHLFdidipgkitFMESKTLTAGETPTIV-DTDVGRIGIGICYDIRFQE 249
Cdd:cd07578  85 LPE-VDSRsgiYYNSAVLIGPSG-VIGRHRKTHPY---------ISEPKWAADGDLGHQVfDTEIGRIALLICMDIHFFE 153
                       170       180
                ....*....|....*....|....*
gi 42573345 250 LAMIYAARGAHLLCYPGAFNMTTGP 274
Cdd:cd07578 154 TARLLALGGADVICHISNWLAERTP 178
PRK13981 PRK13981
NAD synthetase; Provisional
88-290 1.86e-15

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 76.35  E-value: 1.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345   88 FNIGLCQLSVT-SDKKRNISHAKKAIEEAASKGAKLVLLPEIWNSPYS------NDSF----PVYAEEIDAggDASPSTA 156
Cdd:PRK13981   1 LRIALAQLNPTvGDIAGNAAKILAAAAEAADAGADLLLFPELFLSGYPpedlllRPAFlaacEAALERLAA--ATAGGPA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  157 MLsevskrlkitiIGGsiPERVGDRLYNTCCVFgSDGELKAKHRKIHLfdidiPGKITFMESKTLTAGETPTIVDTDVGR 236
Cdd:PRK13981  79 VL-----------VGH--PWREGGKLYNAAALL-DGGEVLATYRKQDL-----PNYGVFDEKRYFAPGPEPGVVELKGVR 139
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 42573345  237 IGIGICYDIRFQELAMIYAARGAHLLCYPGA--FNMTTGPLHWELLqRARATDNQV 290
Cdd:PRK13981 140 IGVPICEDIWNPEPAETLAEAGAELLLVPNAspYHRGKPDLREAVL-RARVRETGL 194
nitrilase_4 cd07582
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
98-289 5.08e-14

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


Pssm-ID: 143606  Cd Length: 294  Bit Score: 70.84  E-value: 5.08e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  98 TSDKKRNISHAKKAIeeAASKG-------AKLVLLPEIW------NSPYSNDSFPVYAEEIDAggdasPSTAMLSEVSKR 164
Cdd:cd07582  16 RADILANIDRINEQI--DAAVGfsgpglpVRLVVLPEYAlqgfpmGEPREVWQFDKAAIDIPG-----PETEALGEKAKE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 165 LKITIIGGSIpERVGD---RLYNTCCVFGSDGELKAKHRKIHlfdIDIPGKIT--------FMESKTLTAGETPTIVDTD 233
Cdd:cd07582  89 LNVYIAANAY-ERDPDfpgLYFNTAFIIDPSGEIILRYRKMN---SLAAEGSPsphdvwdeYIEVYGYGLDALFPVADTE 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 234 VGRIGIGICYDIRFQELAMIYAARGAHLLCYP----GAFNMTTgplhWELLQRARATDNQ 289
Cdd:cd07582 165 IGNLGCLACEEGLYPEVARGLAMNGAEVLLRSssevPSVELDP----WEIANRARALENL 220
GAT_Gln-NAD-synth cd07570
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ...
90-263 1.21e-13

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: 69.04  E-value: 1.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  90 IGLCQLSVT-SDKKRNISHAKKAIEEAASKGAKLVLLPE--IWNspYS-NDSF--PVYAEEIDAGGDAspstamLSEVSK 163
Cdd:cd07570   2 IALAQLNPTvGDLEGNAEKILEAIREAKAQGADLVVFPElsLTG--YPpEDLLlrPDFLEAAEEALEE------LAAATA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 164 RLKITIIGGSiPERVGDRLYNTCCVFgSDGELKAKHRKIHL-----FDidipgkitfmESKTLTAGETPTIVDTDVGRIG 238
Cdd:cd07570  74 DLDIAVVVGL-PLRHDGKLYNAAAVL-QNGKILGVVPKQLLpnygvFD----------EKRYFTPGDKPDVLFFKGLRIG 141
                       170       180
                ....*....|....*....|....*.
gi 42573345 239 IGICYDIRFQELAMIYAA-RGAHLLC 263
Cdd:cd07570 142 VEICEDLWVPDPPSAELAlAGADLIL 167
PLN00202 PLN00202
beta-ureidopropionase
90-288 3.32e-13

beta-ureidopropionase


Pssm-ID: 177792  Cd Length: 405  Bit Score: 69.10  E-value: 3.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345   90 IGLCQLSVT-------SDKKRNI-SHAKKAIEEAASKGAKLVLLPEIWNSPYS----NDSFPVYAEEIDAggdasPSTAM 157
Cdd:PLN00202  89 VGLIQNSIAlpttapfADQKRAImDKVKPMIDAAGAAGVNILCLQEAWTMPFAfctrEKRWCEFAEPVDG-----ESTKF 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  158 LSEVSKRLKITIIGgSIPER---VGDRLYNTCCVFGSDGELKAKHRKIHlfdidIPGKITFMESKTLTAGETPTIV-DTD 233
Cdd:PLN00202 164 LQELARKYNMVIVS-PILERdvnHGETLWNTAVVIGNNGNIIGKHRKNH-----IPRVGDFNESTYYMEGNTGHPVfETA 237
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 42573345  234 VGRIGIGICYDiRFQELA-MIYAARGAHLLCYPGAfnmTTGPLH---WELLQRARATDN 288
Cdd:PLN00202 238 FGKIAVNICYG-RHHPLNwLAFGLNGAEIVFNPSA---TVGDLSepmWPIEARNAAIAN 292
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
112-285 1.09e-11

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: 63.77  E-value: 1.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 112 IEEAASKGAKLVLLPEiwnspysnDSFPVYAEEIDaggdasPSTAMLSEVSKRLKITIIGGSI-PERVGDRLYNTCCVFG 190
Cdd:cd07571  32 TRELADEKPDLVVWPE--------TALPFDLQRDP------DALARLARAARAVGAPLLTGAPrREPGGGRYYNSALLLD 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 191 SDGELKAKHRKIHL----------FDIDIPGKITFMESKTLTAGETPTIVDTD-VGRIGIGICYDIRFQELAMIYAARGA 259
Cdd:cd07571  98 PGGGILGRYDKHHLvpfgeyvplrDLLRFLGLLFDLPMGDFSPGTGPQPLLLGgGVRVGPLICYESIFPELVRDAVRQGA 177
                       170       180       190
                ....*....|....*....|....*....|.
gi 42573345 260 HLLCYP---GAFNMTTGPlhWELLQ--RARA 285
Cdd:cd07571 178 DLLVNItndAWFGDSAGP--YQHLAmaRLRA 206
DCase cd07569
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ...
113-278 1.39e-11

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: 63.87  E-value: 1.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 113 EEAASKGAKLVLLPEIWNSPYsndsFPVY----AEEIDA---GGDASPSTAMLSEVSKRLKITIIGG---SIPERVGDRL 182
Cdd:cd07569  32 EEAASRGAQLVVFPELALTTF----FPRWyfpdEAELDSffeTEMPNPETQPLFDRAKELGIGFYLGyaeLTEDGGVKRR 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 183 YNTCCVFGSDGELKAKHRKIHL---FDIDIPGKITFMESKTLTAGETP-TIVDTDVGRIGIGICYDIRFQELAMIYAARG 258
Cdd:cd07569 108 FNTSILVDKSGKIVGKYRKVHLpghKEPEPYRPFQHLEKRYFEPGDLGfPVFRVPGGIMGMCICNDRRWPETWRVMGLQG 187
                       170       180
                ....*....|....*....|
gi 42573345 259 AHLLCypGAFNMTTGPLHWE 278
Cdd:cd07569 188 VELVL--LGYNTPTHNPPAP 205
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
86-262 3.65e-11

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


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 63.32  E-value: 3.65e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  86 TKFNIGLCQLSVTSDKKRNISHAKKAI-------EEAASKGAKLVLLPEiwnspysnDSFPVYAEEidaggdASPSTAML 158
Cdd:COG0815 193 EPLRVALVQGNIPQDLKWDPEQRREILdryldltRELADDGPDLVVWPE--------TALPFLLDE------DPDALARL 258
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 159 SEVSKRLKITIIGGSI-PERVGDRLYNTCCVFGSDGELKAKHRKIHL-------------------FDIDIPGkitfmes 218
Cdd:COG0815 259 AAAAREAGAPLLTGAPrRDGGGGRYYNSALLLDPDGGILGRYDKHHLvpfgeyvplrdllrplipfLDLPLGD------- 331
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 42573345 219 ktLTAGETPTIVDTDVGRIGIGICYDIRFQELAMIYAARGAHLL 262
Cdd:COG0815 332 --FSPGTGPPVLDLGGVRVGPLICYESIFPELVRDAVRAGADLL 373
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
89-289 3.26e-10

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: 59.09  E-value: 3.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  89 NIGLCQLS-VTSDKKRNISHAKKAIEEAaSKGAKLVLLPEIWNSPYSNDSFPVyAEEIDaggdaSPSTAMLSEVSKRLKi 167
Cdd:cd07575   2 KIALIQTDlVWEDPEANLAHFEEKIEQL-KEKTDLIVLPEMFTTGFSMNAEAL-AEPMN-----GPTLQWMKAQAKKKG- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 168 TIIGGSIPERVGDRLYNTCcVFGS-DGELKaKHRKIHLFDidipgkitfM--ESKTLTAGETPTIVDTDVGRIGIGICYD 244
Cdd:cd07575  74 AAITGSLIIKEGGKYYNRL-YFVTpDGEVY-HYDKRHLFR---------MagEHKVYTAGNERVIVEYKGWKILLQVCYD 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 42573345 245 IRF------QEL--AMIYAArgahllCYPGAFNmttgpLHWELLQRARATDNQ 289
Cdd:cd07575 143 LRFpvwsrnTNDydLLLYVA------NWPAPRR-----AAWDTLLKARAIENQ 184
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
86-288 7.47e-10

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: 58.91  E-value: 7.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345    86 TKFNIGLCQLSVTSDKKRNISHAK-------KAIEEAASKgAKLVLLPEiwnspysnDSFPVYAEEidaggdaSPSTAM- 157
Cdd:TIGR00546 158 PTLNVALVQPNIPQDLKFDSEGLEaileiltSLTKQAVEK-PDLVVWPE--------TAFPFDLEN-------SPQKLAd 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345   158 -LSEVSKRLKITIIGGsIPERVGDR---LYNTCCVFGSDGELKAKHRKIHL--FDIDIP--------GKITFMESKTL-T 222
Cdd:TIGR00546 222 rLKLLVLSKGIPILIG-APDAVPGGpyhYYNSAYLVDPGGEVVQRYDKVKLvpFGEYIPlgflfkwlSKLFFLLSQEDfS 300
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42573345   223 AGETPTIVDTDVGRIGIGICYDIRFQELAMIYAARGAHLLCYP---GAFNMTTGPLHWELLQRARATDN 288
Cdd:TIGR00546 301 RGPGPQVLKLPGGKIAPLICYESIFPDLVRASARQGAELLVNLtndAWFGDSSGPWQHFALARFRAIEN 369
biotinidase_like cd07567
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ...
103-252 7.31e-09

biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin recycling. Biotinidase (EC 3.5.1.12) has both a hydrolase and a transferase activity. It hydrolyzes free biocytin or small biotinyl-peptides produced during the proteolytic degradation of biotin-dependent carboxylases, to release free biotin (vitamin H), and it can transfer biotin to acceptor molecules such as histones. Biotinidase deficiency in humans is an autosomal recessive disorder characterized by neurological and cutaneous symptoms. This subgroup includes the three human vanins, vanin1-3. Vanins are ectoenzymes, Vanin-1, and -2 are membrane associated, vanin-3 is secreted. They are pantotheinases (EC 3.5.1.92, pantetheine hydrolase), which convert pantetheine, to pantothenic acid (vitamin B5) and cysteamine (2-aminoethanethiol, a potent anti-oxidant). They are potential targets for therapeutic intervention in inflammatory disorders. Vanin-1 deficient mice lacking free cysteamine are less susceptible to intestinal inflammation, and expression of vanin-1 and -3 is induced as part of the inflammatory-regenerative differentiation program of human epidermis. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 4. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143591  Cd Length: 299  Bit Score: 55.71  E-value: 7.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 103 RNISHAKKAIEEAASKGAKLVLLPE--IWNSPYSNDSFPVYAEEI-DAGGDASPSTAML----SEVSKRLKITIIGGSI- 174
Cdd:cd07567  24 KNLDIYEEIIKSAAKQGADIIVFPEdgLTGFIFTRFVIYPFLEDVpDPEVNWNPCLDPDrfdyTEVLQRLSCAARENSIy 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 175 -----PERV------------GDRLYNTCCVFGSDGELKAKHRKIHLfdidipgkitFMESKTlTAGETPTIV--DTDVG 235
Cdd:cd07567 104 vvanlGEKQpcdssdphcppdGRYQYNTNVVFDRDGTLIARYRKYNL----------FGEPGF-DVPPEPEIVtfDTDFG 172
                       170
                ....*....|....*...
gi 42573345 236 -RIGIGICYDIRFQELAM 252
Cdd:cd07567 173 vTFGIFTCFDILFKEPAL 190
ScNTA1_like cd07566
Saccharomyces cerevisiae N-terminal amidase NTA1, and related proteins (class 3 nitrilases); ...
100-278 9.44e-09

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: 55.42  E-value: 9.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 100 DKKRNISHA----KKAIEEAASKGAKLVLLPEIWNSPYS----NDSFPvYAEEIDAGgdasPSTAMLSEVSKRLK-ITII 170
Cdd:cd07566  13 QVEENLSRAwellDKTKKRAKLKKPDILVLPELALTGYNfhslEHIKP-YLEPTTSG----PSFEWAREVAKKFNcHVVI 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345 171 GgsIPERVGD---RLYNTCCVFGSDGELKAKHRKIHLFDIDI-------PGKITFMESKTLTAGETPTIVDTDVGRIGIG 240
Cdd:cd07566  88 G--YPEKVDEsspKLYNSALVVDPEGEVVFNYRKSFLYYTDEewgceenPGGFQTFPLPFAKDDDFDGGSVDVTLKTSIG 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 42573345 241 ICYDI---RFQ------ELAMIYAARGAHLLCYPGAFnmttgpLHWE 278
Cdd:cd07566 166 ICMDLnpyKFEapftdfEFATHVLDNGTELIICPMAW------LHSL 206
lnt PRK00302
apolipoprotein N-acyltransferase; Reviewed
89-262 7.80e-07

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 234721 [Multi-domain]  Cd Length: 505  Bit Score: 49.88  E-value: 7.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345   89 NIGLCQLSVTSDKKRNISHAKKAIE------EAASKGAKLVLLPEIwnspysndSFPVYAEEIdaggdASPSTAMLSEVS 162
Cdd:PRK00302 221 KVALVQGNIPQSLKWDPAGLEATLQkyldlsRPALGPADLIIWPET--------AIPFLLEDL-----PQAFLKALDDLA 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  163 KRLKITIIGGSI---PERVGDRLYNTCCVFGSDGELkAKHRKIHL-----FdidIPGKITF----------MESktLTAG 224
Cdd:PRK00302 288 REKGSALITGAPraeNKQGRYDYYNSIYVLGPYGIL-NRYDKHHLvpfgeY---VPLESLLrplapffnlpMGD--FSRG 361
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 42573345  225 E-TPTIVDTDVGRIGIGICYDIRFQELAMIYAARGAHLL 262
Cdd:PRK00302 362 PyVQPPLLAKGLKLAPLICYEIIFPEEVRANVRQGADLL 400
nadE PRK02628
NAD synthetase; Reviewed
100-189 6.46e-05

NAD synthetase; Reviewed


Pssm-ID: 235057 [Multi-domain]  Cd Length: 679  Bit Score: 44.08  E-value: 6.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573345  100 DKKRNISHAKKAIEEAASKGAKLVLLPEIWNSPYSNDSfpVYAEE--IDAGGDAspsTAMLSEVSKRLKITIIGGSiPER 177
Cdd:PRK02628  26 DPAFNAARILALARRAADDGVALAVFPELSLSGYSCDD--LFLQDtlLDAVEDA---LATLVEASADLDPLLVVGA-PLR 99
                         90
                 ....*....|..
gi 42573345  178 VGDRLYNTCCVF 189
Cdd:PRK02628 100 VRHRLYNCAVVI 111
 
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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