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Conserved domains on  [gi|15597270|ref|NP_250764|]
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hypothetical protein PA2074 [Pseudomonas aeruginosa PAO1]

Protein Classification

nitrilase family protein( domain architecture ID 10166098)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
5-270 3.07e-139

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: 392.48  E-value: 3.07e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   5 TVACCQIAPRIGAQEHNLRLAERAIREAARRGANVVVLPELAASGYVFADRGEALALAE-TRDGPSLGLWKALAGELDLV 83
Cdd:cd07580   1 RVACVQFDPRVGDLDANLARSIELIREAADAGANLVVLPELANTGYVFESRDEAFALAEeVPDGASTRAWAELAAELGLY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  84 IVGGFCERLDPqRVANSAALVDADGVRAIYRKAHLWNEESGIFEAGEQPPPVVATRFGRIAVMVCYDLEFPEWVRLPALS 163
Cdd:cd07580  81 IVAGFAERDGD-RLYNSAVLVGPDGVIGTYRKAHLWNEEKLLFEPGDLGLPVFDTPFGRIGVAICYDGWFPETFRLLALQ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 164 GAQLLCAPVNWPAAPRP-EGERPAEVVRVQANASVNRLFIAACDRCGQERGVDWVGGSVIVDADGYPLDGPLQG-EAGML 241
Cdd:cd07580 160 GADIVCVPTNWVPMPRPpEGGPPMANILAMAAAHSNGLFIACADRVGTERGQPFIGQSLIVGPDGWPLAGPASGdEEEIL 239
                       250       260
                ....*....|....*....|....*....
gi 15597270 242 LARLDLAEADEKRISAHNHVHRDRRPELY 270
Cdd:cd07580 240 LADIDLTAARRKRIWNSNDVLRDRRPDLY 268
 
Name Accession Description Interval E-value
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
5-270 3.07e-139

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: 392.48  E-value: 3.07e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   5 TVACCQIAPRIGAQEHNLRLAERAIREAARRGANVVVLPELAASGYVFADRGEALALAE-TRDGPSLGLWKALAGELDLV 83
Cdd:cd07580   1 RVACVQFDPRVGDLDANLARSIELIREAADAGANLVVLPELANTGYVFESRDEAFALAEeVPDGASTRAWAELAAELGLY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  84 IVGGFCERLDPqRVANSAALVDADGVRAIYRKAHLWNEESGIFEAGEQPPPVVATRFGRIAVMVCYDLEFPEWVRLPALS 163
Cdd:cd07580  81 IVAGFAERDGD-RLYNSAVLVGPDGVIGTYRKAHLWNEEKLLFEPGDLGLPVFDTPFGRIGVAICYDGWFPETFRLLALQ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 164 GAQLLCAPVNWPAAPRP-EGERPAEVVRVQANASVNRLFIAACDRCGQERGVDWVGGSVIVDADGYPLDGPLQG-EAGML 241
Cdd:cd07580 160 GADIVCVPTNWVPMPRPpEGGPPMANILAMAAAHSNGLFIACADRVGTERGQPFIGQSLIVGPDGWPLAGPASGdEEEIL 239
                       250       260
                ....*....|....*....|....*....
gi 15597270 242 LARLDLAEADEKRISAHNHVHRDRRPELY 270
Cdd:cd07580 240 LADIDLTAARRKRIWNSNDVLRDRRPDLY 268
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
3-270 1.29e-78

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 238.61  E-value: 1.29e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   3 KVTVACCQIAPRIGAQEHNLRLAERAIREAARRGANVVVLPELAASGYvFADRGEALALAETRDGPSLGLWKALAGELDL 82
Cdd:COG0388   1 TMRIALAQLNPTVGDIEANLAKIEELIREAAAQGADLVVFPELFLTGY-PPEDDDLLELAEPLDGPALAALAELARELGI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  83 VIVGGFCERLDPQRVANSAALVDADG-VRAIYRKAHLWN----EESGIFEAGEQPPpVVATRFGRIAVMVCYDLEFPEWV 157
Cdd:COG0388  80 AVVVGLPERDEGGRLYNTALVIDPDGeILGRYRKIHLPNygvfDEKRYFTPGDELV-VFDTDGGRIGVLICYDLWFPELA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 158 RLPALSGAQLLCAPVNWPAAPrpeGERPAEVVrVQANASVNRLFIAACDRCGQERGVDWVGGSVIVDADGYPLDGPLQGE 237
Cdd:COG0388 159 RALALAGADLLLVPSASPFGR---GKDHWELL-LRARAIENGCYVVAANQVGGEDGLVFDGGSMIVDPDGEVLAEAGDEE 234
                       250       260       270
                ....*....|....*....|....*....|...
gi 15597270 238 aGMLLARLDLAEADEKRisAHNHVHRDRRPELY 270
Cdd:COG0388 235 -GLLVADIDLDRLREAR--RRFPVLRDRRPDLY 264
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
5-254 2.24e-46

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: 155.59  E-value: 2.24e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270     5 TVACCQIAPRIGAQEHNLRLAERAIREAARRGANVVVLPELAASGYvfADRGEALALAETRDGPSLGLWKALAGELDLVI 84
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQKALELIEEAARYGADLIVLPELFITGY--PCWAHFLEAAEVGDGETLAGLAALARKNGIAI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270    85 VGGFCER-LDPQRVANSAALVDADG-VRAIYRKAHLWNE-------ESGIFEAGEqPPPVVATRFGRIAVMVCYDLEFPE 155
Cdd:pfam00795  79 VIGLIERwLTGGRLYNTAVLLDPDGkLVGKYRKLHLFPEprppgfrERVLFEPGD-GGTVFDTPLGKIGAAICYEIRFPE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   156 WVRLPALSGAQLLCAPvnWPAAPRPEGERPAEVVRVQANASV-NRLFIAACDRCGQERGVDW-VGGSVIVDADGYPLDGP 233
Cdd:pfam00795 158 LLRALALKGAEILINP--SARAPFPGSLGPPQWLLLARARALeNGCFVIAANQVGGEEDAPWpYGHSMIIDPDGRILAGA 235
                         250       260
                  ....*....|....*....|.
gi 15597270   234 LQGEAGMLLARLDLAEADEKR 254
Cdd:pfam00795 236 GEWEEGVLIADIDLALVRAWR 256
PLN02747 PLN02747
N-carbamolyputrescine amidase
3-270 1.48e-33

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 123.34  E-value: 1.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270    3 KVTVACCQIAPRiGAQEHNLRLAERAIREAARRGANVVVLPELaASGYVF--ADRGEALALAETRDG-PSLGLWKALAGE 79
Cdd:PLN02747   6 KVVVAALQFACS-DDRAANVDKAERLVREAHAKGANIILIQEL-FEGYYFcqAQREDFFQRAKPYEGhPTIARMQKLAKE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   80 LDLVIVGGFCERLDPQRVaNSAALVDADG-VRAIYRKAHLWN----EESGIFEAGEQPPPVVATRFGRIAVMVCYDLEFP 154
Cdd:PLN02747  84 LGVVIPVSFFEEANNAHY-NSIAIIDADGtDLGLYRKSHIPDgpgyQEKFYFNPGDTGFKVFDTKFAKIGVAICWDQWFP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  155 EWVRLPALSGAQLLCAPVNWPAAPRPEG--ERPAEVVRVQANASVNRLFIAACDRCGQER--------GVDWVGGSVIVD 224
Cdd:PLN02747 163 EAARAMVLQGAEVLLYPTAIGSEPQDPGldSRDHWKRVMQGHAGANLVPLVASNRIGTEIletehgpsKITFYGGSFIAG 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 15597270  225 ADGYPLDGPLQGEAGMLLARLDLAEADEKRisAHNHVHRDRRPELY 270
Cdd:PLN02747 243 PTGEIVAEADDKAEAVLVAEFDLDQIKSKR--ASWGVFRDRRPDLY 286
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
19-173 9.32e-07

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: 49.28  E-value: 9.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270    19 EHNLRLAERAIREAARRgANVVVLPELAA------SGYVFADRGEALALAetrdgpslglWKALageldlvIVGGFcERL 92
Cdd:TIGR00546 181 EAILEILTSLTKQAVEK-PDLVVWPETAFpfdlenSPQKLADRLKLLVLS----------KGIP-------ILIGA-PDA 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270    93 DPQRV---ANSAALVDADG-VRAIYRKAHL--WNEE------------------SGIFEAGEqPPPVVATRFGRIAVMVC 148
Cdd:TIGR00546 242 VPGGPyhyYNSAYLVDPGGeVVQRYDKVKLvpFGEYiplgflfkwlsklffllsQEDFSRGP-GPQVLKLPGGKIAPLIC 320
                         170       180
                  ....*....|....*....|....*
gi 15597270   149 YDLEFPEWVRLPALSGAQLLCAPVN 173
Cdd:TIGR00546 321 YESIFPDLVRASARQGAELLVNLTN 345
 
Name Accession Description Interval E-value
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
5-270 3.07e-139

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: 392.48  E-value: 3.07e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   5 TVACCQIAPRIGAQEHNLRLAERAIREAARRGANVVVLPELAASGYVFADRGEALALAE-TRDGPSLGLWKALAGELDLV 83
Cdd:cd07580   1 RVACVQFDPRVGDLDANLARSIELIREAADAGANLVVLPELANTGYVFESRDEAFALAEeVPDGASTRAWAELAAELGLY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  84 IVGGFCERLDPqRVANSAALVDADGVRAIYRKAHLWNEESGIFEAGEQPPPVVATRFGRIAVMVCYDLEFPEWVRLPALS 163
Cdd:cd07580  81 IVAGFAERDGD-RLYNSAVLVGPDGVIGTYRKAHLWNEEKLLFEPGDLGLPVFDTPFGRIGVAICYDGWFPETFRLLALQ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 164 GAQLLCAPVNWPAAPRP-EGERPAEVVRVQANASVNRLFIAACDRCGQERGVDWVGGSVIVDADGYPLDGPLQG-EAGML 241
Cdd:cd07580 160 GADIVCVPTNWVPMPRPpEGGPPMANILAMAAAHSNGLFIACADRVGTERGQPFIGQSLIVGPDGWPLAGPASGdEEEIL 239
                       250       260
                ....*....|....*....|....*....
gi 15597270 242 LARLDLAEADEKRISAHNHVHRDRRPELY 270
Cdd:cd07580 240 LADIDLTAARRKRIWNSNDVLRDRRPDLY 268
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
3-270 1.29e-78

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 238.61  E-value: 1.29e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   3 KVTVACCQIAPRIGAQEHNLRLAERAIREAARRGANVVVLPELAASGYvFADRGEALALAETRDGPSLGLWKALAGELDL 82
Cdd:COG0388   1 TMRIALAQLNPTVGDIEANLAKIEELIREAAAQGADLVVFPELFLTGY-PPEDDDLLELAEPLDGPALAALAELARELGI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  83 VIVGGFCERLDPQRVANSAALVDADG-VRAIYRKAHLWN----EESGIFEAGEQPPpVVATRFGRIAVMVCYDLEFPEWV 157
Cdd:COG0388  80 AVVVGLPERDEGGRLYNTALVIDPDGeILGRYRKIHLPNygvfDEKRYFTPGDELV-VFDTDGGRIGVLICYDLWFPELA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 158 RLPALSGAQLLCAPVNWPAAPrpeGERPAEVVrVQANASVNRLFIAACDRCGQERGVDWVGGSVIVDADGYPLDGPLQGE 237
Cdd:COG0388 159 RALALAGADLLLVPSASPFGR---GKDHWELL-LRARAIENGCYVVAANQVGGEDGLVFDGGSMIVDPDGEVLAEAGDEE 234
                       250       260       270
                ....*....|....*....|....*....|...
gi 15597270 238 aGMLLARLDLAEADEKRisAHNHVHRDRRPELY 270
Cdd:COG0388 235 -GLLVADIDLDRLREAR--RRFPVLRDRRPDLY 264
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
6-266 3.53e-70

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: 216.81  E-value: 3.53e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   6 VACCQIAPRIGAQEHNLRLAERAIREAARRGANVVVLPELAASGYVFADRGEALALAETRDGPSLGLWKALAGELDLVIV 85
Cdd:cd07197   1 IAAVQLAPKIGDVEANLAKALRLIKEAAEQGADLIVLPELFLTGYSFESAKEDLDLAEELDGPTLEALAELAKELGIYIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  86 GGFCERlDPQRVANSAALVDADG-VRAIYRKAHLWN-EESGIFEAGEQpPPVVATRFGRIAVMVCYDLEFPEWVRLPALS 163
Cdd:cd07197  81 AGIAEK-DGDKLYNTAVVIDPDGeIIGKYRKIHLFDfGERRYFSPGDE-FPVFDTPGGKIGLLICYDLRFPELARELALK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 164 GAQLLCAPVNWPAAPRPEGErpaevVRVQANASVNRLFIAACDRCGQERGVDWVGGSVIVDADGYPLDGpLQGEAGMLLA 243
Cdd:cd07197 159 GADIILVPAAWPTARREHWE-----LLLRARAIENGVYVVAANRVGEEGGLEFAGGSMIVDPDGEVLAE-ASEEEGILVA 232
                       250       260
                ....*....|....*....|...
gi 15597270 244 RLDLAEADEKRisAHNHVHRDRR 266
Cdd:cd07197 233 ELDLDELREAR--KRWSYLRDRR 253
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
5-270 4.83e-67

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: 208.69  E-value: 4.83e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   5 TVACCQIAPRIGAQEHNLRLAERAIREAArrgANVVVLPELAASGYVFADRGEALALAET-RDGPSLGLWKALAGELDLV 83
Cdd:cd07577   1 KVGYVQFNPKFGEVEKNLKKVESLIKGVE---ADLIVLPELFNTGYAFTSKEEVASLAESiPDGPTTRFLQELARETGAY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  84 IVGGFCERlDPQRVANSAALVDADGVRAIYRKAHLWNEESGIFEAGEQPPPVVATRFGRIAVMVCYDLEFPEWVRLPALS 163
Cdd:cd07577  78 IVAGLPER-DGDKFYNSAVVVGPEGYIGIYRKTHLFYEEKLFFEPGDTGFRVFDIGDIRIGVMICFDWYFPEAARTLALK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 164 GAQLLCAPVNW--PAAPRpegerpAEVVRvqanASVNRLFIAACDRCGQE----RGVDWVGGSVIVDADGYPL-DGPLQG 236
Cdd:cd07577 157 GADIIAHPANLvlPYCPK------AMPIR----ALENRVFTITANRIGTEerggETLRFIGKSQITSPKGEVLaRAPEDG 226
                       250       260       270
                ....*....|....*....|....*....|....
gi 15597270 237 EaGMLLARLDLAEADEKRISAHNHVHRDRRPELY 270
Cdd:cd07577 227 E-EVLVAEIDPRLARDKRINEENDIFKDRRPEFY 259
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
5-268 6.09e-58

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: 185.48  E-value: 6.09e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   5 TVACCQIAPRIGAQEHNLRLAERAIREAARRGANVVVLPELAASGYVFADrgEALALAETRDGPSLGLWKALAGELDLVI 84
Cdd:cd07576   1 RLALYQGPARDGDVAANLARLDEAAARAAAAGADLLVFPELFLTGYNIGD--AVARLAEPADGPALQALRAIARRHGIAI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  85 VGGFCERlDPQRVANSAALVDADG-VRAIYRKAHLW-NEESGIFEAGEQPPPVVATRFgRIAVMVCYDLEFPEWVRLPAL 162
Cdd:cd07576  79 VVGYPER-AGGAVYNAAVLIDEDGtVLANYRKTHLFgDSERAAFTPGDRFPVVELRGL-RVGLLICYDVEFPELVRALAL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 163 SGAQLLCAPVnwpAAPRPEGERPAEVVRVQANAsvNRLFIAACDRCGQERGVDWVGGSVIVDADGYPLDGPLQGEAgMLL 242
Cdd:cd07576 157 AGADLVLVPT---ALMEPYGFVARTLVPARAFE--NQIFVAYANRCGAEDGLTYVGLSSIAGPDGTVLARAGRGEA-LLV 230
                       250       260
                ....*....|....*....|....*.
gi 15597270 243 ARLDLAEADEKRiSAHNHVhRDRRPE 268
Cdd:cd07576 231 ADLDPAALAAAR-RENPYL-ADRRPE 254
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
5-266 4.63e-53

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: 172.72  E-value: 4.63e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   5 TVACCQIAPRIGAQEHNLRLAERAIREAARRGANVVVLPELAASGYvFADrgEALALAETRDGPSLGLWKALAGELDLVI 84
Cdd:cd07583   1 KIALIQLDIVWGDPEANIERVESLIEEAAAAGADLIVLPEMWNTGY-FLD--DLYELADEDGGETVSFLSELAKKHGVNI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  85 VGGFCERLDPQRVANSAALVDADG-VRAIYRKAHLWN--EESGIFEAGEQPPpVVATRFGRIAVMVCYDLEFPEWVRLPA 161
Cdd:cd07583  78 VAGSVAEKEGGKLYNTAYVIDPDGeLIATYRKIHLFGlmGEDKYLTAGDELE-VFELDGGKVGLFICYDLRFPELFRKLA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 162 LSGAQLLCAPVNWPAAprpegerpaevvRV-------QANASVNRLFIAACDRCGQERGVDWVGGSVIVDADGYPLDgPL 234
Cdd:cd07583 157 LEGAEILFVPAEWPAA------------RIehwrtllRARAIENQAFVVACNRVGTDGGNEFGGHSMVIDPWGEVLA-EA 223
                       250       260       270
                ....*....|....*....|....*....|..
gi 15597270 235 QGEAGMLLARLDLAEADEKRisAHNHVHRDRR 266
Cdd:cd07583 224 GEEEEILTAEIDLEEVAEVR--KKIPVFKDRR 253
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
4-270 2.18e-52

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: 171.98  E-value: 2.18e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   4 VTVACCQIAPRIGAQEhNLRLAERAIREAARRGANVVVLPELAASGYvFADRGEA--LALAE-TRDGPSLGLWKALAGEL 80
Cdd:cd07573   1 VTVALVQMACSEDPEA-NLAKAEELVREAAAQGAQIVCLQELFETPY-FCQEEDEdyFDLAEpPIPGPTTARFQALAKEL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  81 DLVIVGGFCERLDPQRVANSAALVDADG-VRAIYRKAHLWN----EESGIFEAGEQPPPVVATRFGRIAVMVCYDLEFPE 155
Cdd:cd07573  79 GVVIPVSLFEKRGNGLYYNSAVVIDADGsLLGVYRKMHIPDdpgyYEKFYFTPGDTGFKVFDTRYGRIGVLICWDQWFPE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 156 WVRLPALSGAQLLCAP--VNWPAAPRPEGERPAEV-VRVQ-ANASVNRLFIAACDRCGQE----RGVDWVGGSVIVDADG 227
Cdd:cd07573 159 AARLMALQGAEILFYPtaIGSEPQEPPEGLDQRDAwQRVQrGHAIANGVPVAAVNRVGVEgdpgSGITFYGSSFIADPFG 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15597270 228 YPLDGPLQGEAGMLLARLDLAEADEKRisAHNHVHRDRRPELY 270
Cdd:cd07573 239 EILAQASRDEEEILVAEFDLDEIEEVR--RAWPFFRDRRPDLY 279
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
5-267 5.98e-48

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: 159.84  E-value: 5.98e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   5 TVACCQIAPRIGAQEHNLRLAERAIREAARRGANVVVLPELAASGYVFADRGEAL-ALAETRDGPSLGLWKALAGELDLV 83
Cdd:cd07584   1 KVALIQMDSVLGDVKANLKKAAELCKEAAAEGADLICFPELATTGYRPDLLGPKLwELSEPIDGPTVRLFSELAKELGVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  84 IVGGFCER-LDPQRVANSAALVDADG-VRAIYRKAHLWNEESGIFEAGEQPPpVVATRFGRIAVMVCYDLEFPEWVRLPA 161
Cdd:cd07584  81 IVCGFVEKgGVPGKVYNSAVVIDPEGeSLGVYRKIHLWGLEKQYFREGEQYP-VFDTPFGKIGVMICYDMGFPEVARILT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 162 LSGAQLLCAPVNWpaaprPEGERPAEVVRVQANASVNRLFIAACDRCGQERGVDWVGGSVIVDADGYPLDGPLQGEAGML 241
Cdd:cd07584 160 LKGAEVIFCPSAW-----REQDADIWDINLPARALENTVFVAAVNRVGNEGDLVLFGKSKILNPRGQVLAEASEEAEEIL 234
                       250       260
                ....*....|....*....|....*.
gi 15597270 242 LARLDLAEADEKRISAhnHVHRDRRP 267
Cdd:cd07584 235 YAEIDLDAIADYRMTL--PYLKDRKP 258
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
5-254 2.24e-46

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: 155.59  E-value: 2.24e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270     5 TVACCQIAPRIGAQEHNLRLAERAIREAARRGANVVVLPELAASGYvfADRGEALALAETRDGPSLGLWKALAGELDLVI 84
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQKALELIEEAARYGADLIVLPELFITGY--PCWAHFLEAAEVGDGETLAGLAALARKNGIAI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270    85 VGGFCER-LDPQRVANSAALVDADG-VRAIYRKAHLWNE-------ESGIFEAGEqPPPVVATRFGRIAVMVCYDLEFPE 155
Cdd:pfam00795  79 VIGLIERwLTGGRLYNTAVLLDPDGkLVGKYRKLHLFPEprppgfrERVLFEPGD-GGTVFDTPLGKIGAAICYEIRFPE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   156 WVRLPALSGAQLLCAPvnWPAAPRPEGERPAEVVRVQANASV-NRLFIAACDRCGQERGVDW-VGGSVIVDADGYPLDGP 233
Cdd:pfam00795 158 LLRALALKGAEILINP--SARAPFPGSLGPPQWLLLARARALeNGCFVIAANQVGGEEDAPWpYGHSMIIDPDGRILAGA 235
                         250       260
                  ....*....|....*....|.
gi 15597270   234 LQGEAGMLLARLDLAEADEKR 254
Cdd:pfam00795 236 GEWEEGVLIADIDLALVRAWR 256
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
6-270 2.50e-45

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: 153.24  E-value: 2.50e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   6 VACCQIAPRIGAQEHNLRLAERAIREAARRGANVVVLPELAASGYVFADRGEALAlaETRDGPSLGLWKALAGELDLVIV 85
Cdd:cd07585   2 IALVQFEARVGDKARNLAVIARWTRKAAAQGAELVCFPEMCITGYTHVRALSREA--EVPDGPSTQALSDLARRYGLTIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  86 GGFCERlDPQRVANSAALVDADGVRAIYRKAHLWNEESGIFEAGEQPPpVVATRFGRIAVMVCYDLEFPEWVRLPALSGA 165
Cdd:cd07585  80 AGLIEK-AGDRPYNTYLVCLPDGLVHRYRKLHLFRREHPYIAAGDEYP-VFATPGVRFGILICYDNHFPENVRATALLGA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 166 QLLCAPVNWPAAPRPEGErpAEVVR-VQANASVNRLFIAACDRCGQERGVDWVGGSVIVDADGYPLDGPLQGEAGMLLAR 244
Cdd:cd07585 158 EILFAPHATPGTTSPKGR--EWWMRwLPARAYDNGVFVAACNGVGRDGGEVFPGGAMILDPYGRVLAETTSGGDGMVVAD 235
                       250       260
                ....*....|....*....|....*.
gi 15597270 245 LDLAEADEKRISAHNHVHRDRRPELY 270
Cdd:cd07585 236 LDLDLINTVRGRRWISFLRARRPELY 261
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
6-254 6.10e-45

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: 151.96  E-value: 6.10e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   6 VACCQIAPRiGAQEHNLRLAERAIREAARRGANVVVLPElAASGYVFADRGEALALAETRDGPSLGLWKALAGELDLVIV 85
Cdd:cd07581   1 VALAQFASS-GDKEENLEKVRRLLAEAAAAGADLVVFPE-YTMARFGDGLDDYARVAEPLDGPFVSALARLARELGITVV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  86 GGFCERLDPQRVANSAALVDADG-VRAIYRKAHLWN----EESGIFEAGEQPPPVVATRFG-RIAVMVCYDLEFPEWVRL 159
Cdd:cd07581  79 AGMFEPAGDGRVYNTLVVVGPDGeIIAVYRKIHLYDafgfRESDTVAPGDELPPVVFVVGGvKVGLATCYDLRFPELARA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 160 PALSGAQLLCAPVNWPAAPRPEgERPAEVVRvqANASVNRLFIAACDRCGqERGvdwVGGSVIVDADGYPLdGPLQGEAG 239
Cdd:cd07581 159 LALAGADVIVVPAAWVAGPGKE-EHWETLLR--ARALENTVYVAAAGQAG-PRG---IGRSMVVDPLGVVL-ADLGEREG 230
                       250
                ....*....|....*
gi 15597270 240 MLLARLDLAEADEKR 254
Cdd:cd07581 231 LLVADIDPERVEEAR 245
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
4-269 1.17e-39

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: 138.43  E-value: 1.17e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   4 VTVACCQIAPRIGAQEHNLRLAERAIREAARRGANVVVLPELAASGYVFADRGEALALAETRDGPSLGLWKALAGELDLV 83
Cdd:cd07578   1 YKAAAIQFEPEMGEKERNIERLLALCEEAARAGARLIVTPEMATTGYCWYDRAEIAPFVEPIPGPTTARFAELAREHDCY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  84 IVGGFCErLDPQR--VANSAALVDADGVRAIYRKAHLWNEESGIFEAGEQPPPVVATRFGRIAVMVCYDLEFPEWVRLPA 161
Cdd:cd07578  81 IVVGLPE-VDSRSgiYYNSAVLIGPSGVIGRHRKTHPYISEPKWAADGDLGHQVFDTEIGRIALLICMDIHFFETARLLA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 162 LSGAQLLCAPVNWPAAPRPEgerPAEVVRVQANASvnrlFIAACDRCGQERGVDWVGGSVIVDADGyPLDGPLQGEAGML 241
Cdd:cd07578 160 LGGADVICHISNWLAERTPA---PYWINRAFENGC----YLIESNRWGLERGVQFSGGSCIIEPDG-TIQASIDSGDGVA 231
                       250       260
                ....*....|....*....|....*...
gi 15597270 242 LARLDLAEADEKRISAhNHVHRDRRPEL 269
Cdd:cd07578 232 LGEIDLDRARHRQFPG-ELVFTARRPEL 258
nitrilase_8 cd07586
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
5-266 1.07e-35

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


Pssm-ID: 143610  Cd Length: 269  Bit Score: 128.56  E-value: 1.07e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   5 TVACCQIAPRIGAQEHNLRLAERAIREAARRGANVVVLPELAASGYVFADRgeALALAETRDGPSLGLWKALAGELDLVI 84
Cdd:cd07586   1 RVAIAQIDPVLGDVEENLEKHLEIIETARERGADLVVFPELSLTGYNLGDL--VYEVAMHADDPRLQALAEASGGICVVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  85 vgGFCERLDPQRVANSAALVDADGVRAIYRKAHLWN----EESGIFEAGeQPPPVVATRFGRIAVMVCYDLEFPEWVRLP 160
Cdd:cd07586  79 --GFVEEGRDGRFYNSAAYLEDGRVVHVHRKVYLPTyglfEEGRYFAPG-SHLRAFDTRFGRAGVLICEDAWHPSLPYLL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 161 ALSGAQLLCAPVNWPAapRPEGERPAEVVR----VQANASVNRLFIAACDRCGQERGVDWVGGSVIVDADGYPL-DGPLq 235
Cdd:cd07586 156 ALDGADVIFIPANSPA--RGVGGDFDNEENwetlLKFYAMMNGVYVVFANRVGVEDGVYFWGGSRVVDPDGEVVaEAPL- 232
                       250       260       270
                ....*....|....*....|....*....|.
gi 15597270 236 GEAGMLLARLDLAEADEKRISAhnHVHRDRR 266
Cdd:cd07586 233 FEEDLLVAELDRSAIRRARFFS--PTFRDED 261
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
5-260 1.78e-35

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: 127.54  E-value: 1.78e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   5 TVACCQIapRIGAQ-EHNLRLAERAIREAARRGANVVVLPElaASGYVFADRGEALALAET-RDGPSLGLWKALAGELDL 82
Cdd:cd07572   1 RVALIQM--TSTADkEANLARAKELIEEAAAQGAKLVVLPE--CFNYPGGTDAFKLALAEEeGDGPTLQALSELAKEHGI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  83 VIVGG-FCERLD-PQRVANSAALVDADG-VRAIYRKAHLWN---------EESGIFEAGEQPPpVVATRFGRIAVMVCYD 150
Cdd:cd07572  77 WLVGGsIPERDDdDGKVYNTSLVFDPDGeLVARYRKIHLFDvdvpggisyRESDTLTPGDEVV-VVDTPFGKIGLGICYD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 151 LEFPEWVRLPALSGAQLLCApvnwPAA-PRPEGerPA--EVVrVQANASVNRLFIAACDRCGQERG----------VD-W 216
Cdd:cd07572 156 LRFPELARALARQGADILTV----PAAfTMTTG--PAhwELL-LRARAIENQCYVVAAAQAGDHEAgretyghsmiVDpW 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15597270 217 vgGSVIVDADGYPldgplqgeaGMLLARLDLAEADE--KRISAHNH 260
Cdd:cd07572 229 --GEVLAEAGEGE---------GVVVAEIDLDRLEEvrRQIPVLKH 263
PLN02747 PLN02747
N-carbamolyputrescine amidase
3-270 1.48e-33

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 123.34  E-value: 1.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270    3 KVTVACCQIAPRiGAQEHNLRLAERAIREAARRGANVVVLPELaASGYVF--ADRGEALALAETRDG-PSLGLWKALAGE 79
Cdd:PLN02747   6 KVVVAALQFACS-DDRAANVDKAERLVREAHAKGANIILIQEL-FEGYYFcqAQREDFFQRAKPYEGhPTIARMQKLAKE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   80 LDLVIVGGFCERLDPQRVaNSAALVDADG-VRAIYRKAHLWN----EESGIFEAGEQPPPVVATRFGRIAVMVCYDLEFP 154
Cdd:PLN02747  84 LGVVIPVSFFEEANNAHY-NSIAIIDADGtDLGLYRKSHIPDgpgyQEKFYFNPGDTGFKVFDTKFAKIGVAICWDQWFP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  155 EWVRLPALSGAQLLCAPVNWPAAPRPEG--ERPAEVVRVQANASVNRLFIAACDRCGQER--------GVDWVGGSVIVD 224
Cdd:PLN02747 163 EAARAMVLQGAEVLLYPTAIGSEPQDPGldSRDHWKRVMQGHAGANLVPLVASNRIGTEIletehgpsKITFYGGSFIAG 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 15597270  225 ADGYPLDGPLQGEAGMLLARLDLAEADEKRisAHNHVHRDRRPELY 270
Cdd:PLN02747 243 PTGEIVAEADDKAEAVLVAEFDLDQIKSKR--ASWGVFRDRRPDLY 286
PLN02798 PLN02798
nitrilase
2-254 3.44e-28

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 109.06  E-value: 3.44e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270    2 AKVTVACCQIAPrIGAQEHNLRLAERAIREAARRGANVVVLPElaASGYVFADRGEALALAETRDGPSLGLWKALAGELD 81
Cdd:PLN02798   9 SSVRVAVAQMTS-TNDLAANFATCSRLAKEAAAAGAKLLFLPE--CFSFIGDKDGESLAIAEPLDGPIMQRYRSLARESG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   82 LVI-VGGFCER-LDPQRVANSAALVDADG-VRAIYRKAHLWN---------EESGIFEAGEQPPpVVATRFGRIAVMVCY 149
Cdd:PLN02798  86 LWLsLGGFQEKgPDDSHLYNTHVLIDDSGeIRSSYRKIHLFDvdvpggpvlKESSFTAPGKTIV-AVDSPVGRLGLTVCY 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  150 DLEFPE-WVRLPALSGAQLLCAPvnwPAAPRPEGERPAEVVrVQANASVNRLFIAACDRCGQE-RGVDWVGGSVIVDADG 227
Cdd:PLN02798 165 DLRFPElYQQLRFEHGAQVLLVP---SAFTKPTGEAHWEVL-LRARAIETQCYVIAAAQAGKHnEKRESYGHALIIDPWG 240
                        250       260       270
                 ....*....|....*....|....*....|
gi 15597270  228 Y---PLDGPLQgeAGMLLARLDLAEADEKR 254
Cdd:PLN02798 241 TvvaRLPDRLS--TGIAVADIDLSLLDSVR 268
ML_beta-AS_like cd07568
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
12-270 2.78e-27

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: 106.81  E-value: 2.78e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  12 APRIGAQEHNLRLAERAIREAARRGANVVVLPELAASGYVFADRGEAL-ALAET-RDGPSLGLWKALAGELDLVIVGGFC 89
Cdd:cd07568  19 APIEKQKEAMIQKHVTMIREAAEAGAQIVCLQEIFYGPYFCAEQDTKWyEFAEEiPNGPTTKRFAALAKEYNMVLILPIY 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  90 ERLDPQRVANSAALVDADGVR-AIYRKAHL------WneESGIFEAGEQPPPVVATRFGRIAVMVCYDLEFPEWVRLPAL 162
Cdd:cd07568  99 EKEQGGTLYNTAAVIDADGTYlGKYRKNHIphvggfW--EKFYFRPGNLGYPVFDTAFGKIGVYICYDRHFPEGWRALGL 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 163 SGAQLlcapVNWPAAPRPEGERPAEVVRVQANASVNRLFIAACDRCGQERGV---DWVGGSVIVDADGYPLDGPLQGEAG 239
Cdd:cd07568 177 NGAEI----VFNPSATVAGLSEYLWKLEQPAAAVANGYFVGAINRVGTEAPWnigEFYGSSYFVDPRGQFVASASRDKDE 252
                       250       260       270
                ....*....|....*....|....*....|.
gi 15597270 240 MLLARLDLAEADEKRISAhnHVHRDRRPELY 270
Cdd:cd07568 253 LLVAELDLDLIREVRDTW--QFYRDRRPETY 281
DCase cd07569
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ...
3-270 1.32e-25

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: 102.39  E-value: 1.32e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   3 KVTVACCQIAPrIGAQEHNLRLAERAI---REAARRGANVVVLPELAASG----YVFADRGEALALAETRD-GPSLGLWK 74
Cdd:cd07569   3 QVILAAAQMGP-IARAETRESVVARLIallEEAASRGAQLVVFPELALTTffprWYFPDEAELDSFFETEMpNPETQPLF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  75 ALAGELDLVIVGGFCERLDPQRVA---NSAALVDADG-VRAIYRKAHL--------WNE----ESGIFEAGEQPPPVVAT 138
Cdd:cd07569  82 DRAKELGIGFYLGYAELTEDGGVKrrfNTSILVDKSGkIVGKYRKVHLpghkepepYRPfqhlEKRYFEPGDLGFPVFRV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 139 RFGRIAVMVCYDLEFPEWVRLPALSGAQLLCAPVNWPAAPRPEGERPAEVV-----RVQANASVNRLFIAACDRCGQERG 213
Cdd:cd07569 162 PGGIMGMCICNDRRWPETWRVMGLQGVELVLLGYNTPTHNPPAPEHDHLRLfhnllSMQAGAYQNGTWVVAAAKAGMEDG 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15597270 214 VDWVGGSVIVDADGYPLDGPLQGEAGMLLARLDLAEADEKRISAHNhVHRDRRPELY 270
Cdd:cd07569 242 CDLIGGSCIVAPTGEIVAQATTLEDEVIVADCDLDLCREGRETVFN-FARHRRPEHY 297
nitrilase_1_R2 cd07579
Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
6-188 2.69e-24

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: 98.40  E-value: 2.69e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   6 VACCQIAPRiGAQEHNLRLAERAIREAARRGANVVVLPELAASGyvfADRGEALAlaETRDGPSLGLWKALAGELDLVIV 85
Cdd:cd07579   2 IAVAQFAPT-PDIAGNLATIDRLAAEAKATGAELVVFPELALTG---LDDPASEA--ESDTGPAVSALRRLARRLRLYLV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  86 GGFCERlDPQRVANSAALVDADGVRAIYRKAHLWNEESGIFEAGEQpPPVVATRFGRIAVMVCYDLEFPEWVRLPALSGA 165
Cdd:cd07579  76 AGFAEA-DGDGLYNSAVLVGPEGLVGTYRKTHLIEPERSWATPGDT-WPVYDLPLGRVGLLIGHDALFPEAGRVLALRGC 153
                       170       180
                ....*....|....*....|...
gi 15597270 166 QLLCAPVNwPAAPRPEGERPAEV 188
Cdd:cd07579 154 DLLACPAA-IAIPFVGAHAGTSV 175
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
21-254 2.65e-21

Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily (putative class 13 nitrilases); Uncharacterized subgroup belonging to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup either represents a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. XC1258 is a homotetramer.


Pssm-ID: 143599  Cd Length: 252  Bit Score: 89.91  E-value: 2.65e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  21 NLRLAERAIrEAARRGANVVVLPELAASGYVFadrgEALALAETRDGPSLGLWKALAGELDLVIVGGFCERlDPQRVANS 100
Cdd:cd07575  18 NLAHFEEKI-EQLKEKTDLIVLPEMFTTGFSM----NAEALAEPMNGPTLQWMKAQAKKKGAAITGSLIIK-EGGKYYNR 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 101 AALVDADGVRAIYRKAHLWN--EESGIFEAGEQPppVVATRFG-RIAVMVCYDLEFPEWVRLPALSGAQLLCApvNWPaA 177
Cdd:cd07575  92 LYFVTPDGEVYHYDKRHLFRmaGEHKVYTAGNER--VIVEYKGwKILLQVCYDLRFPVWSRNTNDYDLLLYVA--NWP-A 166
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597270 178 PRpegeRPAEVVRVQANASVNRLFIAACDRCGQ-ERGVDWVGGSVIVDADGYPLdGPLQGEAGMLLARLDLAEADEKR 254
Cdd:cd07575 167 PR----RAAWDTLLKARAIENQAYVIGVNRVGTdGNGLEYSGDSAVIDPLGEPL-AEAEEDEGVLTATLDKEALQEFR 239
ScNTA1_like cd07566
Saccharomyces cerevisiae N-terminal amidase NTA1, and related proteins (class 3 nitrilases); ...
6-174 1.06e-20

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: 88.93  E-value: 1.06e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   6 VACCQIAPRIGAQEHNLRLAE----RAIREAARRGANVVVLPELAASGYVFADRGEALA-LAETRDGPSLGLWKALAGEL 80
Cdd:cd07566   2 IACLQLNPQIGQVEENLSRAWelldKTKKRAKLKKPDILVLPELALTGYNFHSLEHIKPyLEPTTSGPSFEWAREVAKKF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  81 DLVIVGGFCERLD--PQRVANSAALVDADG-VRAIYRKAHLWN-------EESGIFEAGEQPPPVVATRF--------GR 142
Cdd:cd07566  82 NCHVVIGYPEKVDesSPKLYNSALVVDPEGeVVFNYRKSFLYYtdeewgcEENPGGFQTFPLPFAKDDDFdggsvdvtLK 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 15597270 143 IAVMVCYDL-----EFP----EWVRLPALSGAQLLCAPVNW 174
Cdd:cd07566 162 TSIGICMDLnpykfEAPftdfEFATHVLDNGTELIICPMAW 202
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
14-269 1.11e-20

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: 88.80  E-value: 1.11e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  14 RIGAQEHNLRL----------AERAIREAARRGANVVVLPELAASGYV-FADRGEALALAETRDGPSLG-----LWKALA 77
Cdd:cd07574   2 RVAAAQYPLRRyasfeefaakVEYWVAEAAGYGADLLVFPEYFTMELLsLLPEAIDGLDEAIRALAALTpdyvaLFSELA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  78 GELDLVIVGGFCERLDPQRVANSAALVDADGVRAIYRKAHL--WNEESGIFEAGEqPPPVVATRFGRIAVMVCYDLEFPE 155
Cdd:cd07574  82 RKYGINIIAGSMPVREDGRLYNRAYLFGPDGTIGHQDKLHMtpFEREEWGISGGD-KLKVFDTDLGKIGILICYDSEFPE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 156 WVRLPALSGAQLLCAPVnwpAAPRPEGerpAEVVRV--QANASVNRLFIAACDRCGQERGVDWV-----GGSVIVDAD-G 227
Cdd:cd07574 161 LARALAEAGADLLLVPS---CTDTRAG---YWRVRIgaQARALENQCYVVQSGTVGNAPWSPAVdvnygQAAVYTPCDfG 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15597270 228 YPLDGPL----QGEAGMLLARLDLAEADEKRISAHNHVHRDRRPEL 269
Cdd:cd07574 235 FPEDGILaegePNTEGWLIADLDLEALRRLREEGSVRNLRDWREDL 280
nitrilases_CHs cd07564
Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases ...
4-249 4.24e-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: 84.46  E-value: 4.24e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   4 VTVACCQIAPRIGAQEHNLRLAERAIREAARRGANVVVLPELAASGY--------VFADRGEALALAE---TRDGPSLGL 72
Cdd:cd07564   1 VKVAAVQAAPVFLDLAATVEKACRLIEEAAANGAQLVVFPEAFIPGYpywiwfgaPAEGRELFARYYEnsvEVDGPELER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  73 WKALAGELDLVIVGGFCERlDPQRVANSAALVDADG-VRAIYRK----AH---LWNE--ESGIfeageqppPVVATRFGR 142
Cdd:cd07564  81 LAEAARENGIYVVLGVSER-DGGTLYNTQLLIDPDGeLLGKHRKlkptHAerlVWGQgdGSGL--------RVVDTPIGR 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 143 IAVMVCydlefpeWVRLPALS-------GAQLLCAPvnWPAAPRPEGERPAEVVRVQANASVNRLF-IAACDRCGQE--- 211
Cdd:cd07564 152 LGALIC-------WENYMPLAryalyaqGEQIHVAP--WPDFSPYYLSREAWLAASRHYALEGRCFvLSACQVVTEEdip 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15597270 212 ---------RGVDWV--GGSVIVDADGYPLDGPLQGEAGMLLARLDLAE 249
Cdd:cd07564 223 adceddeeaDPLEVLggGGSAIVGPDGEVLAGPLPDEEGILYADIDLDD 271
PRK13981 PRK13981
NAD synthetase; Provisional
4-227 9.03e-19

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 85.59  E-value: 9.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270    4 VTVACCQIAPRIGAQEHNLRLAERAIREAARRGANVVVLPELAASGY---------VFADRGEA----LAlAETRDGPSl 70
Cdd:PRK13981   1 LRIALAQLNPTVGDIAGNAAKILAAAAEAADAGADLLLFPELFLSGYppedlllrpAFLAACEAalerLA-AATAGGPA- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   71 glwkalageldlVIVGGFCERLDpqRVANSAALVDADGVRAIYRKAHLWN----EESGIFEAGEQPPPVVaTRFGRIAVM 146
Cdd:PRK13981  79 ------------VLVGHPWREGG--KLYNAAALLDGGEVLATYRKQDLPNygvfDEKRYFAPGPEPGVVE-LKGVRIGVP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  147 VCYDLEFPEWVRLPALSGAQLLcapVNWPAAPRPEGERPAEVVRVQANASVNRLFIAACDRCGqerGVDWV---GGSVIV 223
Cdd:PRK13981 144 ICEDIWNPEPAETLAEAGAELL---LVPNASPYHRGKPDLREAVLRARVRETGLPLVYLNQVG---GQDELvfdGASFVL 217

                 ....
gi 15597270  224 DADG 227
Cdd:PRK13981 218 NADG 221
GAT_Gln-NAD-synth cd07570
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ...
5-171 6.13e-17

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: 77.90  E-value: 6.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   5 TVACCQIAPRIGAQEHNLRLAERAIREAARRGANVVVLPELAASGY---------VFADRGEAlALAEtrdgpslgLWKA 75
Cdd:cd07570   1 RIALAQLNPTVGDLEGNAEKILEAIREAKAQGADLVVFPELSLTGYppedlllrpDFLEAAEE-ALEE--------LAAA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  76 LAgELDLVIVGGFCERlDPQRVANSAALVDADGVRAIYRKAHLWN----EESGIFEAGEQPPPVVATRFgRIAVMVCYDL 151
Cdd:cd07570  72 TA-DLDIAVVVGLPLR-HDGKLYNAAAVLQNGKILGVVPKQLLPNygvfDEKRYFTPGDKPDVLFFKGL-RIGVEICEDL 148
                       170       180
                ....*....|....*....|.
gi 15597270 152 EFPE-WVRLPALSGAQLLCAP 171
Cdd:cd07570 149 WVPDpPSAELALAGADLILNL 169
aliphatic_amidase cd07565
aliphatic amidases (class 2 nitrilases); Aliphatic amidases catalyze the hydrolysis of ...
4-263 4.00e-16

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: 76.17  E-value: 4.00e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   4 VTVACCQIA-PRIGAQEHNLRLAERAIR--EAARRGA---NVVVLPELAASGyVFADRGEALALAETRDGPSLGLWKALA 77
Cdd:cd07565   1 VGVAVVQYKvPVLHTKEEVLENAERIADmvEGTKRGLpgmDLIVFPEYSTQG-LMYDKWTMDETACTVPGPETDIFAEAC 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  78 GELDLVIVGGFCERLDPQRVA--NSAALVDADG-VRAIYRKAHLWNEESGiFEAGEQPPPVVATRFG-RIAVMVCYDLEF 153
Cdd:cd07565  80 KEAKVWGVFSIMERNPDHGKNpyNTAIIIDDQGeIVLKYRKLHPWVPIEP-WYPGDLGTPVCEGPKGsKIALIICHDGMY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 154 PEWVRLPALSGAQLL--CAPVNWPAaprpegeRPAEVVRVQANASVNRLFIAACDRCGQERGVDWVGGSVIVDADGYPLD 231
Cdd:cd07565 159 PEIARECAYKGAELIirIQGYMYPA-------KDQWIITNKANAWCNLMYTASVNLAGFDGVFSYFGESMIVNFDGRTLG 231
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 15597270 232 GPLQGEAGMLLARLDLAEADEKRIS--AHNHV----HR 263
Cdd:cd07565 232 EGGREPDEIVTAELSPSLVRDARKNwgSENNLyklgHR 269
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
18-173 3.82e-14

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: 70.32  E-value: 3.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  18 QEHNLRLAERAIREAARRGANVVVLPElAASGYVFADRGEALALAEtrdgpslglwKALAGELDLVIVGGFCERLDPQRV 97
Cdd:cd07571  21 RQATLDRYLDLTRELADEKPDLVVWPE-TALPFDLQRDPDALARLA----------RAARAVGAPLLTGAPRREPGGGRY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  98 ANSAALVDADG-VRAIYRKAHL-------------------WNEESGIFEAGEQPPPVVATRFGRIAVMVCYDLEFPEWV 157
Cdd:cd07571  90 YNSALLLDPGGgILGRYDKHHLvpfgeyvplrdllrflgllFDLPMGDFSPGTGPQPLLLGGGVRVGPLICYESIFPELV 169
                       170
                ....*....|....*.
gi 15597270 158 RLPALSGAQLLCAPVN 173
Cdd:cd07571 170 RDAVRQGADLLVNITN 185
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
21-254 7.02e-12

C-N hydrolase family amidase; Provisional


Pssm-ID: 182461  Cd Length: 256  Bit Score: 63.61  E-value: 7.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   21 NLRLAERAIREAARRgaNVVVLPELAASGyvFADRGEALALAETRDGPSLGLWKALAGELdlviVGGFCERLDPQRVANS 100
Cdd:PRK10438  21 NLRHFDRQLEGITGR--DVIVLPEMFTTG--FAMEAAASSLPQDDVVAWMTAKAQQTNAL----IAGSVALQTESGAVNR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  101 AALVDADGVRAIYRKAHLWN--EESGIFEAGEQPPpVVATRFGRIAVMVCYDLEFPEWVRlpALSGAQLLCAPVNWPAAP 178
Cdd:PRK10438  93 FLLVEPGGTVHFYDKRHLFRmaDEHLHYKAGNARV-IVEWRGWRILPLVCYDLRFPVWSR--NRNDYDLALYVANWPAPR 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597270  179 RPEGErpaevVRVQANASVNRLFIAACDRCGQE-RGVDWVGGSVIVDADGYPLDGPLQGEAGMLLARLDLAEADEKR 254
Cdd:PRK10438 170 SLHWQ-----TLLTARAIENQAYVAGCNRVGSDgNGHHYRGDSRIINPQGEIIATAEPHQATRIDAELSLEALQEYR 241
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
18-168 8.41e-12

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


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 64.86  E-value: 8.41e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  18 QEHNLRLAERAIREAARRGANVVVLPELAASGYvfadrgealalaETRDGPSLGLWKALAGELDL-VIVGGFCERLDPQR 96
Cdd:COG0815 215 RREILDRYLDLTRELADDGPDLVVWPETALPFL------------LDEDPDALARLAAAAREAGApLLTGAPRRDGGGGR 282
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  97 VANSAALVDADG-VRAIYRKAHL-------------------WNEESGIFEAGEQPPpVVATRFGRIAVMVCYDLEFPEW 156
Cdd:COG0815 283 YYNSALLLDPDGgILGRYDKHHLvpfgeyvplrdllrplipfLDLPLGDFSPGTGPP-VLDLGGVRVGPLICYESIFPEL 361
                       170
                ....*....|..
gi 15597270 157 VRLPALSGAQLL 168
Cdd:COG0815 362 VRDAVRAGADLL 373
PLN00202 PLN00202
beta-ureidopropionase
27-211 3.25e-10

beta-ureidopropionase


Pssm-ID: 177792  Cd Length: 405  Bit Score: 59.86  E-value: 3.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   27 RAIRE--------AARRGANVVVLPELAASGYVFADRGEALA-LAETRDGPSLGLWKALAGELDLVIVGGFCER--LDPQ 95
Cdd:PLN00202 109 RAIMDkvkpmidaAGAAGVNILCLQEAWTMPFAFCTREKRWCeFAEPVDGESTKFLQELARKYNMVIVSPILERdvNHGE 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   96 RVANSAALVDADG-VRAIYRKAHL-----WNEESGIFEaGEQPPPVVATRFGRIAVMVCYDLEFP-EWVRLpALSGAQLl 168
Cdd:PLN00202 189 TLWNTAVVIGNNGnIIGKHRKNHIprvgdFNESTYYME-GNTGHPVFETAFGKIAVNICYGRHHPlNWLAF-GLNGAEI- 265
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 15597270  169 capVNWPAAPRPEGERPAEVVRVQANASVNRLFIAACDRCGQE 211
Cdd:PLN00202 266 ---VFNPSATVGDLSEPMWPIEARNAAIANSYFVGSINRVGTE 305
nitrilase_4 cd07582
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
40-227 5.07e-09

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: 55.81  E-value: 5.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  40 VVLPELAASGYVFADRGEALAL---AETRDGPSLGLWKALAGELDLVIVGGFCERLD--PQRVANSAALVDADG-VRAIY 113
Cdd:cd07582  46 VVLPEYALQGFPMGEPREVWQFdkaAIDIPGPETEALGEKAKELNVYIAANAYERDPdfPGLYFNTAFIIDPSGeIILRY 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 114 RKAH------------LWNEESGIFEAGEQPP-PVVATRFGRIAVMVCYDLEFPEWVRLPALSGAQLLCAPVnwpaAPRP 180
Cdd:cd07582 126 RKMNslaaegspsphdVWDEYIEVYGYGLDALfPVADTEIGNLGCLACEEGLYPEVARGLAMNGAEVLLRSS----SEVP 201
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15597270 181 EGER-PAEVVRvQANASVNRLFIAACDRCGQER---GVD-WVGGSVIVDADG 227
Cdd:cd07582 202 SVELdPWEIAN-RARALENLAYVVSANSGGIYGspyPADsFGGGSMIVDYKG 252
PLN02504 PLN02504
nitrilase
25-249 7.10e-09

nitrilase


Pssm-ID: 178120  Cd Length: 346  Bit Score: 55.54  E-value: 7.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   25 AERAIREAARRGANVVVLPELAASGYvfaDRGEALALA------ETRD-------------GPSLGLWKALAGELDLVIV 85
Cdd:PLN02504  46 AERLIAEAAAYGSQLVVFPEAFIGGY---PRGSTFGLAigdrspKGREdfrkyhasaidvpGPEVDRLAAMAGKYKVYLV 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   86 GGFCERlDPQRVANSAALVDADGVR-AIYRKAHLWNEESGIFEAGE-QPPPVVATRFGRIAVMVCYDlefpewVRLPAL- 162
Cdd:PLN02504 123 MGVIER-DGYTLYCTVLFFDPQGQYlGKHRKLMPTALERLIWGFGDgSTIPVYDTPIGKIGAVICWE------NRMPLLr 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  163 -----SGAQLLCAPVnwpAAPRPEGERPAEVVRVQANASVnrlfIAACDRC----------------GQERGVD---WVG 218
Cdd:PLN02504 196 tamyaKGIEIYCAPT---ADSRETWQASMRHIALEGGCFV----LSANQFCrrkdyppppeylfsgtEEDLTPDsivCAG 268
                        250       260       270
                 ....*....|....*....|....*....|..
gi 15597270  219 GSVIVDADGYPLDGP-LQGEaGMLLARLDLAE 249
Cdd:PLN02504 269 GSVIISPSGTVLAGPnYEGE-GLITADLDLGE 299
amiF PRK13287
formamidase; Provisional
32-256 2.15e-08

formamidase; Provisional


Pssm-ID: 183950  Cd Length: 333  Bit Score: 54.31  E-value: 2.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   32 AARRGANVVVLPELAASGyVFADRGEALALAETRDGPSLGLWKALAGELDLVIVGGFCER-LDPQRVANSAALVDADG-V 109
Cdd:PRK13287  48 AGYPGLDLIVFPEYSTQG-LNTKKWTTEEFLCTVDGPEVDAFAQACKENKVWGVFSIMERnPDGNEPYNTAIIIDDQGeI 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  110 RAIYRKAHLWNE-ESgiFEAGEQPPPVVATRFG-RIAVMVCYDLEFPEWVRLPALSGAQLL------CAPVN--Wpaapr 179
Cdd:PRK13287 127 ILKYRKLHPWVPvEP--WEPGDLGIPVCDGPGGsKLAVCICHDGMFPEMAREAAYKGANVMirisgySTQVReqW----- 199
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597270  180 pegerpaeVVRVQANASVNRLFIAACDRCGQERGVDWVGGSVIVDADGYPLDGPLQGEAGMLLARLDLAEADEKRIS 256
Cdd:PRK13287 200 --------ILTNRSNAWQNLMYTASVNLAGYDGVFYYFGEGQVCNFDGTTLVQGHRNPWEIVTAEVRPDLADEARLG 268
ML_beta-AS cd07587
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
29-211 3.98e-08

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: 53.52  E-value: 3.98e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270  29 IREAARRGANVVVLPELAASGYVFADRgEALA---LAET-RDGPSLGLWKALAGELDLVIVGGFCERLDPQR--VANSAA 102
Cdd:cd07587  96 IEAAAMAGVNIICFQEAWTMPFAFCTR-EKLPwceFAESaEDGPTTKFCQELAKKYNMVIVSPILERDEEHGdtIWNTAV 174
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270 103 LVDADG-VRAIYRKAHL-----WNEESGIFEaGEQPPPVVATRFGRIAVMVCYDLEFP-EWVRLpALSGAQL-------- 167
Cdd:cd07587 175 VISNSGnVLGKSRKNHIprvgdFNESTYYME-GNTGHPVFETQFGKIAVNICYGRHHPlNWLMY-GLNGAEIvfnpsatv 252
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15597270 168 --LCAPVnWPAAPRpegerpaevvrvqaNASV-NRLFIAACDRCGQE 211
Cdd:cd07587 253 gaLSEPM-WPIEAR--------------NAAIaNSYFTVGINRVGTE 284
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
19-173 9.32e-07

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: 49.28  E-value: 9.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270    19 EHNLRLAERAIREAARRgANVVVLPELAA------SGYVFADRGEALALAetrdgpslglWKALageldlvIVGGFcERL 92
Cdd:TIGR00546 181 EAILEILTSLTKQAVEK-PDLVVWPETAFpfdlenSPQKLADRLKLLVLS----------KGIP-------ILIGA-PDA 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270    93 DPQRV---ANSAALVDADG-VRAIYRKAHL--WNEE------------------SGIFEAGEqPPPVVATRFGRIAVMVC 148
Cdd:TIGR00546 242 VPGGPyhyYNSAYLVDPGGeVVQRYDKVKLvpFGEYiplgflfkwlsklffllsQEDFSRGP-GPQVLKLPGGKIAPLIC 320
                         170       180
                  ....*....|....*....|....*
gi 15597270   149 YDLEFPEWVRLPALSGAQLLCAPVN 173
Cdd:TIGR00546 321 YESIFPDLVRASARQGAELLVNLTN 345
lnt PRK00302
apolipoprotein N-acyltransferase; Reviewed
16-168 8.22e-06

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 234721 [Multi-domain]  Cd Length: 505  Bit Score: 46.80  E-value: 8.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   16 GAQEHNLRLAERAIREAARrGANVVVLPELAAsgyvfadrgeaLALAETRDGPSLGLWKALAGELDL-VIVGGFCERLDP 94
Cdd:PRK00302 238 AGLEATLQKYLDLSRPALG-PADLIIWPETAI-----------PFLLEDLPQAFLKALDDLAREKGSaLITGAPRAENKQ 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   95 QRVA--NSAALVDADGVRAIYRKAHL--------------W-----NEESGIFEAGEQPPPVVATRFGRIAVMVCYDLEF 153
Cdd:PRK00302 306 GRYDyyNSIYVLGPYGILNRYDKHHLvpfgeyvplesllrPlapffNLPMGDFSRGPYVQPPLLAKGLKLAPLICYEIIF 385
                        170
                 ....*....|....*
gi 15597270  154 PEWVRLPALSGAQLL 168
Cdd:PRK00302 386 PEEVRANVRQGADLL 400
nadE PRK02628
NAD synthetase; Reviewed
2-169 9.28e-05

NAD synthetase; Reviewed


Pssm-ID: 235057 [Multi-domain]  Cd Length: 679  Bit Score: 43.31  E-value: 9.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270    2 AKVTVACCQIapRIGAQEHNLRLAERAIREAARRGANVVVLPELAASGY----VFA-----DRGE-ALA--LAETRDgps 69
Cdd:PRK02628  13 VRVAAATPKV--RVADPAFNAARILALARRAADDGVALAVFPELSLSGYscddLFLqdtllDAVEdALAtlVEASAD--- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597270   70 lglwkalageLDLVIVGGFCERLDpQRVANSAALVDADGVRAIYRKAHLWN-----EE----SG---------------- 124
Cdd:PRK02628  88 ----------LDPLLVVGAPLRVR-HRLYNCAVVIHRGRILGVVPKSYLPNyrefyEKrwfaPGdgargetirlcgqevp 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15597270  125 -----IFEAGEQPPPVVatrfgriAVMVCYDLefpeWVRLP-----ALSGAQLLC 169
Cdd:PRK02628 157 fgtdlLFEAEDLPGFVF-------GVEICEDL----WVPIPpssyaALAGATVLA 200
 
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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