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Conserved domains on  [gi|639204049|ref|WP_024542416|]
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MULTISPECIES: hypothetical protein [Ralstonia]

Protein Classification

carbon-nitrogen hydrolase family protein( domain architecture ID 27728)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
nitrilase super family cl11424
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
62-425 3.07e-39

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.


The actual alignment was detected with superfamily member PRK13825:

Pssm-ID: 448250 [Multi-domain]  Cd Length: 388  Bit Score: 145.16  E-value: 3.07e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049  62 ALLSMTLAFRP----KHRRRDVALLFFGWYLGAGSAIPSLWTGFFAGSVAPGVMAWLGWALIMAAPF-LLAPRGRPWIG- 135
Cdd:PRK13825  28 LLLPLALAFPVlwanSPSRLAAALVSAGYFLAASRGLPQGVAAFFGSDLWPGLALWLAASLSFVLVHaALWTAPRGRARa 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049 136 --ILCGLSLGAVPPLGILGMASPLLAAGALFPGWGLAGVALIAALLAIAswssTARTSgnKAVTAALIAALLWGALQAAT 213
Cdd:PRK13825 108 lrYLLAAVLMAVPPFGITGWAHPLTAAGVLFPGWGWWGLGATAAGLAGL----TTRLW--PAVAIALVGLWLWSAAAWTL 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049 214 YRLPA---APDLAWAMTtyLGDYPEALQQRfarqdDLKAQVRRAIDEGARLIVLPEGANAQWNDGQAFYWSDiaELARkK 290
Cdd:PRK13825 182 PRAPAgwvGVDTQLGRS--LGRDASLERRR-----ELIATVRAAAAAGARVVVLPESALGFWTPTTERLWRE--SLRG-S 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049 291 KATVLLGVYETDPltqhDGRDTLLDLVTDQH----YTAQMPMPIGMWRPWADE-----HYPMRAPGGGLQTRYGP-ALIS 360
Cdd:PRK13825 252 DVTVIAGAAVVDP----GGYDNVLVAISAGGgrilYRERMPVPVSMWQPWRPWtgqggGARAHFFANPVVEIDGRrAAPL 327
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 639204049 361 ICYEDLLLWPLIAQRLQmtahgtTPALLISAANQWFAHDGNAVA-QTRAIGMQARIWGVPLLRAVN 425
Cdd:PRK13825 328 ICYEQLLVWPVLQSMLH------SPDVIVAVGNGWWTKGTSIVAiQRASAEAWARLFGVPLVRAFN 387
 
Name Accession Description Interval E-value
PRK13825 PRK13825
conjugal transfer protein TraB; Provisional
62-425 3.07e-39

conjugal transfer protein TraB; Provisional


Pssm-ID: 237523 [Multi-domain]  Cd Length: 388  Bit Score: 145.16  E-value: 3.07e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049  62 ALLSMTLAFRP----KHRRRDVALLFFGWYLGAGSAIPSLWTGFFAGSVAPGVMAWLGWALIMAAPF-LLAPRGRPWIG- 135
Cdd:PRK13825  28 LLLPLALAFPVlwanSPSRLAAALVSAGYFLAASRGLPQGVAAFFGSDLWPGLALWLAASLSFVLVHaALWTAPRGRARa 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049 136 --ILCGLSLGAVPPLGILGMASPLLAAGALFPGWGLAGVALIAALLAIAswssTARTSgnKAVTAALIAALLWGALQAAT 213
Cdd:PRK13825 108 lrYLLAAVLMAVPPFGITGWAHPLTAAGVLFPGWGWWGLGATAAGLAGL----TTRLW--PAVAIALVGLWLWSAAAWTL 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049 214 YRLPA---APDLAWAMTtyLGDYPEALQQRfarqdDLKAQVRRAIDEGARLIVLPEGANAQWNDGQAFYWSDiaELARkK 290
Cdd:PRK13825 182 PRAPAgwvGVDTQLGRS--LGRDASLERRR-----ELIATVRAAAAAGARVVVLPESALGFWTPTTERLWRE--SLRG-S 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049 291 KATVLLGVYETDPltqhDGRDTLLDLVTDQH----YTAQMPMPIGMWRPWADE-----HYPMRAPGGGLQTRYGP-ALIS 360
Cdd:PRK13825 252 DVTVIAGAAVVDP----GGYDNVLVAISAGGgrilYRERMPVPVSMWQPWRPWtgqggGARAHFFANPVVEIDGRrAAPL 327
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 639204049 361 ICYEDLLLWPLIAQRLQmtahgtTPALLISAANQWFAHDGNAVA-QTRAIGMQARIWGVPLLRAVN 425
Cdd:PRK13825 328 ICYEQLLVWPVLQSMLH------SPDVIVAVGNGWWTKGTSIVAiQRASAEAWARLFGVPLVRAFN 387
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
228-425 1.91e-05

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: 46.05  E-value: 1.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049 228 TYLGDYPEALQQRFARQDDLkaqVRRAIDEGARLIVLPEGANAQWNDGQAFYWSDIAELARKKKATVLLGVYETDPLTQH 307
Cdd:cd07571   12 QDEKWDPEQRQATLDRYLDL---TRELADEKPDLVVWPETALPFDLQRDPDALARLARAARAVGAPLLTGAPRREPGGGR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049 308 DgRDTLLdLVTDQHYTAQ-------------MPMPiGMWRPWADEHYPM---RAPGGGLQT----RYGPALISICYEDll 367
Cdd:cd07571   89 Y-YNSAL-LLDPGGGILGrydkhhlvpfgeyVPLR-DLLRFLGLLFDLPmgdFSPGTGPQPlllgGGVRVGPLICYES-- 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639204049 368 LWPLIAQrlQMTAHGttPALLISAANQ-WFahdGN--------AVAQTRAI--GMqariwgvPLLRAVN 425
Cdd:cd07571  164 IFPELVR--DAVRQG--ADLLVNITNDaWF---GDsagpyqhlAMARLRAIetGR-------PLVRAAN 218
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
57-366 2.97e-05

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


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 45.99  E-value: 2.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049  57 MLFGFALLsmTLAFRPKHRRRDVALLffGWYLGAGSAIPSLW-----TGFFAGSVAP-GVMAWLGWALIMAAPFLLA--- 127
Cdd:COG0815    8 AFVALAPL--LLLLRGARSPRRAFLL--GWLFGLGFFLAGLYwlyvsLHVFGGLPAWlAPLAVLLLAAYLALFFALAaal 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049 128 ----PRGRPWIGILCGLSL--------GAVP---PLGILGMA----SPLLAAGALFPGWGLAGVALIAALLAIASWssTA 188
Cdd:COG0815   84 arrlRRRGGLLRPLAFAALwvllewlrGWLFtgfPWLRLGYSqadfSPLAQLAPLGGVYGLSFLVVLVNALLALAL--LR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049 189 RTSGNKAVTAALIAALLWGALQAATYRLPAAPDLAWAM-----TTYLGDYPEALQQRFARQDDLkaqVRRAIDEGARLIV 263
Cdd:COG0815  162 RRRRLAALALALALLLAALRLSPVPWTEPAGEPLRVALvqgniPQDLKWDPEQRREILDRYLDL---TRELADDGPDLVV 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049 264 LPEGANAQWNDGQAFYWSDIAELARKKKATVLLGVYETDPLTQHDgRDTLL----DLVTDQHYTAQMPMPIG-------M 332
Cdd:COG0815  239 WPETALPFLLDEDPDALARLAAAAREAGAPLLTGAPRRDGGGGRY-YNSALlldpDGGILGRYDKHHLVPFGeyvplrdL 317
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 639204049 333 WRPWADE-HYPMR--APGGG---LQTRYGPALISICYEDL 366
Cdd:COG0815  318 LRPLIPFlDLPLGdfSPGTGppvLDLGGVRVGPLICYESI 357
 
Name Accession Description Interval E-value
PRK13825 PRK13825
conjugal transfer protein TraB; Provisional
62-425 3.07e-39

conjugal transfer protein TraB; Provisional


Pssm-ID: 237523 [Multi-domain]  Cd Length: 388  Bit Score: 145.16  E-value: 3.07e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049  62 ALLSMTLAFRP----KHRRRDVALLFFGWYLGAGSAIPSLWTGFFAGSVAPGVMAWLGWALIMAAPF-LLAPRGRPWIG- 135
Cdd:PRK13825  28 LLLPLALAFPVlwanSPSRLAAALVSAGYFLAASRGLPQGVAAFFGSDLWPGLALWLAASLSFVLVHaALWTAPRGRARa 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049 136 --ILCGLSLGAVPPLGILGMASPLLAAGALFPGWGLAGVALIAALLAIAswssTARTSgnKAVTAALIAALLWGALQAAT 213
Cdd:PRK13825 108 lrYLLAAVLMAVPPFGITGWAHPLTAAGVLFPGWGWWGLGATAAGLAGL----TTRLW--PAVAIALVGLWLWSAAAWTL 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049 214 YRLPA---APDLAWAMTtyLGDYPEALQQRfarqdDLKAQVRRAIDEGARLIVLPEGANAQWNDGQAFYWSDiaELARkK 290
Cdd:PRK13825 182 PRAPAgwvGVDTQLGRS--LGRDASLERRR-----ELIATVRAAAAAGARVVVLPESALGFWTPTTERLWRE--SLRG-S 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049 291 KATVLLGVYETDPltqhDGRDTLLDLVTDQH----YTAQMPMPIGMWRPWADE-----HYPMRAPGGGLQTRYGP-ALIS 360
Cdd:PRK13825 252 DVTVIAGAAVVDP----GGYDNVLVAISAGGgrilYRERMPVPVSMWQPWRPWtgqggGARAHFFANPVVEIDGRrAAPL 327
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 639204049 361 ICYEDLLLWPLIAQRLQmtahgtTPALLISAANQWFAHDGNAVA-QTRAIGMQARIWGVPLLRAVN 425
Cdd:PRK13825 328 ICYEQLLVWPVLQSMLH------SPDVIVAVGNGWWTKGTSIVAiQRASAEAWARLFGVPLVRAFN 387
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
228-425 1.91e-05

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: 46.05  E-value: 1.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049 228 TYLGDYPEALQQRFARQDDLkaqVRRAIDEGARLIVLPEGANAQWNDGQAFYWSDIAELARKKKATVLLGVYETDPLTQH 307
Cdd:cd07571   12 QDEKWDPEQRQATLDRYLDL---TRELADEKPDLVVWPETALPFDLQRDPDALARLARAARAVGAPLLTGAPRREPGGGR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049 308 DgRDTLLdLVTDQHYTAQ-------------MPMPiGMWRPWADEHYPM---RAPGGGLQT----RYGPALISICYEDll 367
Cdd:cd07571   89 Y-YNSAL-LLDPGGGILGrydkhhlvpfgeyVPLR-DLLRFLGLLFDLPmgdFSPGTGPQPlllgGGVRVGPLICYES-- 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639204049 368 LWPLIAQrlQMTAHGttPALLISAANQ-WFahdGN--------AVAQTRAI--GMqariwgvPLLRAVN 425
Cdd:cd07571  164 IFPELVR--DAVRQG--ADLLVNITNDaWF---GDsagpyqhlAMARLRAIetGR-------PLVRAAN 218
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
57-366 2.97e-05

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


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 45.99  E-value: 2.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049  57 MLFGFALLsmTLAFRPKHRRRDVALLffGWYLGAGSAIPSLW-----TGFFAGSVAP-GVMAWLGWALIMAAPFLLA--- 127
Cdd:COG0815    8 AFVALAPL--LLLLRGARSPRRAFLL--GWLFGLGFFLAGLYwlyvsLHVFGGLPAWlAPLAVLLLAAYLALFFALAaal 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049 128 ----PRGRPWIGILCGLSL--------GAVP---PLGILGMA----SPLLAAGALFPGWGLAGVALIAALLAIASWssTA 188
Cdd:COG0815   84 arrlRRRGGLLRPLAFAALwvllewlrGWLFtgfPWLRLGYSqadfSPLAQLAPLGGVYGLSFLVVLVNALLALAL--LR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049 189 RTSGNKAVTAALIAALLWGALQAATYRLPAAPDLAWAM-----TTYLGDYPEALQQRFARQDDLkaqVRRAIDEGARLIV 263
Cdd:COG0815  162 RRRRLAALALALALLLAALRLSPVPWTEPAGEPLRVALvqgniPQDLKWDPEQRREILDRYLDL---TRELADDGPDLVV 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049 264 LPEGANAQWNDGQAFYWSDIAELARKKKATVLLGVYETDPLTQHDgRDTLL----DLVTDQHYTAQMPMPIG-------M 332
Cdd:COG0815  239 WPETALPFLLDEDPDALARLAAAAREAGAPLLTGAPRRDGGGGRY-YNSALlldpDGGILGRYDKHHLVPFGeyvplrdL 317
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 639204049 333 WRPWADE-HYPMR--APGGG---LQTRYGPALISICYEDL 366
Cdd:COG0815  318 LRPLIPFlDLPLGdfSPGTGppvLDLGGVRVGPLICYESI 357
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
247-409 1.32e-03

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 40.23  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049 247 LKAQVRRAIDEGARLIVLPEGAN-------------AQWNDGQAFYWsdIAELARKKKATVLLGVYETDP---------L 304
Cdd:COG0388   23 IEELIREAAAQGADLVVFPELFLtgyppedddllelAEPLDGPALAA--LAELARELGIAVVVGLPERDEggrlyntalV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639204049 305 TQHDGRdtlldLVTdqHYTAQMPMPIGMWrpwaDEHYPMrAPGGGLQ---TRYGPALISICYEdlLLWPLIAQRLqmTAH 381
Cdd:COG0388  101 IDPDGE-----ILG--RYRKIHLPNYGVF----DEKRYF-TPGDELVvfdTDGGRIGVLICYD--LWFPELARAL--ALA 164
                        170       180       190
                 ....*....|....*....|....*....|..
gi 639204049 382 GTTpALLISAAnqWFAHDGNA----VAQTRAI 409
Cdd:COG0388  165 GAD-LLLVPSA--SPFGRGKDhwelLLRARAI 193
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
251-314 5.03e-03

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: 38.33  E-value: 5.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 639204049 251 VRRAIDEGARLIVLPEGANAQWNDGQAFYW-----------SDIAELARKKKATVLLGVYETDPltqhDGR--DTLL 314
Cdd:cd07581   23 LAEAAAAGADLVVFPEYTMARFGDGLDDYArvaepldgpfvSALARLARELGITVVAGMFEPAG----DGRvyNTLV 95
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
247-303 8.37e-03

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: 37.69  E-value: 8.37e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 639204049 247 LKAQVRRAIDEGARLIVLPEGAN--------------AQWNDGQAFYWsdIAELARKKKATVLLGVYETDP 303
Cdd:cd07197   20 ALRLIKEAAEQGADLIVLPELFLtgysfesakedldlAEELDGPTLEA--LAELAKELGIYIVAGIAEKDG 88
 
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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