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Conserved domains on  [gi|507085480|ref|WP_016156222|]
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MULTISPECIES: carbon-nitrogen hydrolase family protein [Citrobacter]

Protein Classification

carbon-nitrogen hydrolase family protein( domain architecture ID 10466655)

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
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
 5-195 7.25e-15

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: 71.23  E-value: 7.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085480    5 KIAAAQYEPLQTSVTEHVAHHLQFIQAAAQCQCELLVFPSLSLLGCVDENDALPA--PPDEALLEPLAHAAVTYRMTIIA 82
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQKALELIEEAARYGADLIVLPELFITGYPCWAHFLEAaeVGDGETLAGLAALARKNGIAIVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085480   83 GLSVE--HNNRFVKGIALFSPWMTSPLTFHQSH-----------GACIARQQNAISVVDSQ--------------PE--- 132
Cdd:pfam00795  81 GLIERwlTGGRLYNTAVLLDPDGKLVGKYRKLHlfpeprppgfrERVLFEPGDGGTVFDTPlgkigaaicyeirfPEllr 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507085480  133 -----GIDIDPAYS-LFTSSQSVSEPELLSSTSRLQSFSHKFAIAVLMANAR-------GSSALWDEQGRLIVRAD 195
Cdd:pfam00795 161 alalkGAEILINPSaRAPFPGSLGPPQWLLLARARALENGCFVIAANQVGGEedapwpyGHSMIIDPDGRILAGAG 236
 
Name Accession Description Interval E-value
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
 5-195 7.25e-15

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: 71.23  E-value: 7.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085480    5 KIAAAQYEPLQTSVTEHVAHHLQFIQAAAQCQCELLVFPSLSLLGCVDENDALPA--PPDEALLEPLAHAAVTYRMTIIA 82
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQKALELIEEAARYGADLIVLPELFITGYPCWAHFLEAaeVGDGETLAGLAALARKNGIAIVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085480   83 GLSVE--HNNRFVKGIALFSPWMTSPLTFHQSH-----------GACIARQQNAISVVDSQ--------------PE--- 132
Cdd:pfam00795  81 GLIERwlTGGRLYNTAVLLDPDGKLVGKYRKLHlfpeprppgfrERVLFEPGDGGTVFDTPlgkigaaicyeirfPEllr 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507085480  133 -----GIDIDPAYS-LFTSSQSVSEPELLSSTSRLQSFSHKFAIAVLMANAR-------GSSALWDEQGRLIVRAD 195
Cdd:pfam00795 161 alalkGAEILINPSaRAPFPGSLGPPQWLLLARARALENGCFVIAANQVGGEedapwpyGHSMIIDPDGRILAGAG 236
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
5-101 5.38e-12

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 63.34  E-value: 5.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085480   5 KIAAAQYEPLQTSVTEHVAHHLQFIQAAAQCQCELLVFPSLSLLG--CVDENDALPAPP-DEALLEPLAHAAVTYRMTII 81
Cdd:COG0388    3 RIALAQLNPTVGDIEANLAKIEELIREAAAQGADLVVFPELFLTGypPEDDDLLELAEPlDGPALAALAELARELGIAVV 82

                         90       100
                 ....*....|....*....|.
gi 507085480  82 AGLSVE-HNNRFVKGIALFSP 101
Cdd:COG0388   83 VGLPERdEGGRLYNTALVIDP 103
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
 6-101 1.34e-09

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: 56.18  E-value: 1.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085480   6 IAAAQYEPLQTSVTEHVAHHLQFIQAAAQCQCELLVFPSLSLLG--CVDENDALPA--PPDEALLEPLAHAAVTYRMTII 81
Cdd:cd07197    1 IAAVQLAPKIGDVEANLAKALRLIKEAAEQGADLIVLPELFLTGysFESAKEDLDLaeELDGPTLEALAELAKELGIYIV 80

                         90       100
                 ....*....|....*....|
gi 507085480  82 AGLSVEHNNRFVKGIALFSP 101
Cdd:cd07197   81 AGIAEKDGDKLYNTAVVIDP 100
 
Name Accession Description Interval E-value
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
 5-195 7.25e-15

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: 71.23  E-value: 7.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085480    5 KIAAAQYEPLQTSVTEHVAHHLQFIQAAAQCQCELLVFPSLSLLGCVDENDALPA--PPDEALLEPLAHAAVTYRMTIIA 82
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQKALELIEEAARYGADLIVLPELFITGYPCWAHFLEAaeVGDGETLAGLAALARKNGIAIVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085480   83 GLSVE--HNNRFVKGIALFSPWMTSPLTFHQSH-----------GACIARQQNAISVVDSQ--------------PE--- 132
Cdd:pfam00795  81 GLIERwlTGGRLYNTAVLLDPDGKLVGKYRKLHlfpeprppgfrERVLFEPGDGGTVFDTPlgkigaaicyeirfPEllr 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507085480  133 -----GIDIDPAYS-LFTSSQSVSEPELLSSTSRLQSFSHKFAIAVLMANAR-------GSSALWDEQGRLIVRAD 195
Cdd:pfam00795 161 alalkGAEILINPSaRAPFPGSLGPPQWLLLARARALENGCFVIAANQVGGEedapwpyGHSMIIDPDGRILAGAG 236
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
5-101 5.38e-12

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 63.34  E-value: 5.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085480   5 KIAAAQYEPLQTSVTEHVAHHLQFIQAAAQCQCELLVFPSLSLLG--CVDENDALPAPP-DEALLEPLAHAAVTYRMTII 81
Cdd:COG0388    3 RIALAQLNPTVGDIEANLAKIEELIREAAAQGADLVVFPELFLTGypPEDDDLLELAEPlDGPALAALAELARELGIAVV 82

                         90       100
                 ....*....|....*....|.
gi 507085480  82 AGLSVE-HNNRFVKGIALFSP 101
Cdd:COG0388   83 VGLPERdEGGRLYNTALVIDP 103
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
 6-101 1.34e-09

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: 56.18  E-value: 1.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085480   6 IAAAQYEPLQTSVTEHVAHHLQFIQAAAQCQCELLVFPSLSLLG--CVDENDALPA--PPDEALLEPLAHAAVTYRMTII 81
Cdd:cd07197    1 IAAVQLAPKIGDVEANLAKALRLIKEAAEQGADLIVLPELFLTGysFESAKEDLDLaeELDGPTLEALAELAKELGIYIV 80

                         90       100
                 ....*....|....*....|
gi 507085480  82 AGLSVEHNNRFVKGIALFSP 101
Cdd:cd07197   81 AGIAEKDGDKLYNTAVVIDP 100
nitrilase_8 cd07586
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 5-84 3.88e-07

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: 49.21  E-value: 3.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085480   5 KIAAAQYEPLQTSVTEHVAHHLQFIQAAAQCQCELLVFPSLSLLGCVDENDALPA--PPDEALLEPLAHAAVtyRMTIIA 82
Cdd:cd07586    1 RVAIAQIDPVLGDVEENLEKHLEIIETARERGADLVVFPELSLTGYNLGDLVYEVamHADDPRLQALAEASG--GICVVF 78


                 ..
gi 507085480  83 GL 84
Cdd:cd07586   79 GF 80
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 5-88 2.27e-06

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


Pssm-ID: 143609  Cd Length: 261  Bit Score: 46.93  E-value: 2.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085480   5 KIAAAQYEPLQTSVTEHVAHHLQFIQAAAQCQCELLVFPSLSLLG-CVDENDALPAPPD--EALLEpLAHAAVTYRMTII 81
Cdd:cd07585    1 RIALVQFEARVGDKARNLAVIARWTRKAAAQGAELVCFPEMCITGyTHVRALSREAEVPdgPSTQA-LSDLARRYGLTIL 79


                 ....*..
gi 507085480  82 AGLsVEH 88
Cdd:cd07585   80 AGL-IEK 85
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 5-92 5.71e-06

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


Pssm-ID: 143607  Cd Length: 253  Bit Score: 45.61  E-value: 5.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085480   5 KIAAAQYEPLQTSVTEHVAHHLQFIQAAAQCQCELLVFPSLSLLG-CVDENDALPAPPDEALLEPLAHAAVTYRMTIIAG 83
Cdd:cd07583    1 KIALIQLDIVWGDPEANIERVESLIEEAAAAGADLIVLPEMWNTGyFLDDLYELADEDGGETVSFLSELAKKHGVNIVAG 80

                         90
                 ....*....|
gi 507085480  84 -LSVEHNNRF 92
Cdd:cd07583   81 sVAEKEGGKL 90
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
 5-101 7.44e-06

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: 45.65  E-value: 7.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085480   5 KIAAAQYEPLQTSVTEHVAHHL-QFIQAAAQCQCELLVFP---SLSLLGCVDE-----NDALPAPPD--EALLEPLAHAA 73
Cdd:cd07574    2 RVAAAQYPLRRYASFEEFAAKVeYWVAEAAGYGADLLVFPeyfTMELLSLLPEaidglDEAIRALAAltPDYVALFSELA 81

                         90       100
                 ....*....|....*....|....*....
gi 507085480  74 VTYRMTIIAG-LSVEHNNRFVKGIALFSP 101
Cdd:cd07574   82 RKYGINIIAGsMPVREDGRLYNRAYLFGP 110
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
 5-113 3.04e-05

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: 43.72  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085480   5 KIAAAQYEPLQTSVTEHVAHHLQFIQAAAQCQCELLVFPSLSLLGCV--DENDALPAPPDEALLEPLAHAAVTYRMTIIA 82
Cdd:cd07576    1 RLALYQGPARDGDVAANLARLDEAAARAAAAGADLLVFPELFLTGYNigDAVARLAEPADGPALQALRAIARRHGIAIVV 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 507085480  83 GLSVEHNNRFVKGIALFSPWMTSPLTFHQSH 113
Cdd:cd07576   81 GYPERAGGAVYNAAVLIDEDGTVLANYRKTH 111
GAT_Gln-NAD-synth cd07570
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ...
 5-91 4.21e-05

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: 43.23  E-value: 4.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085480   5 KIAAAQYEPLQTSVTEHVAHHLQFIQAAAQCQCELLVFPSLSLLGcvdendalpAPPDEALLEP------------LAHA 72
Cdd:cd07570    1 RIALAQLNPTVGDLEGNAEKILEAIREAKAQGADLVVFPELSLTG---------YPPEDLLLRPdfleaaeealeeLAAA 71

                         90
                 ....*....|....*....
gi 507085480  73 AVTYRMTIIAGLSVEHNNR 91
Cdd:cd07570   72 TADLDIAVVVGLPLRHDGK 90
nitrilase_1_R2 cd07579
Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
 5-101 2.35e-03

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: 37.92  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085480   5 KIAAAQYEPlQTSVTEHVAHHLQFIQAAAQCQCELLVFPSLSLLGcVDENDALPAPPDEALLEPLAHAAVTYRMTIIAGL 84
Cdd:cd07579    1 RIAVAQFAP-TPDIAGNLATIDRLAAEAKATGAELVVFPELALTG-LDDPASEAESDTGPAVSALRRLARRLRLYLVAGF 78

                         90
                 ....*....|....*..
gi 507085480  85 SVEHNNRFVKGIALFSP 101
Cdd:cd07579   79 AEADGDGLYNSAVLVGP 95
 
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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