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Conserved domains on  [gi|696367412|ref|WP_032942424|]
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MULTISPECIES: amidohydrolase [Citrobacter]

Protein Classification

nitrilase family protein( domain architecture ID 10013522)

nitrilase family protein is a member of a large superfamily and predicted to act as a carbon-nitrogen hydrolase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
1-255 0e+00

C-N hydrolase family amidase; Provisional


:

Pssm-ID: 182461  Cd Length: 256  Bit Score: 565.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412   1 MPGLKITLLQQPLIWMDGPANLRHFDRQLETVAGRDVIVLPEMFTSGFAMEAANKSLPQEEVVSWMRVKAQQTNALIAGS 80
Cdd:PRK10438   1 MSGLKITLLQQPLVWMDGPANLRHFDRQLEGITGRDVIVLPEMFTTGFAMEAAASSLPQDDVVAWMTAKAQQTNALIAGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  81 AAIQSERGPVNRFFLVEPEGNVHFYDKRHLFRMADEHQHYQAGDARVIVEWRGWRILPLVCYDLRFPVWSRNRNDYDLAL 160
Cdd:PRK10438  81 VALQTESGAVNRFLLVEPGGTVHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNRNDYDLAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 161 YVANWPAPRSLHWQLLLAARAIENQAYVAGCNRVGTDGNGHHYRGDSRVINPQGEIIATAEPHQATRIDAELSLSALREY 240
Cdd:PRK10438 161 YVANWPAPRSLHWQTLLTARAIENQAYVAGCNRVGSDGNGHHYRGDSRIINPQGEIIATAEPHQATRIDAELSLEALQEY 240
                        250
                 ....*....|....*
gi 696367412 241 REKFPAWQDADPFTL 255
Cdd:PRK10438 241 REKFPAWRDADEFTL 255
 
Name Accession Description Interval E-value
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
1-255 0e+00

C-N hydrolase family amidase; Provisional


Pssm-ID: 182461  Cd Length: 256  Bit Score: 565.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412   1 MPGLKITLLQQPLIWMDGPANLRHFDRQLETVAGRDVIVLPEMFTSGFAMEAANKSLPQEEVVSWMRVKAQQTNALIAGS 80
Cdd:PRK10438   1 MSGLKITLLQQPLVWMDGPANLRHFDRQLEGITGRDVIVLPEMFTTGFAMEAAASSLPQDDVVAWMTAKAQQTNALIAGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  81 AAIQSERGPVNRFFLVEPEGNVHFYDKRHLFRMADEHQHYQAGDARVIVEWRGWRILPLVCYDLRFPVWSRNRNDYDLAL 160
Cdd:PRK10438  81 VALQTESGAVNRFLLVEPGGTVHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNRNDYDLAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 161 YVANWPAPRSLHWQLLLAARAIENQAYVAGCNRVGTDGNGHHYRGDSRVINPQGEIIATAEPHQATRIDAELSLSALREY 240
Cdd:PRK10438 161 YVANWPAPRSLHWQTLLTARAIENQAYVAGCNRVGSDGNGHHYRGDSRIINPQGEIIATAEPHQATRIDAELSLEALQEY 240
                        250
                 ....*....|....*
gi 696367412 241 REKFPAWQDADPFTL 255
Cdd:PRK10438 241 REKFPAWRDADEFTL 255
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
4-254 4.65e-153

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: 426.18  E-value: 4.65e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412   4 LKITLLQQPLIWMDGPANLRHFDRQLETVAGR-DVIVLPEMFTSGFAMEAANKSLP-QEEVVSWMRVKAQQTNALIAGSA 81
Cdd:cd07575    1 LKIALIQTDLVWEDPEANLAHFEEKIEQLKEKtDLIVLPEMFTTGFSMNAEALAEPmNGPTLQWMKAQAKKKGAAITGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  82 AIQSERGPVNRFFLVEPEGNVHFYDKRHLFRMADEHQHYQAGDARVIVEWRGWRILPLVCYDLRFPVWSRNRNDYDLALY 161
Cdd:cd07575   81 IIKEGGKYYNRLYFVTPDGEVYHYDKRHLFRMAGEHKVYTAGNERVIVEYKGWKILLQVCYDLRFPVWSRNTNDYDLLLY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 162 VANWPAPRSLHWQLLLAARAIENQAYVAGCNRVGTDGNGHHYRGDSRVINPQGEIIATAEPHQATRIdAELSLSALREYR 241
Cdd:cd07575  161 VANWPAPRRAAWDTLLKARAIENQAYVIGVNRVGTDGNGLEYSGDSAVIDPLGEPLAEAEEDEGVLT-ATLDKEALQEFR 239
                        250
                 ....*....|...
gi 696367412 242 EKFPAWQDADPFT 254
Cdd:cd07575  240 EKFPFLKDADSFT 252
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
4-253 3.28e-74

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 226.67  E-value: 3.28e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412   4 LKITLLQQPLIWMDGPANLRHFDRQLETVAGR--DVIVLPEMFTSGFAMEAANKSLPQEEV----VSWMRVKAQQTNALI 77
Cdd:COG0388    2 MRIALAQLNPTVGDIEANLAKIEELIREAAAQgaDLVVFPELFLTGYPPEDDDLLELAEPLdgpaLAALAELARELGIAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  78 AGSAAIQSERGPV-NRFFLVEPEGN-VHFYDKRHLFRM--ADEHQHYQAGDARVIVEWRGWRILPLVCYDLRFPVWSRN- 152
Cdd:COG0388   82 VVGLPERDEGGRLyNTALVIDPDGEiLGRYRKIHLPNYgvFDEKRYFTPGDELVVFDTDGGRIGVLICYDLWFPELARAl 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 153 -RNDYDLALYVANWPAPRSL-HWQLLLAARAIENQAYVAGCNRVGTDGnGHHYRGDSRVINPQGEIIATAePHQATRIDA 230
Cdd:COG0388  162 aLAGADLLLVPSASPFGRGKdHWELLLRARAIENGCYVVAANQVGGED-GLVFDGGSMIVDPDGEVLAEA-GDEEGLLVA 239
                        250       260
                 ....*....|....*....|...
gi 696367412 231 ELSLSALREYREKFPAWQDADPF 253
Cdd:COG0388  240 DIDLDRLREARRRFPVLRDRRPD 262
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
5-241 6.50e-31

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: 115.15  E-value: 6.50e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412    5 KITLLQQPLIWMDGPANLRHFDRQLETVAGR--DVIVLPEMFTSGFAMEA---ANKSLPQEEVVSWMRVKAQQTNALIAG 79
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQKALELIEEAARYgaDLIVLPELFITGYPCWAhflEAAEVGDGETLAGLAALARKNGIAIVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412   80 SAAIQSERGPV--NRFFLVEPEGNVHF-YDKRHLFRMAD-----EHQHYQAGDARVIVEWRGWRILPLVCYDLRFPVWSR 151
Cdd:pfam00795  81 GLIERWLTGGRlyNTAVLLDPDGKLVGkYRKLHLFPEPRppgfrERVLFEPGDGGTVFDTPLGKIGAAICYEIRFPELLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  152 --NRNDYDLALYVAN----WPAPRSLHWQLLLAARAIENQAYVAGCNRVGTDGNGHHYRGDSRVINPQGEIIATAEPHQA 225
Cdd:pfam00795 161 alALKGAEILINPSArapfPGSLGPPQWLLLARARALENGCFVIAANQVGGEEDAPWPYGHSMIIDPDGRILAGAGEWEE 240
                         250
                  ....*....|....*.
gi 696367412  226 TRIDAELSLSALREYR 241
Cdd:pfam00795 241 GVLIADIDLALVRAWR 256
de_GSH_amidase NF033621
deaminated glutathione amidase;
105-245 1.17e-14

deaminated glutathione amidase;


Pssm-ID: 468114  Cd Length: 260  Bit Score: 71.47  E-value: 1.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 105 YDKRHL---FRMaDEHQHYQAGDA-RVIVEWRGWRILPLVCYDLRFPVWSRNrndydLALYVAN---WPAP------RSL 171
Cdd:NF033621 107 YRKLHLydaFSM-QESRRVDAGNEiPPLVEVAGMKVGLMTCYDLRFPELARR-----LALDGADvlvLPAAwvrgplKEH 180
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 696367412 172 HWQLLLAARAIENQAYVAGcnrVGTDGNghhyR--GDSRVINPQGEIIATAePHQATRIDAELSLSALREYREKFP 245
Cdd:NF033621 181 HWETLLAARALENTCYMVA---VGECGN----RniGQSMVVDPLGVTIAAA-AEAPALIFAELDPERIAHAREQLP 248
 
Name Accession Description Interval E-value
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
1-255 0e+00

C-N hydrolase family amidase; Provisional


Pssm-ID: 182461  Cd Length: 256  Bit Score: 565.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412   1 MPGLKITLLQQPLIWMDGPANLRHFDRQLETVAGRDVIVLPEMFTSGFAMEAANKSLPQEEVVSWMRVKAQQTNALIAGS 80
Cdd:PRK10438   1 MSGLKITLLQQPLVWMDGPANLRHFDRQLEGITGRDVIVLPEMFTTGFAMEAAASSLPQDDVVAWMTAKAQQTNALIAGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  81 AAIQSERGPVNRFFLVEPEGNVHFYDKRHLFRMADEHQHYQAGDARVIVEWRGWRILPLVCYDLRFPVWSRNRNDYDLAL 160
Cdd:PRK10438  81 VALQTESGAVNRFLLVEPGGTVHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNRNDYDLAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 161 YVANWPAPRSLHWQLLLAARAIENQAYVAGCNRVGTDGNGHHYRGDSRVINPQGEIIATAEPHQATRIDAELSLSALREY 240
Cdd:PRK10438 161 YVANWPAPRSLHWQTLLTARAIENQAYVAGCNRVGSDGNGHHYRGDSRIINPQGEIIATAEPHQATRIDAELSLEALQEY 240
                        250
                 ....*....|....*
gi 696367412 241 REKFPAWQDADPFTL 255
Cdd:PRK10438 241 REKFPAWRDADEFTL 255
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
4-254 4.65e-153

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: 426.18  E-value: 4.65e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412   4 LKITLLQQPLIWMDGPANLRHFDRQLETVAGR-DVIVLPEMFTSGFAMEAANKSLP-QEEVVSWMRVKAQQTNALIAGSA 81
Cdd:cd07575    1 LKIALIQTDLVWEDPEANLAHFEEKIEQLKEKtDLIVLPEMFTTGFSMNAEALAEPmNGPTLQWMKAQAKKKGAAITGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  82 AIQSERGPVNRFFLVEPEGNVHFYDKRHLFRMADEHQHYQAGDARVIVEWRGWRILPLVCYDLRFPVWSRNRNDYDLALY 161
Cdd:cd07575   81 IIKEGGKYYNRLYFVTPDGEVYHYDKRHLFRMAGEHKVYTAGNERVIVEYKGWKILLQVCYDLRFPVWSRNTNDYDLLLY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 162 VANWPAPRSLHWQLLLAARAIENQAYVAGCNRVGTDGNGHHYRGDSRVINPQGEIIATAEPHQATRIdAELSLSALREYR 241
Cdd:cd07575  161 VANWPAPRRAAWDTLLKARAIENQAYVIGVNRVGTDGNGLEYSGDSAVIDPLGEPLAEAEEDEGVLT-ATLDKEALQEFR 239
                        250
                 ....*....|...
gi 696367412 242 EKFPAWQDADPFT 254
Cdd:cd07575  240 EKFPFLKDADSFT 252
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
5-249 4.63e-80

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: 241.29  E-value: 4.63e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412   5 KITLLQQPLIWMDGPANLRHFDRQLETVAGR--DVIVLPEMFTSGFAMEAANKS--LPQEEVVSWMRVKAQQTNA-LIAG 79
Cdd:cd07583    1 KIALIQLDIVWGDPEANIERVESLIEEAAAAgaDLIVLPEMWNTGYFLDDLYELadEDGGETVSFLSELAKKHGVnIVAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  80 SAAIQSERGPVNRFFLVEPEGN-VHFYDKRHLFRMADEHQHYQAGDARVIVEWRGWRILPLVCYDLRFPVWSRN--RNDY 156
Cdd:cd07583   81 SVAEKEGGKLYNTAYVIDPDGElIATYRKIHLFGLMGEDKYLTAGDELEVFELDGGKVGLFICYDLRFPELFRKlaLEGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 157 DLALYVANWPAPRSLHWQLLLAARAIENQAYVAGCNRVGTDGNGhHYRGDSRVINPQGEIIATAEPHQATrIDAELSLSA 236
Cdd:cd07583  161 EILFVPAEWPAARIEHWRTLLRARAIENQAFVVACNRVGTDGGN-EFGGHSMVIDPWGEVLAEAGEEEEI-LTAEIDLEE 238
                        250
                 ....*....|...
gi 696367412 237 LREYREKFPAWQD 249
Cdd:cd07583  239 VAEVRKKIPVFKD 251
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
4-253 3.28e-74

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 226.67  E-value: 3.28e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412   4 LKITLLQQPLIWMDGPANLRHFDRQLETVAGR--DVIVLPEMFTSGFAMEAANKSLPQEEV----VSWMRVKAQQTNALI 77
Cdd:COG0388    2 MRIALAQLNPTVGDIEANLAKIEELIREAAAQgaDLVVFPELFLTGYPPEDDDLLELAEPLdgpaLAALAELARELGIAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  78 AGSAAIQSERGPV-NRFFLVEPEGN-VHFYDKRHLFRM--ADEHQHYQAGDARVIVEWRGWRILPLVCYDLRFPVWSRN- 152
Cdd:COG0388   82 VVGLPERDEGGRLyNTALVIDPDGEiLGRYRKIHLPNYgvFDEKRYFTPGDELVVFDTDGGRIGVLICYDLWFPELARAl 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 153 -RNDYDLALYVANWPAPRSL-HWQLLLAARAIENQAYVAGCNRVGTDGnGHHYRGDSRVINPQGEIIATAePHQATRIDA 230
Cdd:COG0388  162 aLAGADLLLVPSASPFGRGKdHWELLLRARAIENGCYVVAANQVGGED-GLVFDGGSMIVDPDGEVLAEA-GDEEGLLVA 239
                        250       260
                 ....*....|....*....|...
gi 696367412 231 ELSLSALREYREKFPAWQDADPF 253
Cdd:COG0388  240 DIDLDRLREARRRFPVLRDRRPD 262
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
6-249 2.31e-59

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: 188.30  E-value: 2.31e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412   6 ITLLQQPLIWMDGPANLRHFDRQLETVA--GRDVIVLPEMFTSGFAMEAANKSLPQEE-----VVSWMRVKAQQTNALIA 78
Cdd:cd07197    1 IAAVQLAPKIGDVEANLAKALRLIKEAAeqGADLIVLPELFLTGYSFESAKEDLDLAEeldgpTLEALAELAKELGIYIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  79 GSAAIQSERGPVNRFFLVEPEGN-VHFYDKRHLFRMaDEHQHYQAGDARVIVEWRGWRILPLVCYDLRFPVWSR--NRND 155
Cdd:cd07197   81 AGIAEKDGDKLYNTAVVIDPDGEiIGKYRKIHLFDF-GERRYFSPGDEFPVFDTPGGKIGLLICYDLRFPELARelALKG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 156 YDLALYVANWPAPRSLHWQLLLAARAIENQAYVAGCNRVGTDGNGHHYrGDSRVINPQGEIIATAEPHQATRIdAELSLS 235
Cdd:cd07197  160 ADIILVPAAWPTARREHWELLLRARAIENGVYVVAANRVGEEGGLEFA-GGSMIVDPDGEVLAEASEEEGILV-AELDLD 237
                        250
                 ....*....|....
gi 696367412 236 ALREYREKFPAWQD 249
Cdd:cd07197  238 ELREARKRWSYLRD 251
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
20-248 2.65e-38

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: 134.48  E-value: 2.65e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  20 ANLRHFDRQLETVA--GRDVIVLPEMFTS----GFAMEAANKSLPQEEVVSWMRVKAQQTN-ALIAGSAAIQSERG--PV 90
Cdd:cd07572   15 ANLARAKELIEEAAaqGAKLVVLPECFNYpggtDAFKLALAEEEGDGPTLQALSELAKEHGiWLVGGSIPERDDDDgkVY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  91 NRFFLVEPEGN-VHFYDKRHLFRM--ADEHQ-----HYQAGDARVIVEWRGWRILPLVCYDLRFPVWSR--NRNDYDLAL 160
Cdd:cd07572   95 NTSLVFDPDGElVARYRKIHLFDVdvPGGISyresdTLTPGDEVVVVDTPFGKIGLGICYDLRFPELARalARQGADILT 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 161 YvanwPA-------PrsLHWQLLLAARAIENQAYVAGCNRVGTDGNGHHYRGDSRVINPQGEIIATAEPHQATrIDAELS 233
Cdd:cd07572  175 V----PAaftmttgP--AHWELLLRARAIENQCYVVAAAQAGDHEAGRETYGHSMIVDPWGEVLAEAGEGEGV-VVAEID 247
                        250
                 ....*....|....*
gi 696367412 234 LSALREYREKFPAWQ 248
Cdd:cd07572  248 LDRLEEVRRQIPVLK 262
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
5-249 2.22e-35

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: 126.54  E-value: 2.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412   5 KITLLQQPLIWMDGPANLRHFDRQLETVAGR--DVIVLPEMFTSGFAM--EAANKSLPQE-EVVSWMRVKAQQTN-ALIA 78
Cdd:cd07576    1 RLALYQGPARDGDVAANLARLDEAAARAAAAgaDLLVFPELFLTGYNIgdAVARLAEPADgPALQALRAIARRHGiAIVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  79 GSAaiqsERGPvNRFF----LVEPEGNV-HFYDKRHLFRmADEHQHYQAGDARVIVEWRGWRILPLVCYDLRFPVWSRnr 153
Cdd:cd07576   81 GYP----ERAG-GAVYnaavLIDEDGTVlANYRKTHLFG-DSERAAFTPGDRFPVVELRGLRVGLLICYDVEFPELVR-- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 154 ndyDLALYVANW---PAPRSLHW----QLLLAARAIENQAYVAGCNRVGTDGnGHHYRGDSRVINPQGEIIATAEPHqAT 226
Cdd:cd07576  153 ---ALALAGADLvlvPTALMEPYgfvaRTLVPARAFENQIFVAYANRCGAED-GLTYVGLSSIAGPDGTVLARAGRG-EA 227
                        250       260
                 ....*....|....*....|...
gi 696367412 227 RIDAELSLSALREYREKFPAWQD 249
Cdd:cd07576  228 LLVADLDPAALAAARRENPYLAD 250
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
5-241 6.50e-31

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: 115.15  E-value: 6.50e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412    5 KITLLQQPLIWMDGPANLRHFDRQLETVAGR--DVIVLPEMFTSGFAMEA---ANKSLPQEEVVSWMRVKAQQTNALIAG 79
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQKALELIEEAARYgaDLIVLPELFITGYPCWAhflEAAEVGDGETLAGLAALARKNGIAIVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412   80 SAAIQSERGPV--NRFFLVEPEGNVHF-YDKRHLFRMAD-----EHQHYQAGDARVIVEWRGWRILPLVCYDLRFPVWSR 151
Cdd:pfam00795  81 GLIERWLTGGRlyNTAVLLDPDGKLVGkYRKLHLFPEPRppgfrERVLFEPGDGGTVFDTPLGKIGAAICYEIRFPELLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  152 --NRNDYDLALYVAN----WPAPRSLHWQLLLAARAIENQAYVAGCNRVGTDGNGHHYRGDSRVINPQGEIIATAEPHQA 225
Cdd:pfam00795 161 alALKGAEILINPSArapfPGSLGPPQWLLLARARALENGCFVIAANQVGGEEDAPWPYGHSMIIDPDGRILAGAGEWEE 240
                         250
                  ....*....|....*.
gi 696367412  226 TRIDAELSLSALREYR 241
Cdd:pfam00795 241 GVLIADIDLALVRAWR 256
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
36-243 9.99e-29

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: 109.31  E-value: 9.99e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  36 DVIVLPEMFTSGFAM----EAAN--KSLPQEEVVSWMRVKAQQTNALIAGSAAIQSERGPVNRFFLVEPEGNVHFYDKRH 109
Cdd:cd07577   31 DLIVLPELFNTGYAFtskeEVASlaESIPDGPTTRFLQELARETGAYIVAGLPERDGDKFYNSAVVVGPEGYIGIYRKTH 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 110 LFRmaDEHQHYQAGD-ARVIVEWRGWRILPLVCYDLRFPVWSRNrndydLAL-------YVANWPAPrslHWQLLLAARA 181
Cdd:cd07577  111 LFY--EEKLFFEPGDtGFRVFDIGDIRIGVMICFDWYFPEAART-----LALkgadiiaHPANLVLP---YCPKAMPIRA 180
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 696367412 182 IENQAYVAGCNRVGTDGNGH---HYRGDSRVINPQGEIIATAEPHQATRIDAELSlsaLREYREK 243
Cdd:cd07577  181 LENRVFTITANRIGTEERGGetlRFIGKSQITSPKGEVLARAPEDGEEVLVAEID---PRLARDK 242
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
16-245 9.65e-28

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: 106.51  E-value: 9.65e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  16 MDGPANLRHFDRQLE--TVAGRDVIVLPE--MFTSGFAMEAANkslPQEEV-----VSWMRVKAQQTNALIAGSAAIQSE 86
Cdd:cd07581   10 GDKEENLEKVRRLLAeaAAAGADLVVFPEytMARFGDGLDDYA---RVAEPldgpfVSALARLARELGITVVAGMFEPAG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  87 RG-PVNRFFLVEPEGNVH-FYDKRHLFrmaD-----EHQHYQAGD--ARVIVEWRGWRILPLVCYDLRFPVWSRN--RND 155
Cdd:cd07581   87 DGrVYNTLVVVGPDGEIIaVYRKIHLY---DafgfrESDTVAPGDelPPVVFVVGGVKVGLATCYDLRFPELARAlaLAG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 156 YDLALYVANW-PAPRSL-HWQLLLAARAIENQAYVAGCNRVgtdgnGHHYRGDSRVINPQGEIIATAEPHQATRIdAELS 233
Cdd:cd07581  164 ADVIVVPAAWvAGPGKEeHWETLLRARALENTVYVAAAGQA-----GPRGIGRSMVVDPLGVVLADLGEREGLLV-ADID 237
                        250
                 ....*....|..
gi 696367412 234 LSALREYREKFP 245
Cdd:cd07581  238 PERVEEAREALP 249
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
5-252 1.21e-26

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: 103.99  E-value: 1.21e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412   5 KITLLQQPLIWMDGPANLR---HFDRQLETvAGRDVIVLPEMFTSGFAMEAANKSL------PQEEVVSWMRVKAQQTNA 75
Cdd:cd07584    1 KVALIQMDSVLGDVKANLKkaaELCKEAAA-EGADLICFPELATTGYRPDLLGPKLwelsepIDGPTVRLFSELAKELGV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  76 -LIAGSaaiqSERG-----PVNRFFLVEPEGN-VHFYDKRHLFrmADEHQHYQAGDARVIVEWRGWRILPLVCYDLRFPV 148
Cdd:cd07584   80 yIVCGF----VEKGgvpgkVYNSAVVIDPEGEsLGVYRKIHLW--GLEKQYFREGEQYPVFDTPFGKIGVMICYDMGFPE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 149 WSRnrndyDLALYVAN-------WPAPRSLHWQLLLAARAIENQAYVAGCNRVGTDGNGHHYrGDSRVINPQGEIIATAE 221
Cdd:cd07584  154 VAR-----ILTLKGAEvifcpsaWREQDADIWDINLPARALENTVFVAAVNRVGNEGDLVLF-GKSKILNPRGQVLAEAS 227
                        250       260       270
                 ....*....|....*....|....*....|.
gi 696367412 222 PHQATRIDAELSLSALREYREKFPAWQDADP 252
Cdd:cd07584  228 EEAEEILYAEIDLDAIADYRMTLPYLKDRKP 258
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
26-242 1.91e-25

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


Pssm-ID: 143609  Cd Length: 261  Bit Score: 100.85  E-value: 1.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  26 DRQLETVA---------GRDVIVLPEMFTSGFAMEAAnksLPQEEVV----SWMRVK--AQQTNALIAGSAAIQSERGPV 90
Cdd:cd07585   15 ARNLAVIArwtrkaaaqGAELVCFPEMCITGYTHVRA---LSREAEVpdgpSTQALSdlARRYGLTILAGLIEKAGDRPY 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  91 NRFFLVEPEGNVHFYDKRHLFRMadEHQHYQAGDARVIVEWRGWRILPLVCYDLRFPVWSRNrndydLALYVA------- 163
Cdd:cd07585   92 NTYLVCLPDGLVHRYRKLHLFRR--EHPYIAAGDEYPVFATPGVRFGILICYDNHFPENVRA-----TALLGAeilfaph 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 164 ----NWPAPRSLHWQLLLAARAIENQAYVAGCNRVGTDGnGHHYRGDSRVINPQGEIIATAEPHQATRIDAELSLSALRE 239
Cdd:cd07585  165 atpgTTSPKGREWWMRWLPARAYDNGVFVAACNGVGRDG-GEVFPGGAMILDPYGRVLAETTSGGDGMVVADLDLDLINT 243

                 ...
gi 696367412 240 YRE 242
Cdd:cd07585  244 VRG 246
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
4-251 2.52e-22

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: 92.65  E-value: 2.52e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412   4 LKITLLQQPliwMDGPANLRHFDRQLE----TVAGR--DVIVLPEMFT---SGFAMEAANKSLPQ--------EEVVSWM 66
Cdd:cd07574    1 VRVAAAQYP---LRRYASFEEFAAKVEywvaEAAGYgaDLLVFPEYFTmelLSLLPEAIDGLDEAiralaaltPDYVALF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  67 RVKAQQTNA-LIAGSAAIQSERGPVNRFFLVEPEGNVHFYDKRHLFRMADEHQHYQAGDARVIVEWRGWRILPLVCYDLR 145
Cdd:cd07574   78 SELARKYGInIIAGSMPVREDGRLYNRAYLFGPDGTIGHQDKLHMTPFEREEWGISGGDKLKVFDTDLGKIGILICYDSE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 146 FPVWSRNrndydLA------LYVANWPAPRSLHWQLLL--AARAIENQAYVAGCNRVG---TDGNGHHYRGDSRVINP-- 212
Cdd:cd07574  158 FPELARA-----LAeagadlLLVPSCTDTRAGYWRVRIgaQARALENQCYVVQSGTVGnapWSPAVDVNYGQAAVYTPcd 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 696367412 213 -----QGeIIATAEPHQATRIDAELSLSALREYREKFPAWQDAD 251
Cdd:cd07574  233 fgfpeDG-ILAEGEPNTEGWLIADLDLEALRRLREEGSVRNLRD 275
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
20-241 9.76e-19

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: 82.78  E-value: 9.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  20 ANLRHFDRQLETVA--GRDVIVLPEMFTSGFAMEAANKSLPQ-EEVVS------WMRVkAQQTNALIAGSAAiqsERGPV 90
Cdd:cd07580   16 ANLARSIELIREAAdaGANLVVLPELANTGYVFESRDEAFALaEEVPDgastraWAEL-AAELGLYIVAGFA---ERDGD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  91 ---NRFFLVEPEGNVHFYDKRHLFrmADEHQHYQAGDARV-IVEWRGWRILPLVCYDLRFPVWSRNrndydLALYVA--- 163
Cdd:cd07580   92 rlyNSAVLVGPDGVIGTYRKAHLW--NEEKLLFEPGDLGLpVFDTPFGRIGVAICYDGWFPETFRL-----LALQGAdiv 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 164 ----NW-PAPRSLHWQL-----LLAARAIENQAYVAGCNRVGTDgNGHHYRGDSRVINPQGEIIAT-AEPHQATRIDAEL 232
Cdd:cd07580  165 cvptNWvPMPRPPEGGPpmaniLAMAAAHSNGLFIACADRVGTE-RGQPFIGQSLIVGPDGWPLAGpASGDEEEILLADI 243

                 ....*....
gi 696367412 233 SLSALREYR 241
Cdd:cd07580  244 DLTAARRKR 252
nitrilase_8 cd07586
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
33-251 1.07e-16

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


Pssm-ID: 143610  Cd Length: 269  Bit Score: 77.33  E-value: 1.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  33 AGRDVIVLPEMFTSGFAMEAanksLPQEevVSwMRVKAQQTNALIAGSAAIQS-----ERGPVNRFF----LVEPEGNVH 103
Cdd:cd07586   31 RGADLVVFPELSLTGYNLGD----LVYE--VA-MHADDPRLQALAEASGGICVvfgfvEEGRDGRFYnsaaYLEDGRVVH 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 104 FYDKRHL--FRMADEHQHYQAGDARVIVEWRGWRILPLVCYDLrfpvW--------SRNRNDYDLALyvANWPAPRSLH- 172
Cdd:cd07586  104 VHRKVYLptYGLFEEGRYFAPGSHLRAFDTRFGRAGVLICEDA----WhpslpyllALDGADVIFIP--ANSPARGVGGd 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 173 ------WQLLLAARAIENQAYVAGCNRVGTDGnGHHYRGDSRVINPQGEIIATAEPHQATRIDAELSLSALREYREKFPA 246
Cdd:cd07586  178 fdneenWETLLKFYAMMNGVYVVFANRVGVED-GVYFWGGSRVVDPDGEVVAEAPLFEEDLLVAELDRSAIRRARFFSPT 256

                 ....*
gi 696367412 247 WQDAD 251
Cdd:cd07586  257 FRDED 261
PLN02798 PLN02798
nitrilase
33-245 3.42e-16

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 75.94  E-value: 3.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  33 AGRDVIVLPEMFtsGFAMEAANKSLPQEE-----VVSWMRVKAQQTNALIagSAAIQSERGP-----VNRFFLVEPEGNV 102
Cdd:PLN02798  41 AGAKLLFLPECF--SFIGDKDGESLAIAEpldgpIMQRYRSLARESGLWL--SLGGFQEKGPddshlYNTHVLIDDSGEI 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 103 H-FYDKRHLF-------RMADEHQHYQAGDARVIVEWRGWRILPLVCYDLRFP-VWSRNRNDYDL-ALYVanwPAPRSL- 171
Cdd:PLN02798 117 RsSYRKIHLFdvdvpggPVLKESSFTAPGKTIVAVDSPVGRLGLTVCYDLRFPeLYQQLRFEHGAqVLLV---PSAFTKp 193
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 696367412 172 ----HWQLLLAARAIENQAYVAGCNRVGTDGNGHHYRGDSRVINPQGEIIATAEPHQATRID-AELSLSALREYREKFP 245
Cdd:PLN02798 194 tgeaHWEVLLRARAIETQCYVIAAAQAGKHNEKRESYGHALIIDPWGTVVARLPDRLSTGIAvADIDLSLLDSVRTKMP 272
de_GSH_amidase NF033621
deaminated glutathione amidase;
105-245 1.17e-14

deaminated glutathione amidase;


Pssm-ID: 468114  Cd Length: 260  Bit Score: 71.47  E-value: 1.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 105 YDKRHL---FRMaDEHQHYQAGDA-RVIVEWRGWRILPLVCYDLRFPVWSRNrndydLALYVAN---WPAP------RSL 171
Cdd:NF033621 107 YRKLHLydaFSM-QESRRVDAGNEiPPLVEVAGMKVGLMTCYDLRFPELARR-----LALDGADvlvLPAAwvrgplKEH 180
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 696367412 172 HWQLLLAARAIENQAYVAGcnrVGTDGNghhyR--GDSRVINPQGEIIATAePHQATRIDAELSLSALREYREKFP 245
Cdd:NF033621 181 HWETLLAARALENTCYMVA---VGECGN----RniGQSMVVDPLGVTIAAA-AEAPALIFAELDPERIAHAREQLP 248
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
4-235 1.87e-12

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: 65.31  E-value: 1.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412   4 LKITLLQQ---PLIWMDGPANLRHFDRQLETVA-----GRDVIVLPEmfTSGFAMEAANKSLPQEevvswMRVKAQQTNA 75
Cdd:cd07571    1 LRVALVQGnipQDEKWDPEQRQATLDRYLDLTReladeKPDLVVWPE--TALPFDLQRDPDALAR-----LARAARAVGA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  76 -LIAGSAAIQSERGPV-NRFFLVEPEGN-VHFYDKRHL-----------------FRMADEHQHYQAGDARVIVEWRG-W 134
Cdd:cd07571   74 pLLTGAPRREPGGGRYyNSALLLDPGGGiLGRYDKHHLvpfgeyvplrdllrflgLLFDLPMGDFSPGTGPQPLLLGGgV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 135 RILPLVCYDLRFP--VWSRNRNDYDLALYVAN--WPAPRSLHWQLLLAA--RAIENQAYVAgcnRVGTDGnghhyrgDSR 208
Cdd:cd07571  154 RVGPLICYESIFPelVRDAVRQGADLLVNITNdaWFGDSAGPYQHLAMArlRAIETGRPLV---RAANTG-------ISA 223
                        250       260
                 ....*....|....*....|....*..
gi 696367412 209 VINPQGEIIATAEPHQATRIDAELSLS 235
Cdd:cd07571  224 VIDPDGRIVARLPLFEAGVLVAEVPLR 250
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
2-234 7.37e-12

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


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 64.48  E-value: 7.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412   2 PGLKITLLQ----QPLIWMDG--PANLRHFDRQLETVAGR--DVIVLPEMFTSGFAMEAAnkslpqeEVVSWMRVKAQQT 73
Cdd:COG0815  193 EPLRVALVQgnipQDLKWDPEqrREILDRYLDLTRELADDgpDLVVWPETALPFLLDEDP-------DALARLAAAAREA 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  74 NA-LIAGSAAIQSERGPV-NRFFLVEPEGNVH-FYDKRHLF-----------------RMADEHQHYQAGDARVIVEWRG 133
Cdd:COG0815  266 GApLLTGAPRRDGGGGRYyNSALLLDPDGGILgRYDKHHLVpfgeyvplrdllrplipFLDLPLGDFSPGTGPPVLDLGG 345
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 134 WRILPLVCYDLRFP--VWSRNRNDYDLALYVAN--WPAPRSLHWQLLLAA--RAIENQAYVAgcnRVGTDGnghhyrgDS 207
Cdd:COG0815  346 VRVGPLICYESIFPelVRDAVRAGADLLVNITNdaWFGDSIGPYQHLAIArlRAIETGRPVV---RATNTG-------IS 415
                        250       260
                 ....*....|....*....|....*..
gi 696367412 208 RVINPQGEIIATAEPHQATRIDAELSL 234
Cdd:COG0815  416 AVIDPDGRVLARLPLFTRGVLVAEVPL 442
nitrilase_4 cd07582
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
38-243 1.66e-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: 56.97  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  38 IVLPEMFTSGFAMEA---------ANKSLPQEEVVSwMRVKAQQTNALIAGSAAIQSERGPVNRF---FLVEPEGNVhFY 105
Cdd:cd07582   46 VVLPEYALQGFPMGEprevwqfdkAAIDIPGPETEA-LGEKAKELNVYIAANAYERDPDFPGLYFntaFIIDPSGEI-IL 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 106 DKRHLFRMADEHQH--YQAGDARVIVEWRGW------------RILPLVCYDLRFPVWSRNrndydLAL--------YVA 163
Cdd:cd07582  124 RYRKMNSLAAEGSPspHDVWDEYIEVYGYGLdalfpvadteigNLGCLACEEGLYPEVARG-----LAMngaevllrSSS 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 164 NWPAPRSLHWQLLLAARAIENQAYVAGCNR---VGTDGNGHHYRGDSRVINPQGEIIATAEP-HQATRIDAELSLSALRE 239
Cdd:cd07582  199 EVPSVELDPWEIANRARALENLAYVVSANSggiYGSPYPADSFGGGSMIVDYKGRVLAEAGYgPGSMVAGAEIDIEALRR 278

                 ....
gi 696367412 240 YREK 243
Cdd:cd07582  279 ARAR 282
lnt PRK00302
apolipoprotein N-acyltransferase; Reviewed
2-234 8.04e-09

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 234721 [Multi-domain]  Cd Length: 505  Bit Score: 55.66  E-value: 8.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412   2 PGLKITLLQ----QPLIWmdGPANL-----RHFDRQLETVAGRDVIVLPEmftsgFAMEAANKSLPQEeVVSWMRVKAQQ 72
Cdd:PRK00302 218 PALKVALVQgnipQSLKW--DPAGLeatlqKYLDLSRPALGPADLIIWPE-----TAIPFLLEDLPQA-FLKALDDLARE 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  73 TN-ALIAGSAAIQSERGPV---NRFFLVEPEGNVHFYDKRHL------------FR-----MADEHQHYQAGDAR-VIVE 130
Cdd:PRK00302 290 KGsALITGAPRAENKQGRYdyyNSIYVLGPYGILNRYDKHHLvpfgeyvpleslLRplapfFNLPMGDFSRGPYVqPPLL 369
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 131 WRGWRILPLVCYDLRFP--VWSRNRNDYDLALYVAN--W----PAPrslhWQ-LLLAA-RAIENQAYVA-GCNrvgtdgN 199
Cdd:PRK00302 370 AKGLKLAPLICYEIIFPeeVRANVRQGADLLLNISNdaWfgdsIGP----YQhFQMARmRALELGRPLIrATN------T 439
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 696367412 200 GHhyrgdSRVINPQGEIIATAEPHQATRIDAELSL 234
Cdd:PRK00302 440 GI-----TAVIDPLGRIIAQLPQFTEGVLDGTVPP 469
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
172-249 9.32e-09

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: 54.88  E-value: 9.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 172 HWQLLLAARAIENQAYVAGCNRVGT---DGNGHHYRGDSRVINPQGEIIATAEPHQATRIDAELSLSALREYREKFPAWQ 248
Cdd:cd07573  193 AWQRVQRGHAIANGVPVAAVNRVGVegdPGSGITFYGSSFIADPFGEILAQASRDEEEILVAEFDLDEIEEVRRAWPFFR 272

                 .
gi 696367412 249 D 249
Cdd:cd07573  273 D 273
DCase cd07569
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ...
34-243 8.05e-08

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: 51.93  E-value: 8.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  34 GRDVIVLPEM-FTSGFAM-----EAA-----NKSLPQEEVVSWMRVKAQQTNALIAGSAAIQSERGPVNRF---FLVEPE 99
Cdd:cd07569   38 GAQLVVFPELaLTTFFPRwyfpdEAEldsffETEMPNPETQPLFDRAKELGIGFYLGYAELTEDGGVKRRFntsILVDKS 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 100 GNVHF-YDKRHL-----FRMADEHQH-----YQAGDarviVEWRGWRILP-----LVCYDLRFPVWSRN---------RN 154
Cdd:cd07569  118 GKIVGkYRKVHLpghkePEPYRPFQHlekryFEPGD----LGFPVFRVPGgimgmCICNDRRWPETWRVmglqgvelvLL 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 155 DYDLALYVANWPAP---RSLHWQLLLAARAIENQAYVAGCNRVGTDgNGHHYRGDSRVINPQGEIIATAEPHQATRIDAE 231
Cdd:cd07569  194 GYNTPTHNPPAPEHdhlRLFHNLLSMQAGAYQNGTWVVAAAKAGME-DGCDLIGGSCIVAPTGEIVAQATTLEDEVIVAD 272
                        250
                 ....*....|..
gi 696367412 232 LSLSALREYREK 243
Cdd:cd07569  273 CDLDLCREGRET 284
aliphatic_amidase cd07565
aliphatic amidases (class 2 nitrilases); Aliphatic amidases catalyze the hydrolysis of ...
6-242 6.37e-07

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: 49.21  E-value: 6.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412   6 ITLLQQPLIWMDGPANLrhfDRQLETVA-----------GRDVIVLPEMFTSGFA-----MEAANKSLPQEEVVswmRVK 69
Cdd:cd07565    3 VAVVQYKVPVLHTKEEV---LENAERIAdmvegtkrglpGMDLIVFPEYSTQGLMydkwtMDETACTVPGPETD---IFA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  70 AQQTNALIAGSAAI-----QSERGPVNRFFLVEPEGN-VHFYDKRHLFRMADEHQhyqAGDARVIVEW--RGWRILPLVC 141
Cdd:cd07565   77 EACKEAKVWGVFSImernpDHGKNPYNTAIIIDDQGEiVLKYRKLHPWVPIEPWY---PGDLGTPVCEgpKGSKIALIIC 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 142 YDLRFPVWSRN--RNDYDLALYVANWPAPRSLHWQLLLAARAIENQAYVAGCNRVGTDGNgHHYRGDSRVINPQGEIIAT 219
Cdd:cd07565  154 HDGMYPEIAREcaYKGAELIIRIQGYMYPAKDQWIITNKANAWCNLMYTASVNLAGFDGV-FSYFGESMIVNFDGRTLGE 232
                        250       260
                 ....*....|....*....|...
gi 696367412 220 AEPHQATRIDAELSLSALREYRE 242
Cdd:cd07565  233 GGREPDEIVTAELSPSLVRDARK 255
ML_beta-AS_like cd07568
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
173-252 3.35e-06

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: 47.11  E-value: 3.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 173 WQLLLAARAIENQAYVAGCNRVGTD--GNGHHYRGDSRVINPQGEIIATAEPHQATRIDAELSLSALREYREKFPAWQDA 250
Cdd:cd07568  197 WKLEQPAAAVANGYFVGAINRVGTEapWNIGEFYGSSYFVDPRGQFVASASRDKDELLVAELDLDLIREVRDTWQFYRDR 276

                 ..
gi 696367412 251 DP 252
Cdd:cd07568  277 RP 278
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
32-219 6.42e-06

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: 45.99  E-value: 6.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  32 VAGRDVIVLPEMFTSGFA------MEAANKSLPQEEVVSWMRVKAQQTNALIAGSAAIQSERGPV-NRFFLVEPEGNVHF 104
Cdd:cd07578   31 RAGARLIVTPEMATTGYCwydraeIAPFVEPIPGPTTARFAELAREHDCYIVVGLPEVDSRSGIYyNSAVLIGPSGVIGR 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 105 YDKRHLF-----RMADEHQHYQAGDARVivewrgWRILPLVCYDLRFPVWSR--NRNDYDLALYVANW-----PAPrslH 172
Cdd:cd07578  111 HRKTHPYisepkWAADGDLGHQVFDTEI------GRIALLICMDIHFFETARllALGGADVICHISNWlaertPAP---Y 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 696367412 173 WqlllAARAIENQAYVAGCNRVGTDgNGHHYRGDSRVINPQGEIIAT 219
Cdd:cd07578  182 W----INRAFENGCYLIESNRWGLE-RGVQFSGGSCIIEPDGTIQAS 223
nitrilase_1_R2 cd07579
Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
20-236 1.32e-05

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: 45.24  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  20 ANLRHFDRQLETV--AGRDVIVLPEMFTSGF---AMEAANKSLPQeeVVSWMRVKAQQTNALIAGSAaiqsERGP---VN 91
Cdd:cd07579   15 GNLATIDRLAAEAkaTGAELVVFPELALTGLddpASEAESDTGPA--VSALRRLARRLRLYLVAGFA----EADGdglYN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412  92 RFFLVEPEGNVHFYDKRHLfrMADEHQHYQAGDARVIVEWRGWRILPLVCYDLRFPVWSRNrndydLAL----YVA---- 163
Cdd:cd07579   89 SAVLVGPEGLVGTYRKTHL--IEPERSWATPGDTWPVYDLPLGRVGLLIGHDALFPEAGRV-----LALrgcdLLAcpaa 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 164 ----------------NWPAPRS---LHWQlLLAARAIENQAYVAGCNRVGTDGNghhYRGDSRVINPqgeiIATAEPHQ 224
Cdd:cd07579  162 iaipfvgahagtsvpqPYPIPTGadpTHWH-LARVRAGENNVYFAFANVPDPARG---YTGWSGVFGP----DTFAFPRQ 233
                        250
                 ....*....|..
gi 696367412 225 ATRIDAELSLSA 236
Cdd:cd07579  234 EAAIGDEEGIAW 245
PLN02747 PLN02747
N-carbamolyputrescine amidase
172-252 1.16e-03

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 39.37  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696367412 172 HWQLLLAARAIENQAYVAGCNRVGTD-------GNGHHYRGDSRVINPQGEIIATAEPHQATRIDAELSLSALREYREKF 244
Cdd:PLN02747 196 HWKRVMQGHAGANLVPLVASNRIGTEiletehgPSKITFYGGSFIAGPTGEIVAEADDKAEAVLVAEFDLDQIKSKRASW 275

                 ....*...
gi 696367412 245 PAWQDADP 252
Cdd:PLN02747 276 GVFRDRRP 283
 
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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