|
Name |
Accession |
Description |
Interval |
E-value |
| nadE |
PRK02628 |
NAD synthetase; Reviewed |
1-640 |
0e+00 |
|
NAD synthetase; Reviewed
Pssm-ID: 235057 [Multi-domain] Cd Length: 679 Bit Score: 1010.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 1 MRDGFIKIAAATPDLHVADCEYNAAEIIRQAKQAASKGAKLITFPELCLTGYTCGDLFLQETLLEGAMQALGTVCRETAE 80
Cdd:PRK02628 8 YRHGFVRVAAATPKVRVADPAFNAARILALARRAADDGVALAVFPELSLSGYSCDDLFLQDTLLDAVEDALATLVEASAD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 81 LAAVIVVGLPLRVKGKLYNVAAVVNAGDVLAFVPKTYIPNYSEFYEQRHFVSADTLSGmENVRIKAADgepcwVPLVTDT 160
Cdd:PRK02628 88 LDPLLVVGAPLRVRHRLYNCAVVIHRGRILGVVPKSYLPNYREFYEKRWFAPGDGARG-ETIRLCGQE-----VPFGTDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 161 IFQCDEQPLFTFGVEICEDLWVPNPPSTTLAQMGAHIIVNLSASDEIIGKAGYRRDLVRQQSGRLLCAYLYADAGFGEST 240
Cdd:PRK02628 162 LFEAEDLPGFVFGVEICEDLWVPIPPSSYAALAGATVLANLSASNITVGKADYRRLLVASQSARCLAAYVYAAAGVGEST 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 241 QDLVFAGHDLIAENGALLAESKMFEQG--IIYADIDLQRLAHERQRMNTFE-----SIEGSEF---SFSLEPVENDLA-D 309
Cdd:PRK02628 242 TDLAWDGQTLIYENGELLAESERFPREeqLIVADVDLERLRQERLRNGSFDdnarhRDESAPFrtiPFALDPPAGDLGlR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 310 RSFPRTPFVPANKALRDERCEEILTLQATGLATRLRHTHAKTAVVGLSGGLDSTLALIVLVHAFDMLELDRKGILAVTMP 389
Cdd:PRK02628 322 RPVERFPFVPSDPARLDQRCYEAYNIQVSGLAQRLRATGLKKVVIGISGGLDSTHALLVAAKAMDRLGLPRKNILAYTMP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 390 CFGTTARTKGNAEKLAEAYGVTLETVDIKAAVDQHFEDIG----QSKEDLSVTFENGQARMRTLVLMNLANKTGGMVVGT 465
Cdd:PRK02628 402 GFATTDRTKNNAVALMKALGVTAREIDIRPAALQMLKDIGhpfaRGEPVYDVTFENVQAGERTQILFRLANQHGGIVIGT 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 466 GDLSELALGWATYN-GDHMSMYGVNGSIPKTLVRYLVAY--EADRVQGELSDVLRDVLDTPVSPELLPP-KDGEISQKTE 541
Cdd:PRK02628 482 GDLSELALGWCTYGvGDHMSHYNVNASVPKTLIQHLIRWviASGQFDEAVSEVLLDILDTEISPELVPAdKEGEIVQSTE 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 542 DLVGPYELHDFFLYYMLRFGYPPRKIYRAARKTFAGV---------------YDDATIKKWLTTFVRRFFTQQFKRSCLP 606
Cdd:PRK02628 562 DIIGPYELQDFFLYYFLRYGFRPSKIAFLAWHAWKDAergawpgfpedkrpaYDLATIKKWLEVFLRRFFSSQFKRSALP 641
|
650 660 670
....*....|....*....|....*....|....*
gi 2789482484 607 DGPKVGT-VTLSPRGDWRMPSDAVSALWLREAENL 640
Cdd:PRK02628 642 NGPKVGSgGSLSPRGDWRAPSDASAAAWLDELERL 676
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
52-628 |
6.51e-132 |
|
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 439941 [Multi-domain] Cd Length: 542 Bit Score: 398.07 E-value: 6.51e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 52 YTCGDLFLQETLLEGAMQALGTVCRETAELAAVIVVGLPLRVKGKLYNVAAVVNAGDVLAFVPKTYIPNYSEFYEQRHFV 131
Cdd:COG0171 3 LLLALLLLAAALLDAAAAAAAALAALAAAAAALLLLLLLLLLLLLLLLALLLLLAAARLLVAAAALLLLALAAGGGAALA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 132 SADTLSGMENVRIKAAdgepcwVPLVTDTIFQCDEQPLFTFGVEICEDLWVPNPPSTTLAQMGAHIIVNLSASDEIIGKA 211
Cdd:COG0171 83 GGGGGAGGGLLNGAAL------VLGGGDLLFFADDFLLLLLVVEEEEEEFVGGPPPPPAALGGAGVLLILSSSSSAVGAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 212 GYRRDLVRQQSGRLLCAYLYADAGFGESTQDL--VFAGHDLIAENGALLAESKMFEQGIIYADIDLQRLAHERQRmntfe 289
Cdd:COG0171 157 AAAAALAAALLSSLSSAAYYAAAGGGESTTDLarGGGGGLLLVVLLLVGGGDDDFFDGGSAAVDDDDLLLLLRRR----- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 290 siegsEFSFSLEPVENDLADRSFPRTPFVPANKALRDERCEEILTLQATGLATRLRHTHAKTAVVGLSGGLDSTLALIVL 369
Cdd:COG0171 232 -----REEELLLARARDADGGRRVAAEAAPPPPEEEEMDLEEVYDALVLGLRDYVRKNGFKGVVLGLSGGIDSALVAALA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 370 VHAfdmleLDRKGILAVTMPCFGTTARTKGNAEKLAEAYGVTLETVDIKAAVDQHFEDIGQSKEDLS--VTFENGQARMR 447
Cdd:COG0171 307 VDA-----LGPENVLGVTMPSRYTSDESLEDAEELAENLGIEYEEIDITPAVEAFLEALPHAFGGELddVAEENLQARIR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 448 TLVLMNLANKTGGMVVGTGDLSELALGWATYNGDHMSMYGVNGSIPKTLVRYLVAYeadrVQGELSDVLRDVLDTPVSPE 527
Cdd:COG0171 382 MVILMALANKFGGLVLGTGNKSELAVGYFTKYGDGAGDLAPIADLYKTQVYALARW----LNRNGEVIPEDIIDKPPSAE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 528 LLPpkdgeiSQKTEDLVGPYELHDFFLYYMLRFGYPPRKIYRAArktfagvYDdatiKKWLTTFVRRFFTQQFKRSCLPD 607
Cdd:COG0171 458 LRP------GQTDEDELGPYEVLDAILYAYVEEGLSPEEIAAAG-------YD----REWVERVLRLVRRNEYKRRQPPP 520
|
570 580
....*....|....*....|.
gi 2789482484 608 GPKVGTVTLSPrgDWRMPSDA 628
Cdd:COG0171 521 GPKVSSRAFGR--GRRYPIDS 539
|
|
| GAT_Gln-NAD-synth |
cd07570 |
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ... |
7-292 |
8.04e-115 |
|
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: 344.07 E-value: 8.04e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 7 KIAAATPDLHVADCEYNAAEIIRQAKQAASKGAKLITFPELCLTGYTCGDLFLQETLLEGAMQALGTVCRETAELAAVIV 86
Cdd:cd07570 1 RIALAQLNPTVGDLEGNAEKILEAIREAKAQGADLVVFPELSLTGYPPEDLLLRPDFLEAAEEALEELAAATADLDIAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 87 VGLPLRVKGKLYNVAAVVNAGDVLAFVPKTYIPNYSEFYEQRHFVSADTlsgmenvrikaadgepcwvplvTDTIFQCDe 166
Cdd:cd07570 81 VGLPLRHDGKLYNAAAVLQNGKILGVVPKQLLPNYGVFDEKRYFTPGDK----------------------PDVLFFKG- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 167 qplFTFGVEICEDLWVPNPPSTTLAQMGAHIIVNLSASDEIIGKAGYRRDLVRQQSGRLLCAYLYADAgfGESTQDLVFA 246
Cdd:cd07570 138 ---LRIGVEICEDLWVPDPPSAELALAGADLILNLSASPFHLGKQDYRRELVSSRSARTGLPYVYVNQ--VGGQDDLVFD 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2789482484 247 GHDLIAEN-GALLAESKMFEqgIIYADIDLQRLAHERQRMNTFESIE 292
Cdd:cd07570 213 GGSFIADNdGELLAEAPRFE--EDLADVDLDRLRSERRRNSSFLDEE 257
|
|
| NAD_synthase |
cd00553 |
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ... |
327-602 |
2.99e-74 |
|
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de novo nicotinamide adenine dinucleotide (NAD(+)) biosynthesis, an amide transfer from either ammonia or glutamine to nicotinic acid adenine dinucleotide (NaAD). The conversion of NaAD to NAD(+) occurs via a NAD-adenylate intermediate and requires ATP and Mg(2+). The intermediate is subsequently cleaved into NAD(+) and AMP. In many prokaryotes, such as Escherichia coli, NAD synthase consists of a single domain and is strictly ammonia dependent. In contrast, eukaryotes and other prokaryotes have an additional N-terminal amidohydrolase domain that prefer glutamine. Interestingly, NAD(+) synthases in these prokaryotes, can also utilize ammonia as an amide source.
Pssm-ID: 467484 [Multi-domain] Cd Length: 248 Bit Score: 238.22 E-value: 2.99e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 327 ERCEEILTLQATGLATRLRHTHAKTAVVGLSGGLDSTLALIVLVHAFDmleldRKGILAVTMPCFGTTARTKGNAEKLAE 406
Cdd:cd00553 1 IDPEEIIEALVCFLRDYLRKSGAKGFVLGLSGGIDSAVVAALAVRALG-----AENVLALIMPSRYSSKETRDDAKALAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 407 AYGVTLETVDIKAAVDQHFEDIGQSKEDL--SVTFENGQARMRTLVLMNLANKTGGMVVGTGDLSELALGWATYNGDHMS 484
Cdd:cd00553 76 NLGIEYRTIDIDPIVDAFLKALEHAGGSEaeDLALGNIQARLRMVLLYALANLLGGLVLGTGNKSELLLGYFTKYGDGAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 485 MYGVNGSIPKTLVRYLVAYeadrvqgeLSdVLRDVLDTPVSPELlppkdgEISQKTEDLVG-PYELHDFFLYYMLRFGYP 563
Cdd:cd00553 156 DINPIGDLYKTQVRELARY--------LG-VPEEIIEKPPSAEL------WPGQTDEDELGmPYEELDLILYGLVDGKLG 220
|
250 260 270
....*....|....*....|....*....|....*....
gi 2789482484 564 PRKIYRAARktfagvyddatIKKWLTTFVRRFFTQQFKR 602
Cdd:cd00553 221 PEEILSPGE-----------DEEKVKRIFRLYRRNEHKR 248
|
|
| PRK13981 |
PRK13981 |
NAD synthetase; Provisional |
6-625 |
8.51e-71 |
|
NAD synthetase; Provisional
Pssm-ID: 237577 [Multi-domain] Cd Length: 540 Bit Score: 238.52 E-value: 8.51e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 6 IKIAAATPDLHVADCEYNAAEIIRQAKQAASKGAKLITFPELCLTGYTCGDLFLQETLLEGAMQALGTVCRETAELAAVi 85
Cdd:PRK13981 1 LRIALAQLNPTVGDIAGNAAKILAAAAEAADAGADLLLFPELFLSGYPPEDLLLRPAFLAACEAALERLAAATAGGPAV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 86 VVGLPLRVKGKLYNVAAVVNAGDVLAFVPKTYIPNYSEFYEQRHFvsadtlsgmenvrikAADGEPCWVPLvtDTIfqcd 165
Cdd:PRK13981 80 LVGHPWREGGKLYNAAALLDGGEVLATYRKQDLPNYGVFDEKRYF---------------APGPEPGVVEL--KGV---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 166 eqplfTFGVEICEDLWVPNPPStTLAQMGAHIIVNLSASDEIIGKAGYRRDLVRQQSGRLLCAYLYADAGFGestQD-LV 244
Cdd:PRK13981 139 -----RIGVPICEDIWNPEPAE-TLAEAGAELLLVPNASPYHRGKPDLREAVLRARVRETGLPLVYLNQVGG---QDeLV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 245 FAGHDL-IAENGALLAESKMFEqgiiyadidlqrlaherqrmntfESIEGSEFsfslepvendlaDRSFPRTPFVPANKA 323
Cdd:PRK13981 210 FDGASFvLNADGELAARLPAFE-----------------------EQIAVVDF------------DRGEDGWRPLPGPIA 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 324 LRDERCEEI---LTLqatGLATRLRHTHAKTAVVGLSGGLDSTLaliVLVHAFDMLELDRkgILAVTMPCFGTTARTKGN 400
Cdd:PRK13981 255 PPPEGEAEDyraLVL---GLRDYVRKNGFPGVVLGLSGGIDSAL---VAAIAVDALGAER--VRAVMMPSRYTSEESLDD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 401 AEKLAEAYGVTLETVDIKAAVDQHFEDIGQSKEDLS--VTFENGQARMRTLVLMNLANKTGGMVVGTGDLSELALGWATY 478
Cdd:PRK13981 327 AAALAKNLGVRYDIIPIEPAFEAFEAALAPLFAGTEpdITEENLQSRIRGTLLMALSNKFGSLVLTTGNKSEMAVGYATL 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 479 NGDhmsM---YGVNGSIPKTLVRYLVAYEADRVQGElsdVLRD-VLDTPVSPELLPpkdgeiSQKTEDLVGPYELHDFFL 554
Cdd:PRK13981 407 YGD---MaggFAPIKDVYKTLVYRLCRWRNTVSPGE---VIPErIITKPPSAELRP------NQTDQDSLPPYDVLDAIL 474
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2789482484 555 YYMLRFGYPPRKIYRAArktfagvYDDATIKKwLTTFVRRfftQQFKRSCLPDGPKVgtvtlSPRG---DWRMP 625
Cdd:PRK13981 475 ERLVEEEQSVAEIVAAG-------FDRATVRR-VERLLYI---AEYKRRQAAPGVKI-----TRRAfgrDRRYP 532
|
|
| Nit2 |
COG0388 |
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]; |
6-289 |
3.46e-62 |
|
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
Pssm-ID: 440157 [Multi-domain] Cd Length: 264 Bit Score: 207.41 E-value: 3.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 6 IKIAAATPDLHVADCEYNAAEIIRQAKQAASKGAKLITFPELCLTGYTCGD---LFLQETLLEGAMQALgtvCRETAELA 82
Cdd:COG0388 2 MRIALAQLNPTVGDIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDddlLELAEPLDGPALAAL---AELARELG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 83 AVIVVGLPLRV-KGKLYNVAAVVNA-GDVLAFVPKTYIPNYSEFYEQRHFVSADTlsgmenvrikaadgepcwvPLVTDT 160
Cdd:COG0388 79 IAVVVGLPERDeGGRLYNTALVIDPdGEILGRYRKIHLPNYGVFDEKRYFTPGDE-------------------LVVFDT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 161 ifqcdeqPLFTFGVEICEDLWVPnPPSTTLAQMGAHIIVNLSASDEIIGKAgYRRDLVRQQSGRLLCAYLYADAGFGEst 240
Cdd:COG0388 140 -------DGGRIGVLICYDLWFP-ELARALALAGADLLLVPSASPFGRGKD-HWELLLRARAIENGCYVVAANQVGGE-- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2789482484 241 QDLVFAGHDLIAE-NGALLAESKmFEQGIIYADIDLQRLAHERQRMNTFE 289
Cdd:COG0388 209 DGLVFDGGSMIVDpDGEVLAEAG-DEEGLLVADIDLDRLREARRRFPVLR 257
|
|
| nitrilase |
cd07197 |
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ... |
8-289 |
2.45e-35 |
|
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: 133.99 E-value: 2.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 8 IAAATPDLHVADCEYNAAEIIRQAKQAASKGAKLITFPELCLTGYTC----GDLFLQETLLEGAMQALGTVCRetaELAA 83
Cdd:cd07197 1 IAAVQLAPKIGDVEANLAKALRLIKEAAEQGADLIVLPELFLTGYSFesakEDLDLAEELDGPTLEALAELAK---ELGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 84 VIVVGLPLRVKGKLYNVAAVVNA-GDVLAFVPKTYIPNyseFYEQRHFVSADTlsgmenvrikaadgepcwvPLVTDTif 162
Cdd:cd07197 78 YIVAGIAEKDGDKLYNTAVVIDPdGEIIGKYRKIHLFD---FGERRYFSPGDE-------------------FPVFDT-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 163 qcdeqPLFTFGVEICEDLWVPnPPSTTLAQMGAHIIVNLSASDEIIGKagYRRDLVRQQSGRLLCAYLYADAGFGEStqD 242
Cdd:cd07197 134 -----PGGKIGLLICYDLRFP-ELARELALKGADIILVPAAWPTARRE--HWELLLRARAIENGVYVVAANRVGEEG--G 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2789482484 243 LVFAGHDLIAE-NGALLAESKMFEqGIIYADIDLQRLAHERQRMNTFE 289
Cdd:cd07197 204 LEFAGGSMIVDpDGEVLAEASEEE-GILVAELDLDELREARKRWSYLR 250
|
|
| PLN02339 |
PLN02339 |
NAD+ synthase (glutamine-hydrolysing) |
19-570 |
2.75e-24 |
|
NAD+ synthase (glutamine-hydrolysing)
Pssm-ID: 177973 [Multi-domain] Cd Length: 700 Bit Score: 107.85 E-value: 2.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 19 DCEYNAAEI---IRQAKQAaskGAKLITFPELCLTGYTCGDLFLQETLLEGAMQALGTVCRETAELAAVIVVGLPLRVKG 95
Cdd:PLN02339 17 DFDGNLKRIkesIAEAKAA---GAVYRVGPELEITGYGCEDHFLELDTVTHSWECLAEILVGDLTDGILCDIGMPVIHGG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 96 KLYNVAAVVNAGDVLAFVPKTYIPNYSEFYEQRHFVSADTLSGMENVR----IKAADGEPCwVPLvTDTIFQCDEQPLft 171
Cdd:PLN02339 94 VRYNCRVFCLNRKILLIRPKMWLANDGNYRELRWFTAWKHKKKVEDFQlpeeIAEATSQKS-VPF-GDGYLQFLDTAV-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 172 fGVEICEDLWVPNPPSTTLAQMGAHIIVNLSASDEIIGKAGYRRDLVRQQSGRLLCAYLYA-----DAGfgestqDLVFA 246
Cdd:PLN02339 170 -AAETCEELFTPQAPHIDLALNGVEIISNGSGSHHQLRKLNTRLDLIRSATHKCGGVYLYAnqrgcDGG------RLYYD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 247 GHDLIAENGALLAESKMF---EQGIIYADIDLQRLAHERQRMNTFeSIEGSE----------FSFSLEPVENDLADRSFP 313
Cdd:PLN02339 243 GCACIVVNGEVVAQGSQFslqDVEVVTACVDLDAVVSFRGSISSF-REQASSkkrvpsvavpFKLCPPFSLSLVPSSPLK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 314 RTPFVPAnkalrdercEEILTLQATGLATRLRHTHAKTAVVGLSGGLDST-LALIV-----LVHAF-------------- 373
Cdd:PLN02339 322 IRYHSPE---------EEIALGPACWLWDYLRRSGASGFLLPLSGGADSSsVAAIVgsmcqLVVKAiregdeqvkadarr 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 374 -----------DMLELDRKGILAVTMPCFGTTARTKGNAEKLAEAYG-----VTLETVdiKAAVDQHFE----------- 426
Cdd:PLN02339 393 ignyadgevptDSKEFAKRIFYTVYMGSENSSEETRSRAKQLADEIGsshldVKIDGV--VSAVLSLFQtltgkrprykv 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 427 DIGQSKEDLSVtfENGQARMRTLVLMNLA-------NKTGG-MVVGTGDLSELALGWAT-YNgdhMSMYGVN--GSIPKT 495
Cdd:PLN02339 471 DGGSNAENLAL--QNIQARIRMVLAFMLAsllpwvrGKSGFlLVLGSANVDEGLRGYLTkYD---CSSADINpiGGISKQ 545
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2789482484 496 LVRYLVAYEADRVQGElsdVLRDVLDTPVSPELLPPKDGEISQKTEDLVGPYElhDFFLYYMLrfgyppRKIYRA 570
Cdd:PLN02339 546 DLRSFLRWAATNLGYP---SLAEVEAAPPTAELEPIRDDYSQTDEEDMGMTYE--ELGVYGRL------RKIFRC 609
|
|
| PRK13980 |
PRK13980 |
NAD synthetase; Provisional |
349-615 |
5.03e-23 |
|
NAD synthetase; Provisional
Pssm-ID: 184435 [Multi-domain] Cd Length: 265 Bit Score: 99.13 E-value: 5.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 349 AKTAVVGLSGGLDSTLALIVLVHAfdmleLDRKGILAVTMPCFGTTARTKGNAEKLAEAYGVTLETVDIKAAVDQHFEDI 428
Cdd:PRK13980 30 AKGVVLGLSGGIDSAVVAYLAVKA-----LGKENVLALLMPSSVSPPEDLEDAELVAEDLGIEYKVIEITPIVDAFFSAI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 429 GQSKedlSVTFENGQARMRTLVLMNLANKTGGMVVGTGDLSELALGWATYNGDHMSMYGVNGSIPKTLVRYLvayeadrv 508
Cdd:PRK13980 105 PDAD---RLRVGNIMARTRMVLLYDYANRENRLVLGTGNKSELLLGYFTKYGDGAVDLNPIGDLYKTQVREL-------- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 509 qGELSDVLRDVLDTPVSPELLPpkdgeiSQKTEDLVG-PYELHDFFLYYMLRFGYPPRKIYRAarktfAGVydDATIKKW 587
Cdd:PRK13980 174 -ARHLGVPEDIIEKPPSADLWE------GQTDEGELGfSYETIDEILYLLFDKKMSREEILEE-----LGV--PEDLVDR 239
|
250 260
....*....|....*....|....*...
gi 2789482484 588 LTTFVRRfftQQFKRScLPDGPKVGTVT 615
Cdd:PRK13980 240 VRRLVQR---SQHKRR-LPPIPKLSGRT 263
|
|
| NAD_synthase |
pfam02540 |
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ... |
344-569 |
7.23e-23 |
|
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is induced by stress factors such as heat shock and glucose limitation.
Pssm-ID: 396888 [Multi-domain] Cd Length: 241 Bit Score: 97.84 E-value: 7.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 344 LRHTHAKTAVVGLSGGLDSTLALIVLVHAFDmleldRKGILAVTMPCFGTTARTKGNAEKLAEAYGVTLETVDIKAAVDQ 423
Cdd:pfam02540 13 VQKAGFKGVVLGLSGGIDSSLVAYLAVKALG-----KENVLALIMPSSQSSEEDVQDALALAENLGIEYKTIDIKPIVRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 424 HFEDIGQSKEDLSVtfENGQARMRTLVLMNLANKTGGMVVGTGDLSELALGWATYNGDHMSMYGVNGSIPKTLVRYLVAY 503
Cdd:pfam02540 88 FSQLFQDASEDFAK--GNLKARIRMAILYYIANKFNYLVLGTGNKSELAVGYFTKYGDGACDIAPIGDLYKTQVYELARY 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2789482484 504 EAdrvqgelsdVLRDVLDTPVSPELLPpkdgeiSQKTEDLVG-PYELHDFFLYY---------MLRFGYPPRKIYR 569
Cdd:pfam02540 166 LN---------VPERIIKKPPSADLWP------GQTDEEELGiPYDELDDILKLvekklspeeIIGKGLPAEVVRR 226
|
|
| nitrilase_8 |
cd07586 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
7-288 |
8.74e-23 |
|
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: 98.51 E-value: 8.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 7 KIAAATPDLHVADCEYNAAEIIRQAKQAASKGAKLITFPELCLTGYtcgdlFLQETLLEGAMQALGTVCRETAELAA--V 84
Cdd:cd07586 1 RVAIAQIDPVLGDVEENLEKHLEIIETARERGADLVVFPELSLTGY-----NLGDLVYEVAMHADDPRLQALAEASGgiC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 85 IVVGLPLRV-KGKLYNVAAVVNAGDVLAFVPKTYIPNYSEFYEQRHFVSADTLsgmenvrikaadgepcwvplvtdTIFQ 163
Cdd:cd07586 76 VVFGFVEEGrDGRFYNSAAYLEDGRVVHVHRKVYLPTYGLFEEGRYFAPGSHL-----------------------RAFD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 164 CDEqplFTFGVEICEDLWVPNPPStTLAQMGAHIIVNLSAS-----DEIIGKAGYRRDLVRQQSGRLLCAYLYADAgFGe 238
Cdd:cd07586 133 TRF---GRAGVLICEDAWHPSLPY-LLALDGADVIFIPANSpargvGGDFDNEENWETLLKFYAMMNGVYVVFANR-VG- 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2789482484 239 sTQDLV--FAGHDLIAENGALLAESKMFEQGIIYADIDLQRLAHERQRMNTF 288
Cdd:cd07586 207 -VEDGVyfWGGSRVVDPDGEVVAEAPLFEEDLLVAELDRSAIRRARFFSPTF 257
|
|
| nitrilase_7 |
cd07585 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
7-284 |
3.16e-22 |
|
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: 96.62 E-value: 3.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 7 KIAAATPDLHVADCEYNAAEIIRQAKQAASKGAKLITFPELCLTGYT-CGDLFLQETLLEG-AMQALGTVCRETaelAAV 84
Cdd:cd07585 1 RIALVQFEARVGDKARNLAVIARWTRKAAAQGAELVCFPEMCITGYThVRALSREAEVPDGpSTQALSDLARRY---GLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 85 IVVGLPLRVKGKLYNVAAVVNAGDVLAFVPKTYIPNysefYEQRHFVSADTLsgmenvrikaadgepcwvplvtdTIFqc 164
Cdd:cd07585 78 ILAGLIEKAGDRPYNTYLVCLPDGLVHRYRKLHLFR----REHPYIAAGDEY-----------------------PVF-- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 165 dEQPLFTFGVEICEDLWVPNpPSTTLAQMGAHIIVNLSASDEIIGKAGyRRDLVRQQSGRLL--CAYLYADAGFGEStQD 242
Cdd:cd07585 129 -ATPGVRFGILICYDNHFPE-NVRATALLGAEILFAPHATPGTTSPKG-REWWMRWLPARAYdnGVFVAACNGVGRD-GG 204
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2789482484 243 LVFAGHDLIAE-NGALLAESKMFEQGIIYADIDLQRLAHERQR 284
Cdd:cd07585 205 EVFPGGAMILDpYGRVLAETTSGGDGMVVADLDLDLINTVRGR 247
|
|
| CN_hydrolase |
pfam00795 |
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ... |
7-279 |
1.58e-19 |
|
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: 88.57 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 7 KIAAATPDLHVADCEYNAAEIIRQAKQAASKGAKLITFPELCLTGYTCGDLFLQ--ETLLEGAMQALGTVCRETAElaaV 84
Cdd:pfam00795 1 RVALVQLPQGFWDLEANLQKALELIEEAARYGADLIVLPELFITGYPCWAHFLEaaEVGDGETLAGLAALARKNGI---A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 85 IVVGLPLRVK--GKLYNVAAVVNAGDVLAFVpktyipnysefYEQRHFVSADTLSGmenvrikaADGEPCWVPLVTDTIF 162
Cdd:pfam00795 78 IVIGLIERWLtgGRLYNTAVLLDPDGKLVGK-----------YRKLHLFPEPRPPG--------FRERVLFEPGDGGTVF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 163 QCdeqPLFTFGVEICEDLWVPNpPSTTLAQMGAHIIVNLSASDEIIGKAG-YRRDLVRQQSGRLLCAYLYADAGFGESTQ 241
Cdd:pfam00795 139 DT---PLGKIGAAICYEIRFPE-LLRALALKGAEILINPSARAPFPGSLGpPQWLLLARARALENGCFVIAANQVGGEED 214
|
250 260 270
....*....|....*....|....*....|....*....
gi 2789482484 242 DLVFAGHD-LIAENGALLAESKMFEQGIIYADIDLQRLA 279
Cdd:pfam00795 215 APWPYGHSmIIDPDGRILAGAGEWEEGVLIADIDLALVR 253
|
|
| nitrilase_2 |
cd07580 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
7-277 |
8.17e-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: 86.63 E-value: 8.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 7 KIAAATPDLHVADCEYNAAEIIRQAKQAASKGAKLITFPELCLTGYTCGDlfLQETLLEGAMQALGTVCRETAELAA--- 83
Cdd:cd07580 1 RVACVQFDPRVGDLDANLARSIELIREAADAGANLVVLPELANTGYVFES--RDEAFALAEEVPDGASTRAWAELAAelg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 84 -VIVVGLPLRVKGKLYNVAAVVNAGDVLAFVPKTYIPNysefYEQRHFVSADTlsgmenvrikaadGEPcwvplVTDTif 162
Cdd:cd07580 79 lYIVAGFAERDGDRLYNSAVLVGPDGVIGTYRKAHLWN----EEKLLFEPGDL-------------GLP-----VFDT-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 163 qcdeqPLFTFGVEICEDLWVPNPPStTLAQMGAHII---VN--LSASDEIIGKA-GYRRDLVRQQSGRLLCAylYADAGF 236
Cdd:cd07580 135 -----PFGRIGVAICYDGWFPETFR-LLALQGADIVcvpTNwvPMPRPPEGGPPmANILAMAAAHSNGLFIA--CADRVG 206
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2789482484 237 GESTQDlvFAGHDLIAE-NG-ALLAESKMFEQGIIYADIDLQR 277
Cdd:cd07580 207 TERGQP--FIGQSLIVGpDGwPLAGPASGDEEEILLADIDLTA 247
|
|
| nadE |
TIGR00552 |
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ... |
344-554 |
1.52e-17 |
|
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the biosynthesis of the essensial cofactor NAD. The member of this family from Bacillus subtilis is a strictly NH(3)-dependent NAD(+) synthetase of 272 amino acids. Proteins consisting only of the domain modeled here may be named as NH3-dependent NAD+ synthetase. Amidotransferase activity may reside in a separate protein, or not be present. Some other members of the family, such as from Mycobacterium tuberculosis, are considerably longer, contain an apparent amidotransferase domain, and show glutamine-dependent as well as NH(3)-dependent activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]
Pssm-ID: 273132 [Multi-domain] Cd Length: 250 Bit Score: 82.82 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 344 LRHTHAKTAVVGLSGGLDSTLALIVLVHAFDmleldrKGILAVTMPCFGTTART-KGNAEKLAEAYGVTLETVDIK---A 419
Cdd:TIGR00552 17 VQKSGAKGVVLGLSGGIDSAVVAALCVEALG------EQNHALLLPHSVQTPEQdVQDALALAEPLGINYKNIDIApiaA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 420 AVDQHFEDIGQSKEDLsvTFENGQARMRTLVLMNLANKTGGMVVGTGDLSELALGWATYNGDHMSMYGVNGSIPKTLVRY 499
Cdd:TIGR00552 91 SFQAQTETGDELSDFL--AKGNLKARLRMAALYAIANKHNLLVLGTGNKSELMLGYFTKYGDGGCDIAPIGDLFKTQVYE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2789482484 500 LVAYEAdrvqgelsdVLRDVLDTPVSPELLPPKDGEisqktEDLVGPYELHDFFL 554
Cdd:TIGR00552 169 LAKRLN---------VPERIIEKPPTADLFDGQTDE-----TELGITYDELDDYL 209
|
|
| R-amidase_like |
cd07576 |
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ... |
7-284 |
9.40e-17 |
|
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: 80.32 E-value: 9.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 7 KIAAATPDLHVADCEYNAAEIIRQAKQAASKGAKLITFPELCLTGYTCGDLflqetLLEGAMQALGTVCRETAELAA--- 83
Cdd:cd07576 1 RLALYQGPARDGDVAANLARLDEAAARAAAAGADLLVFPELFLTGYNIGDA-----VARLAEPADGPALQALRAIARrhg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 84 -VIVVGLPLRVKGKLYNVAAVVNA-GDVLAFVPKTYIPnysEFYEQRHFVSADTLsgmenvrikaadgepcwvplvtdTI 161
Cdd:cd07576 76 iAIVVGYPERAGGAVYNAAVLIDEdGTVLANYRKTHLF---GDSERAAFTPGDRF-----------------------PV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 162 FQCDEqplFTFGVEICEDLWVPnPPSTTLAQMGAHIIVNLSASDEIIGKAGYRRDLVRQQSGRLLCAYL-YADAGfgest 240
Cdd:cd07576 130 VELRG---LRVGLLICYDVEFP-ELVRALALAGADLVLVPTALMEPYGFVARTLVPARAFENQIFVAYAnRCGAE----- 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2789482484 241 QDLVFAGHDLIAE-NGALLAESKMfEQGIIYADIDLQRLAHERQR 284
Cdd:cd07576 201 DGLTYVGLSSIAGpDGTVLARAGR-GEALLVADLDPAALAAARRE 244
|
|
| nitrilase_6 |
cd07584 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
7-284 |
2.25e-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: 143608 Cd Length: 258 Bit Score: 79.34 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 7 KIAAATPDLHVADCEYNAAEIIRQAKQAASKGAKLITFPELCLTGYTcgdlflqETLLEGAMQALG---------TVCRE 77
Cdd:cd07584 1 KVALIQMDSVLGDVKANLKKAAELCKEAAAEGADLICFPELATTGYR-------PDLLGPKLWELSepidgptvrLFSEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 78 TAELAAVIVVGLPLR--VKGKLYNVAAVVNA-GDVLAFVPKTYIpnYSEfyEQRHFVSADTLSgmenvrikaadgepcwv 154
Cdd:cd07584 74 AKELGVYIVCGFVEKggVPGKVYNSAVVIDPeGESLGVYRKIHL--WGL--EKQYFREGEQYP----------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 155 plVTDTifqcdeqPLFTFGVEICEDLWVPNpPSTTLAQMGAHIIVNLSASDEiigKAGYRRDLvrQQSGRLL--CAYLYA 232
Cdd:cd07584 133 --VFDT-------PFGKIGVMICYDMGFPE-VARILTLKGAEVIFCPSAWRE---QDADIWDI--NLPARALenTVFVAA 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2789482484 233 DAGFGESTQDLVFAGHDLIAENGALLAESKMFEQGIIYADIDLQRLAHERQR 284
Cdd:cd07584 198 VNRVGNEGDLVLFGKSKILNPRGQVLAEASEEAEEILYAEIDLDAIADYRMT 249
|
|
| CPA |
cd07573 |
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ... |
18-283 |
1.50e-14 |
|
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: 74.52 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 18 ADCEYNAAEIIRQAKQAASKGAKLITFPELCLTGYTC----GDLF-LQETLLEG----AMQALGtvcretAELAAVIVVG 88
Cdd:cd07573 12 EDPEANLAKAEELVREAAAQGAQIVCLQELFETPYFCqeedEDYFdLAEPPIPGpttaRFQALA------KELGVVIPVS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 89 L-PLRVKGKLYNVAAVVNA-GDVLAFVPKTYIPNYSEFYEQRHFVSADTlsgmenvrikaadGEPCWvplvtDTIFQCde 166
Cdd:cd07573 86 LfEKRGNGLYYNSAVVIDAdGSLLGVYRKMHIPDDPGYYEKFYFTPGDT-------------GFKVF-----DTRYGR-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 167 qplftFGVEICEDLWVPNpPSTTLAQMGAHIIVNLSAsdeiIG------KAGYR-RDLVRQ-QSGRLLCAYLYADA---- 234
Cdd:cd07573 146 -----IGVLICWDQWFPE-AARLMALQGAEILFYPTA----IGsepqepPEGLDqRDAWQRvQRGHAIANGVPVAAvnrv 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2789482484 235 GF-GESTQDLVFAGHDLIA-ENGALLAESKMFEQGIIYADIDLQRLAHERQ 283
Cdd:cd07573 216 GVeGDPGSGITFYGSSFIAdPFGEILAQASRDEEEILVAEFDLDEIEEVRR 266
|
|
| Ph0642_like |
cd07577 |
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ... |
39-291 |
3.17e-11 |
|
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: 64.24 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 39 AKLITFPELCLTGYtcgdLF--------LQETLLEG-AMQALGTVCRETAelaAVIVVGLPLRVKGKLYNVAAVVNAGDV 109
Cdd:cd07577 30 ADLIVLPELFNTGY----AFtskeevasLAESIPDGpTTRFLQELARETG---AYIVAGLPERDGDKFYNSAVVVGPEGY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 110 LAFVPKTYIpnyseFYEQRHFVSADtlsgmenvrikaadgepcwvplvtDTIFQCDEQPLFTFGVEICEDlWVPNPPSTT 189
Cdd:cd07577 103 IGIYRKTHL-----FYEEKLFFEPG------------------------DTGFRVFDIGDIRIGVMICFD-WYFPEAART 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 190 LAQMGAHIIVNLSasdeiigkagyrrDLVR---QQS--GRLLCAYLYA--------DAGFGEStqdLVFAGHDLIAE-NG 255
Cdd:cd07577 153 LALKGADIIAHPA-------------NLVLpycPKAmpIRALENRVFTitanrigtEERGGET---LRFIGKSQITSpKG 216
|
250 260 270
....*....|....*....|....*....|....*.
gi 2789482484 256 ALLAESKMFEQGIIYADIDLqRLAHERqRMNTFESI 291
Cdd:cd07577 217 EVLARAPEDGEEVLVAEIDP-RLARDK-RINEENDI 250
|
|
| nitrilase_5 |
cd07583 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
7-290 |
3.59e-10 |
|
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: 61.01 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 7 KIAAATPDLHVADCEYNAAEIIRQAKQAASKGAKLITFPELCLTGYtcgDLFLQETLLEGAMQALGTVCRETA-ELAAVI 85
Cdd:cd07583 1 KIALIQLDIVWGDPEANIERVESLIEEAAAAGADLIVLPEMWNTGY---FLDDLYELADEDGGETVSFLSELAkKHGVNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 86 VVG-LPLRVKGKLYNVAAVVNA-GDVLAfvpktyipNYSefyeQRHFVSadtLSGmENVRIKAADgEPCWVPLvtdtifq 163
Cdd:cd07583 78 VAGsVAEKEGGKLYNTAYVIDPdGELIA--------TYR----KIHLFG---LMG-EDKYLTAGD-ELEVFEL------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 164 cdeqPLFTFGVEICEDL----WvpnppSTTLAQMGAHIIVNLSASDEiigkagyrrdlVRQQSGRLLcayLYADA----- 234
Cdd:cd07583 134 ----DGGKVGLFICYDLrfpeL-----FRKLALEGAEILFVPAEWPA-----------ARIEHWRTL---LRARAienqa 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2789482484 235 ------GFGEStQDLVFAGHDL-IAENGALLAESKMfEQGIIYADIDLQRLAHERQRMNTFES 290
Cdd:cd07583 191 fvvacnRVGTD-GGNEFGGHSMvIDPWGEVLAEAGE-EEEILTAEIDLEEVAEVRKKIPVFKD 251
|
|
| nit |
cd07572 |
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ... |
18-285 |
1.83e-09 |
|
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: 58.98 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 18 ADCEYNAAEIIRQAKQAASKGAKLITFPE--LCLTGYTCGDLFLQETLLEGAMQAlgtVCRETA-ELAAVIVVG-LPLR- 92
Cdd:cd07572 11 ADKEANLARAKELIEEAAAQGAKLVVLPEcfNYPGGTDAFKLALAEEEGDGPTLQ---ALSELAkEHGIWLVGGsIPERd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 93 -VKGKLYNVAAVVNA-GDVLAfvpkTY---------IPNYSEFYEqrhfvSADTLSGMEnvrikaadgepcwvPLVTDTi 161
Cdd:cd07572 88 dDDGKVYNTSLVFDPdGELVA----RYrkihlfdvdVPGGISYRE-----SDTLTPGDE--------------VVVVDT- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 162 fqcdeqPLFTFGVEICEDLWVPnPPSTTLAQMGAHIIVNLSASDEIIGKAGYrrdlvrqqsgRLLC--------AYLYAD 233
Cdd:cd07572 144 ------PFGKIGLGICYDLRFP-ELARALARQGADILTVPAAFTMTTGPAHW----------ELLLraraienqCYVVAA 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2789482484 234 AGFGESTQDLVFAGHDLIAEN-GALLAE-SKmfEQGIIYADIDLQRLAHERQRM 285
Cdd:cd07572 207 AQAGDHEAGRETYGHSMIVDPwGEVLAEaGE--GEGVVVAEIDLDRLEEVRRQI 258
|
|
| PLN02747 |
PLN02747 |
N-carbamolyputrescine amidase |
18-288 |
1.45e-08 |
|
N-carbamolyputrescine amidase
Pssm-ID: 215398 Cd Length: 296 Bit Score: 56.70 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 18 ADCEYNAAEIIRQAKQAASKGAKLITFPELCLTGYTCG----DLFLQETLLEG-----AMQALGtvcretAELAAVIVVG 88
Cdd:PLN02747 18 DDRAANVDKAERLVREAHAKGANIILIQELFEGYYFCQaqreDFFQRAKPYEGhptiaRMQKLA------KELGVVIPVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 89 LPLRVKGKLYNVAAVVNA-GDVLAFVPKTYIPNYSEFYEQRHFVSADTlsGMEnvrikaadgepcwvplVTDTIFQcdeq 167
Cdd:PLN02747 92 FFEEANNAHYNSIAIIDAdGTDLGLYRKSHIPDGPGYQEKFYFNPGDT--GFK----------------VFDTKFA---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 168 plfTFGVEICEDLWVPNpPSTTLAQMGAHIIVNLSA-----SDEIIGKAGYRRDLVRQQSGRLLCAyLYADAGFG----- 237
Cdd:PLN02747 150 ---KIGVAICWDQWFPE-AARAMVLQGAEVLLYPTAigsepQDPGLDSRDHWKRVMQGHAGANLVP-LVASNRIGteile 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2789482484 238 --ESTQDLVFAGHDLIAEN-GALLAESKMFEQGIIYADIDLQRLAHERQRMNTF 288
Cdd:PLN02747 225 teHGPSKITFYGGSFIAGPtGEIVAEADDKAEAVLVAEFDLDQIKSKRASWGVF 278
|
|
| nadE |
PRK00768 |
ammonia-dependent NAD(+) synthetase; |
340-465 |
3.73e-07 |
|
ammonia-dependent NAD(+) synthetase;
Pssm-ID: 234831 [Multi-domain] Cd Length: 268 Bit Score: 52.07 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 340 LATRLRHTHAKTAVVGLSGGLDSTLA--LIVLvhAFDMLELDRKGI----LAVTMPcfgttartkgnaeklaeaYGV--- 410
Cdd:PRK00768 29 LKDYLKKSGLKSLVLGISGGQDSTLAgrLAQL--AVEELRAETGDDdyqfIAVRLP------------------YGVqad 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2789482484 411 ------TLE--------TVDIKAAVD---QHFEDIGQSKEDlsvtFENG--QARMRTLVLMNLANKTGGMVVGT 465
Cdd:PRK00768 89 eddaqdALAfiqpdrvlTVNIKPAVDasvAALEAAGIELSD----FVKGniKARERMIAQYAIAGATGGLVVGT 158
|
|
| nitrilases_CHs |
cd07564 |
Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases ... |
6-283 |
1.47e-06 |
|
Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases (nitrile aminohydrolases, EC:3.5.5.1) hydrolyze nitriles (RCN) to ammonia and the corresponding carboxylic acid. Most nitrilases prefer aromatic nitriles, some prefer arylacetonitriles and others aliphatic nitriles. This group includes the nitrilase cyanide dihydratase (CDH), which hydrolyzes inorganic cyanide (HCN) to produce formate. It also includes cyanide hydratase (CH), which hydrolyzes HCN to formamide. This group includes four Arabidopsis thaliana nitrilases (Ath)NIT1-4. AthNIT1-3 have a strong substrate preference for phenylpropionitrile (PPN) and other nitriles which may originate from the breakdown of glucosinolates. The product of PPN hydrolysis, phenylacetic acid has auxin activity. AthNIT1-3 can also convert indoacetonitrile to indole-3-acetic acid (IAA, auxin), but with a lower affinity and velocity. From their expression patterns, it has been speculated that NIT3 may produce IAA during the early stages of germination, and that NIT3 may produce IAA during embryo development and maturation. AthNIT4 has a strong substrate specificity for the nitrile, beta-cyano-L-alanine (Ala(CN)), an intermediate of cyanide detoxification. AthNIT4 has both a nitrilase activity and a nitrile hydratase (NHase) activity, which generate aspartic acid and asparagine respectively from Ala(CN). NHase catalyzes the hydration of nitriles to their corresponding amides. This subgroup belongs to a larger nitrilase superfamily comprised of belong to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 1.
Pssm-ID: 143588 Cd Length: 297 Bit Score: 50.56 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 6 IKIAAAtpdlHVADCEYNAAE----IIRQAKQAASKGAKLITFPELCLTGY--------TCGDLFLQETLLEGA------ 67
Cdd:cd07564 1 VKVAAV----QAAPVFLDLAAtvekACRLIEEAAANGAQLVVFPEAFIPGYpywiwfgaPAEGRELFARYYENSvevdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 68 -MQALGTVCRETaelAAVIVVGLPLRVKGKLYNVAAVVNA-GDVLAfVPKTYIPNYSEfyeqR---------HFVSADTL 136
Cdd:cd07564 77 eLERLAEAAREN---GIYVVLGVSERDGGTLYNTQLLIDPdGELLG-KHRKLKPTHAE----RlvwgqgdgsGLRVVDTP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 137 SGmenvRIKAADgepCW---VPLvtdtifqcDEQPLFTFGVEI-CE---DLWVPNP-PSTTLAQMGAHII----VNLSAS 204
Cdd:cd07564 149 IG----RLGALI---CWenyMPL--------ARYALYAQGEQIhVApwpDFSPYYLsREAWLAASRHYALegrcFVLSAC 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 205 DeIIGKAGYRRDLVRQQSGRLLcaylyadagfgestqDLVFAGHDLI-AENGALLAESKMFEQGIIYADIDLQRLAHERQ 283
Cdd:cd07564 214 Q-VVTEEDIPADCEDDEEADPL---------------EVLGGGGSAIvGPDGEVLAGPLPDEEGILYADIDLDDIVEAKL 277
|
|
| ScNTA1_like |
cd07566 |
Saccharomyces cerevisiae N-terminal amidase NTA1, and related proteins (class 3 nitrilases); ... |
23-149 |
1.24e-04 |
|
Saccharomyces cerevisiae N-terminal amidase NTA1, and related proteins (class 3 nitrilases); Saccharomyces cerevisiae NTA1 functions in the N-end rule protein degradation pathway. It specifically deaminates the N-terminal asparagine and glutamine residues of substrates of this pathway, to aspartate and glutamate respectively, these latter are the destabilizing residues. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 3.
Pssm-ID: 143590 Cd Length: 295 Bit Score: 44.25 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 23 NAAEIIRQAKQAAS-KGAKLITFPELCLTGYTCGDL-----FLQETlLEGAMQALgtvCRETAE-LAAVIVVGLPLRVKG 95
Cdd:cd07566 20 RAWELLDKTKKRAKlKKPDILVLPELALTGYNFHSLehikpYLEPT-TSGPSFEW---AREVAKkFNCHVVIGYPEKVDE 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 96 ---KLYNVAAVVNA-GDVLAFVPKTYI------------PNYSEFYEQRHFVSADTLSGMENVRIKAADG 149
Cdd:cd07566 96 sspKLYNSALVVDPeGEVVFNYRKSFLyytdeewgceenPGGFQTFPLPFAKDDDFDGGSVDVTLKTSIG 165
|
|
| ML_beta-AS_like |
cd07568 |
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ... |
32-204 |
1.72e-04 |
|
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: 44.02 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 32 KQAASKGAKLITFPELCLTGYTCGD-----LFLQETLLEGA----MQALGTvcretaELAAVIVVGLPLRVK-GKLYNVA 101
Cdd:cd07568 37 REAAEAGAQIVCLQEIFYGPYFCAEqdtkwYEFAEEIPNGPttkrFAALAK------EYNMVLILPIYEKEQgGTLYNTA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 102 AVVNA-GDVLAFVPKTYIPNYSEFYEQRHFVSADTlsgmenvrikaadGEPcwvplVTDTIFQcdeqplfTFGVEICEDL 180
Cdd:cd07568 111 AVIDAdGTYLGKYRKNHIPHVGGFWEKFYFRPGNL-------------GYP-----VFDTAFG-------KIGVYICYDR 165
|
170 180
....*....|....*....|....
gi 2789482484 181 WVPNpPSTTLAQMGAHIIVNLSAS 204
Cdd:cd07568 166 HFPE-GWRALGLNGAEIVFNPSAT 188
|
|
| nitrilase_1_R2 |
cd07579 |
Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ... |
6-198 |
5.88e-04 |
|
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: 42.16 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 6 IKIAAATPDLHVADceyNAAEIIRQAKQAASKGAKLITFPELCLTGYTcGDLFLQETLLEGAMQALGTVCRetaELAAVI 85
Cdd:cd07579 2 IAVAQFAPTPDIAG---NLATIDRLAAEAKATGAELVVFPELALTGLD-DPASEAESDTGPAVSALRRLAR---RLRLYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 86 VVGLPLRVKGKLYNVAAVVNAGDVLAFVPKTYIpnysefyeqrhfvsadtlsgMENVRIKAADGEpCWVplVTDTifqcd 165
Cdd:cd07579 75 VAGFAEADGDGLYNSAVLVGPEGLVGTYRKTHL--------------------IEPERSWATPGD-TWP--VYDL----- 126
|
170 180 190
....*....|....*....|....*....|...
gi 2789482484 166 eqPLFTFGVEICEDLWVPNpPSTTLAQMGAHII 198
Cdd:cd07579 127 --PLGRVGLLIGHDALFPE-AGRVLALRGCDLL 156
|
|
| PTZ00323 |
PTZ00323 |
NAD+ synthase; Provisional |
344-558 |
7.72e-04 |
|
NAD+ synthase; Provisional
Pssm-ID: 185554 [Multi-domain] Cd Length: 294 Bit Score: 42.07 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 344 LRHTHAKTAVVGLSGGLDSTLALIVLVHAFDMLELDRKGILAVTMPCFgTTARTKGNAEKLAEAYGVTLETVDIKAAVDQ 423
Cdd:PTZ00323 41 MRRCGLKGCVTSVSGGIDSAVVLALCARAMRMPNSPIQKNVGLCQPIH-SSAWALNRGRENIQACGATEVTVDQTEIHTQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 424 HFEDIGQSKEDLSVTFENGQAR--MRTLV------LMNlANKTGGMVVGTGDLSE-LALGWATYNGDhmsmygvnGSIPK 494
Cdd:PTZ00323 120 LSSLVEKAVGIKGGAFARGQLRsyMRTPVafyvaqLLS-QEGTPAVVMGTGNFDEdGYLGYFCKAGD--------GVVDV 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2789482484 495 TLVRYLVAYEADRVQGELSdVLRDVLDTPVSPELLppkDGeisQKTEDLVG-PYELHDFFLYYML 558
Cdd:PTZ00323 191 QLISDLHKSEVFLVARELG-VPENTLQAAPSADLW---EG---QTDEDELGfPYDFVELYTEWYL 248
|
|
| nadE |
PRK00876 |
NAD(+) synthase; |
331-422 |
8.27e-04 |
|
NAD(+) synthase;
Pssm-ID: 179150 [Multi-domain] Cd Length: 326 Bit Score: 41.86 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 331 EILTLQATGLATRLRHT---------HAKTAVVGLSGGLDSTLALIVLVHAfdmleLDRKGILAVTMPCFGTTARTKGNA 401
Cdd:PRK00876 6 DVLKIDAAAEAERIRAAireqvrgtlRRRGVVLGLSGGIDSSVTAALCVRA-----LGKERVYGLLMPERDSSPESLRLG 80
|
90 100
....*....|....*....|.
gi 2789482484 402 EKLAEAYGVTLETVDIKAAVD 422
Cdd:PRK00876 81 REVAEHLGVEYVVEDITPALE 101
|
|
| COG1365 |
COG1365 |
Predicted ATPase, PP-loop superfamily [General function prediction only]; |
327-492 |
1.29e-03 |
|
Predicted ATPase, PP-loop superfamily [General function prediction only];
Pssm-ID: 440976 Cd Length: 256 Bit Score: 41.19 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 327 ERCEEILTLQATGLATRLRHTHAK--TAVVGLSGGLDSTLALIVLVHA-FDmleldrkgILAVTmpCFGT---TARTKGN 400
Cdd:COG1365 36 ERLRELLEKRLNGPKEFLKRSKEKnpKVVVAFSGGVDSSASLIIAKWIgFD--------VEAVT--VKSTiilPQMFKKN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 401 AEKLAEAYGVTLETVDIkaavdqhfeDIGQSKEDLsvtfENGQA----RMRTLV---LMNLANKTGGMVVGTGDLseLAL 473
Cdd:COG1365 106 IKELCKKLNVKHEFIEI---------DLGEIIEDA----LKGKFhpcgRCHSLIeeaVEDYAKKNGIKIVIFGDL--LSV 170
|
170
....*....|....*....
gi 2789482484 474 GwatyngdHMSMYGVNGSI 492
Cdd:COG1365 171 G-------YLSIYKKDGIV 182
|
|
| DCase |
cd07569 |
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ... |
25-130 |
2.15e-03 |
|
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: 40.76 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 25 AEIIRQAKQAASKGAKLITFPELCLTG----YTCGDLFLQETLLEGAMQALGTVC--RETAELAAVIVVGLP-LRVKGKL 97
Cdd:cd07569 25 ARLIALLEEAASRGAQLVVFPELALTTffprWYFPDEAELDSFFETEMPNPETQPlfDRAKELGIGFYLGYAeLTEDGGV 104
|
90 100 110
....*....|....*....|....*....|....*..
gi 2789482484 98 ---YNVAAVVNA-GDVLAFVPKTYIPNYSEFYEQRHF 130
Cdd:cd07569 105 krrFNTSILVDKsGKIVGKYRKVHLPGHKEPEPYRPF 141
|
|
| QueC |
pfam06508 |
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ... |
351-431 |
3.66e-03 |
|
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis of 7-carboxy-7-deazaguanine. They catalyze the conversion of 7-deaza-7-carboxyguanine to preQ0.
Pssm-ID: 428982 [Multi-domain] Cd Length: 210 Bit Score: 39.14 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789482484 351 TAVVGLSGGLDSTLALIVLVHAFDMLEldrkgilAVTMPCFGTTARTKGNAEKLAEAYGVTLETVDIkaavdQHFEDIGQ 430
Cdd:pfam06508 1 KAVVLLSGGLDSTTCLAWAKKEGYEVY-------ALSFDYGQRHRKELECAKKIAKALGVEHKILDL-----DFLKQIGG 68
|
.
gi 2789482484 431 S 431
Cdd:pfam06508 69 S 69
|
|
| |
