|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02339 |
PLN02339 |
NAD+ synthase (glutamine-hydrolysing) |
3-699 |
0e+00 |
|
NAD+ synthase (glutamine-hydrolysing)
Pssm-ID: 177973 [Multi-domain] Cd Length: 700 Bit Score: 1095.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 3 RKVTVATCALNQWALDFEGNLQRILKSIEIAKNRGARYRLGPELEICGYGCWDHYYESDTLLHSFQVLAALVESPVTQDI 82
Cdd:PLN02339 2 RLLKVATCNLNQWAMDFDGNLKRIKESIAEAKAAGAVYRVGPELEITGYGCEDHFLELDTVTHSWECLAEILVGDLTDGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 83 ICDVGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANEGNYRELRWFTPWSRSRHTEEYFLPRMIQDLTKQETVPFGDAV 162
Cdd:PLN02339 82 LCDIGMPVIHGGVRYNCRVFCLNRKILLIRPKMWLANDGNYRELRWFTAWKHKKKVEDFQLPEEIAEATSQKSVPFGDGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 163 LVTWDTCIGSEICEELWTPHSPHIDMGLDGVEIITNASGSHQVLRKANTRVDLVTMVTSKNGGIYLLANQKGCDGDRLYY 242
Cdd:PLN02339 162 LQFLDTAVAAETCEELFTPQAPHIDLALNGVEIISNGSGSHHQLRKLNTRLDLIRSATHKCGGVYLYANQRGCDGGRLYY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 243 DGCAMIAMNGSVFAQGSQFSLDDVEVLTATLDLEDVRSYRAEISSRNLAASRASPYPRVKVDFALSCHEDLLAPISEPIE 322
Cdd:PLN02339 242 DGCACIVVNGEVVAQGSQFSLQDVEVVTACVDLDAVVSFRGSISSFREQASSKKRVPSVAVPFKLCPPFSLSLVPSSPLK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 323 WKYHSPEEEISLGPACWLWDFLRRSQQAGFLLPLSGGVDSAATACLIYSMCCQVCEAVRSGNEEVLADVRTIVNQIS-YT 401
Cdd:PLN02339 322 IRYHSPEEEIALGPACWLWDYLRRSGASGFLLPLSGGADSSSVAAIVGSMCQLVVKAIREGDEQVKADARRIGNYADgEV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 402 PQDPRDLCGRILTTCYMASKNSSQETCTRARELAQQIGSHHISLNIDPAVKAVMGIFSLVTGKSPLFAAHGGSSRENLAL 481
Cdd:PLN02339 402 PTDSKEFAKRIFYTVYMGSENSSEETRSRAKQLADEIGSSHLDVKIDGVVSAVLSLFQTLTGKRPRYKVDGGSNAENLAL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 482 QNVQARIRMVLAYLFAQLSLWSRGVHGGLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFVQFCIQRFQLP 561
Cdd:PLN02339 482 QNIQARIRMVLAFMLASLLPWVRGKSGFLLVLGSANVDEGLRGYLTKYDCSSADINPIGGISKQDLRSFLRWAATNLGYP 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 562 ALQSILLAPATAELEPLADGQvSQTDEEDMGMTYAELSVYGKLRKVAKMGPYSMFCKLLGMWRHICTPRQVADKVKRFFS 641
Cdd:PLN02339 562 SLAEVEAAPPTAELEPIRDDY-SQTDEEDMGMTYEELGVYGRLRKIFRCGPVSMFKNLCHEWNGRLSPSEVAAKVKDFFK 640
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 41393551 642 KYSMNRHKMTTLTPAYHAENYSPEDNRFDLRPFLYNTSWPWQFRCIENQVLQLERAEP 699
Cdd:PLN02339 641 YYSINRHKMTTLTPSYHAESYSPDDNRFDLRQFLYNTRWPYQFRKIDELVEELDGETV 698
|
|
| GAT_Gln-NAD-synth |
cd07570 |
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ... |
6-298 |
2.18e-94 |
|
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: 293.22 E-value: 2.18e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 6 TVATCALNQWALDFEGNLQRILKSIEIAKNRGARYRLGPELEICGYGCWDHYYESDTLLHSFQVLAALVESPVTQDIICD 85
Cdd:cd07570 1 RIALAQLNPTVGDLEGNAEKILEAIREAKAQGADLVVFPELSLTGYPPEDLLLRPDFLEAAEEALEELAAATADLDIAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 86 VGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANEGNYRELRWFTPWSRSrhteeyflprmiqdltkqetvpfgdAVLVT 165
Cdd:cd07570 81 VGLPLRHDGKLYNAAAVLQNGKILGVVPKQLLPNYGVFDEKRYFTPGDKP-------------------------DVLFF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 166 WDTCIGSEICEELWTPHSPHIDMGLDGVEIITNASGSHQVLRKANTRVDLVTMVTSKNGGIYLLANQkGCDGDRLYYDGC 245
Cdd:cd07570 136 KGLRIGVEICEDLWVPDPPSAELALAGADLILNLSASPFHLGKQDYRRELVSSRSARTGLPYVYVNQ-VGGQDDLVFDGG 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 41393551 246 AMIAMN-GSVFAQGSQFslddvEVLTATLDLEDVRSYRAEISSrnLAASRASPY 298
Cdd:cd07570 215 SFIADNdGELLAEAPRF-----EEDLADVDLDRLRSERRRNSS--FLDEEAEIY 261
|
|
| CN_hydrolase |
pfam00795 |
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ... |
6-283 |
1.21e-50 |
|
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: 177.16 E-value: 1.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 6 TVATCALNQWALDFEGNLQRILKSIEIAKNRGARYRLGPELEICGYGCWDHYYESDTlLHSFQVLAALVESPVTQDIICD 85
Cdd:pfam00795 1 RVALVQLPQGFWDLEANLQKALELIEEAARYGADLIVLPELFITGYPCWAHFLEAAE-VGDGETLAGLAALARKNGIAIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 86 VGmpVMHRNVrYNCRviFLNRKILLIRPKMALaneGNYRELRWFTPWSRSRHTEEyflprmiqdltkqETVPFGDAVLV- 164
Cdd:pfam00795 80 IG--LIERWL-TGGR--LYNTAVLLDPDGKLV---GKYRKLHLFPEPRPPGFRER-------------VLFEPGDGGTVf 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 165 -TWDTCIGSEICEELWTPHSPHIdMGLDGVEIITNAS-GSHQVLRKANTRVDLVTMVTSKNGGIYLL-ANQKGCDGD-RL 240
Cdd:pfam00795 139 dTPLGKIGAAICYEIRFPELLRA-LALKGAEILINPSaRAPFPGSLGPPQWLLLARARALENGCFVIaANQVGGEEDaPW 217
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 41393551 241 YYDGCAMIAMNGSVFAQGSQFSLddvEVLTATLDLEDVRSYRA 283
Cdd:pfam00795 218 PYGHSMIIDPDGRILAGAGEWEE---GVLIADIDLALVRAWRY 257
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
68-658 |
5.94e-43 |
|
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: 163.48 E-value: 5.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 68 QVLAALVESPVTQDIICDVGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANEGNYRELRWFTPWsrsRHTEEYFLPRMI 147
Cdd:COG0171 20 AAAAALAALAAAAAALLLLLLLLLLLLLLLLALLLLLAAARLLVAAAALLLLALAAGGGAALAGG---GGGAGGGLLNGA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 148 QDLTKQETVPFGDAVLVTWDTCIGSEICEELWTPHSPHIDMGLDGVEIITNASGSHQVLRKANTRVDLVTMVTSKNGGIY 227
Cdd:COG0171 97 ALVLGGGDLLFFADDFLLLLLVVEEEEEEFVGGPPPPPAALGGAGVLLILSSSSSAVGAAAAAAALAAALLSSLSSAAYY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 228 LLANQKGCDGDRLYYDGCAMIAMNGSVFAQGSQFSLDDVEVLTATLDLEDVRSYRAEISSRNLAASRASPYPRvkvdfal 307
Cdd:COG0171 177 AAAGGGESTTDLARGGGGGLLLVVLLLVGGGDDDFFDGGSAAVDDDDLLLLLRRRREEELLLARARDADGGRR------- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 308 sCHEDLLAPISEPIEWKYHSPEEEISLGpacwLWDFLRRSQQAGFLLPLSGGVDSAATACLiysmccqVCEAVrsGNEEV 387
Cdd:COG0171 250 -VAAEAAPPPPEEEEMDLEEVYDALVLG----LRDYVRKNGFKGVVLGLSGGIDSALVAAL-------AVDAL--GPENV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 388 LAdvrtivnqisytpqdprdlcgrilttCYMASKNSSQETCTRARELAQQIGSHHISLNIDPAVKAVMGIFSLVTGKSPl 467
Cdd:COG0171 316 LG--------------------------VTMPSRYTSDESLEDAEELAENLGIEYEEIDITPAVEAFLEALPHAFGGEL- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 468 faahggssrENLALQNVQARIRMVLAYLFAQLslwsrgvHGGlLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDL 547
Cdd:COG0171 369 ---------DDVAEENLQARIRMVILMALANK-------FGG-LVLGTGNKSELAVGYFTKYGDGAGDLAPIADLYKTQV 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 548 RAFVQFcIQRFQLPALQSILLAPATAELEPladgqvSQTDEEDMGmTYAELSvygklrkvakmgpysmFCkLLGMWRHIC 627
Cdd:COG0171 432 YALARW-LNRNGEVIPEDIIDKPPSAELRP------GQTDEDELG-PYEVLD----------------AI-LYAYVEEGL 486
|
570 580 590
....*....|....*....|....*....|....*..
gi 41393551 628 TPRQVA------DKVKRFFSKYSMNRHKMTTLTPAYH 658
Cdd:COG0171 487 SPEEIAaagydrEWVERVLRLVRRNEYKRRQPPPGPK 523
|
|
| nadE |
TIGR00552 |
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ... |
340-665 |
1.39e-35 |
|
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: 134.82 E-value: 1.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 340 LWDFLR----RSQQAGFLLPLSGGVDSAATACLiysmccqvceAVRSGNEEVLAdvrtivnqisytpqdprdlcGRIltt 415
Cdd:TIGR00552 9 IEDFLRgyvqKSGAKGVVLGLSGGIDSAVVAAL----------CVEALGEQNHA--------------------LLL--- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 416 cyMASKNSSQETCTRARELAQQIGSHHISLNIDPAVKAVMGIFSLVTGKSPLfaahggssrenLALQNVQARIRMVLAYL 495
Cdd:TIGR00552 56 --PHSVQTPEQDVQDALALAEPLGINYKNIDIAPIAASFQAQTETGDELSDF-----------LAKGNLKARLRMAALYA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 496 FAQLSlwsrgvhgGLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFVqfciQRFQLPalQSILLAPATAEL 575
Cdd:TIGR00552 123 IANKH--------NLLVLGTGNKSELMLGYFTKYGDGGCDIAPIGDLFKTQVYELA----KRLNVP--ERIIEKPPTADL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 576 EPladgqvSQTDEEDMGMTYAELSVYGKLRKVAKmgpysmfckllgmwrhictpRQVADKVKRFFSKYSMNRHKMTtlTP 655
Cdd:TIGR00552 189 FD------GQTDETELGITYDELDDYLKGIEELS--------------------QTVQEVVKRIESLVQKSEHKRR--LP 240
|
330
....*....|
gi 41393551 656 AYHAENYSPE 665
Cdd:TIGR00552 241 ATIFDLFWKQ 250
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02339 |
PLN02339 |
NAD+ synthase (glutamine-hydrolysing) |
3-699 |
0e+00 |
|
NAD+ synthase (glutamine-hydrolysing)
Pssm-ID: 177973 [Multi-domain] Cd Length: 700 Bit Score: 1095.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 3 RKVTVATCALNQWALDFEGNLQRILKSIEIAKNRGARYRLGPELEICGYGCWDHYYESDTLLHSFQVLAALVESPVTQDI 82
Cdd:PLN02339 2 RLLKVATCNLNQWAMDFDGNLKRIKESIAEAKAAGAVYRVGPELEITGYGCEDHFLELDTVTHSWECLAEILVGDLTDGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 83 ICDVGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANEGNYRELRWFTPWSRSRHTEEYFLPRMIQDLTKQETVPFGDAV 162
Cdd:PLN02339 82 LCDIGMPVIHGGVRYNCRVFCLNRKILLIRPKMWLANDGNYRELRWFTAWKHKKKVEDFQLPEEIAEATSQKSVPFGDGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 163 LVTWDTCIGSEICEELWTPHSPHIDMGLDGVEIITNASGSHQVLRKANTRVDLVTMVTSKNGGIYLLANQKGCDGDRLYY 242
Cdd:PLN02339 162 LQFLDTAVAAETCEELFTPQAPHIDLALNGVEIISNGSGSHHQLRKLNTRLDLIRSATHKCGGVYLYANQRGCDGGRLYY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 243 DGCAMIAMNGSVFAQGSQFSLDDVEVLTATLDLEDVRSYRAEISSRNLAASRASPYPRVKVDFALSCHEDLLAPISEPIE 322
Cdd:PLN02339 242 DGCACIVVNGEVVAQGSQFSLQDVEVVTACVDLDAVVSFRGSISSFREQASSKKRVPSVAVPFKLCPPFSLSLVPSSPLK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 323 WKYHSPEEEISLGPACWLWDFLRRSQQAGFLLPLSGGVDSAATACLIYSMCCQVCEAVRSGNEEVLADVRTIVNQIS-YT 401
Cdd:PLN02339 322 IRYHSPEEEIALGPACWLWDYLRRSGASGFLLPLSGGADSSSVAAIVGSMCQLVVKAIREGDEQVKADARRIGNYADgEV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 402 PQDPRDLCGRILTTCYMASKNSSQETCTRARELAQQIGSHHISLNIDPAVKAVMGIFSLVTGKSPLFAAHGGSSRENLAL 481
Cdd:PLN02339 402 PTDSKEFAKRIFYTVYMGSENSSEETRSRAKQLADEIGSSHLDVKIDGVVSAVLSLFQTLTGKRPRYKVDGGSNAENLAL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 482 QNVQARIRMVLAYLFAQLSLWSRGVHGGLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFVQFCIQRFQLP 561
Cdd:PLN02339 482 QNIQARIRMVLAFMLASLLPWVRGKSGFLLVLGSANVDEGLRGYLTKYDCSSADINPIGGISKQDLRSFLRWAATNLGYP 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 562 ALQSILLAPATAELEPLADGQvSQTDEEDMGMTYAELSVYGKLRKVAKMGPYSMFCKLLGMWRHICTPRQVADKVKRFFS 641
Cdd:PLN02339 562 SLAEVEAAPPTAELEPIRDDY-SQTDEEDMGMTYEELGVYGRLRKIFRCGPVSMFKNLCHEWNGRLSPSEVAAKVKDFFK 640
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 41393551 642 KYSMNRHKMTTLTPAYHAENYSPEDNRFDLRPFLYNTSWPWQFRCIENQVLQLERAEP 699
Cdd:PLN02339 641 YYSINRHKMTTLTPSYHAESYSPDDNRFDLRQFLYNTRWPYQFRKIDELVEELDGETV 698
|
|
| GAT_Gln-NAD-synth |
cd07570 |
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ... |
6-298 |
2.18e-94 |
|
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: 293.22 E-value: 2.18e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 6 TVATCALNQWALDFEGNLQRILKSIEIAKNRGARYRLGPELEICGYGCWDHYYESDTLLHSFQVLAALVESPVTQDIICD 85
Cdd:cd07570 1 RIALAQLNPTVGDLEGNAEKILEAIREAKAQGADLVVFPELSLTGYPPEDLLLRPDFLEAAEEALEELAAATADLDIAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 86 VGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANEGNYRELRWFTPWSRSrhteeyflprmiqdltkqetvpfgdAVLVT 165
Cdd:cd07570 81 VGLPLRHDGKLYNAAAVLQNGKILGVVPKQLLPNYGVFDEKRYFTPGDKP-------------------------DVLFF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 166 WDTCIGSEICEELWTPHSPHIDMGLDGVEIITNASGSHQVLRKANTRVDLVTMVTSKNGGIYLLANQkGCDGDRLYYDGC 245
Cdd:cd07570 136 KGLRIGVEICEDLWVPDPPSAELALAGADLILNLSASPFHLGKQDYRRELVSSRSARTGLPYVYVNQ-VGGQDDLVFDGG 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 41393551 246 AMIAMN-GSVFAQGSQFslddvEVLTATLDLEDVRSYRAEISSrnLAASRASPY 298
Cdd:cd07570 215 SFIADNdGELLAEAPRF-----EEDLADVDLDRLRSERRRNSS--FLDEEAEIY 261
|
|
| NAD_synthase |
cd00553 |
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ... |
327-650 |
1.95e-91 |
|
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: 284.83 E-value: 1.95e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 327 SPEEEISLGPACWLWDFLRRSQQAGFLLPLSGGVDSAATACLIYSMCCqvceavrsgneevladvrtivnqisytpqdpr 406
Cdd:cd00553 1 IDPEEIIEALVCFLRDYLRKSGAKGFVLGLSGGIDSAVVAALAVRALG-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 407 dlCGRILTTCYMaSKNSSQETCTRARELAQQIGSHHISLNIDPAVKAVMGIFSLVtgksplfaahGGSSRENLALQNVQA 486
Cdd:cd00553 49 --AENVLALIMP-SRYSSKETRDDAKALAENLGIEYRTIDIDPIVDAFLKALEHA----------GGSEAEDLALGNIQA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 487 RIRMVLAYLFAQLSlwsrgvhgGLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFVQFCIqrfqlpALQSI 566
Cdd:cd00553 116 RLRMVLLYALANLL--------GGLVLGTGNKSELLLGYFTKYGDGAADINPIGDLYKTQVRELARYLG------VPEEI 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 567 LLAPATAELEPladgqvSQTDEEDMGMTYAELSVYGKLRKVAKMGPYSmfckllgmwrhICTPRQVADKVKRFFSKYSMN 646
Cdd:cd00553 182 IEKPPSAELWP------GQTDEDELGMPYEELDLILYGLVDGKLGPEE-----------ILSPGEDEEKVKRIFRLYRRN 244
|
....
gi 41393551 647 RHKM 650
Cdd:cd00553 245 EHKR 248
|
|
| CN_hydrolase |
pfam00795 |
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ... |
6-283 |
1.21e-50 |
|
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: 177.16 E-value: 1.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 6 TVATCALNQWALDFEGNLQRILKSIEIAKNRGARYRLGPELEICGYGCWDHYYESDTlLHSFQVLAALVESPVTQDIICD 85
Cdd:pfam00795 1 RVALVQLPQGFWDLEANLQKALELIEEAARYGADLIVLPELFITGYPCWAHFLEAAE-VGDGETLAGLAALARKNGIAIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 86 VGmpVMHRNVrYNCRviFLNRKILLIRPKMALaneGNYRELRWFTPWSRSRHTEEyflprmiqdltkqETVPFGDAVLV- 164
Cdd:pfam00795 80 IG--LIERWL-TGGR--LYNTAVLLDPDGKLV---GKYRKLHLFPEPRPPGFRER-------------VLFEPGDGGTVf 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 165 -TWDTCIGSEICEELWTPHSPHIdMGLDGVEIITNAS-GSHQVLRKANTRVDLVTMVTSKNGGIYLL-ANQKGCDGD-RL 240
Cdd:pfam00795 139 dTPLGKIGAAICYEIRFPELLRA-LALKGAEILINPSaRAPFPGSLGPPQWLLLARARALENGCFVIaANQVGGEEDaPW 217
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 41393551 241 YYDGCAMIAMNGSVFAQGSQFSLddvEVLTATLDLEDVRSYRA 283
Cdd:pfam00795 218 PYGHSMIIDPDGRILAGAGEWEE---GVLIADIDLALVRAWRY 257
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
68-658 |
5.94e-43 |
|
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: 163.48 E-value: 5.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 68 QVLAALVESPVTQDIICDVGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANEGNYRELRWFTPWsrsRHTEEYFLPRMI 147
Cdd:COG0171 20 AAAAALAALAAAAAALLLLLLLLLLLLLLLLALLLLLAAARLLVAAAALLLLALAAGGGAALAGG---GGGAGGGLLNGA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 148 QDLTKQETVPFGDAVLVTWDTCIGSEICEELWTPHSPHIDMGLDGVEIITNASGSHQVLRKANTRVDLVTMVTSKNGGIY 227
Cdd:COG0171 97 ALVLGGGDLLFFADDFLLLLLVVEEEEEEFVGGPPPPPAALGGAGVLLILSSSSSAVGAAAAAAALAAALLSSLSSAAYY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 228 LLANQKGCDGDRLYYDGCAMIAMNGSVFAQGSQFSLDDVEVLTATLDLEDVRSYRAEISSRNLAASRASPYPRvkvdfal 307
Cdd:COG0171 177 AAAGGGESTTDLARGGGGGLLLVVLLLVGGGDDDFFDGGSAAVDDDDLLLLLRRRREEELLLARARDADGGRR------- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 308 sCHEDLLAPISEPIEWKYHSPEEEISLGpacwLWDFLRRSQQAGFLLPLSGGVDSAATACLiysmccqVCEAVrsGNEEV 387
Cdd:COG0171 250 -VAAEAAPPPPEEEEMDLEEVYDALVLG----LRDYVRKNGFKGVVLGLSGGIDSALVAAL-------AVDAL--GPENV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 388 LAdvrtivnqisytpqdprdlcgrilttCYMASKNSSQETCTRARELAQQIGSHHISLNIDPAVKAVMGIFSLVTGKSPl 467
Cdd:COG0171 316 LG--------------------------VTMPSRYTSDESLEDAEELAENLGIEYEEIDITPAVEAFLEALPHAFGGEL- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 468 faahggssrENLALQNVQARIRMVLAYLFAQLslwsrgvHGGlLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDL 547
Cdd:COG0171 369 ---------DDVAEENLQARIRMVILMALANK-------FGG-LVLGTGNKSELAVGYFTKYGDGAGDLAPIADLYKTQV 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 548 RAFVQFcIQRFQLPALQSILLAPATAELEPladgqvSQTDEEDMGmTYAELSvygklrkvakmgpysmFCkLLGMWRHIC 627
Cdd:COG0171 432 YALARW-LNRNGEVIPEDIIDKPPSAELRP------GQTDEDELG-PYEVLD----------------AI-LYAYVEEGL 486
|
570 580 590
....*....|....*....|....*....|....*..
gi 41393551 628 TPRQVA------DKVKRFFSKYSMNRHKMTTLTPAYH 658
Cdd:COG0171 487 SPEEIAaagydrEWVERVLRLVRRNEYKRRQPPPGPK 523
|
|
| NAD_synthase |
pfam02540 |
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ... |
339-649 |
1.82e-36 |
|
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: 137.13 E-value: 1.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 339 WLWDFLRRSQQAGFLLPLSGGVDSAATACLiysmcCQvcEAVrsGNEEVLAdvrtivnqisytpqdprdlcgrilttCYM 418
Cdd:pfam02540 8 FLRDYVQKAGFKGVVLGLSGGIDSSLVAYL-----AV--KAL--GKENVLA--------------------------LIM 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 419 ASKNSSQETCTRARELAQQIGSHHISLNIDPAVKAvmgifslvtgksplFAAHGGSSRENLALQNVQARIRMVLAYLFAQ 498
Cdd:pfam02540 53 PSSQSSEEDVQDALALAENLGIEYKTIDIKPIVRA--------------FSQLFQDASEDFAKGNLKARIRMAILYYIAN 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 499 LSlwsrgvhgGLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFVqfciQRFQLPalQSILLAPATAELEPl 578
Cdd:pfam02540 119 KF--------NYLVLGTGNKSELAVGYFTKYGDGACDIAPIGDLYKTQVYELA----RYLNVP--ERIIKKPPSADLWP- 183
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41393551 579 adgqvSQTDEEDMGMTYAELSVYGKLRKvAKMGPYSMFCKLLgmwrhictPRQVadkVKRFFSKYSMNRHK 649
Cdd:pfam02540 184 -----GQTDEEELGIPYDELDDILKLVE-KKLSPEEIIGKGL--------PAEV---VRRIENLIQKSEHK 237
|
|
| nadE |
PRK02628 |
NAD synthetase; Reviewed |
4-592 |
6.32e-36 |
|
NAD synthetase; Reviewed
Pssm-ID: 235057 [Multi-domain] Cd Length: 679 Bit Score: 144.24 E-value: 6.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 4 KVTVATCALNqwALDFEGNLQRILKSIEIAKNRGARYRLGPELEICGYGCWDhYYESDTLLH-SFQVLAALVESPVTQDI 82
Cdd:PRK02628 14 RVAAATPKVR--VADPAFNAARILALARRAADDGVALAVFPELSLSGYSCDD-LFLQDTLLDaVEDALATLVEASADLDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 83 ICDVGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANEGNYRELRWFTPWSRsrhteeyfLPRMIQDLTKQEtVPFGDAV 162
Cdd:PRK02628 91 LLVVGAPLRVRHRLYNCAVVIHRGRILGVVPKSYLPNYREFYEKRWFAPGDG--------ARGETIRLCGQE-VPFGTDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 163 LVTWDT----CIGSEICEELWTPHSPHIDMGLDGVEIITNASGSHQVLRKANTRVDLVTMVTSKNGGIYLLANqKGC--- 235
Cdd:PRK02628 162 LFEAEDlpgfVFGVEICEDLWVPIPPSSYAALAGATVLANLSASNITVGKADYRRLLVASQSARCLAAYVYAA-AGVges 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 236 --DgdrLYYDGCAMIAMNGSVFAQGSQFSlDDVEVLTATLDLEDVRSYRAEISSRNLAASRASPYPR-VKVDFALSCHED 312
Cdd:PRK02628 241 ttD---LAWDGQTLIYENGELLAESERFP-REEQLIVADVDLERLRQERLRNGSFDDNARHRDESAPfRTIPFALDPPAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 313 LLaPISEPIEWKYHSPEEEISLGPACW-LWDF-----LRRSQQAG---FLLPLSGGVDSaaTACLIysmccqVCeavrsg 383
Cdd:PRK02628 317 DL-GLRRPVERFPFVPSDPARLDQRCYeAYNIqvsglAQRLRATGlkkVVIGISGGLDS--THALL------VA------ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 384 neevladVRTIvnqisytpqdprDLCGR----ILtTCYMASKNSSQETCTRARELAQQIGSHHISLNIDPAVK---AVMG 456
Cdd:PRK02628 382 -------AKAM------------DRLGLprknIL-AYTMPGFATTDRTKNNAVALMKALGVTAREIDIRPAALqmlKDIG 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 457 ifslvtgksplfaaHGGSSREN---LALQNVQARIRMvlAYLF--AQLslwsrgvHGGlLVLGSANVDESLLGYLTkYDC 531
Cdd:PRK02628 442 --------------HPFARGEPvydVTFENVQAGERT--QILFrlANQ-------HGG-IVIGTGDLSELALGWCT-YGV 496
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41393551 532 ----SSADINpiGGISKTDLRAFVQFCIQRFQLPA-----LQSILLAPATAELEP-LADGQVSQTDEEDMG 592
Cdd:PRK02628 497 gdhmSHYNVN--ASVPKTLIQHLIRWVIASGQFDEavsevLLDILDTEISPELVPaDKEGEIVQSTEDIIG 565
|
|
| nadE |
TIGR00552 |
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ... |
340-665 |
1.39e-35 |
|
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: 134.82 E-value: 1.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 340 LWDFLR----RSQQAGFLLPLSGGVDSAATACLiysmccqvceAVRSGNEEVLAdvrtivnqisytpqdprdlcGRIltt 415
Cdd:TIGR00552 9 IEDFLRgyvqKSGAKGVVLGLSGGIDSAVVAAL----------CVEALGEQNHA--------------------LLL--- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 416 cyMASKNSSQETCTRARELAQQIGSHHISLNIDPAVKAVMGIFSLVTGKSPLfaahggssrenLALQNVQARIRMVLAYL 495
Cdd:TIGR00552 56 --PHSVQTPEQDVQDALALAEPLGINYKNIDIAPIAASFQAQTETGDELSDF-----------LAKGNLKARLRMAALYA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 496 FAQLSlwsrgvhgGLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFVqfciQRFQLPalQSILLAPATAEL 575
Cdd:TIGR00552 123 IANKH--------NLLVLGTGNKSELMLGYFTKYGDGGCDIAPIGDLFKTQVYELA----KRLNVP--ERIIEKPPTADL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 576 EPladgqvSQTDEEDMGMTYAELSVYGKLRKVAKmgpysmfckllgmwrhictpRQVADKVKRFFSKYSMNRHKMTtlTP 655
Cdd:TIGR00552 189 FD------GQTDETELGITYDELDDYLKGIEELS--------------------QTVQEVVKRIESLVQKSEHKRR--LP 240
|
330
....*....|
gi 41393551 656 AYHAENYSPE 665
Cdd:TIGR00552 241 ATIFDLFWKQ 250
|
|
| PRK13981 |
PRK13981 |
NAD synthetase; Provisional |
5-588 |
1.37e-28 |
|
NAD synthetase; Provisional
Pssm-ID: 237577 [Multi-domain] Cd Length: 540 Bit Score: 120.65 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 5 VTVATCALNQWALDFEGNLQRILKSIEIAKNRGARYRLGPELEICGYGCWDHYYESDTLLHSFQVLAALVESpVTQDIIC 84
Cdd:PRK13981 1 LRIALAQLNPTVGDIAGNAAKILAAAAEAADAGADLLLFPELFLSGYPPEDLLLRPAFLAACEAALERLAAA-TAGGPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 85 DVGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANEGNYRELRWFTPWSRSrhteeyflprmiqdltkqETVPFGDAVlv 164
Cdd:PRK13981 80 LVGHPWREGGKLYNAAALLDGGEVLATYRKQDLPNYGVFDEKRYFAPGPEP------------------GVVELKGVR-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 165 twdtcIGSEICEELWTPhSPHIDMGLDGVEIITNASGSHQVLRKANTRVDLVTMVTSKNGG--IYLlaNQKGcdG-DRLY 241
Cdd:PRK13981 140 -----IGVPICEDIWNP-EPAETLAEAGAELLLVPNASPYHRGKPDLREAVLRARVRETGLplVYL--NQVG--GqDELV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 242 YDGCAmIAMN--GSVFAQGSQFsldDVEVLTATLDLEDVRsyraeissrnlaasraspyprvkvdfaLSCHEDLLAPISE 319
Cdd:PRK13981 210 FDGAS-FVLNadGELAARLPAF---EEQIAVVDFDRGEDG---------------------------WRPLPGPIAPPPE 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 320 PIEWKYHSpeeeISLGpacwLWDFLRRSQQAGFLLPLSGGVDSAATACLiysmccqVCEAVrsGNEEVLAdvrtivnqis 399
Cdd:PRK13981 259 GEAEDYRA----LVLG----LRDYVRKNGFPGVVLGLSGGIDSALVAAI-------AVDAL--GAERVRA---------- 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 400 ytpqdprdlcgrilttCYMASKNSSQETCTRARELAQQIGSHHISLNIDPAVKAVMGIFslvtgkSPLFAAHGgssrENL 479
Cdd:PRK13981 312 ----------------VMMPSRYTSEESLDDAAALAKNLGVRYDIIPIEPAFEAFEAAL------APLFAGTE----PDI 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 480 ALQNVQARIR----MVLAYLFaqlslwsrgvhgGLLVLGSANVDESLLGYLTKYdcssADIN----PIGGISKTDLrafv 551
Cdd:PRK13981 366 TEENLQSRIRgtllMALSNKF------------GSLVLTTGNKSEMAVGYATLY----GDMAggfaPIKDVYKTLV---- 425
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 41393551 552 qfciqrFQLPAL-----------QSILLAPATAELEPladgqvSQTDE 588
Cdd:PRK13981 426 ------YRLCRWrntvspgevipERIITKPPSAELRP------NQTDQ 461
|
|
| PRK13980 |
PRK13980 |
NAD synthetase; Provisional |
342-598 |
9.54e-28 |
|
NAD synthetase; Provisional
Pssm-ID: 184435 [Multi-domain] Cd Length: 265 Bit Score: 113.00 E-value: 9.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 342 DFLRRSQQAGFLLPLSGGVDSAATACLiysmccqvceAVRS-GNEEVLAdvrtivnqisytpqdprdlcgrilttCYMAS 420
Cdd:PRK13980 23 EEVEKAGAKGVVLGLSGGIDSAVVAYL----------AVKAlGKENVLA--------------------------LLMPS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 421 KNSSQETCTRARELAQQIGSHHISLNIDPAVKAvmgifslvtgkspLFAAHGGSSRenLALQNVQARIRMVLAYLFAQls 500
Cdd:PRK13980 67 SVSPPEDLEDAELVAEDLGIEYKVIEITPIVDA-------------FFSAIPDADR--LRVGNIMARTRMVLLYDYAN-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 501 lwsrgvHGGLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRafvqfciqrfQLPAL----QSILLAPATAELE 576
Cdd:PRK13980 130 ------RENRLVLGTGNKSELLLGYFTKYGDGAVDLNPIGDLYKTQVR----------ELARHlgvpEDIIEKPPSADLW 193
|
250 260
....*....|....*....|..
gi 41393551 577 PladgqvSQTDEEDMGMTYAEL 598
Cdd:PRK13980 194 E------GQTDEGELGFSYETI 209
|
|
| Nit2 |
COG0388 |
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]; |
4-287 |
8.59e-27 |
|
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
Pssm-ID: 440157 [Multi-domain] Cd Length: 264 Bit Score: 109.95 E-value: 8.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 4 KVTVATCALNQWALDFEGNLQRILKSIEIAKNRGARYRLGPELEICGYGCWDHYYEsdtllhsfqVLAALVESPVTQ--- 80
Cdd:COG0388 1 TMRIALAQLNPTVGDIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLL---------ELAEPLDGPALAala 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 81 ------DIICDVGMPV-MHRNVRYNCRVIFLNR-KILLIRPKMALANEGNYRELRWFTPwsrsrhteeyflprmiqdltk 152
Cdd:COG0388 72 elarelGIAVVVGLPErDEGGRLYNTALVIDPDgEILGRYRKIHLPNYGVFDEKRYFTP--------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 153 qetvpfGDAvLVTWDT---CIGSEICEELWTPHSPHIdMGLDGVEIITNASGSHQVLRKAntRVDLVTMVTSKNGGIYLL 229
Cdd:COG0388 131 ------GDE-LVVFDTdggRIGVLICYDLWFPELARA-LALAGADLLLVPSASPFGRGKD--HWELLLRARAIENGCYVV 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 230 -ANQKGCDGDRLYYdGCAMIA-MNGSVFAQGSqfslDDVEVLTATLDLEDVRSYRAEISS 287
Cdd:COG0388 201 aANQVGGEDGLVFD-GGSMIVdPDGEVLAEAG----DEEGLLVADIDLDRLREARRRFPV 255
|
|
| nitrilase_8 |
cd07586 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
18-286 |
1.88e-12 |
|
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: 68.08 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 18 DFEGNLQRILKSIEIAKNRGARYRLGPELEICGYGCWDHYYESDTLLHSfQVLAALVESPVTQDIICdvGMPVMHRNVR- 96
Cdd:cd07586 13 DVEENLEKHLEIIETARERGADLVVFPELSLTGYNLGDLVYEVAMHADD-PRLQALAEASGGICVVF--GFVEEGRDGRf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 97 YNCRVIFLNRKILLIRPKMALANEGNYRELRWFTPWSRSRHTEEYFLpRMiqdltkqetvpfgdavlvtwdtciGSEICE 176
Cdd:cd07586 90 YNSAAYLEDGRVVHVHRKVYLPTYGLFEEGRYFAPGSHLRAFDTRFG-RA------------------------GVLICE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 177 ELWTPHSPHIDMgLDGVEII---TNASGSHQVLRKANTRV--DLVTMVTSKNGGIYLLANQKGCDGDRLYYDGCAMIAMN 251
Cdd:cd07586 145 DAWHPSLPYLLA-LDGADVIfipANSPARGVGGDFDNEENweTLLKFYAMMNGVYVVFANRVGVEDGVYFWGGSRVVDPD 223
|
250 260 270
....*....|....*....|....*....|....*
gi 41393551 252 GSVFAQGSQFSLDdveVLTATLDLEDVRSYRAEIS 286
Cdd:cd07586 224 GEVVAEAPLFEED---LLVAELDRSAIRRARFFSP 255
|
|
| nadE |
PRK00768 |
ammonia-dependent NAD(+) synthetase; |
440-603 |
6.61e-11 |
|
ammonia-dependent NAD(+) synthetase;
Pssm-ID: 234831 [Multi-domain] Cd Length: 268 Bit Score: 63.62 E-value: 6.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 440 SHHISLNIDPAVKAVMGifSLvtgksplfaAHGGSSRENLALQNVQARIRMVLAYLFAqlslwsrGVHGGLlVLGSANVD 519
Cdd:PRK00768 102 DRVLTVNIKPAVDASVA--AL---------EAAGIELSDFVKGNIKARERMIAQYAIA-------GATGGL-VVGTDHAA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393551 520 ESLLGYLTKYDCSSADINPIGGISKTDLRAFVQFciqrfqLPALQSILLAPATAELEplaDGQVSQTDEEDMGMTYAELS 599
Cdd:PRK00768 163 EAVTGFFTKFGDGGADILPLFGLNKRQGRALLAA------LGAPEHLYEKVPTADLE---DDRPGLPDEVALGVTYDQID 233
|
....*.
gi 41393551 600 VY--GK 603
Cdd:PRK00768 234 DYleGK 239
|
|
|