|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02339 |
PLN02339 |
NAD+ synthase (glutamine-hydrolysing) |
3-696 |
0e+00 |
|
NAD+ synthase (glutamine-hydrolysing)
Pssm-ID: 177973 [Multi-domain] Cd Length: 700 Bit Score: 1094.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 3 RKVTVATCALNQWALDFEGNLQRILKSIEIAKHRGARYRLGPELEICGYGCWDHYYESDTLLHSLQVLAALLESPVTQDI 82
Cdd:PLN02339 2 RLLKVATCNLNQWAMDFDGNLKRIKESIAEAKAAGAVYRVGPELEITGYGCEDHFLELDTVTHSWECLAEILVGDLTDGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 83 ICDVGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANEGNYRELRWFTPWSRSRQTEEYFLPRMLQDLTKQETVPFGDAV 162
Cdd:PLN02339 82 LCDIGMPVIHGGVRYNCRVFCLNRKILLIRPKMWLANDGNYRELRWFTAWKHKKKVEDFQLPEEIAEATSQKSVPFGDGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 163 LSTWDTCIGSEVCEELWTPHSPHVDMGLDGVEIFTNASGSHHVLRKAHARVDLVTMATTKNGGIYLLANQKGCDGDRLYY 242
Cdd:PLN02339 162 LQFLDTAVAAETCEELFTPQAPHIDLALNGVEIISNGSGSHHQLRKLNTRLDLIRSATHKCGGVYLYANQRGCDGGRLYY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 243 DGCALIAMNGSIFAQGSQFSLDDVEVLTATLDLEDIRSYRAEISSRNLAASRVSPYPRVKVDFALSCHEDLLEPVSEPIE 322
Cdd:PLN02339 242 DGCACIVVNGEVVAQGSQFSLQDVEVVTACVDLDAVVSFRGSISSFREQASSKKRVPSVAVPFKLCPPFSLSLVPSSPLK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 323 WKYHSPAEEISLGPACWLWDFLRRSRQAGFFLPLSGGVDSAATACLVYSMCHQVCEAVKRGNLEVLADVRTIVNQLS-YT 401
Cdd:PLN02339 322 IRYHSPEEEIALGPACWLWDYLRRSGASGFLLPLSGGADSSSVAAIVGSMCQLVVKAIREGDEQVKADARRIGNYADgEV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 402 PQDPRELCGRVLTTCYMASENSSQETCDRARELAQQIGSHHIGLHIDPVVKALVGLFSLVTGASPRFAVHGGSDRENLAL 481
Cdd:PLN02339 402 PTDSKEFAKRIFYTVYMGSENSSEETRSRAKQLADEIGSSHLDVKIDGVVSAVLSLFQTLTGKRPRYKVDGGSNAENLAL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 482 QNVQARVRMVIAYLFAQLSLWSRGAPGGLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFVQLCVERFQLP 561
Cdd:PLN02339 482 QNIQARIRMVLAFMLASLLPWVRGKSGFLLVLGSANVDEGLRGYLTKYDCSSADINPIGGISKQDLRSFLRWAATNLGYP 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 562 ALQSILAAPATAELEPLaHGRVSQTDEEDMGMTYAELSVYGRLRKVAKTGPYSMFCKLLDMWRDTCSPRQVADKVKCFFS 641
Cdd:PLN02339 562 SLAEVEAAPPTAELEPI-RDDYSQTDEEDMGMTYEELGVYGRLRKIFRCGPVSMFKNLCHEWNGRLSPSEVAAKVKDFFK 640
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 77735841 642 KYSMNRHKMTTLTPAYHAESYSPDDNRFDLRPFLYNTRWPWQFRCIENQVLQLEG 696
Cdd:PLN02339 641 YYSINRHKMTTLTPSYHAESYSPDDNRFDLRQFLYNTRWPYQFRKIDELVEELDG 695
|
|
| GAT_Gln-NAD-synth |
cd07570 |
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ... |
6-287 |
7.60e-93 |
|
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: 288.98 E-value: 7.60e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 6 TVATCALNQWALDFEGNLQRILKSIEIAKHRGARYRLGPELEICGYGCWDHYYESDTLLHSLQVLAALLESPVTQDIICD 85
Cdd:cd07570 1 RIALAQLNPTVGDLEGNAEKILEAIREAKAQGADLVVFPELSLTGYPPEDLLLRPDFLEAAEEALEELAAATADLDIAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 86 VGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANEGNYRELRWFTPWSRSrqteeyflprmlqdltkqetvpfgdAVLST 165
Cdd:cd07570 81 VGLPLRHDGKLYNAAAVLQNGKILGVVPKQLLPNYGVFDEKRYFTPGDKP-------------------------DVLFF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 166 WDTCIGSEVCEELWTPHSPHVDMGLDGVEIFTNASGSHHVLRKAHARVDLVTMATTKNGGIYLLANQkGCDGDRLYYDGC 245
Cdd:cd07570 136 KGLRIGVEICEDLWVPDPPSAELALAGADLILNLSASPFHLGKQDYRRELVSSRSARTGLPYVYVNQ-VGGQDDLVFDGG 214
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 77735841 246 ALIAMN-GSIFAQGSQFslddvEVLTATLDLEDIRSYRAEISS 287
Cdd:cd07570 215 SFIADNdGELLAEAPRF-----EEDLADVDLDRLRSERRRNSS 252
|
|
| CN_hydrolase |
pfam00795 |
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ... |
6-283 |
3.21e-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: 176.01 E-value: 3.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 6 TVATCALNQWALDFEGNLQRILKSIEIAKHRGARYRLGPELEICGYGCWDHYYESDTlLHSLQVLAALLESPVTQDIICD 85
Cdd:pfam00795 1 RVALVQLPQGFWDLEANLQKALELIEEAARYGADLIVLPELFITGYPCWAHFLEAAE-VGDGETLAGLAALARKNGIAIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 86 VGmpVMHRNVrYNCRviFLNRKILLIRPKMALaneGNYRELRWFTPWSRSRQTEEyflprmlqdltkqETVPFGDA--VL 163
Cdd:pfam00795 80 IG--LIERWL-TGGR--LYNTAVLLDPDGKLV---GKYRKLHLFPEPRPPGFRER-------------VLFEPGDGgtVF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 164 STWDTCIGSEVCEELWTPHSPHVdMGLDGVEIFTNAS-GSHHVLRKAHARVDLVTMATTKNGGIYLL-ANQKGCDGD-RL 240
Cdd:pfam00795 139 DTPLGKIGAAICYEIRFPELLRA-LALKGAEILINPSaRAPFPGSLGPPQWLLLARARALENGCFVIaANQVGGEEDaPW 217
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 77735841 241 YYDGCALIAMNGSIFAQGSQFSLddvEVLTATLDLEDIRSYRA 283
Cdd:pfam00795 218 PYGHSMIIDPDGRILAGAGEWEE---GVLIADIDLALVRAWRY 257
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
67-669 |
8.97e-40 |
|
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: 154.23 E-value: 8.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 67 LQVLAALLESPVTQDIICDVGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANEGNYRELRWFTPWSRSRQTEEYFLPRM 146
Cdd:COG0171 22 AAALAALAAAAAALLLLLLLLLLLLLLLLALLLLLAAARLLVAAAALLLLALAAGGGAALAGGGGGAGGGLLNGAALVLG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 147 LQDLTKQETVPFGDAVlstwdtCIGSEVCEELWTPHSPHVDMGLDGVEIFTNASGSHHVLRKAHARVDLVTMATTKNGGI 226
Cdd:COG0171 102 GGDLLFFADDFLLLLL------VVEEEEEEFVGGPPPPPAALGGAGVLLILSSSSSAVGAAAAAAALAAALLSSLSSAAY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 227 YLLANQKGCDGDRLYYDGCALIAMNGSIFAQGSQFSLDDVEVLTATLDLEDIRSYRAEISSRNLAASRVSPYPRvkvdfa 306
Cdd:COG0171 176 YAAAGGGESTTDLARGGGGGLLLVVLLLVGGGDDDFFDGGSAAVDDDDLLLLLRRRREEELLLARARDADGGRR------ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 307 lsCHEDLLEPVSEPIEWKYHSPAEEISLGpacwLWDFLRRSRQAGFFLPLSGGVDSAATACLVysmchqvCEAVKRGNle 386
Cdd:COG0171 250 --VAAEAAPPPPEEEEMDLEEVYDALVLG----LRDYVRKNGFKGVVLGLSGGIDSALVAALA-------VDALGPEN-- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 387 vladVRTIvnqlsytpqdprelcgrvlttcYMASENSSQETCDRARELAQQIGSHHIGLHIDPVVKALVGlfslvtgasp 466
Cdd:COG0171 315 ----VLGV----------------------TMPSRYTSDESLEDAEELAENLGIEYEEIDITPAVEAFLE---------- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 467 RFAVHGGSDRENLALQNVQARVRMVIAYLFAQLSlwsrgapgGLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTD 546
Cdd:COG0171 359 ALPHAFGGELDDVAEENLQARIRMVILMALANKF--------GGLVLGTGNKSELAVGYFTKYGDGAGDLAPIADLYKTQ 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 547 LRafvQLC--VERFQLPALQSILAAPATAELEPlahgrvSQTDEEDMgmtyaelsvygrlrkvaktGPYSmfckLLD--- 621
Cdd:COG0171 431 VY---ALArwLNRNGEVIPEDIIDKPPSAELRP------GQTDEDEL-------------------GPYE----VLDail 478
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 77735841 622 --MWRDTCSPRQVA------DKVKCFFSKYSMNRHKMTTLTPAYHAESYSPD-DNRF 669
Cdd:COG0171 479 yaYVEEGLSPEEIAaagydrEWVERVLRLVRRNEYKRRQPPPGPKVSSRAFGrGRRY 535
|
|
| nadE |
TIGR00552 |
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ... |
340-649 |
3.81e-32 |
|
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: 125.19 E-value: 3.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 340 LWDFLR----RSRQAGFFLPLSGGVDSAATACLvysmchqvceAVKRGNLEVLAdvrtivnqlsytpqdprelcGRVltt 415
Cdd:TIGR00552 9 IEDFLRgyvqKSGAKGVVLGLSGGIDSAVVAAL----------CVEALGEQNHA--------------------LLL--- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 416 cyMASENSSQETCDRARELAQQIGSHHIGLHIDPVVKALVGLFslvtgasprfaVHGGSDRENLALQNVQARVRMVIAYL 495
Cdd:TIGR00552 56 --PHSVQTPEQDVQDALALAEPLGINYKNIDIAPIAASFQAQT-----------ETGDELSDFLAKGNLKARLRMAALYA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 496 FAQLSlwsrgapgGLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRafvQLCvERFQLPalQSILAAPATAEL 575
Cdd:TIGR00552 123 IANKH--------NLLVLGTGNKSELMLGYFTKYGDGGCDIAPIGDLFKTQVY---ELA-KRLNVP--ERIIEKPPTADL 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 77735841 576 EPlahgrvSQTDEEDMGMTYAELSVYgrlrkvaktgpysmFCKLLDMwrdtcsPRQVADKVKCFFSKYSMNRHK 649
Cdd:TIGR00552 189 FD------GQTDETELGITYDELDDY--------------LKGIEEL------SQTVQEVVKRIESLVQKSEHK 236
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02339 |
PLN02339 |
NAD+ synthase (glutamine-hydrolysing) |
3-696 |
0e+00 |
|
NAD+ synthase (glutamine-hydrolysing)
Pssm-ID: 177973 [Multi-domain] Cd Length: 700 Bit Score: 1094.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 3 RKVTVATCALNQWALDFEGNLQRILKSIEIAKHRGARYRLGPELEICGYGCWDHYYESDTLLHSLQVLAALLESPVTQDI 82
Cdd:PLN02339 2 RLLKVATCNLNQWAMDFDGNLKRIKESIAEAKAAGAVYRVGPELEITGYGCEDHFLELDTVTHSWECLAEILVGDLTDGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 83 ICDVGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANEGNYRELRWFTPWSRSRQTEEYFLPRMLQDLTKQETVPFGDAV 162
Cdd:PLN02339 82 LCDIGMPVIHGGVRYNCRVFCLNRKILLIRPKMWLANDGNYRELRWFTAWKHKKKVEDFQLPEEIAEATSQKSVPFGDGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 163 LSTWDTCIGSEVCEELWTPHSPHVDMGLDGVEIFTNASGSHHVLRKAHARVDLVTMATTKNGGIYLLANQKGCDGDRLYY 242
Cdd:PLN02339 162 LQFLDTAVAAETCEELFTPQAPHIDLALNGVEIISNGSGSHHQLRKLNTRLDLIRSATHKCGGVYLYANQRGCDGGRLYY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 243 DGCALIAMNGSIFAQGSQFSLDDVEVLTATLDLEDIRSYRAEISSRNLAASRVSPYPRVKVDFALSCHEDLLEPVSEPIE 322
Cdd:PLN02339 242 DGCACIVVNGEVVAQGSQFSLQDVEVVTACVDLDAVVSFRGSISSFREQASSKKRVPSVAVPFKLCPPFSLSLVPSSPLK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 323 WKYHSPAEEISLGPACWLWDFLRRSRQAGFFLPLSGGVDSAATACLVYSMCHQVCEAVKRGNLEVLADVRTIVNQLS-YT 401
Cdd:PLN02339 322 IRYHSPEEEIALGPACWLWDYLRRSGASGFLLPLSGGADSSSVAAIVGSMCQLVVKAIREGDEQVKADARRIGNYADgEV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 402 PQDPRELCGRVLTTCYMASENSSQETCDRARELAQQIGSHHIGLHIDPVVKALVGLFSLVTGASPRFAVHGGSDRENLAL 481
Cdd:PLN02339 402 PTDSKEFAKRIFYTVYMGSENSSEETRSRAKQLADEIGSSHLDVKIDGVVSAVLSLFQTLTGKRPRYKVDGGSNAENLAL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 482 QNVQARVRMVIAYLFAQLSLWSRGAPGGLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFVQLCVERFQLP 561
Cdd:PLN02339 482 QNIQARIRMVLAFMLASLLPWVRGKSGFLLVLGSANVDEGLRGYLTKYDCSSADINPIGGISKQDLRSFLRWAATNLGYP 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 562 ALQSILAAPATAELEPLaHGRVSQTDEEDMGMTYAELSVYGRLRKVAKTGPYSMFCKLLDMWRDTCSPRQVADKVKCFFS 641
Cdd:PLN02339 562 SLAEVEAAPPTAELEPI-RDDYSQTDEEDMGMTYEELGVYGRLRKIFRCGPVSMFKNLCHEWNGRLSPSEVAAKVKDFFK 640
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 77735841 642 KYSMNRHKMTTLTPAYHAESYSPDDNRFDLRPFLYNTRWPWQFRCIENQVLQLEG 696
Cdd:PLN02339 641 YYSINRHKMTTLTPSYHAESYSPDDNRFDLRQFLYNTRWPYQFRKIDELVEELDG 695
|
|
| GAT_Gln-NAD-synth |
cd07570 |
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ... |
6-287 |
7.60e-93 |
|
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: 288.98 E-value: 7.60e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 6 TVATCALNQWALDFEGNLQRILKSIEIAKHRGARYRLGPELEICGYGCWDHYYESDTLLHSLQVLAALLESPVTQDIICD 85
Cdd:cd07570 1 RIALAQLNPTVGDLEGNAEKILEAIREAKAQGADLVVFPELSLTGYPPEDLLLRPDFLEAAEEALEELAAATADLDIAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 86 VGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANEGNYRELRWFTPWSRSrqteeyflprmlqdltkqetvpfgdAVLST 165
Cdd:cd07570 81 VGLPLRHDGKLYNAAAVLQNGKILGVVPKQLLPNYGVFDEKRYFTPGDKP-------------------------DVLFF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 166 WDTCIGSEVCEELWTPHSPHVDMGLDGVEIFTNASGSHHVLRKAHARVDLVTMATTKNGGIYLLANQkGCDGDRLYYDGC 245
Cdd:cd07570 136 KGLRIGVEICEDLWVPDPPSAELALAGADLILNLSASPFHLGKQDYRRELVSSRSARTGLPYVYVNQ-VGGQDDLVFDGG 214
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 77735841 246 ALIAMN-GSIFAQGSQFslddvEVLTATLDLEDIRSYRAEISS 287
Cdd:cd07570 215 SFIADNdGELLAEAPRF-----EEDLADVDLDRLRSERRRNSS 252
|
|
| NAD_synthase |
cd00553 |
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ... |
327-650 |
5.84e-87 |
|
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: 273.28 E-value: 5.84e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 327 SPAEEISLGPACWLWDFLRRSRQAGFFLPLSGGVDSAATACLVYSMChqvceavkrgnlevladvrtivnqlsytpqdPR 406
Cdd:cd00553 1 IDPEEIIEALVCFLRDYLRKSGAKGFVLGLSGGIDSAVVAALAVRAL-------------------------------GA 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 407 ElcgRVLTTCYMaSENSSQETCDRARELAQQIGSHHIGLHIDPVVKALVGLFSLVtgasprfavhGGSDRENLALQNVQA 486
Cdd:cd00553 50 E---NVLALIMP-SRYSSKETRDDAKALAENLGIEYRTIDIDPIVDAFLKALEHA----------GGSEAEDLALGNIQA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 487 RVRMVIAYLFAQLSlwsrgapgGLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFVQlcverfQLPALQSI 566
Cdd:cd00553 116 RLRMVLLYALANLL--------GGLVLGTGNKSELLLGYFTKYGDGAADINPIGDLYKTQVRELAR------YLGVPEEI 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 567 LAAPATAELEPlahgrvSQTDEEDMGMTYAELSVYGRLRKVAKTGPysmfcklldmwRDTCSPRQVADKVKCFFSKYSMN 646
Cdd:cd00553 182 IEKPPSAELWP------GQTDEDELGMPYEELDLILYGLVDGKLGP-----------EEILSPGEDEEKVKRIFRLYRRN 244
|
....
gi 77735841 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 |
3.21e-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: 176.01 E-value: 3.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 6 TVATCALNQWALDFEGNLQRILKSIEIAKHRGARYRLGPELEICGYGCWDHYYESDTlLHSLQVLAALLESPVTQDIICD 85
Cdd:pfam00795 1 RVALVQLPQGFWDLEANLQKALELIEEAARYGADLIVLPELFITGYPCWAHFLEAAE-VGDGETLAGLAALARKNGIAIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 86 VGmpVMHRNVrYNCRviFLNRKILLIRPKMALaneGNYRELRWFTPWSRSRQTEEyflprmlqdltkqETVPFGDA--VL 163
Cdd:pfam00795 80 IG--LIERWL-TGGR--LYNTAVLLDPDGKLV---GKYRKLHLFPEPRPPGFRER-------------VLFEPGDGgtVF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 164 STWDTCIGSEVCEELWTPHSPHVdMGLDGVEIFTNAS-GSHHVLRKAHARVDLVTMATTKNGGIYLL-ANQKGCDGD-RL 240
Cdd:pfam00795 139 DTPLGKIGAAICYEIRFPELLRA-LALKGAEILINPSaRAPFPGSLGPPQWLLLARARALENGCFVIaANQVGGEEDaPW 217
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 77735841 241 YYDGCALIAMNGSIFAQGSQFSLddvEVLTATLDLEDIRSYRA 283
Cdd:pfam00795 218 PYGHSMIIDPDGRILAGAGEWEE---GVLIADIDLALVRAWRY 257
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
67-669 |
8.97e-40 |
|
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: 154.23 E-value: 8.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 67 LQVLAALLESPVTQDIICDVGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANEGNYRELRWFTPWSRSRQTEEYFLPRM 146
Cdd:COG0171 22 AAALAALAAAAAALLLLLLLLLLLLLLLLALLLLLAAARLLVAAAALLLLALAAGGGAALAGGGGGAGGGLLNGAALVLG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 147 LQDLTKQETVPFGDAVlstwdtCIGSEVCEELWTPHSPHVDMGLDGVEIFTNASGSHHVLRKAHARVDLVTMATTKNGGI 226
Cdd:COG0171 102 GGDLLFFADDFLLLLL------VVEEEEEEFVGGPPPPPAALGGAGVLLILSSSSSAVGAAAAAAALAAALLSSLSSAAY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 227 YLLANQKGCDGDRLYYDGCALIAMNGSIFAQGSQFSLDDVEVLTATLDLEDIRSYRAEISSRNLAASRVSPYPRvkvdfa 306
Cdd:COG0171 176 YAAAGGGESTTDLARGGGGGLLLVVLLLVGGGDDDFFDGGSAAVDDDDLLLLLRRRREEELLLARARDADGGRR------ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 307 lsCHEDLLEPVSEPIEWKYHSPAEEISLGpacwLWDFLRRSRQAGFFLPLSGGVDSAATACLVysmchqvCEAVKRGNle 386
Cdd:COG0171 250 --VAAEAAPPPPEEEEMDLEEVYDALVLG----LRDYVRKNGFKGVVLGLSGGIDSALVAALA-------VDALGPEN-- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 387 vladVRTIvnqlsytpqdprelcgrvlttcYMASENSSQETCDRARELAQQIGSHHIGLHIDPVVKALVGlfslvtgasp 466
Cdd:COG0171 315 ----VLGV----------------------TMPSRYTSDESLEDAEELAENLGIEYEEIDITPAVEAFLE---------- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 467 RFAVHGGSDRENLALQNVQARVRMVIAYLFAQLSlwsrgapgGLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTD 546
Cdd:COG0171 359 ALPHAFGGELDDVAEENLQARIRMVILMALANKF--------GGLVLGTGNKSELAVGYFTKYGDGAGDLAPIADLYKTQ 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 547 LRafvQLC--VERFQLPALQSILAAPATAELEPlahgrvSQTDEEDMgmtyaelsvygrlrkvaktGPYSmfckLLD--- 621
Cdd:COG0171 431 VY---ALArwLNRNGEVIPEDIIDKPPSAELRP------GQTDEDEL-------------------GPYE----VLDail 478
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 77735841 622 --MWRDTCSPRQVA------DKVKCFFSKYSMNRHKMTTLTPAYHAESYSPD-DNRF 669
Cdd:COG0171 479 yaYVEEGLSPEEIAaagydrEWVERVLRLVRRNEYKRRQPPPGPKVSSRAFGrGRRY 535
|
|
| nadE |
TIGR00552 |
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ... |
340-649 |
3.81e-32 |
|
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: 125.19 E-value: 3.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 340 LWDFLR----RSRQAGFFLPLSGGVDSAATACLvysmchqvceAVKRGNLEVLAdvrtivnqlsytpqdprelcGRVltt 415
Cdd:TIGR00552 9 IEDFLRgyvqKSGAKGVVLGLSGGIDSAVVAAL----------CVEALGEQNHA--------------------LLL--- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 416 cyMASENSSQETCDRARELAQQIGSHHIGLHIDPVVKALVGLFslvtgasprfaVHGGSDRENLALQNVQARVRMVIAYL 495
Cdd:TIGR00552 56 --PHSVQTPEQDVQDALALAEPLGINYKNIDIAPIAASFQAQT-----------ETGDELSDFLAKGNLKARLRMAALYA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 496 FAQLSlwsrgapgGLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRafvQLCvERFQLPalQSILAAPATAEL 575
Cdd:TIGR00552 123 IANKH--------NLLVLGTGNKSELMLGYFTKYGDGGCDIAPIGDLFKTQVY---ELA-KRLNVP--ERIIEKPPTADL 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 77735841 576 EPlahgrvSQTDEEDMGMTYAELSVYgrlrkvaktgpysmFCKLLDMwrdtcsPRQVADKVKCFFSKYSMNRHK 649
Cdd:TIGR00552 189 FD------GQTDETELGITYDELDDY--------------LKGIEEL------SQTVQEVVKRIESLVQKSEHK 236
|
|
| 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 |
6.89e-32 |
|
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: 124.03 E-value: 6.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 339 WLWDFLRRSRQAGFFLPLSGGVDSAATACLvysmchqvceAVKR-GNLEVLAdvrtivnqlsytpqdprelcgrvlttCY 417
Cdd:pfam02540 8 FLRDYVQKAGFKGVVLGLSGGIDSSLVAYL----------AVKAlGKENVLA--------------------------LI 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 418 MASENSSQETCDRARELAQQIGSHHIGLHIDPVVKALVGLFSlvtgasprfavhggSDRENLALQNVQARVRMVIAYLFA 497
Cdd:pfam02540 52 MPSSQSSEEDVQDALALAENLGIEYKTIDIKPIVRAFSQLFQ--------------DASEDFAKGNLKARIRMAILYYIA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 498 QLSlwsrgapgGLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRafvQLCvERFQLPalQSILAAPATAELEP 577
Cdd:pfam02540 118 NKF--------NYLVLGTGNKSELAVGYFTKYGDGACDIAPIGDLYKTQVY---ELA-RYLNVP--ERIIKKPPSADLWP 183
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 77735841 578 lahgrvSQTDEEDMGMTYAELSVYgrLRKVAKTGPYSMFCKLldmwrdtCSPRQVADKVkcfFSKYSMNRHK 649
Cdd:pfam02540 184 ------GQTDEEELGIPYDELDDI--LKLVEKKLSPEEIIGK-------GLPAEVVRRI---ENLIQKSEHK 237
|
|
| nadE |
PRK02628 |
NAD synthetase; Reviewed |
4-592 |
8.83e-32 |
|
NAD synthetase; Reviewed
Pssm-ID: 235057 [Multi-domain] Cd Length: 679 Bit Score: 131.52 E-value: 8.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 4 KVTVATCALNqwALDFEGNLQRILKSIEIAKHRGARYRLGPELEICGYGCWDhYYESDTLLH-SLQVLAALLESPVTQDI 82
Cdd:PRK02628 14 RVAAATPKVR--VADPAFNAARILALARRAADDGVALAVFPELSLSGYSCDD-LFLQDTLLDaVEDALATLVEASADLDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 83 ICDVGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANEGNYRELRWFTPwSRSRQTEEYFLPRmlqdltkqETVPFGDAV 162
Cdd:PRK02628 91 LLVVGAPLRVRHRLYNCAVVIHRGRILGVVPKSYLPNYREFYEKRWFAP-GDGARGETIRLCG--------QEVPFGTDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 163 LSTWDT----CIGSEVCEELWTPHSPHVDMGLDGVEIFTNASGSHHVLRKAHARVDLVTMATTKNGGIYLLANqKGC--- 235
Cdd:PRK02628 162 LFEAEDlpgfVFGVEICEDLWVPIPPSSYAALAGATVLANLSASNITVGKADYRRLLVASQSARCLAAYVYAA-AGVges 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 236 --DgdrLYYDGCALIAMNGSIFAQGSQFSlDDVEVLTATLDLEDIRSYRAEISSRNLAASR---VSPYPRVKVDFALSCH 310
Cdd:PRK02628 241 ttD---LAWDGQTLIYENGELLAESERFP-REEQLIVADVDLERLRQERLRNGSFDDNARHrdeSAPFRTIPFALDPPAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 311 EDLLEpvsEPIEWKYHSPAEEISLGPACW-LWDF-----LRRSRQAG---FFLPLSGGVDSaaTACLVysmchqVC-EAV 380
Cdd:PRK02628 317 DLGLR---RPVERFPFVPSDPARLDQRCYeAYNIqvsglAQRLRATGlkkVVIGISGGLDS--THALL------VAaKAM 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 381 KRGNLEvladvRTivNQLSYTpqdprelcgrvlttcyMASENSSQETCDRARELAQQIGSHHIGLHIDPVVKAL---VGl 457
Cdd:PRK02628 386 DRLGLP-----RK--NILAYT----------------MPGFATTDRTKNNAVALMKALGVTAREIDIRPAALQMlkdIG- 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 458 fslvtgasprfavHGGSDREN---LALQNVQARVRMviAYLFaqlslwsRGAP--GGlLVLGSANVDESLLGYLTkYDC- 531
Cdd:PRK02628 442 -------------HPFARGEPvydVTFENVQAGERT--QILF-------RLANqhGG-IVIGTGDLSELALGWCT-YGVg 497
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 532 ---SSADINpiGGISKTDLRAFVQLCVERFQLPA-----LQSILAAPATAELEP-LAHGRVSQTDEEDMG 592
Cdd:PRK02628 498 dhmSHYNVN--ASVPKTLIQHLIRWVIASGQFDEavsevLLDILDTEISPELVPaDKEGEIVQSTEDIIG 565
|
|
| PRK13980 |
PRK13980 |
NAD synthetase; Provisional |
342-598 |
5.49e-27 |
|
NAD synthetase; Provisional
Pssm-ID: 184435 [Multi-domain] Cd Length: 265 Bit Score: 110.68 E-value: 5.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 342 DFLRRS-RQAGF---FLPLSGGVDSAATACLVysmchqvCEAVKRGNleVLAdvrtivnqlsytpqdprelcgrvlttCY 417
Cdd:PRK13980 19 DFIREEvEKAGAkgvVLGLSGGIDSAVVAYLA-------VKALGKEN--VLA--------------------------LL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 418 MASENSSQETCDRARELAQQIGSHHIGLHIDPVVKALVGLFSlvtgasprfavhggsDRENLALQNVQARVRMVIAYLFA 497
Cdd:PRK13980 64 MPSSVSPPEDLEDAELVAEDLGIEYKVIEITPIVDAFFSAIP---------------DADRLRVGNIMARTRMVLLYDYA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 498 QLSlwsrgapgGLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRafvQLcVERFQLPalQSILAAPATAELEP 577
Cdd:PRK13980 129 NRE--------NRLVLGTGNKSELLLGYFTKYGDGAVDLNPIGDLYKTQVR---EL-ARHLGVP--EDIIEKPPSADLWE 194
|
250 260
....*....|....*....|.
gi 77735841 578 lahgrvSQTDEEDMGMTYAEL 598
Cdd:PRK13980 195 ------GQTDEGELGFSYETI 209
|
|
| PRK13981 |
PRK13981 |
NAD synthetase; Provisional |
5-588 |
6.25e-26 |
|
NAD synthetase; Provisional
Pssm-ID: 237577 [Multi-domain] Cd Length: 540 Bit Score: 112.56 E-value: 6.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 5 VTVATCALNQWALDFEGNLQRILKSIEIAKHRGARYRLGPELEICGYGcwdhyyESDTLLHS---------LQVLAALLE 75
Cdd:PRK13981 1 LRIALAQLNPTVGDIAGNAAKILAAAAEAADAGADLLLFPELFLSGYP------PEDLLLRPaflaaceaaLERLAAATA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 76 SpvtqDIICDVGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANEGNYRELRWFTPWSRSrqteeyflprmlqdltkqET 155
Cdd:PRK13981 75 G----GPAVLVGHPWREGGKLYNAAALLDGGEVLATYRKQDLPNYGVFDEKRYFAPGPEP------------------GV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 156 VPFGDAVlstwdtcIGSEVCEELWTPhSPHVDMGLDGVEIFTNASGSHHVLRKAHARVDLVTMATTKNGG--IYLlaNQK 233
Cdd:PRK13981 133 VELKGVR-------IGVPICEDIWNP-EPAETLAEAGAELLLVPNASPYHRGKPDLREAVLRARVRETGLplVYL--NQV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 234 GcdG-DRLYYDGCALiAMN--GSIFAQGSQFsldDVEVLTATLDLEDIRsyraeissrnlaasrvspyprvkvdfaLSCH 310
Cdd:PRK13981 203 G--GqDELVFDGASF-VLNadGELAARLPAF---EEQIAVVDFDRGEDG---------------------------WRPL 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 311 EDLLEPVSEPIEWKYHSpaeeISLGpacwLWDFLRRSRQAGFFLPLSGGVDSAATACLvysmchqVCEAVKRGNlevlad 390
Cdd:PRK13981 250 PGPIAPPPEGEAEDYRA----LVLG----LRDYVRKNGFPGVVLGLSGGIDSALVAAI-------AVDALGAER------ 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 391 VRTIvnqlsytpqdprelcgrvlttcYMASENSSQETCDRARELAQQIGSHHIGLHIDPVVKALVGLFslvtgaSPRFAv 470
Cdd:PRK13981 309 VRAV----------------------MMPSRYTSEESLDDAAALAKNLGVRYDIIPIEPAFEAFEAAL------APLFA- 359
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 471 hgGSDReNLALQNVQARVRMVIayLFAqLSLwSRGApgglLVLGSANVDESLLGYLTKYdcssADIN----PIGGISKTd 546
Cdd:PRK13981 360 --GTEP-DITEENLQSRIRGTL--LMA-LSN-KFGS----LVLTTGNKSEMAVGYATLY----GDMAggfaPIKDVYKT- 423
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 77735841 547 lRAFvQLC------VERFQLPalQSILAAPATAELEPlahgrvSQTDE 588
Cdd:PRK13981 424 -LVY-RLCrwrntvSPGEVIP--ERIITKPPSAELRP------NQTDQ 461
|
|
| Nit2 |
COG0388 |
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]; |
4-287 |
2.38e-25 |
|
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
Pssm-ID: 440157 [Multi-domain] Cd Length: 264 Bit Score: 106.10 E-value: 2.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 4 KVTVATCALNQWALDFEGNLQRILKSIEIAKHRGARYRLGPELEICGYGCWDHYYEsdtllhslqVLAALLESPVTQ--- 80
Cdd:COG0388 1 TMRIALAQLNPTVGDIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLL---------ELAEPLDGPALAala 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 81 ------DIICDVGMPV-MHRNVRYNCRVIFLNR-KILLIRPKMALANEGNYRELRWFTPwsrsrqteeyflprmlqdltk 152
Cdd:COG0388 72 elarelGIAVVVGLPErDEGGRLYNTALVIDPDgEILGRYRKIHLPNYGVFDEKRYFTP--------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 153 qetvpfGDAVLsTWDT---CIGSEVCEELWTPHSPHVdMGLDGVEIFTNASGSHHVLRKAHARVDLVTMAttKNGGIYLL 229
Cdd:COG0388 131 ------GDELV-VFDTdggRIGVLICYDLWFPELARA-LALAGADLLLVPSASPFGRGKDHWELLLRARA--IENGCYVV 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 77735841 230 -ANQKGCDGDRLYYDGCALIAMNGSIFAQGSqfslDDVEVLTATLDLEDIRSYRAEISS 287
Cdd:COG0388 201 aANQVGGEDGLVFDGGSMIVDPDGEVLAEAG----DEEGLLVADIDLDRLREARRRFPV 255
|
|
| nitrilase_8 |
cd07586 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
18-286 |
2.60e-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: 143610 Cd Length: 269 Bit Score: 61.53 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 18 DFEGNLQRILKSIEIAKHRGARYRLGPELEICGYGCWDHYYESDTLLHSlQVLAALLESPVTQDIICdvGMPVMHRNVR- 96
Cdd:cd07586 13 DVEENLEKHLEIIETARERGADLVVFPELSLTGYNLGDLVYEVAMHADD-PRLQALAEASGGICVVF--GFVEEGRDGRf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 97 YNCRVIFLNRKILLIRPKMALANEGNYRELRWFTPWSRSRQTEEYFLpRMlqdltkqetvpfgdavlstwdtciGSEVCE 176
Cdd:cd07586 90 YNSAAYLEDGRVVHVHRKVYLPTYGLFEEGRYFAPGSHLRAFDTRFG-RA------------------------GVLICE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 177 ELWTPHSPHVDMgLDGVE-IFTNAS-----GSH--------HVLRKAHARVdlvtmattkNGGIYLLANQKGCDGDRLYY 242
Cdd:cd07586 145 DAWHPSLPYLLA-LDGADvIFIPANspargVGGdfdneenwETLLKFYAMM---------NGVYVVFANRVGVEDGVYFW 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 77735841 243 DGCALIAMNGSIFAQGSQFSLDdveVLTATLDLEDIRSYRAEIS 286
Cdd:cd07586 215 GGSRVVDPDGEVVAEAPLFEED---LLVAELDRSAIRRARFFSP 255
|
|
| nadE |
PRK00768 |
ammonia-dependent NAD(+) synthetase; |
483-598 |
1.63e-09 |
|
ammonia-dependent NAD(+) synthetase;
Pssm-ID: 234831 [Multi-domain] Cd Length: 268 Bit Score: 59.39 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77735841 483 NVQARVRMVIAYLFAqlslwsrGAPGGLlVLGSANVDESLLGYLTKYDCSSADINPIGGISKTdlrafvqlcverfQLPA 562
Cdd:PRK00768 134 NIKARERMIAQYAIA-------GATGGL-VVGTDHAAEAVTGFFTKFGDGGADILPLFGLNKR-------------QGRA 192
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 77735841 563 LQSILAAPA-------TAELEPLahgRVSQTDEEDMGMTYAEL 598
Cdd:PRK00768 193 LLAALGAPEhlyekvpTADLEDD---RPGLPDEVALGVTYDQI 232
|
|
|