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Conserved domains on  [gi|77735841|ref|NP_001029615|]
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glutamine-dependent NAD(+) synthetase [Bos taurus]

Protein Classification

glutamine-dependent NAD(+) synthetase( domain architecture ID 1003107)

glutamine-dependent NAD(+) synthetase catalyzes the ATP-dependent amidation of deamido-NAD to form NAD; uses L-glutamine as a nitrogen source

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02339 super family cl31864
NAD+ synthase (glutamine-hydrolysing)
3-696 0e+00

NAD+ synthase (glutamine-hydrolysing)


The actual alignment was detected with superfamily member PLN02339:

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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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