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Conserved domains on  [gi|1039780384|ref|XP_017167890|]
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glutamine-dependent NAD(+) synthetase isoform X2 [Mus musculus]

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

CATH:  3.40.50.620|3.60.110.10
EC:  6.3.5.1
Gene Ontology:  GO:0004359|GO:0003952|GO:0005524|GO:0009435

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02339 super family cl31864
NAD+ synthase (glutamine-hydrolysing)
 1-583 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: 906.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384   1 MALANEGNYRELRWFTPWTRSRQTEEYVLPRMLQDLTKQKTVPFGDVVLATQDTCVGSEICEELWTPRSPHIDMGLDGVE 80
Cdd:PLN02339  114 MWLANDGNYRELRWFTAWKHKKKVEDFQLPEEIAEATSQKSVPFGDGYLQFLDTAVAAETCEELFTPQAPHIDLALNGVE 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384  81 IITNASGSHHVLRKAHTRVDLVTMATSKNGGIYLLANQKGCDGDRLYYDGCAMIAMNGSIFAQGTQFSLDDVEVLTATLD 160
Cdd:PLN02339  194 IISNGSGSHHQLRKLNTRLDLIRSATHKCGGVYLYANQRGCDGGRLYYDGCACIVVNGEVVAQGSQFSLQDVEVVTACVD 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 161 LEDVRSYKAEISSRNLEATRVSPYPRVTVDFALSVSEDLLEPVSEPMEWTYHRPEEEISLGPACWLWDFLRRSKQAGFFL 240
Cdd:PLN02339  274 LDAVVSFRGSISSFREQASSKKRVPSVAVPFKLCPPFSLSLVPSSPLKIRYHSPEEEIALGPACWLWDYLRRSGASGFLL 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 241 PLSGGVDSAASACIVYSMCCLVCDAVKSGNQQVLTDVQNLVD-ESSYTPQDPRELCGRLLTTCYMASENSSQETHSRATK 319
Cdd:PLN02339  354 PLSGGADSSSVAAIVGSMCQLVVKAIREGDEQVKADARRIGNyADGEVPTDSKEFAKRIFYTVYMGSENSSEETRSRAKQ 433

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 320 LAQLIGSYHINLSIDTAVKAVLGIFSLMTGKLPRFSAHGGSSRENLALQNVQARIRMVLAYLFAQLSLWSRGARGSLLVL 399
Cdd:PLN02339  434 LADEIGSSHLDVKIDGVVSAVLSLFQTLTGKRPRYKVDGGSNAENLALQNIQARIRMVLAFMLASLLPWVRGKSGFLLVL 513

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 400 GSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFVQFCAERFQLPVLQTILSAPATAELEPLADGQvSQMDEEDMGM 479
Cdd:PLN02339  514 GSANVDEGLRGYLTKYDCSSADINPIGGISKQDLRSFLRWAATNLGYPSLAEVEAAPPTAELEPIRDDY-SQTDEEDMGM 592

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 480 TYAELSIFGRLRKVAKAGPYSMFCKLLNMWRDSYTPTQVAEKVKLFFSKYSMNRHKMTTLTPAYHAENYSPDDNRFDLRP 559
Cdd:PLN02339  593 TYEELGVYGRLRKIFRCGPVSMFKNLCHEWNGRLSPSEVAAKVKDFFKYYSINRHKMTTLTPSYHAESYSPDDNRFDLRQ 672

                         570       580
                  ....*....|....*....|....
gi 1039780384 560 FLYNTRWPWQFLCIDNQVLQLERK 583
Cdd:PLN02339  673 FLYNTRWPYQFRKIDELVEELDGE 696
 
Name Accession Description Interval E-value
PLN02339 PLN02339
NAD+ synthase (glutamine-hydrolysing)
 1-583 0e+00

NAD+ synthase (glutamine-hydrolysing)


Pssm-ID: 177973 [Multi-domain]  Cd Length: 700  Bit Score: 906.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384   1 MALANEGNYRELRWFTPWTRSRQTEEYVLPRMLQDLTKQKTVPFGDVVLATQDTCVGSEICEELWTPRSPHIDMGLDGVE 80
Cdd:PLN02339  114 MWLANDGNYRELRWFTAWKHKKKVEDFQLPEEIAEATSQKSVPFGDGYLQFLDTAVAAETCEELFTPQAPHIDLALNGVE 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384  81 IITNASGSHHVLRKAHTRVDLVTMATSKNGGIYLLANQKGCDGDRLYYDGCAMIAMNGSIFAQGTQFSLDDVEVLTATLD 160
Cdd:PLN02339  194 IISNGSGSHHQLRKLNTRLDLIRSATHKCGGVYLYANQRGCDGGRLYYDGCACIVVNGEVVAQGSQFSLQDVEVVTACVD 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 161 LEDVRSYKAEISSRNLEATRVSPYPRVTVDFALSVSEDLLEPVSEPMEWTYHRPEEEISLGPACWLWDFLRRSKQAGFFL 240
Cdd:PLN02339  274 LDAVVSFRGSISSFREQASSKKRVPSVAVPFKLCPPFSLSLVPSSPLKIRYHSPEEEIALGPACWLWDYLRRSGASGFLL 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 241 PLSGGVDSAASACIVYSMCCLVCDAVKSGNQQVLTDVQNLVD-ESSYTPQDPRELCGRLLTTCYMASENSSQETHSRATK 319
Cdd:PLN02339  354 PLSGGADSSSVAAIVGSMCQLVVKAIREGDEQVKADARRIGNyADGEVPTDSKEFAKRIFYTVYMGSENSSEETRSRAKQ 433

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 320 LAQLIGSYHINLSIDTAVKAVLGIFSLMTGKLPRFSAHGGSSRENLALQNVQARIRMVLAYLFAQLSLWSRGARGSLLVL 399
Cdd:PLN02339  434 LADEIGSSHLDVKIDGVVSAVLSLFQTLTGKRPRYKVDGGSNAENLALQNIQARIRMVLAFMLASLLPWVRGKSGFLLVL 513

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 400 GSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFVQFCAERFQLPVLQTILSAPATAELEPLADGQvSQMDEEDMGM 479
Cdd:PLN02339  514 GSANVDEGLRGYLTKYDCSSADINPIGGISKQDLRSFLRWAATNLGYPSLAEVEAAPPTAELEPIRDDY-SQTDEEDMGM 592

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 480 TYAELSIFGRLRKVAKAGPYSMFCKLLNMWRDSYTPTQVAEKVKLFFSKYSMNRHKMTTLTPAYHAENYSPDDNRFDLRP 559
Cdd:PLN02339  593 TYEELGVYGRLRKIFRCGPVSMFKNLCHEWNGRLSPSEVAAKVKDFFKYYSINRHKMTTLTPSYHAESYSPDDNRFDLRQ 672

                         570       580
                  ....*....|....*....|....
gi 1039780384 560 FLYNTRWPWQFLCIDNQVLQLERK 583
Cdd:PLN02339  673 FLYNTRWPYQFRKIDELVEELDGE 696
NAD_synthase cd00553
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ...
 214-536 1.92e-85

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: 266.73  E-value: 1.92e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 214 PEEEISLGPACWLWDFLRRSKQAGFFLPLSGGVDSAASACIVYSMCClvcdavksgnqqvltdvqnlvdessytpqdpre 293
Cdd:cd00553     2 DPEEIIEALVCFLRDYLRKSGAKGFVLGLSGGIDSAVVAALAVRALG--------------------------------- 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 294 lCGRLLTTCYMaSENSSQETHSRATKLAQLIGSYHINLSIDTAVKAVLGIFSLMtgklprfsahGGSSRENLALQNVQAR 373
Cdd:cd00553    49 -AENVLALIMP-SRYSSKETRDDAKALAENLGIEYRTIDIDPIVDAFLKALEHA----------GGSEAEDLALGNIQAR 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 374 IRMVLAYLFAQLSlwsrgargSLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFVQFCAerfqlpVLQTIL 453
Cdd:cd00553   117 LRMVLLYALANLL--------GGLVLGTGNKSELLLGYFTKYGDGAADINPIGDLYKTQVRELARYLG------VPEEII 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 454 SAPATAELEPladgqvSQMDEEDMGMTYAELSIFGRLRKVAKAGPysmfckllnmwRDSYTPTQVAEKVKLFFSKYSMNR 533
Cdd:cd00553   183 EKPPSAELWP------GQTDEDELGMPYEELDLILYGLVDGKLGP-----------EEILSPGEDEEKVKRIFRLYRRNE 245


                  ...
gi 1039780384 534 HKM 536
Cdd:cd00553   246 HKR 248
NadE COG0171
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ...
 59-555 1.27e-35

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: 141.14  E-value: 1.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384  59 EICEELWTPRSPHIDMGLDGVEIITNASGSHHVLRKAHTRVDLVTMATSKNGGIYLLANQKGCDGDRLYYDGCAMIAMNG 138
Cdd:COG0171   120 EEEEEEFVGGPPPPPAALGGAGVLLILSSSSSAVGAAAAAAALAAALLSSLSSAAYYAAAGGGESTTDLARGGGGGLLLV 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 139 SIFAQGTQFSLDDVEVLTATLDLEDVRSYKAEISSRNLEATRVSPYPRVTVDFALSVSEDLLEPVSEPMEWtyhrpeEEI 218
Cdd:COG0171   200 VLLLVGGGDDDFFDGGSAAVDDDDLLLLLRRRREEELLLARARDADGGRRVAAEAAPPPPEEEEMDLEEVY------DAL 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 219 SLGpacwLWDFLRRSKQAGFFLPLSGGVDSAASACivysmccLVCDAVksGNQQVLTdvqnlvdessytpqdprelcgrl 298
Cdd:COG0171   274 VLG----LRDYVRKNGFKGVVLGLSGGIDSALVAA-------LAVDAL--GPENVLG----------------------- 317

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 299 lttCYMASENSSQETHSRATKLAQLIG-SYHInLSIDTAVKAVLGIFSLMTGKLPrfsahggssrENLALQNVQARIRMV 377
Cdd:COG0171   318 ---VTMPSRYTSDESLEDAEELAENLGiEYEE-IDITPAVEAFLEALPHAFGGEL----------DDVAEENLQARIRMV 383

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 378 LAYLFAQLslwsRGArgslLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFVQFCAERFQlPVLQTILSAPA 457
Cdd:COG0171   384 ILMALANK----FGG----LVLGTGNKSELAVGYFTKYGDGAGDLAPIADLYKTQVYALARWLNRNGE-VIPEDIIDKPP 454

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 458 TAELEPladgqvSQMDEEDMGmTYAELSIFgrlrkvakagpysmfckLLNMWRDSYTPTQVA------EKVKLFFSKYSM 531
Cdd:COG0171   455 SAELRP------GQTDEDELG-PYEVLDAI-----------------LYAYVEEGLSPEEIAaagydrEWVERVLRLVRR 510

                         490       500
                  ....*....|....*....|....*
gi 1039780384 532 NRHKMTTLTPAYHAENYSPD-DNRF 555
Cdd:COG0171   511 NEYKRRQPPPGPKVSSRAFGrGRRY 535
nadE TIGR00552
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ...
 226-535 1.03e-31

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: 123.27  E-value: 1.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 226 LWDFLR----RSKQAGFFLPLSGGVDSAASACIvysmcclvcdAVKSGNQQVLTdvqnlvdessytpqdprelcGRLltt 301
Cdd:TIGR00552   9 IEDFLRgyvqKSGAKGVVLGLSGGIDSAVVAAL----------CVEALGEQNHA--------------------LLL--- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 302 cyMASENSSQETHSRATKLAQLIGSYHINLSIDTAvkavlgIFSLMTGKLPrfsahGGSSRENLALQNVQARIRMVLAYL 381
Cdd:TIGR00552  56 --PHSVQTPEQDVQDALALAEPLGINYKNIDIAPI------AASFQAQTET-----GDELSDFLAKGNLKARLRMAALYA 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 382 FAQLSlwsrgargSLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFvqfcAERFQLPvlQTILSAPATAEL 461
Cdd:TIGR00552 123 IANKH--------NLLVLGTGNKSELMLGYFTKYGDGGCDIAPIGDLFKTQVYEL----AKRLNVP--ERIIEKPPTADL 188

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039780384 462 EPladGQVsqmDEEDMGMTYAEL-SIFGRLRKVakagpysmfckllnmwrdsytPTQVAEKVKLFFSKYSMNRHK 535
Cdd:TIGR00552 189 FD---GQT---DETELGITYDELdDYLKGIEEL---------------------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 ...
 225-535 2.53e-30

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: 119.02  E-value: 2.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 225 WLWDFLRRSKQAGFFLPLSGGVDSAASACIvysmcclvcdAVKS-GNQQVLtdvqnlvdessytpqdprelcgrlltTCY 303
Cdd:pfam02540   8 FLRDYVQKAGFKGVVLGLSGGIDSSLVAYL----------AVKAlGKENVL--------------------------ALI 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 304 MASENSSQETHSRATKLAQLIGSYHINLSIDTAVKAvlgifslmtgklprFSAHGGSSRENLALQNVQARIRMVLAYLFA 383
Cdd:pfam02540  52 MPSSQSSEEDVQDALALAENLGIEYKTIDIKPIVRA--------------FSQLFQDASEDFAKGNLKARIRMAILYYIA 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 384 QLSlwsrgargSLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFvqfcAERFQLPvlQTILSAPATAELEP 463
Cdd:pfam02540 118 NKF--------NYLVLGTGNKSELAVGYFTKYGDGACDIAPIGDLYKTQVYEL----ARYLNVP--ERIIKKPPSADLWP 183

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039780384 464 ladgqvSQMDEEDMGMTYAEL-SIFGRLRKvaKAGPYSMFCKLLnmwrdsytPTQVAEKVklfFSKYSMNRHK 535
Cdd:pfam02540 184 ------GQTDEEELGIPYDELdDILKLVEK--KLSPEEIIGKGL--------PAEVVRRI---ENLIQKSEHK 237
 
Name Accession Description Interval E-value
PLN02339 PLN02339
NAD+ synthase (glutamine-hydrolysing)
 1-583 0e+00

NAD+ synthase (glutamine-hydrolysing)


Pssm-ID: 177973 [Multi-domain]  Cd Length: 700  Bit Score: 906.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384   1 MALANEGNYRELRWFTPWTRSRQTEEYVLPRMLQDLTKQKTVPFGDVVLATQDTCVGSEICEELWTPRSPHIDMGLDGVE 80
Cdd:PLN02339  114 MWLANDGNYRELRWFTAWKHKKKVEDFQLPEEIAEATSQKSVPFGDGYLQFLDTAVAAETCEELFTPQAPHIDLALNGVE 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384  81 IITNASGSHHVLRKAHTRVDLVTMATSKNGGIYLLANQKGCDGDRLYYDGCAMIAMNGSIFAQGTQFSLDDVEVLTATLD 160
Cdd:PLN02339  194 IISNGSGSHHQLRKLNTRLDLIRSATHKCGGVYLYANQRGCDGGRLYYDGCACIVVNGEVVAQGSQFSLQDVEVVTACVD 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 161 LEDVRSYKAEISSRNLEATRVSPYPRVTVDFALSVSEDLLEPVSEPMEWTYHRPEEEISLGPACWLWDFLRRSKQAGFFL 240
Cdd:PLN02339  274 LDAVVSFRGSISSFREQASSKKRVPSVAVPFKLCPPFSLSLVPSSPLKIRYHSPEEEIALGPACWLWDYLRRSGASGFLL 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 241 PLSGGVDSAASACIVYSMCCLVCDAVKSGNQQVLTDVQNLVD-ESSYTPQDPRELCGRLLTTCYMASENSSQETHSRATK 319
Cdd:PLN02339  354 PLSGGADSSSVAAIVGSMCQLVVKAIREGDEQVKADARRIGNyADGEVPTDSKEFAKRIFYTVYMGSENSSEETRSRAKQ 433

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 320 LAQLIGSYHINLSIDTAVKAVLGIFSLMTGKLPRFSAHGGSSRENLALQNVQARIRMVLAYLFAQLSLWSRGARGSLLVL 399
Cdd:PLN02339  434 LADEIGSSHLDVKIDGVVSAVLSLFQTLTGKRPRYKVDGGSNAENLALQNIQARIRMVLAFMLASLLPWVRGKSGFLLVL 513

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 400 GSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFVQFCAERFQLPVLQTILSAPATAELEPLADGQvSQMDEEDMGM 479
Cdd:PLN02339  514 GSANVDEGLRGYLTKYDCSSADINPIGGISKQDLRSFLRWAATNLGYPSLAEVEAAPPTAELEPIRDDY-SQTDEEDMGM 592

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 480 TYAELSIFGRLRKVAKAGPYSMFCKLLNMWRDSYTPTQVAEKVKLFFSKYSMNRHKMTTLTPAYHAENYSPDDNRFDLRP 559
Cdd:PLN02339  593 TYEELGVYGRLRKIFRCGPVSMFKNLCHEWNGRLSPSEVAAKVKDFFKYYSINRHKMTTLTPSYHAESYSPDDNRFDLRQ 672

                         570       580
                  ....*....|....*....|....
gi 1039780384 560 FLYNTRWPWQFLCIDNQVLQLERK 583
Cdd:PLN02339  673 FLYNTRWPYQFRKIDELVEELDGE 696
NAD_synthase cd00553
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ...
 214-536 1.92e-85

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: 266.73  E-value: 1.92e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 214 PEEEISLGPACWLWDFLRRSKQAGFFLPLSGGVDSAASACIVYSMCClvcdavksgnqqvltdvqnlvdessytpqdpre 293
Cdd:cd00553     2 DPEEIIEALVCFLRDYLRKSGAKGFVLGLSGGIDSAVVAALAVRALG--------------------------------- 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 294 lCGRLLTTCYMaSENSSQETHSRATKLAQLIGSYHINLSIDTAVKAVLGIFSLMtgklprfsahGGSSRENLALQNVQAR 373
Cdd:cd00553    49 -AENVLALIMP-SRYSSKETRDDAKALAENLGIEYRTIDIDPIVDAFLKALEHA----------GGSEAEDLALGNIQAR 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 374 IRMVLAYLFAQLSlwsrgargSLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFVQFCAerfqlpVLQTIL 453
Cdd:cd00553   117 LRMVLLYALANLL--------GGLVLGTGNKSELLLGYFTKYGDGAADINPIGDLYKTQVRELARYLG------VPEEII 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 454 SAPATAELEPladgqvSQMDEEDMGMTYAELSIFGRLRKVAKAGPysmfckllnmwRDSYTPTQVAEKVKLFFSKYSMNR 533
Cdd:cd00553   183 EKPPSAELWP------GQTDEDELGMPYEELDLILYGLVDGKLGP-----------EEILSPGEDEEKVKRIFRLYRRNE 245


                  ...
gi 1039780384 534 HKM 536
Cdd:cd00553   246 HKR 248
GAT_Gln-NAD-synth cd07570
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ...
 1-173 1.35e-40

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: 148.39  E-value: 1.35e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384   1 MALANEGNYRELRWFTPWTRSrqteeyvlprmlqdltkqktvpfgdVVLATQDTCVGSEICEELWTPRSPHIDMGLDGVE 80
Cdd:cd07570   110 QLLPNYGVFDEKRYFTPGDKP-------------------------DVLFFKGLRIGVEICEDLWVPDPPSAELALAGAD 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384  81 IITNASGSHHVLRKAHTRVDLVTMATSKNGGIYLLANQkGCDGDRLYYDGCAMIAMN-GSIFAQGTQFslddvEVLTATL 159
Cdd:cd07570   165 LILNLSASPFHLGKQDYRRELVSSRSARTGLPYVYVNQ-VGGQDDLVFDGGSFIADNdGELLAEAPRF-----EEDLADV 238

                         170
                  ....*....|....
gi 1039780384 160 DLEDVRSYKAEISS 173
Cdd:cd07570   239 DLDRLRSERRRNSS 252
NadE COG0171
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ...
 59-555 1.27e-35

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: 141.14  E-value: 1.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384  59 EICEELWTPRSPHIDMGLDGVEIITNASGSHHVLRKAHTRVDLVTMATSKNGGIYLLANQKGCDGDRLYYDGCAMIAMNG 138
Cdd:COG0171   120 EEEEEEFVGGPPPPPAALGGAGVLLILSSSSSAVGAAAAAAALAAALLSSLSSAAYYAAAGGGESTTDLARGGGGGLLLV 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 139 SIFAQGTQFSLDDVEVLTATLDLEDVRSYKAEISSRNLEATRVSPYPRVTVDFALSVSEDLLEPVSEPMEWtyhrpeEEI 218
Cdd:COG0171   200 VLLLVGGGDDDFFDGGSAAVDDDDLLLLLRRRREEELLLARARDADGGRRVAAEAAPPPPEEEEMDLEEVY------DAL 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 219 SLGpacwLWDFLRRSKQAGFFLPLSGGVDSAASACivysmccLVCDAVksGNQQVLTdvqnlvdessytpqdprelcgrl 298
Cdd:COG0171   274 VLG----LRDYVRKNGFKGVVLGLSGGIDSALVAA-------LAVDAL--GPENVLG----------------------- 317

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 299 lttCYMASENSSQETHSRATKLAQLIG-SYHInLSIDTAVKAVLGIFSLMTGKLPrfsahggssrENLALQNVQARIRMV 377
Cdd:COG0171   318 ---VTMPSRYTSDESLEDAEELAENLGiEYEE-IDITPAVEAFLEALPHAFGGEL----------DDVAEENLQARIRMV 383

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 378 LAYLFAQLslwsRGArgslLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFVQFCAERFQlPVLQTILSAPA 457
Cdd:COG0171   384 ILMALANK----FGG----LVLGTGNKSELAVGYFTKYGDGAGDLAPIADLYKTQVYALARWLNRNGE-VIPEDIIDKPP 454

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 458 TAELEPladgqvSQMDEEDMGmTYAELSIFgrlrkvakagpysmfckLLNMWRDSYTPTQVA------EKVKLFFSKYSM 531
Cdd:COG0171   455 SAELRP------GQTDEDELG-PYEVLDAI-----------------LYAYVEEGLSPEEIAaagydrEWVERVLRLVRR 510

                         490       500
                  ....*....|....*....|....*
gi 1039780384 532 NRHKMTTLTPAYHAENYSPD-DNRF 555
Cdd:COG0171   511 NEYKRRQPPPGPKVSSRAFGrGRRY 535
nadE TIGR00552
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ...
 226-535 1.03e-31

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: 123.27  E-value: 1.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 226 LWDFLR----RSKQAGFFLPLSGGVDSAASACIvysmcclvcdAVKSGNQQVLTdvqnlvdessytpqdprelcGRLltt 301
Cdd:TIGR00552   9 IEDFLRgyvqKSGAKGVVLGLSGGIDSAVVAAL----------CVEALGEQNHA--------------------LLL--- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 302 cyMASENSSQETHSRATKLAQLIGSYHINLSIDTAvkavlgIFSLMTGKLPrfsahGGSSRENLALQNVQARIRMVLAYL 381
Cdd:TIGR00552  56 --PHSVQTPEQDVQDALALAEPLGINYKNIDIAPI------AASFQAQTET-----GDELSDFLAKGNLKARLRMAALYA 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 382 FAQLSlwsrgargSLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFvqfcAERFQLPvlQTILSAPATAEL 461
Cdd:TIGR00552 123 IANKH--------NLLVLGTGNKSELMLGYFTKYGDGGCDIAPIGDLFKTQVYEL----AKRLNVP--ERIIEKPPTADL 188

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039780384 462 EPladGQVsqmDEEDMGMTYAEL-SIFGRLRKVakagpysmfckllnmwrdsytPTQVAEKVKLFFSKYSMNRHK 535
Cdd:TIGR00552 189 FD---GQT---DETELGITYDELdDYLKGIEEL---------------------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 ...
 225-535 2.53e-30

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: 119.02  E-value: 2.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 225 WLWDFLRRSKQAGFFLPLSGGVDSAASACIvysmcclvcdAVKS-GNQQVLtdvqnlvdessytpqdprelcgrlltTCY 303
Cdd:pfam02540   8 FLRDYVQKAGFKGVVLGLSGGIDSSLVAYL----------AVKAlGKENVL--------------------------ALI 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 304 MASENSSQETHSRATKLAQLIGSYHINLSIDTAVKAvlgifslmtgklprFSAHGGSSRENLALQNVQARIRMVLAYLFA 383
Cdd:pfam02540  52 MPSSQSSEEDVQDALALAENLGIEYKTIDIKPIVRA--------------FSQLFQDASEDFAKGNLKARIRMAILYYIA 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 384 QLSlwsrgargSLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFvqfcAERFQLPvlQTILSAPATAELEP 463
Cdd:pfam02540 118 NKF--------NYLVLGTGNKSELAVGYFTKYGDGACDIAPIGDLYKTQVYEL----ARYLNVP--ERIIKKPPSADLWP 183

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039780384 464 ladgqvSQMDEEDMGMTYAEL-SIFGRLRKvaKAGPYSMFCKLLnmwrdsytPTQVAEKVklfFSKYSMNRHK 535
Cdd:pfam02540 184 ------GQTDEEELGIPYDELdDILKLVEK--KLSPEEIIGKGL--------PAEVVRRI---ENLIQKSEHK 237
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
 7-169 5.87e-27

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: 110.14  E-value: 5.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384   7 GNYRELRWFTPWTRSRQTEEYVLPRmlqdltkqktvpfGDV--VLATQDTCVGSEICEELWTPRSPHIdMGLDGVEIITN 84
Cdd:pfam00795 107 GKYRKLHLFPEPRPPGFRERVLFEP-------------GDGgtVFDTPLGKIGAAICYEIRFPELLRA-LALKGAEILIN 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384  85 AS-GSHHVLRKAHTRVDLVTMATSKNGGIYLL-ANQKGCDGD-RLYYDGCAMIAMNGSIFAQGTQFSLddvEVLTATLDL 161
Cdd:pfam00795 173 PSaRAPFPGSLGPPQWLLLARARALENGCFVIaANQVGGEEDaPWPYGHSMIIDPDGRILAGAGEWEE---GVLIADIDL 249


                  ....*...
gi 1039780384 162 EDVRSYKA 169
Cdd:pfam00795 250 ALVRAWRY 257
PRK13980 PRK13980
NAD synthetase; Provisional
 228-484 8.65e-22

NAD synthetase; Provisional


Pssm-ID: 184435 [Multi-domain]  Cd Length: 265  Bit Score: 95.28  E-value: 8.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 228 DFLRRSKQAGFFLPLSGGVDSAasacivysmccLVCD-AVKS-GNQQVLTdvqnlvdessytpqdprelcgrllttCYMA 305
Cdd:PRK13980   23 EEVEKAGAKGVVLGLSGGIDSA-----------VVAYlAVKAlGKENVLA--------------------------LLMP 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 306 SENSSQETHSRATKLAQLIGSYHINLSIDTAVKAVlgifslmtgklprFSAHGGSSRenLALQNVQARIRMVLAYLFAql 385
Cdd:PRK13980   66 SSVSPPEDLEDAELVAEDLGIEYKVIEITPIVDAF-------------FSAIPDADR--LRVGNIMARTRMVLLYDYA-- 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 386 slwsrgARGSLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFvqfcAERFQLPvlQTILSAPATAELEPla 465
Cdd:PRK13980  129 ------NRENRLVLGTGNKSELLLGYFTKYGDGAVDLNPIGDLYKTQVREL----ARHLGVP--EDIIEKPPSADLWE-- 194

                         250
                  ....*....|....*....
gi 1039780384 466 dgqvSQMDEEDMGMTYAEL 484
Cdd:PRK13980  195 ----GQTDEGELGFSYETI 209
nadE PRK02628
NAD synthetase; Reviewed
 8-478 6.64e-18

NAD synthetase; Reviewed


Pssm-ID: 235057 [Multi-domain]  Cd Length: 679  Bit Score: 87.61  E-value: 6.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384   8 NYR---ELRWFTPwTRSRQTEEYVLPRmlqdltkqKTVPFG-DVVLATQDT---CVGSEICEELWTPRSPHIDMGLDGVE 80
Cdd:PRK02628  127 NYRefyEKRWFAP-GDGARGETIRLCG--------QEVPFGtDLLFEAEDLpgfVFGVEICEDLWVPIPPSSYAALAGAT 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384  81 IITNASGSHHVLRKAHTRVDLVTMATSKNGGIYLLANqKGC-----DgdrLYYDGCAMIAMNGSIFAQGTQFSlDDVEVL 155
Cdd:PRK02628  198 VLANLSASNITVGKADYRRLLVASQSARCLAAYVYAA-AGVgesttD---LAWDGQTLIYENGELLAESERFP-REEQLI 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 156 TATLDLEDVR-------SYKAEISSRNLEAtrvsPYPRVTVDFALSVSEDLLEpvsepmewtyhRPEEEISLGPAcwlwD 228
Cdd:PRK02628  273 VADVDLERLRqerlrngSFDDNARHRDESA----PFRTIPFALDPPAGDLGLR-----------RPVERFPFVPS----D 333

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 229 FLRRSK--QAGFFLP-------------------LSGGVDSaASACIVysmCCLVCDAVKSGNQQVLTdvqnlvdessYT 287
Cdd:PRK02628  334 PARLDQrcYEAYNIQvsglaqrlratglkkvvigISGGLDS-THALLV---AAKAMDRLGLPRKNILA----------YT 399

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 288 pqdprelcgrllttcyMASENSSQETHSRATKLAQLIGSYHINLSIdtaVKAVLGIFSLMtgklprfsAHGGSSREN--- 364
Cdd:PRK02628  400 ----------------MPGFATTDRTKNNAVALMKALGVTAREIDI---RPAALQMLKDI--------GHPFARGEPvyd 452

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 365 LALQNVQARIRMvlAYLF--AQLslwsRGArgslLVLGSANVDESLLGYLTkYDC----SSADINpiGGISKTDLRAFVQ 438
Cdd:PRK02628  453 VTFENVQAGERT--QILFrlANQ----HGG----IVIGTGDLSELALGWCT-YGVgdhmSHYNVN--ASVPKTLIQHLIR 519

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 1039780384 439 FCAERFQL-----PVLQTILSAPATAELEP-LADGQVSQMDEEDMG 478
Cdd:PRK02628  520 WVIASGQFdeavsEVLLDILDTEISPELVPaDKEGEIVQSTEDIIG 565
PRK13981 PRK13981
NAD synthetase; Provisional
 56-471 6.58e-14

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 74.42  E-value: 6.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384  56 VGSEICEELWTPrSPHIDMGLDGVEIITNASGSHHVLRKAHTRVDLVTmATSKNGGIYLL-ANQKGcdG-DRLYYDGCAm 133
Cdd:PRK13981  140 IGVPICEDIWNP-EPAETLAEAGAELLLVPNASPYHRGKPDLREAVLR-ARVRETGLPLVyLNQVG--GqDELVFDGAS- 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 134 IAMN--GSIFAQGTQFSlddvevltatldlEDVrsykaeissrnleatrvspyprVTVDFALsvSEDLLEPVSEPMEwty 211
Cdd:PRK13981  215 FVLNadGELAARLPAFE-------------EQI----------------------AVVDFDR--GEDGWRPLPGPIA--- 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 212 HRPEEEISLGPACWLW--DFLRRSKQAGFFLPLSGGVDSAASACIvysmcclVCDAVksGNQQVLtdvqnlvdessytpq 289
Cdd:PRK13981  255 PPPEGEAEDYRALVLGlrDYVRKNGFPGVVLGLSGGIDSALVAAI-------AVDAL--GAERVR--------------- 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 290 dprelcgrlltTCYMASENSSQETHSRATKLAQLIG-SYHInLSIDTAVKAVLGIFSLMTGKLPRfsahgGSSRENLalq 368
Cdd:PRK13981  311 -----------AVMMPSRYTSEESLDDAAALAKNLGvRYDI-IPIEPAFEAFEAALAPLFAGTEP-----DITEENL--- 370

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 369 nvQARIRMVLayLFAqLSlwsrGARGSlLVLGSANVDESLLGYLTKYdcssADIN----PIGGISKTDLRAFVQFCAERF 444
Cdd:PRK13981  371 --QSRIRGTL--LMA-LS----NKFGS-LVLTTGNKSEMAVGYATLY----GDMAggfaPIKDVYKTLVYRLCRWRNTVS 436

                         410       420
                  ....*....|....*....|....*...
gi 1039780384 445 QLPVL-QTILSAPATAELEPladGQVSQ 471
Cdd:PRK13981  437 PGEVIpERIITKPPSAELRP---NQTDQ 461
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
3-173 4.79e-12

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 66.43  E-value: 4.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384   3 LANEGNYRELRWFTPWTRSrqteeyvlprmlqdltkqktvpfgdVVLATQDTCVGSEICEELWTPRSPHIdMGLDGVEII 82
Cdd:COG0388   116 LPNYGVFDEKRYFTPGDEL-------------------------VVFDTDGGRIGVLICYDLWFPELARA-LALAGADLL 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384  83 TNASGSHHVLRKAHtrVDLVTMATSKNGGIYLL-ANQKGCDGDRLYYdGCAMIA-MNGSIFAQGTqfslDDVEVLTATLD 160
Cdd:COG0388   170 LVPSASPFGRGKDH--WELLLRARAIENGCYVVaANQVGGEDGLVFD-GGSMIVdPDGEVLAEAG----DEEGLLVADID 242

                         170
                  ....*....|...
gi 1039780384 161 LEDVRSYKAEISS 173
Cdd:COG0388   243 LDRLREARRRFPV 255
nadE PRK00768
ammonia-dependent NAD(+) synthetase;
369-484 2.34e-09

ammonia-dependent NAD(+) synthetase;


Pssm-ID: 234831 [Multi-domain]  Cd Length: 268  Bit Score: 58.62  E-value: 2.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780384 369 NVQARIRMVLAYLFAqlslwsrGARGsLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFVQF--CAERfql 446
Cdd:PRK00768  134 NIKARERMIAQYAIA-------GATG-GLVVGTDHAAEAVTGFFTKFGDGGADILPLFGLNKRQGRALLAAlgAPEH--- 202

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1039780384 447 pvlqTILSAPaTAELEplaDGQVSQMDEEDMGMTYAEL 484
Cdd:PRK00768  203 ----LYEKVP-TADLE---DDRPGLPDEVALGVTYDQI 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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