|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02339 |
PLN02339 |
NAD+ synthase (glutamine-hydrolysing) |
1-696 |
0e+00 |
|
NAD+ synthase (glutamine-hydrolysing)
Pssm-ID: 177973 [Multi-domain] Cd Length: 700 Bit Score: 1481.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 1 MRLVKVSTCSLNQWAMDFEGNLGRINESIRQARAAGSMLRVGPELEITGYGCDDHFLENDTSAHAWECLAEILSSDLTYG 80
Cdd:PLN02339 1 MRLLKVATCNLNQWAMDFDGNLKRIKESIAEAKAAGAVYRVGPELEITGYGCEDHFLELDTVTHSWECLAEILVGDLTDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 81 IVCDIGMPVVSDGVRYNCRVFCLDGKILLIRPKKFLANDGNYRELRWFAAWQHHNSVIEYKLPEIIWSKTSQKTVTFGDA 160
Cdd:PLN02339 81 ILCDIGMPVIHGGVRYNCRVFCLNRKILLIRPKMWLANDGNYRELRWFTAWKHKKKVEDFQLPEEIAEATSQKSVPFGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 161 YVSFLDTAVAVETCEELFTPSSPHIGLALNGVEIIVNGSGSHHQLRKLNTRIELMQGATHKAGGVYLYANQQGCDGARLY 240
Cdd:PLN02339 161 YLQFLDTAVAAETCEELFTPQAPHIDLALNGVEIISNGSGSHHQLRKLNTRLDLIRSATHKCGGVYLYANQRGCDGGRLY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 241 YDGCATVFVNGDMVVQGSQFSLADVEVLTACVDLDAVSTFRGSISSLREQASQHKFMPYVSVDFRLSrPDDSLLLFPTLP 320
Cdd:PLN02339 241 YDGCACIVVNGEVVAQGSQFSLQDVEVVTACVDLDAVVSFRGSISSFREQASSKKRVPSVAVPFKLC-PPFSLSLVPSSP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 321 ILPRYYLPEEEIALGPACWLWDYLRRCGATGYLLPLSGGADSSAVAAIVGSMCQLVIRAIEEGDEQVLNDAIRIGNYENG 400
Cdd:PLN02339 320 LKIRYHSPEEEIALGPACWLWDYLRRSGASGFLLPLSGGADSSSVAAIVGSMCQLVVKAIREGDEQVKADARRIGNYADG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 401 KVPKSAEEFANRIVFTVYMGSENSSAQTLNRAAQLASQIGASHMDLKIDKIVSALVSLFTSLTGKVPRYKVDGGSTAENL 480
Cdd:PLN02339 400 EVPTDSKEFAKRIFYTVYMGSENSSEETRSRAKQLADEIGSSHLDVKIDGVVSAVLSLFQTLTGKRPRYKVDGGSNAENL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 481 ALQNLQARIRMVIAYMLASLLPWVKGKRGFFLVLGSANVDEGLRGYLTKYDCSSADLNPIGGISKQDLRSFLRWCANNLH 560
Cdd:PLN02339 480 ALQNIQARIRMVLAFMLASLLPWVRGKSGFLLVLGSANVDEGLRGYLTKYDCSSADINPIGGISKQDLRSFLRWAATNLG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 561 YPILAEVVSAPPTAELEPIRENYSQTDEEDMGMTYEELSMYGRLRKIFHCGPVSMFKNLCHRWHGKLDPGQVAIKVKDFF 640
Cdd:PLN02339 560 YPSLAEVEAAPPTAELEPIRDDYSQTDEEDMGMTYEELGVYGRLRKIFRCGPVSMFKNLCHEWNGRLSPSEVAAKVKDFF 639
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 302788997 641 RFYSINRHKMTTITPAYHAENYSPDDNRFDQRQFLYNTRWPWQFKKIDEIVERAAK 696
Cdd:PLN02339 640 KYYSINRHKMTTLTPSYHAESYSPDDNRFDLRQFLYNTRWPYQFRKIDELVEELDG 695
|
|
| GAT_Gln-NAD-synth |
cd07570 |
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ... |
5-294 |
7.76e-91 |
|
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: 284.36 E-value: 7.76e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 5 KVSTCSLNQWAMDFEGNLGRINESIRQARAAGSMLRVGPELEITGYGCDDHFLENDTSAHAWECLAEILSSDLTYGIVCD 84
Cdd:cd07570 1 RIALAQLNPTVGDLEGNAEKILEAIREAKAQGADLVVFPELSLTGYPPEDLLLRPDFLEAAEEALEELAAATADLDIAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 85 IGMPVVSDGVRYNCRVFCLDGKILLIRPKKFLANDGNYRELRWFAAWQHHNsvieyklpeiiwsktsqktvtfgdaYVSF 164
Cdd:cd07570 81 VGLPLRHDGKLYNAAAVLQNGKILGVVPKQLLPNYGVFDEKRYFTPGDKPD-------------------------VLFF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 165 LDTAVAVETCEELFTPSSPHIGLALNGVEIIVNGSGSHHQLRKLNTRIELMQGATHKAGGVYLYANqQGCDGARLYYDGC 244
Cdd:cd07570 136 KGLRIGVEICEDLWVPDPPSAELALAGADLILNLSASPFHLGKQDYRRELVSSRSARTGLPYVYVN-QVGGQDDLVFDGG 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 302788997 245 ATVFVN-GDMVVQGSQFsladvEVLTACVDLDAVSTFRGSISSLREQASQH 294
Cdd:cd07570 215 SFIADNdGELLAEAPRF-----EEDLADVDLDRLRSERRRNSSFLDEEAEI 260
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
63-669 |
8.01e-47 |
|
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: 174.65 E-value: 8.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 63 AHAWECLAEILSSDLTYGIVCDIGMPVVSDGVRYNCRVFCLDGKILLIRPKKFLANDGNYRELRWFAAWQHHNSVIEYKL 142
Cdd:COG0171 16 DAAAAAAAALAALAAAAAALLLLLLLLLLLLLLLLALLLLLAAARLLVAAAALLLLALAAGGGAALAGGGGGAGGGLLNG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 143 PEIIWsktsqKTVTFGDAYVSFLDTAVAVETCEELFTPSSPHIGLALNGVEIIVNGSGSHHQLRKLNTRIELMQGATHKA 222
Cdd:COG0171 96 AALVL-----GGGDLLFFADDFLLLLLVVEEEEEEFVGGPPPPPAALGGAGVLLILSSSSSAVGAAAAAAALAAALLSSL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 223 GGVYLYANQQGCDGARLYYDGCATVFVNGDMVVQGSQFSLADVEVLTACVDLDavstfrgsissLREQASQHKFMPYVSV 302
Cdd:COG0171 171 SSAAYYAAAGGGESTTDLARGGGGGLLLVVLLLVGGGDDDFFDGGSAAVDDDD-----------LLLLLRRRREEELLLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 303 DFRLSRPDDSLLLFPTLPILPRYYLPEEEIALGPACWLWDYLRRCGATGYLLPLSGGADSSAVAAivgsmcqLVIRAIee 382
Cdd:COG0171 240 RARDADGGRRVAAEAAPPPPEEEEMDLEEVYDALVLGLRDYVRKNGFKGVVLGLSGGIDSALVAA-------LAVDAL-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 383 GDEQVLndairignyengkvpksaeefanrivfTVYMGSENSSAQTLNRAAQLASQIGASHMDLKIDKIVSALVSLFtsl 462
Cdd:COG0171 311 GPENVL---------------------------GVTMPSRYTSDESLEDAEELAENLGIEYEEIDITPAVEAFLEAL--- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 463 tgkvpryKVDGGSTAENLALQNLQARIRMVIAYMLAsllpwvkGKRGfFLVLGSANVDEGLRGYLTKYDCSSADLNPIGG 542
Cdd:COG0171 361 -------PHAFGGELDDVAEENLQARIRMVILMALA-------NKFG-GLVLGTGNKSELAVGYFTKYGDGAGDLAPIAD 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 543 ISKQDLRSFLRWCaNNLHYPILAEVVSAPPTAELEPirenySQTDEEDMGmTYEELS--MYGRLRKifhcgpvsmfknlc 620
Cdd:COG0171 426 LYKTQVYALARWL-NRNGEVIPEDIIDKPPSAELRP-----GQTDEDELG-PYEVLDaiLYAYVEE-------------- 484
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 302788997 621 hrwhgKLDPGQVAIK------VKDFFRFYSINRHKMTTITPAYHAENYSPD-DNRF 669
Cdd:COG0171 485 -----GLSPEEIAAAgydrewVERVLRLVRRNEYKRRQPPPGPKVSSRAFGrGRRY 535
|
|
| NAD_synthase |
pfam02540 |
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ... |
339-601 |
1.05e-33 |
|
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: 129.42 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 339 WLWDYLRRCGATGYLLPLSGGADSSAVAAivgsMCQLVIraieeGDEQVLndairignyengkvpksaeefanrivfTVY 418
Cdd:pfam02540 8 FLRDYVQKAGFKGVVLGLSGGIDSSLVAY----LAVKAL-----GKENVL---------------------------ALI 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 419 MGSENSSAQTLNRAAQLASQIGASHMDLKIDKIVSALVSLFtsltgkvprykvdgGSTAENLALQNLQARIRMVIAYMLA 498
Cdd:pfam02540 52 MPSSQSSEEDVQDALALAENLGIEYKTIDIKPIVRAFSQLF--------------QDASEDFAKGNLKARIRMAILYYIA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 499 sllpwvkGKRGFfLVLGSANVDEGLRGYLTKYDCSSADLNPIGGISKQDLRSFLRWCAnnlhypILAEVVSAPPTAELEP 578
Cdd:pfam02540 118 -------NKFNY-LVLGTGNKSELAVGYFTKYGDGACDIAPIGDLYKTQVYELARYLN------VPERIIKKPPSADLWP 183
|
250 260
....*....|....*....|...
gi 302788997 579 irenySQTDEEDMGMTYEELSMY 601
Cdd:pfam02540 184 -----GQTDEEELGIPYDELDDI 201
|
|
| nadE |
TIGR00552 |
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ... |
339-642 |
2.15e-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: 125.96 E-value: 2.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 339 WLWDYLRRCGATGYLLPLSGGADSSAVAAIvgsmcqlvirAIEEGDEQVLndAIRIgnyengkvpksaeefanrivftvy 418
Cdd:TIGR00552 12 FLRGYVQKSGAKGVVLGLSGGIDSAVVAAL----------CVEALGEQNH--ALLL------------------------ 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 419 MGSENSSAQTLNRAAQLASQIGASHMDLKIDKIVSALVSLFtsltgkvprykVDGGSTAENLALQNLQARIRMVIAYMLA 498
Cdd:TIGR00552 56 PHSVQTPEQDVQDALALAEPLGINYKNIDIAPIAASFQAQT-----------ETGDELSDFLAKGNLKARLRMAALYAIA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 499 sllpwvkGKRGfFLVLGSANVDEGLRGYLTKYDCSSADLNPIGGISKQDLRSFLRWcannLHYPilAEVVSAPPTAELEP 578
Cdd:TIGR00552 125 -------NKHN-LLVLGTGNKSELMLGYFTKYGDGGCDIAPIGDLFKTQVYELAKR----LNVP--ERIIEKPPTADLFD 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 302788997 579 irenySQTDEEDMGMTYEELSMYGRLRKIFHCGPVSMFKNLCHRWHGKLDPGQVAIKVKDFFRF 642
Cdd:TIGR00552 191 -----GQTDETELGITYDELDDYLKGIEELSQTVQEVVKRIESLVQKSEHKRRLPATIFDLFWK 249
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02339 |
PLN02339 |
NAD+ synthase (glutamine-hydrolysing) |
1-696 |
0e+00 |
|
NAD+ synthase (glutamine-hydrolysing)
Pssm-ID: 177973 [Multi-domain] Cd Length: 700 Bit Score: 1481.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 1 MRLVKVSTCSLNQWAMDFEGNLGRINESIRQARAAGSMLRVGPELEITGYGCDDHFLENDTSAHAWECLAEILSSDLTYG 80
Cdd:PLN02339 1 MRLLKVATCNLNQWAMDFDGNLKRIKESIAEAKAAGAVYRVGPELEITGYGCEDHFLELDTVTHSWECLAEILVGDLTDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 81 IVCDIGMPVVSDGVRYNCRVFCLDGKILLIRPKKFLANDGNYRELRWFAAWQHHNSVIEYKLPEIIWSKTSQKTVTFGDA 160
Cdd:PLN02339 81 ILCDIGMPVIHGGVRYNCRVFCLNRKILLIRPKMWLANDGNYRELRWFTAWKHKKKVEDFQLPEEIAEATSQKSVPFGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 161 YVSFLDTAVAVETCEELFTPSSPHIGLALNGVEIIVNGSGSHHQLRKLNTRIELMQGATHKAGGVYLYANQQGCDGARLY 240
Cdd:PLN02339 161 YLQFLDTAVAAETCEELFTPQAPHIDLALNGVEIISNGSGSHHQLRKLNTRLDLIRSATHKCGGVYLYANQRGCDGGRLY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 241 YDGCATVFVNGDMVVQGSQFSLADVEVLTACVDLDAVSTFRGSISSLREQASQHKFMPYVSVDFRLSrPDDSLLLFPTLP 320
Cdd:PLN02339 241 YDGCACIVVNGEVVAQGSQFSLQDVEVVTACVDLDAVVSFRGSISSFREQASSKKRVPSVAVPFKLC-PPFSLSLVPSSP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 321 ILPRYYLPEEEIALGPACWLWDYLRRCGATGYLLPLSGGADSSAVAAIVGSMCQLVIRAIEEGDEQVLNDAIRIGNYENG 400
Cdd:PLN02339 320 LKIRYHSPEEEIALGPACWLWDYLRRSGASGFLLPLSGGADSSSVAAIVGSMCQLVVKAIREGDEQVKADARRIGNYADG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 401 KVPKSAEEFANRIVFTVYMGSENSSAQTLNRAAQLASQIGASHMDLKIDKIVSALVSLFTSLTGKVPRYKVDGGSTAENL 480
Cdd:PLN02339 400 EVPTDSKEFAKRIFYTVYMGSENSSEETRSRAKQLADEIGSSHLDVKIDGVVSAVLSLFQTLTGKRPRYKVDGGSNAENL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 481 ALQNLQARIRMVIAYMLASLLPWVKGKRGFFLVLGSANVDEGLRGYLTKYDCSSADLNPIGGISKQDLRSFLRWCANNLH 560
Cdd:PLN02339 480 ALQNIQARIRMVLAFMLASLLPWVRGKSGFLLVLGSANVDEGLRGYLTKYDCSSADINPIGGISKQDLRSFLRWAATNLG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 561 YPILAEVVSAPPTAELEPIRENYSQTDEEDMGMTYEELSMYGRLRKIFHCGPVSMFKNLCHRWHGKLDPGQVAIKVKDFF 640
Cdd:PLN02339 560 YPSLAEVEAAPPTAELEPIRDDYSQTDEEDMGMTYEELGVYGRLRKIFRCGPVSMFKNLCHEWNGRLSPSEVAAKVKDFF 639
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 302788997 641 RFYSINRHKMTTITPAYHAENYSPDDNRFDQRQFLYNTRWPWQFKKIDEIVERAAK 696
Cdd:PLN02339 640 KYYSINRHKMTTLTPSYHAESYSPDDNRFDLRQFLYNTRWPYQFRKIDELVEELDG 695
|
|
| GAT_Gln-NAD-synth |
cd07570 |
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ... |
5-294 |
7.76e-91 |
|
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: 284.36 E-value: 7.76e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 5 KVSTCSLNQWAMDFEGNLGRINESIRQARAAGSMLRVGPELEITGYGCDDHFLENDTSAHAWECLAEILSSDLTYGIVCD 84
Cdd:cd07570 1 RIALAQLNPTVGDLEGNAEKILEAIREAKAQGADLVVFPELSLTGYPPEDLLLRPDFLEAAEEALEELAAATADLDIAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 85 IGMPVVSDGVRYNCRVFCLDGKILLIRPKKFLANDGNYRELRWFAAWQHHNsvieyklpeiiwsktsqktvtfgdaYVSF 164
Cdd:cd07570 81 VGLPLRHDGKLYNAAAVLQNGKILGVVPKQLLPNYGVFDEKRYFTPGDKPD-------------------------VLFF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 165 LDTAVAVETCEELFTPSSPHIGLALNGVEIIVNGSGSHHQLRKLNTRIELMQGATHKAGGVYLYANqQGCDGARLYYDGC 244
Cdd:cd07570 136 KGLRIGVEICEDLWVPDPPSAELALAGADLILNLSASPFHLGKQDYRRELVSSRSARTGLPYVYVN-QVGGQDDLVFDGG 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 302788997 245 ATVFVN-GDMVVQGSQFsladvEVLTACVDLDAVSTFRGSISSLREQASQH 294
Cdd:cd07570 215 SFIADNdGELLAEAPRF-----EEDLADVDLDRLRSERRRNSSFLDEEAEI 260
|
|
| NAD_synthase |
cd00553 |
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ... |
327-650 |
1.19e-84 |
|
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: 267.88 E-value: 1.19e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 327 LPEEEIALGPACWLWDYLRRCGATGYLLPLSGGADSSAVAAIVGSMCqlviraieeGDEQVLndairignyengkvpksa 406
Cdd:cd00553 1 IDPEEIIEALVCFLRDYLRKSGAKGFVLGLSGGIDSAVVAALAVRAL---------GAENVL------------------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 407 eefanrivfTVYMGSENSSAQTLNRAAQLASQIGASHMDLKIDKIVSALVSLFtsltgkvpryKVDGGSTAENLALQNLQ 486
Cdd:cd00553 54 ---------ALIMPSRYSSKETRDDAKALAENLGIEYRTIDIDPIVDAFLKAL----------EHAGGSEAEDLALGNIQ 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 487 ARIRMVIAYMLASLLpwvkgkrgFFLVLGSANVDEGLRGYLTKYDCSSADLNPIGGISKQDLRSFLRWCAnnlhypILAE 566
Cdd:cd00553 115 ARLRMVLLYALANLL--------GGLVLGTGNKSELLLGYFTKYGDGAADINPIGDLYKTQVRELARYLG------VPEE 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 567 VVSAPPTAELEPirenySQTDEEDMGMTYEELSMYGRLRKIFHCGPVSmfknlchrwhgKLDPGQVAIKVKDFFRFYSIN 646
Cdd:cd00553 181 IIEKPPSAELWP-----GQTDEDELGMPYEELDLILYGLVDGKLGPEE-----------ILSPGEDEEKVKRIFRLYRRN 244
|
....
gi 302788997 647 RHKM 650
Cdd:cd00553 245 EHKR 248
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
63-669 |
8.01e-47 |
|
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: 174.65 E-value: 8.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 63 AHAWECLAEILSSDLTYGIVCDIGMPVVSDGVRYNCRVFCLDGKILLIRPKKFLANDGNYRELRWFAAWQHHNSVIEYKL 142
Cdd:COG0171 16 DAAAAAAAALAALAAAAAALLLLLLLLLLLLLLLLALLLLLAAARLLVAAAALLLLALAAGGGAALAGGGGGAGGGLLNG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 143 PEIIWsktsqKTVTFGDAYVSFLDTAVAVETCEELFTPSSPHIGLALNGVEIIVNGSGSHHQLRKLNTRIELMQGATHKA 222
Cdd:COG0171 96 AALVL-----GGGDLLFFADDFLLLLLVVEEEEEEFVGGPPPPPAALGGAGVLLILSSSSSAVGAAAAAAALAAALLSSL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 223 GGVYLYANQQGCDGARLYYDGCATVFVNGDMVVQGSQFSLADVEVLTACVDLDavstfrgsissLREQASQHKFMPYVSV 302
Cdd:COG0171 171 SSAAYYAAAGGGESTTDLARGGGGGLLLVVLLLVGGGDDDFFDGGSAAVDDDD-----------LLLLLRRRREEELLLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 303 DFRLSRPDDSLLLFPTLPILPRYYLPEEEIALGPACWLWDYLRRCGATGYLLPLSGGADSSAVAAivgsmcqLVIRAIee 382
Cdd:COG0171 240 RARDADGGRRVAAEAAPPPPEEEEMDLEEVYDALVLGLRDYVRKNGFKGVVLGLSGGIDSALVAA-------LAVDAL-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 383 GDEQVLndairignyengkvpksaeefanrivfTVYMGSENSSAQTLNRAAQLASQIGASHMDLKIDKIVSALVSLFtsl 462
Cdd:COG0171 311 GPENVL---------------------------GVTMPSRYTSDESLEDAEELAENLGIEYEEIDITPAVEAFLEAL--- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 463 tgkvpryKVDGGSTAENLALQNLQARIRMVIAYMLAsllpwvkGKRGfFLVLGSANVDEGLRGYLTKYDCSSADLNPIGG 542
Cdd:COG0171 361 -------PHAFGGELDDVAEENLQARIRMVILMALA-------NKFG-GLVLGTGNKSELAVGYFTKYGDGAGDLAPIAD 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 543 ISKQDLRSFLRWCaNNLHYPILAEVVSAPPTAELEPirenySQTDEEDMGmTYEELS--MYGRLRKifhcgpvsmfknlc 620
Cdd:COG0171 426 LYKTQVYALARWL-NRNGEVIPEDIIDKPPSAELRP-----GQTDEDELG-PYEVLDaiLYAYVEE-------------- 484
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 302788997 621 hrwhgKLDPGQVAIK------VKDFFRFYSINRHKMTTITPAYHAENYSPD-DNRF 669
Cdd:COG0171 485 -----GLSPEEIAAAgydrewVERVLRLVRRNEYKRRQPPPGPKVSSRAFGrGRRY 535
|
|
| PRK13981 |
PRK13981 |
NAD synthetase; Provisional |
4-588 |
6.34e-34 |
|
NAD synthetase; Provisional
Pssm-ID: 237577 [Multi-domain] Cd Length: 540 Bit Score: 136.83 E-value: 6.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 4 VKVSTCSLNQWAMDFEGNLGRINESIRQARAAGSMLRVGPELEITGYGCDDHFLENDTSAHAWECLAEiLSSDLTYGIVC 83
Cdd:PRK13981 1 LRIALAQLNPTVGDIAGNAAKILAAAAEAADAGADLLLFPELFLSGYPPEDLLLRPAFLAACEAALER-LAAATAGGPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 84 DIGMPVVSDGVRYNCRVFCLDGKILLIRPKKFLANDGNYRELRWFAAWQHHNsVIEYklpeiiwsktsqKTVTFGdayvs 163
Cdd:PRK13981 80 LVGHPWREGGKLYNAAALLDGGEVLATYRKQDLPNYGVFDEKRYFAPGPEPG-VVEL------------KGVRIG----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 164 fldtavaVETCEELFTPSSPHIgLALNGVEIIVNGSGSHHQLRKLNTRIELMQGATHKAGGVYLYANQQGcdGA-RLYYD 242
Cdd:PRK13981 142 -------VPICEDIWNPEPAET-LAEAGAELLLVPNASPYHRGKPDLREAVLRARVRETGLPLVYLNQVG--GQdELVFD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 243 GCATVF-VNGDMVVQGSQFSlADVEVltacVDLDAvstfrgsisslreqasqhkfmpyvsvDFRLSRPDDSlllfPTLPI 321
Cdd:PRK13981 212 GASFVLnADGELAARLPAFE-EQIAV----VDFDR--------------------------GEDGWRPLPG----PIAPP 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 322 LPRyylpEEEI----ALGpacwLWDYLRRCGATGYLLPLSGGADSSAVAAIvgsmcqlvirAIeegdeqvlnDAirIGNy 397
Cdd:PRK13981 257 PEG----EAEDyralVLG----LRDYVRKNGFPGVVLGLSGGIDSALVAAI----------AV---------DA--LGA- 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 398 ENgkvpksaeefanriVFTVYMGSENSSAQTLNRAAQLASQIGASHMDLKIDKIV----SALVSLFTsltgkvprykvdg 473
Cdd:PRK13981 307 ER--------------VRAVMMPSRYTSEESLDDAAALAKNLGVRYDIIPIEPAFeafeAALAPLFA------------- 359
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 474 gSTAENLALQNLQARIRMVIAYMLASllpwvkgKRGfFLVLGSANVDEGLRGYLTKYDCSSADLNPIGGISKQDLRSFLR 553
Cdd:PRK13981 360 -GTEPDITEENLQSRIRGTLLMALSN-------KFG-SLVLTTGNKSEMAVGYATLYGDMAGGFAPIKDVYKTLVYRLCR 430
|
570 580 590
....*....|....*....|....*....|....*...
gi 302788997 554 WcaNNLHYP---ILAEVVSAPPTAELepiRENysQTDE 588
Cdd:PRK13981 431 W--RNTVSPgevIPERIITKPPSAEL---RPN--QTDQ 461
|
|
| NAD_synthase |
pfam02540 |
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ... |
339-601 |
1.05e-33 |
|
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: 129.42 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 339 WLWDYLRRCGATGYLLPLSGGADSSAVAAivgsMCQLVIraieeGDEQVLndairignyengkvpksaeefanrivfTVY 418
Cdd:pfam02540 8 FLRDYVQKAGFKGVVLGLSGGIDSSLVAY----LAVKAL-----GKENVL---------------------------ALI 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 419 MGSENSSAQTLNRAAQLASQIGASHMDLKIDKIVSALVSLFtsltgkvprykvdgGSTAENLALQNLQARIRMVIAYMLA 498
Cdd:pfam02540 52 MPSSQSSEEDVQDALALAENLGIEYKTIDIKPIVRAFSQLF--------------QDASEDFAKGNLKARIRMAILYYIA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 499 sllpwvkGKRGFfLVLGSANVDEGLRGYLTKYDCSSADLNPIGGISKQDLRSFLRWCAnnlhypILAEVVSAPPTAELEP 578
Cdd:pfam02540 118 -------NKFNY-LVLGTGNKSELAVGYFTKYGDGACDIAPIGDLYKTQVYELARYLN------VPERIIKKPPSADLWP 183
|
250 260
....*....|....*....|...
gi 302788997 579 irenySQTDEEDMGMTYEELSMY 601
Cdd:pfam02540 184 -----GQTDEEELGIPYDELDDI 201
|
|
| nadE |
TIGR00552 |
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ... |
339-642 |
2.15e-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: 125.96 E-value: 2.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 339 WLWDYLRRCGATGYLLPLSGGADSSAVAAIvgsmcqlvirAIEEGDEQVLndAIRIgnyengkvpksaeefanrivftvy 418
Cdd:TIGR00552 12 FLRGYVQKSGAKGVVLGLSGGIDSAVVAAL----------CVEALGEQNH--ALLL------------------------ 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 419 MGSENSSAQTLNRAAQLASQIGASHMDLKIDKIVSALVSLFtsltgkvprykVDGGSTAENLALQNLQARIRMVIAYMLA 498
Cdd:TIGR00552 56 PHSVQTPEQDVQDALALAEPLGINYKNIDIAPIAASFQAQT-----------ETGDELSDFLAKGNLKARLRMAALYAIA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 499 sllpwvkGKRGfFLVLGSANVDEGLRGYLTKYDCSSADLNPIGGISKQDLRSFLRWcannLHYPilAEVVSAPPTAELEP 578
Cdd:TIGR00552 125 -------NKHN-LLVLGTGNKSELMLGYFTKYGDGGCDIAPIGDLFKTQVYELAKR----LNVP--ERIIEKPPTADLFD 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 302788997 579 irenySQTDEEDMGMTYEELSMYGRLRKIFHCGPVSMFKNLCHRWHGKLDPGQVAIKVKDFFRF 642
Cdd:TIGR00552 191 -----GQTDETELGITYDELDDYLKGIEELSQTVQEVVKRIESLVQKSEHKRRLPATIFDLFWK 249
|
|
| CN_hydrolase |
pfam00795 |
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ... |
5-281 |
3.30e-32 |
|
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: 125.55 E-value: 3.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 5 KVSTCSLNQWAMDFEGNLGRINESIRQARAAGSMLRVGPELEITGYGCDDHFLENDTsAHAWECLAEILSSDLTYGIVCD 84
Cdd:pfam00795 1 RVALVQLPQGFWDLEANLQKALELIEEAARYGADLIVLPELFITGYPCWAHFLEAAE-VGDGETLAGLAALARKNGIAIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 85 IGMPVVSDgvrYNCRVFCldGKILLIRPKKFLandGNYRELRWFAAWQhHNSVIEYKLPEiiwsktsqktvtFGDAYVSF 164
Cdd:pfam00795 80 IGLIERWL---TGGRLYN--TAVLLDPDGKLV---GKYRKLHLFPEPR-PPGFRERVLFE------------PGDGGTVF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 165 lDTAVA---VETCEELFTPSSPHIgLALNGVEIIVNGS-GSHHQLRKLNTRIELMQGATHKAGGVY-LYANQQGCDG-AR 238
Cdd:pfam00795 139 -DTPLGkigAAICYEIRFPELLRA-LALKGAEILINPSaRAPFPGSLGPPQWLLLARARALENGCFvIAANQVGGEEdAP 216
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 302788997 239 LYYDGCATVFVNGDMVVQGSQFSLadvEVLTACVDLDAVSTFR 281
Cdd:pfam00795 217 WPYGHSMIIDPDGRILAGAGEWEE---GVLIADIDLALVRAWR 256
|
|
| nadE |
PRK02628 |
NAD synthetase; Reviewed |
4-320 |
1.61e-30 |
|
NAD synthetase; Reviewed
Pssm-ID: 235057 [Multi-domain] Cd Length: 679 Bit Score: 128.06 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 4 VKVSTCSLNQWAMDFEGNLGRINESIRQARAAGSMLRVGPELEITGYGCDDHFLEN---DTSAHAwecLAEIL--SSDLT 78
Cdd:PRK02628 13 VRVAAATPKVRVADPAFNAARILALARRAADDGVALAVFPELSLSGYSCDDLFLQDtllDAVEDA---LATLVeaSADLD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 79 ygIVCDIGMPVVSDGVRYNCRVFCLDGKILLIRPKKFLANDGNYRELRWFAAWqhhnsviEYKLPEIIwsKTSQKTVTFG 158
Cdd:PRK02628 90 --PLLVVGAPLRVRHRLYNCAVVIHRGRILGVVPKSYLPNYREFYEKRWFAPG-------DGARGETI--RLCGQEVPFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 159 ------DAYVSFLdtAVAVETCEELFTPSSPHIGLALNGVEIIVNGSGSHHQLRKLNTRIELM--QGATHKAGgvYLYAN 230
Cdd:PRK02628 159 tdllfeAEDLPGF--VFGVEICEDLWVPIPPSSYAALAGATVLANLSASNITVGKADYRRLLVasQSARCLAA--YVYAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 231 Q-QGCDGARLYYDGCATVFVNGDMVVQGSQFSLaDVEVLTACVDLD-------AVSTFRGSISSLREQAsqhkfmPYVSV 302
Cdd:PRK02628 235 AgVGESTTDLAWDGQTLIYENGELLAESERFPR-EEQLIVADVDLErlrqerlRNGSFDDNARHRDESA------PFRTI 307
|
330 340
....*....|....*....|....
gi 302788997 303 DFRLSRPDDSLLL------FPTLP 320
Cdd:PRK02628 308 PFALDPPAGDLGLrrpverFPFVP 331
|
|
| Nit2 |
COG0388 |
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]; |
4-288 |
9.78e-28 |
|
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
Pssm-ID: 440157 [Multi-domain] Cd Length: 264 Bit Score: 113.03 E-value: 9.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 4 VKVSTCSLNQWAMDFEGNLGRINESIRQARAAGSMLRVGPELEITGYGCDDHFLEndtsAHAWECLAEILS--SDLT--Y 79
Cdd:COG0388 2 MRIALAQLNPTVGDIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLL----ELAEPLDGPALAalAELAreL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 80 GIVCDIGMPVVS-DGVRYNC-RVFCLDGKILLIRPKKFLANDGNYRELRWFAAwqhhnsvieyklpeiiwsktsqktvtf 157
Cdd:COG0388 78 GIAVVVGLPERDeGGRLYNTaLVIDPDGEILGRYRKIHLPNYGVFDEKRYFTP--------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 158 GDAYVSFlDTA---VAVETCEELFTPSSPHIgLALNGVEIIVNGSGSHHQlRKLNTRIELMQGATHKAGGVYLYANQQGC 234
Cdd:COG0388 131 GDELVVF-DTDggrIGVLICYDLWFPELARA-LALAGADLLLVPSASPFG-RGKDHWELLLRARAIENGCYVVAANQVGG 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 302788997 235 DGARLYYdGCATVF-VNGDMVVQGSqfslADVEVLTACVDLDAVSTFRGSISSLR 288
Cdd:COG0388 208 EDGLVFD-GGSMIVdPDGEVLAEAG----DEEGLLVADIDLDRLREARRRFPVLR 257
|
|
| PRK13980 |
PRK13980 |
NAD synthetase; Provisional |
342-598 |
4.27e-24 |
|
NAD synthetase; Provisional
Pssm-ID: 184435 [Multi-domain] Cd Length: 265 Bit Score: 102.21 E-value: 4.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 342 DYLRRCGATGYLLPLSGGADSSAVAAivgsmcqLVIRAIeeGDEQVLndairignyengkvpksaeefanrivfTVYMGS 421
Cdd:PRK13980 23 EEVEKAGAKGVVLGLSGGIDSAVVAY-------LAVKAL--GKENVL---------------------------ALLMPS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 422 ENSSAQTLNRAAQLASQIGASHMDLKIDKIVSALVSLFtsltgkvprykvdggSTAENLALQNLQARIRMVIAYMLASLL 501
Cdd:PRK13980 67 SVSPPEDLEDAELVAEDLGIEYKVIEITPIVDAFFSAI---------------PDADRLRVGNIMARTRMVLLYDYANRE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 502 PwvkgkrgfFLVLGSANVDEGLRGYLTKYDCSSADLNPIGGISKQDLRSFLRwcannlHYPILAEVVSAPPTAELEPire 581
Cdd:PRK13980 132 N--------RLVLGTGNKSELLLGYFTKYGDGAVDLNPIGDLYKTQVRELAR------HLGVPEDIIEKPPSADLWE--- 194
|
250
....*....|....*..
gi 302788997 582 nySQTDEEDMGMTYEEL 598
Cdd:PRK13980 195 --GQTDEGELGFSYETI 209
|
|
| nitrilase_8 |
cd07586 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
17-288 |
1.27e-12 |
|
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.
Pssm-ID: 143610 Cd Length: 269 Bit Score: 68.85 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 17 DFEGNLGRINESIRQARAAGSMLRVGPELEITGYGCDDHFLE--NDTSAHAWECLAEiLSSDLTygIVCDiGMPVVSDGV 94
Cdd:cd07586 13 DVEENLEKHLEIIETARERGADLVVFPELSLTGYNLGDLVYEvaMHADDPRLQALAE-ASGGIC--VVFG-FVEEGRDGR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 95 RYNCRVFCLDGKILLIRPKKFLANDGNYRELRWFAAWQHHNsVIEYKlpeiiwsktsqktvtFGdayvsfldtAVAVETC 174
Cdd:cd07586 89 FYNSAAYLEDGRVVHVHRKVYLPTYGLFEEGRYFAPGSHLR-AFDTR---------------FG---------RAGVLIC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 175 EELFTPSSPHIgLALNGVEII-----------VNGSGSHHQLRKLNTRIELMQgathkagGVY-LYANQQGCDGARLYYD 242
Cdd:cd07586 144 EDAWHPSLPYL-LALDGADVIfipanspargvGGDFDNEENWETLLKFYAMMN-------GVYvVFANRVGVEDGVYFWG 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 302788997 243 GCATVFVNGDMVVQGSQFslaDVEVLTACVDLDAVSTFRGSISSLR 288
Cdd:cd07586 216 GSRVVDPDGEVVAEAPLF---EEDLLVAELDRSAIRRARFFSPTFR 258
|
|
| nadE |
PRK00768 |
ammonia-dependent NAD(+) synthetase; |
328-598 |
6.61e-11 |
|
ammonia-dependent NAD(+) synthetase;
Pssm-ID: 234831 [Multi-domain] Cd Length: 268 Bit Score: 63.62 E-value: 6.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 328 PEEEIALGPAcWLWDYLRRCGATGYLLPLSGGADSSavaaIVGSMCQLvirAIEEgdeqvLNDAIRIGNYEngkvpksae 407
Cdd:PRK00768 18 PEEEIRRRVD-FLKDYLKKSGLKSLVLGISGGQDST----LAGRLAQL---AVEE-----LRAETGDDDYQ--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 408 eF-ANRIVFTVymgsenssaQTLNRAAQLASQ-IGASHmDLKIDkIVSALVSLFTSLtgkvprykVDGGSTAENLALQNL 485
Cdd:PRK00768 76 -FiAVRLPYGV---------QADEDDAQDALAfIQPDR-VLTVN-IKPAVDASVAAL--------EAAGIELSDFVKGNI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 486 QARIRMVIAYMLASLlpwVKGkrgffLVLGSANVDEGLRGYLTKYDCSSADLNPIGGISKQDLRSFLRwcanNLHYPilA 565
Cdd:PRK00768 136 KARERMIAQYAIAGA---TGG-----LVVGTDHAAEAVTGFFTKFGDGGADILPLFGLNKRQGRALLA----ALGAP--E 201
|
250 260 270
....*....|....*....|....*....|...
gi 302788997 566 EVVSAPPTAELEPIREnySQTDEEDMGMTYEEL 598
Cdd:PRK00768 202 HLYEKVPTADLEDDRP--GLPDEVALGVTYDQI 232
|
|
| nitrilase |
cd07197 |
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ... |
15-288 |
3.43e-10 |
|
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes; This superfamily (also known as the C-N hydrolase superfamily) contains hydrolases that break carbon-nitrogen bonds; it includes nitrilases, cyanide dihydratases, aliphatic amidases, N-terminal amidases, beta-ureidopropionases, biotinidases, pantotheinase, N-carbamyl-D-amino acid amidohydrolases, the glutaminase domain of glutamine-dependent NAD+ synthetase, apolipoprotein N-acyltransferases, and N-carbamoylputrescine amidohydrolases, among others. These enzymes depend on a Glu-Lys-Cys catalytic triad, and work through a thiol acylenzyme intermediate. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. These oligomers include dimers, tetramers, hexamers, octamers, tetradecamers, octadecamers, as well as variable length helical arrangements and homo-oligomeric spirals. These proteins have roles in vitamin and co-enzyme metabolism, in detoxifying small molecules, in the synthesis of signaling molecules, and in the post-translational modification of proteins. They are used industrially, as biocatalysts in the fine chemical and pharmaceutical industry, in cyanide remediation, and in the treatment of toxic effluent. This superfamily has been classified previously in the literature, based on global and structure-based sequence analysis, into thirteen different enzyme classes (referred to as 1-13). This hierarchy includes those thirteen classes and a few additional subfamilies. A putative distant relative, the plasmid-borne TraB family, has not been included in the hierarchy.
Pssm-ID: 143587 [Multi-domain] Cd Length: 253 Bit Score: 61.19 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 15 AMDFEGNLGRINESIRQARAAGSMLRVGPELEITGYGCDDhfLENDTSAHAW---ECLAEILSSDLTYGIVCDIGMPVVS 91
Cdd:cd07197 10 IGDVEANLAKALRLIKEAAEQGADLIVLPELFLTGYSFES--AKEDLDLAEEldgPTLEALAELAKELGIYIVAGIAEKD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 92 DGVRYN-CRVFCLDGKILLIRPKKFLANDGnyrELRWFAAwqhhnsvieyklpeiiwsktsqktvtfGDAYVSFlDTA-- 168
Cdd:cd07197 88 GDKLYNtAVVIDPDGEIIGKYRKIHLFDFG---ERRYFSP---------------------------GDEFPVF-DTPgg 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 169 -VAVETCEELFTPSSPHIgLALNGVEIIVNGSGSHHQlRKLNTRIELMQGATHKagGVYL-YANQQGCDGaRLYYDGCAT 246
Cdd:cd07197 137 kIGLLICYDLRFPELARE-LALKGADIILVPAAWPTA-RREHWELLLRARAIEN--GVYVvAANRVGEEG-GLEFAGGSM 211
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 302788997 247 VFV-NGDMVVQGSqfslADVEVLTACVDLDAVSTFRGSISSLR 288
Cdd:cd07197 212 IVDpDGEVLAEAS----EEEGILVAELDLDELREARKRWSYLR 250
|
|
| nitrilase_2 |
cd07580 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
5-195 |
3.76e-05 |
|
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.
Pssm-ID: 143604 Cd Length: 268 Bit Score: 46.19 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 5 KVSTCSLNQWAMDFEGNLGRINESIRQARAAGSMLRVGPELEITGYGCDDhflENDTSAHAwECLAEILSSDLTYGIVCD 84
Cdd:cd07580 1 RVACVQFDPRVGDLDANLARSIELIREAADAGANLVVLPELANTGYVFES---RDEAFALA-EEVPDGASTRAWAELAAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 85 IGMPVVS-----DGVR-YNCRVFCLDGKILLIRPKKFLANDgnyrELRWFAAwqhhnsvieyklpeiiwsktsqktvtfG 158
Cdd:cd07580 77 LGLYIVAgfaerDGDRlYNSAVLVGPDGVIGTYRKAHLWNE----EKLLFEP---------------------------G 125
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 302788997 159 DAYVSFLDTA---VAVETCEELFTPSSPHIgLALNGVEII 195
Cdd:cd07580 126 DLGLPVFDTPfgrIGVAICYDGWFPETFRL-LALQGADIV 164
|
|
| R-amidase_like |
cd07576 |
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ... |
15-116 |
2.77e-04 |
|
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); Pseudomonas sp. MCI3434 R-amidase hydrolyzes (R,S)-piperazine-2-tert-butylcarboxamide to form (R)-piperazine-2-carboxylic acid. It does so with strict R-stereoselectively. Its preferred substrates are carboxamide compounds which have the amino or imino group connected to their beta- or gamma-carbon. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), class 13 represents proteins that at the time were difficult to place in a distinct similarity group. It has been suggested that this subgroup represents a new class. Members of the nitrilase superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Native R-amidase however appears to be a monomer.
Pssm-ID: 143600 Cd Length: 254 Bit Score: 43.34 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 15 AMDFEGNLGRINESIRQARAAGSMLRVGPELEITGYGCDDhflendtsAHAWecLAEILSSDL---------TYGIVCDI 85
Cdd:cd07576 11 DGDVAANLARLDEAAARAAAAGADLLVFPELFLTGYNIGD--------AVAR--LAEPADGPAlqalraiarRHGIAIVV 80
|
90 100 110
....*....|....*....|....*....|..
gi 302788997 86 GMPVVSDGVRYN-CRVFCLDGKILLIRPKKFL 116
Cdd:cd07576 81 GYPERAGGAVYNaAVLIDEDGTVLANYRKTHL 112
|
|
| nitrilase_7 |
cd07585 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
17-282 |
1.11e-03 |
|
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.
Pssm-ID: 143609 Cd Length: 261 Bit Score: 41.53 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 17 DFEGNLGRINESIRQARAAGSMLRVGPELEITGYGCDDHF---LENDTSAhAWECLAEILSSdltYGIVCDIGMPVVSDG 93
Cdd:cd07585 13 DKARNLAVIARWTRKAAAQGAELVCFPEMCITGYTHVRALsreAEVPDGP-STQALSDLARR---YGLTILAGLIEKAGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 94 VRYNCRVFCL-DGKIllirpkkflandGNYRELRWFAAWQHHnsvieyklpeiiwsktsqktVTFGDAYVSF--LDTAVA 170
Cdd:cd07585 89 RPYNTYLVCLpDGLV------------HRYRKLHLFRREHPY--------------------IAAGDEYPVFatPGVRFG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302788997 171 VETCEELFTPSSPHIgLALNGVEII-------VNGSGSHHQ--LRKLntrielmqGATHKAGGVYLYA-NQQGCDGARLy 240
Cdd:cd07585 137 ILICYDNHFPENVRA-TALLGAEILfaphatpGTTSPKGREwwMRWL--------PARAYDNGVFVAAcNGVGRDGGEV- 206
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 302788997 241 YDGCATVF-VNGDMVVQgsQFSLADvEVLTACVDLDAVSTFRG 282
Cdd:cd07585 207 FPGGAMILdPYGRVLAE--TTSGGD-GMVVADLDLDLINTVRG 246
|
|
| |
