|
Name |
Accession |
Description |
Interval |
E-value |
| nadE |
PRK02628 |
NAD synthetase; Reviewed |
5-670 |
0e+00 |
|
NAD synthetase; Reviewed
Pssm-ID: 235057 [Multi-domain] Cd Length: 679 Bit Score: 1143.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 5 PSFFNLYRHNFARIAVAVPRAHVADPASNARETIALMREADADHAAVTLFPELGLSAYSCDDLFHQRALLDASLAALNDV 84
Cdd:PRK02628 2 MDFFSIYRHGFVRVAAATPKVRVADPAFNAARILALARRAADDGVALAVFPELSLSGYSCDDLFLQDTLLDAVEDALATL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 85 VAASRDIGSIVVVGLPLEIDALLFNCAAVVHRGAIIGVVPKTYLPNYREFYEPRQFARGDRLLRDSISLLGQsDVPCGNA 164
Cdd:PRK02628 82 VEASADLDPLLVVGAPLRVRHRLYNCAVVIHRGRILGVVPKSYLPNYREFYEKRWFAPGDGARGETIRLCGQ-EVPFGTD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 165 LLFRFGQQPLLTFHIEICEDLWVPVPPSSFAALAGATVLLNLSASNVTVGKADFRRELVGGQSARCLAAYAYSAAGYGES 244
Cdd:PRK02628 161 LLFEAEDLPGFVFGVEICEDLWVPIPPSSYAALAGATVLANLSASNITVGKADYRRLLVASQSARCLAAYVYAAAGVGES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 245 TTDLAWDGHGVIYENGNALAETRRFLDAPQCIFADVDLDRLISERMRQTTFGDTAhAHRDACARFRTVTVPAVLPTTiRL 324
Cdd:PRK02628 241 TTDLAWDGQTLIYENGELLAESERFPREEQLIVADVDLERLRQERLRNGSFDDNA-RHRDESAPFRTIPFALDPPAG-DL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 325 PLARKYERFPYVPSDPARRDERCREIYDIQVQGLVTRMRAARASRLVIGVSGGLDSTQALLVCMHAVQALQLPTTAVIGC 404
Cdd:PRK02628 319 GLRRPVERFPFVPSDPARLDQRCYEAYNIQVSGLAQRLRATGLKKVVIGISGGLDSTHALLVAAKAMDRLGLPRKNILAY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 405 IMPGFGTSERTLDQARRLVAALGCEAREIDIRPSCLRMLEDIGHPYANGEPVHDITFENVQAGERTSHLFRMANQSGALV 484
Cdd:PRK02628 399 TMPGFATTDRTKNNAVALMKALGVTAREIDIRPAALQMLKDIGHPFARGEPVYDVTFENVQAGERTQILFRLANQHGGIV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 485 VGTGDLSELALGWCTYGVGDQMSHYGVNASVPKTLIQYLIRRSAQAGPFSAQASAVLLDVLDTEISPELIPAGEAGG-VQ 563
Cdd:PRK02628 479 IGTGDLSELALGWCTYGVGDHMSHYNVNASVPKTLIQHLIRWVIASGQFDEAVSEVLLDILDTEISPELVPADKEGEiVQ 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 564 RTEDTVGPYELQDFNLYYVLRFGYRPSKVAFLAWTAWHDAASGAWPDLPPEKQHGYEIGTIRQWLGVFLQRFFgGQQFKR 643
Cdd:PRK02628 559 STEDIIGPYELQDFFLYYFLRYGFRPSKIAFLAWHAWKDAERGAWPGFPEDKRPAYDLATIKKWLEVFLRRFF-SSQFKR 637
|
650 660
....*....|....*....|....*..
gi 1331740938 644 SCLPNGPKVGSGGSLSPRGDYRAPSDS 670
Cdd:PRK02628 638 SALPNGPKVGSGGSLSPRGDWRAPSDA 664
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
61-670 |
6.72e-119 |
|
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: 366.48 E-value: 6.72e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 61 AYSCDDLFHQRALLDASLAALNDVVAASRDIGSIVVVGLPLEIDALLFNCAAVVHRGAIIGVVPKTYLPNYREFYEPRQF 140
Cdd:COG0171 2 LLLLALLLLAAALLDAAAAAAAALAALAAAAAALLLLLLLLLLLLLLLLALLLLLAAARLLVAAAALLLLALAAGGGAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 141 ARGDRLLRDSISLLGQSDVPCGNaLLFRFGQQPLLTFHIEICEDLWVPVPPSSFAALAGATVLLNLSASNVTVGKADFRR 220
Cdd:COG0171 82 AGGGGGAGGGLLNGAALVLGGGD-LLFFADDFLLLLLVVEEEEEEFVGGPPPPPAALGGAGVLLILSSSSSAVGAAAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 221 ELVGGQSARCLAAYAYSAAGYGESTTDLAWDGHGVIYENGNALAETRRFLDAPQCIFADVDLDRLISERMRQTTFGDTAH 300
Cdd:COG0171 161 ALAAALLSSLSSAAYYAAAGGGESTTDLARGGGGGLLLVVLLLVGGGDDDFFDGGSAAVDDDDLLLLLRRRREEELLLAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 301 AHRDACARFRTVTVPavlpttirlplarkyerfpyvPSDPARRDERCREIYDIQVQGLVTRMRAARASRLVIGVSGGLDS 380
Cdd:COG0171 241 ARDADGGRRVAAEAA---------------------PPPPEEEEMDLEEVYDALVLGLRDYVRKNGFKGVVLGLSGGIDS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 381 TQALLVCmhaVQALqlPTTAVIGCIMPGFGTSERTLDQARRLVAALGCEAREIDIRPSCLRMLEDIGHPYanGEPVHDIT 460
Cdd:COG0171 300 ALVAALA---VDAL--GPENVLGVTMPSRYTSDESLEDAEELAENLGIEYEEIDITPAVEAFLEALPHAF--GGELDDVA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 461 FENVQAGERTSHLFRMANQSGALVVGTGDLSELALGWCTYGvGDQMSHYGVNASVPKTLIQYLIRRSAQAGPfsaqasAV 540
Cdd:COG0171 373 EENLQARIRMVILMALANKFGGLVLGTGNKSELAVGYFTKY-GDGAGDLAPIADLYKTQVYALARWLNRNGE------VI 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 541 LLDVLDTEISPELIPAgeaggvQRTEDTVGPYELQDFNLYYVLRFGYRPSKVAflawtawhdaasgawpdlppekQHGYE 620
Cdd:COG0171 446 PEDIIDKPPSAELRPG------QTDEDELGPYEVLDAILYAYVEEGLSPEEIA----------------------AAGYD 497
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1331740938 621 igtiRQWLGVFLQRFFgGQQFKRSCLPNGPKVGSgGSLSPrgDYRAPSDS 670
Cdd:COG0171 498 ----REWVERVLRLVR-RNEYKRRQPPPGPKVSS-RAFGR--GRRYPIDS 539
|
|
| GAT_Gln-NAD-synth |
cd07570 |
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ... |
17-297 |
6.73e-87 |
|
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: 273.19 E-value: 6.73e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 17 RIAVAVPRAHVADPASNARETIALMREADADHAAVTLFPELGLSAYSCDDLFHQRALLDASLAALNDVVAASRDIGSIVV 96
Cdd:cd07570 1 RIALAQLNPTVGDLEGNAEKILEAIREAKAQGADLVVFPELSLTGYPPEDLLLRPDFLEAAEEALEELAAATADLDIAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 97 VGLPLEIDALLFNCAAVVHRGAIIGVVPKTYLPNYREFYEPRQFARGDRLlrdsisllgqsdvpcgnALLFRFGqqplLT 176
Cdd:cd07570 81 VGLPLRHDGKLYNAAAVLQNGKILGVVPKQLLPNYGVFDEKRYFTPGDKP-----------------DVLFFKG----LR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 177 FHIEICEDLWVPVPPSSFAALAGATVLLNLSASNVTVGKADFRRELVGGQSARCLaaYAYSAAGYGESTTDLAWDGHGVI 256
Cdd:cd07570 140 IGVEICEDLWVPDPPSAELALAGADLILNLSASPFHLGKQDYRRELVSSRSARTG--LPYVYVNQVGGQDDLVFDGGSFI 217
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1331740938 257 YEN-GNALAETRRFldapQCIFADVDLDRLISERMRQTTFGD 297
Cdd:cd07570 218 ADNdGELLAEAPRF----EEDLADVDLDRLRSERRRNSSFLD 255
|
|
| NAD_synthase |
pfam02540 |
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ... |
367-547 |
8.08e-19 |
|
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: 86.28 E-value: 8.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 367 ASRLVIGVSGGLDSTQALLVCMHAVQALQlpttaVIGCIMPGFGTSERTLDQARRLVAALGCEAREIDIRPSCLRMLEDI 446
Cdd:pfam02540 18 FKGVVLGLSGGIDSSLVAYLAVKALGKEN-----VLALIMPSSQSSEEDVQDALALAENLGIEYKTIDIKPIVRAFSQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 447 GHpyaNGEpvhDITFENVQAGERTSHLFRMANQSGALVVGTGDLSELALGWCT-YGVG--DQMSHYGVNASVPKTLIQYL 523
Cdd:pfam02540 93 QD---ASE---DFAKGNLKARIRMAILYYIANKFNYLVLGTGNKSELAVGYFTkYGDGacDIAPIGDLYKTQVYELARYL 166
|
170 180 190
....*....|....*....|....*....|....
gi 1331740938 524 ------IRRSAQAGPFSAQASAVLL----DVLDT 547
Cdd:pfam02540 167 nvperiIKKPPSADLWPGQTDEEELgipyDELDD 200
|
|
| nadE |
TIGR00552 |
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ... |
367-547 |
5.06e-14 |
|
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: 72.42 E-value: 5.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 367 ASRLVIGVSGGLDStqaLLVCMHAVQALqlPTTAVIGCIMPGFGTSERTLDQARRLVAALGCEAREIDIRPSclrMLEDI 446
Cdd:TIGR00552 22 AKGVVLGLSGGIDS---AVVAALCVEAL--GEQNHALLLPHSVQTPEQDVQDALALAEPLGINYKNIDIAPI---AASFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 447 GHPYANGEPVHDITFENVQAGERTSHLFRMANQSGALVVGTGDLSELALGWCT-YGVG--DQMSHYGVNASVPKTLIQYL 523
Cdd:TIGR00552 94 AQTETGDELSDFLAKGNLKARLRMAALYAIANKHNLLVLGTGNKSELMLGYFTkYGDGgcDIAPIGDLFKTQVYELAKRL 173
|
170 180 190
....*....|....*....|....*....|....
gi 1331740938 524 ------IRRSAQAGPFSAQASAVLL----DVLDT 547
Cdd:TIGR00552 174 nvperiIEKPPTADLFDGQTDETELgityDELDD 207
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| nadE |
PRK02628 |
NAD synthetase; Reviewed |
5-670 |
0e+00 |
|
NAD synthetase; Reviewed
Pssm-ID: 235057 [Multi-domain] Cd Length: 679 Bit Score: 1143.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 5 PSFFNLYRHNFARIAVAVPRAHVADPASNARETIALMREADADHAAVTLFPELGLSAYSCDDLFHQRALLDASLAALNDV 84
Cdd:PRK02628 2 MDFFSIYRHGFVRVAAATPKVRVADPAFNAARILALARRAADDGVALAVFPELSLSGYSCDDLFLQDTLLDAVEDALATL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 85 VAASRDIGSIVVVGLPLEIDALLFNCAAVVHRGAIIGVVPKTYLPNYREFYEPRQFARGDRLLRDSISLLGQsDVPCGNA 164
Cdd:PRK02628 82 VEASADLDPLLVVGAPLRVRHRLYNCAVVIHRGRILGVVPKSYLPNYREFYEKRWFAPGDGARGETIRLCGQ-EVPFGTD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 165 LLFRFGQQPLLTFHIEICEDLWVPVPPSSFAALAGATVLLNLSASNVTVGKADFRRELVGGQSARCLAAYAYSAAGYGES 244
Cdd:PRK02628 161 LLFEAEDLPGFVFGVEICEDLWVPIPPSSYAALAGATVLANLSASNITVGKADYRRLLVASQSARCLAAYVYAAAGVGES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 245 TTDLAWDGHGVIYENGNALAETRRFLDAPQCIFADVDLDRLISERMRQTTFGDTAhAHRDACARFRTVTVPAVLPTTiRL 324
Cdd:PRK02628 241 TTDLAWDGQTLIYENGELLAESERFPREEQLIVADVDLERLRQERLRNGSFDDNA-RHRDESAPFRTIPFALDPPAG-DL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 325 PLARKYERFPYVPSDPARRDERCREIYDIQVQGLVTRMRAARASRLVIGVSGGLDSTQALLVCMHAVQALQLPTTAVIGC 404
Cdd:PRK02628 319 GLRRPVERFPFVPSDPARLDQRCYEAYNIQVSGLAQRLRATGLKKVVIGISGGLDSTHALLVAAKAMDRLGLPRKNILAY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 405 IMPGFGTSERTLDQARRLVAALGCEAREIDIRPSCLRMLEDIGHPYANGEPVHDITFENVQAGERTSHLFRMANQSGALV 484
Cdd:PRK02628 399 TMPGFATTDRTKNNAVALMKALGVTAREIDIRPAALQMLKDIGHPFARGEPVYDVTFENVQAGERTQILFRLANQHGGIV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 485 VGTGDLSELALGWCTYGVGDQMSHYGVNASVPKTLIQYLIRRSAQAGPFSAQASAVLLDVLDTEISPELIPAGEAGG-VQ 563
Cdd:PRK02628 479 IGTGDLSELALGWCTYGVGDHMSHYNVNASVPKTLIQHLIRWVIASGQFDEAVSEVLLDILDTEISPELVPADKEGEiVQ 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 564 RTEDTVGPYELQDFNLYYVLRFGYRPSKVAFLAWTAWHDAASGAWPDLPPEKQHGYEIGTIRQWLGVFLQRFFgGQQFKR 643
Cdd:PRK02628 559 STEDIIGPYELQDFFLYYFLRYGFRPSKIAFLAWHAWKDAERGAWPGFPEDKRPAYDLATIKKWLEVFLRRFF-SSQFKR 637
|
650 660
....*....|....*....|....*..
gi 1331740938 644 SCLPNGPKVGSGGSLSPRGDYRAPSDS 670
Cdd:PRK02628 638 SALPNGPKVGSGGSLSPRGDWRAPSDA 664
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
61-670 |
6.72e-119 |
|
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: 366.48 E-value: 6.72e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 61 AYSCDDLFHQRALLDASLAALNDVVAASRDIGSIVVVGLPLEIDALLFNCAAVVHRGAIIGVVPKTYLPNYREFYEPRQF 140
Cdd:COG0171 2 LLLLALLLLAAALLDAAAAAAAALAALAAAAAALLLLLLLLLLLLLLLLALLLLLAAARLLVAAAALLLLALAAGGGAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 141 ARGDRLLRDSISLLGQSDVPCGNaLLFRFGQQPLLTFHIEICEDLWVPVPPSSFAALAGATVLLNLSASNVTVGKADFRR 220
Cdd:COG0171 82 AGGGGGAGGGLLNGAALVLGGGD-LLFFADDFLLLLLVVEEEEEEFVGGPPPPPAALGGAGVLLILSSSSSAVGAAAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 221 ELVGGQSARCLAAYAYSAAGYGESTTDLAWDGHGVIYENGNALAETRRFLDAPQCIFADVDLDRLISERMRQTTFGDTAH 300
Cdd:COG0171 161 ALAAALLSSLSSAAYYAAAGGGESTTDLARGGGGGLLLVVLLLVGGGDDDFFDGGSAAVDDDDLLLLLRRRREEELLLAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 301 AHRDACARFRTVTVPavlpttirlplarkyerfpyvPSDPARRDERCREIYDIQVQGLVTRMRAARASRLVIGVSGGLDS 380
Cdd:COG0171 241 ARDADGGRRVAAEAA---------------------PPPPEEEEMDLEEVYDALVLGLRDYVRKNGFKGVVLGLSGGIDS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 381 TQALLVCmhaVQALqlPTTAVIGCIMPGFGTSERTLDQARRLVAALGCEAREIDIRPSCLRMLEDIGHPYanGEPVHDIT 460
Cdd:COG0171 300 ALVAALA---VDAL--GPENVLGVTMPSRYTSDESLEDAEELAENLGIEYEEIDITPAVEAFLEALPHAF--GGELDDVA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 461 FENVQAGERTSHLFRMANQSGALVVGTGDLSELALGWCTYGvGDQMSHYGVNASVPKTLIQYLIRRSAQAGPfsaqasAV 540
Cdd:COG0171 373 EENLQARIRMVILMALANKFGGLVLGTGNKSELAVGYFTKY-GDGAGDLAPIADLYKTQVYALARWLNRNGE------VI 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 541 LLDVLDTEISPELIPAgeaggvQRTEDTVGPYELQDFNLYYVLRFGYRPSKVAflawtawhdaasgawpdlppekQHGYE 620
Cdd:COG0171 446 PEDIIDKPPSAELRPG------QTDEDELGPYEVLDAILYAYVEEGLSPEEIA----------------------AAGYD 497
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1331740938 621 igtiRQWLGVFLQRFFgGQQFKRSCLPNGPKVGSgGSLSPrgDYRAPSDS 670
Cdd:COG0171 498 ----REWVERVLRLVR-RNEYKRRQPPPGPKVSS-RAFGR--GRRYPIDS 539
|
|
| GAT_Gln-NAD-synth |
cd07570 |
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ... |
17-297 |
6.73e-87 |
|
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: 273.19 E-value: 6.73e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 17 RIAVAVPRAHVADPASNARETIALMREADADHAAVTLFPELGLSAYSCDDLFHQRALLDASLAALNDVVAASRDIGSIVV 96
Cdd:cd07570 1 RIALAQLNPTVGDLEGNAEKILEAIREAKAQGADLVVFPELSLTGYPPEDLLLRPDFLEAAEEALEELAAATADLDIAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 97 VGLPLEIDALLFNCAAVVHRGAIIGVVPKTYLPNYREFYEPRQFARGDRLlrdsisllgqsdvpcgnALLFRFGqqplLT 176
Cdd:cd07570 81 VGLPLRHDGKLYNAAAVLQNGKILGVVPKQLLPNYGVFDEKRYFTPGDKP-----------------DVLFFKG----LR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 177 FHIEICEDLWVPVPPSSFAALAGATVLLNLSASNVTVGKADFRRELVGGQSARCLaaYAYSAAGYGESTTDLAWDGHGVI 256
Cdd:cd07570 140 IGVEICEDLWVPDPPSAELALAGADLILNLSASPFHLGKQDYRRELVSSRSARTG--LPYVYVNQVGGQDDLVFDGGSFI 217
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1331740938 257 YEN-GNALAETRRFldapQCIFADVDLDRLISERMRQTTFGD 297
Cdd:cd07570 218 ADNdGELLAEAPRF----EEDLADVDLDRLRSERRRNSSFLD 255
|
|
| NAD_synthase |
cd00553 |
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ... |
345-589 |
8.81e-61 |
|
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: 203.94 E-value: 8.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 345 ERCREIYDIQVQGLVTRMRAARASRLVIGVSGGLDSTQALLVCMHAVQALQlpttaVIGCIMPGFGTSERTLDQARRLVA 424
Cdd:cd00553 1 IDPEEIIEALVCFLRDYLRKSGAKGFVLGLSGGIDSAVVAALAVRALGAEN-----VLALIMPSRYSSKETRDDAKALAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 425 ALGCEAREIDIRPSCLRMLEDIGHpyANGEPVHDITFENVQAGERTSHLFRMANQSGALVVGTGDLSELALGWCTYGvGD 504
Cdd:cd00553 76 NLGIEYRTIDIDPIVDAFLKALEH--AGGSEAEDLALGNIQARLRMVLLYALANLLGGLVLGTGNKSELLLGYFTKY-GD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 505 QMSHYGVNASVPKTLIQYLirrsaqagpfsAQASAVLLDVLDTEISPELIPAgeaggvQRTEDTVG-PYELQDFNLYYVL 583
Cdd:cd00553 153 GAADINPIGDLYKTQVREL-----------ARYLGVPEEIIEKPPSAELWPG------QTDEDELGmPYEELDLILYGLV 215
|
....*.
gi 1331740938 584 RFGYRP 589
Cdd:cd00553 216 DGKLGP 221
|
|
| PRK13981 |
PRK13981 |
NAD synthetase; Provisional |
17-519 |
1.93e-46 |
|
NAD synthetase; Provisional
Pssm-ID: 237577 [Multi-domain] Cd Length: 540 Bit Score: 173.03 E-value: 1.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 17 RIAVAVPRAHVADPASNARETIALMREADADHAAVTLFPELGLSAYSCDDL-----FHQRALLDAslaalNDVVAASRDi 91
Cdd:PRK13981 2 RIALAQLNPTVGDIAGNAAKILAAAAEAADAGADLLLFPELFLSGYPPEDLllrpaFLAACEAAL-----ERLAAATAG- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 92 GSIVVVGLPLEIDALLFNCAAVVHRGAIIGVVPKTYLPNYREFYEPRQFARGdrllrdsisllgqsDVPCgnalLFRFGQ 171
Cdd:PRK13981 76 GPAVLVGHPWREGGKLYNAAALLDGGEVLATYRKQDLPNYGVFDEKRYFAPG--------------PEPG----VVELKG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 172 qplLTFHIEICEDLWVPVPPSSFAAlAGATVLLNLSASNVTVGKADFRRELVGGQSARclaayaysaagygestTDLAwd 251
Cdd:PRK13981 138 ---VRIGVPICEDIWNPEPAETLAE-AGAELLLVPNASPYHRGKPDLREAVLRARVRE----------------TGLP-- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 252 ghgVIYEN-----------GNALAetrrfldapqcifadVDLDRLISERMRQttFgDTAHAHRDacarfrtvtvpavlpt 320
Cdd:PRK13981 196 ---LVYLNqvggqdelvfdGASFV---------------LNADGELAARLPA--F-EEQIAVVD---------------- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 321 tirlpLARKYERFPYVPSDPARRDERCREIYDIQVQGLVTRMRAARASRLVIGVSGGLDStqALLVCMhAVQALQlpTTA 400
Cdd:PRK13981 239 -----FDRGEDGWRPLPGPIAPPPEGEAEDYRALVLGLRDYVRKNGFPGVVLGLSGGIDS--ALVAAI-AVDALG--AER 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 401 VIGCIMPGFGTSERTLDQARRLVAALGCEAREIDIRP---SCLRMLEDIghpYANGEPvhDITFENVQAGERTSHLFRMA 477
Cdd:PRK13981 309 VRAVMMPSRYTSEESLDDAAALAKNLGVRYDIIPIEPafeAFEAALAPL---FAGTEP--DITEENLQSRIRGTLLMALS 383
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1331740938 478 NQSGALVVGTGDLSELALGWCT-YgvGDQMSHYGVNASVPKTL 519
Cdd:PRK13981 384 NKFGSLVLTTGNKSEMAVGYATlY--GDMAGGFAPIKDVYKTL 424
|
|
| Nit2 |
COG0388 |
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]; |
17-297 |
2.54e-42 |
|
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
Pssm-ID: 440157 [Multi-domain] Cd Length: 264 Bit Score: 154.25 E-value: 2.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 17 RIAVAVPRAHVADPASNARETIALMREADADHAAVTLFPELGLSAYSCDDLFHQRALLDASLAALNDVVAASRDIGSIVV 96
Cdd:COG0388 3 RIALAQLNPTVGDIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDGPALAALAELARELGIAVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 97 VGLPLEI-DALLFNCAAVVHR-GAIIGVVPKTYLPNYREFYEPRQFARGDRLlrdsisllgqsdvpcgnaLLFRFgqqPL 174
Cdd:COG0388 83 VGLPERDeGGRLYNTALVIDPdGEILGRYRKIHLPNYGVFDEKRYFTPGDEL------------------VVFDT---DG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 175 LTFHIEICEDLWVPVPPSSfAALAGATVLLNLSASNVTVGKADFRRELvggqSARCLaayaysaagygE----------- 243
Cdd:COG0388 142 GRIGVLICYDLWFPELARA-LALAGADLLLVPSASPFGRGKDHWELLL----RARAI-----------Engcyvvaanqv 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1331740938 244 -STTDLAWDGHGVIYE-NGNALAETRrflDAPQCIFADVDLDRLISERMRQTTFGD 297
Cdd:COG0388 206 gGEDGLVFDGGSMIVDpDGEVLAEAG---DEEGLLVADIDLDRLREARRRFPVLRD 258
|
|
| PLN02339 |
PLN02339 |
NAD+ synthase (glutamine-hydrolysing) |
33-447 |
2.46e-23 |
|
NAD+ synthase (glutamine-hydrolysing)
Pssm-ID: 177973 [Multi-domain] Cd Length: 700 Bit Score: 105.15 E-value: 2.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 33 NARETIALMREADADHAAVTLFPELGLSAYSCDDLFHQRALLDASLAALNDVVAASRDIGSIVVVGLPLEIDALLFNCAA 112
Cdd:PLN02339 21 NLKRIKESIAEAKAAGAVYRVGPELEITGYGCEDHFLELDTVTHSWECLAEILVGDLTDGILCDIGMPVIHGGVRYNCRV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 113 VVHRGAIIGVVPKTYLP---NYREF--YEPRQFARG--DRLLRDSIS-LLGQSDVPCGNALLfRFGQQPLLTfhiEICED 184
Cdd:PLN02339 101 FCLNRKILLIRPKMWLAndgNYRELrwFTAWKHKKKveDFQLPEEIAeATSQKSVPFGDGYL-QFLDTAVAA---ETCEE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 185 LWVPVPPSSFAALAGATVLLNLSASNVTVGKADFRRELVGGQSARClaayAYSAAGYGESTTD---LAWDGHGVIYENGN 261
Cdd:PLN02339 177 LFTPQAPHIDLALNGVEIISNGSGSHHQLRKLNTRLDLIRSATHKC----GGVYLYANQRGCDggrLYYDGCACIVVNGE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 262 ALAETRRF-LDAPQCIFADVDLDRLISERMRQTTFGDTAHAHRdacaRFRTVTVPAVL--PTTIRLPLARKYERFPYVPS 338
Cdd:PLN02339 253 VVAQGSQFsLQDVEVVTACVDLDAVVSFRGSISSFREQASSKK----RVPSVAVPFKLcpPFSLSLVPSSPLKIRYHSPE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 339 D-----PArrderCreiydiqvqGLVTRMRAARASRLVIGVSGGLDS--TQALLVCMhavqaLQLPTTAV---------- 401
Cdd:PLN02339 329 EeialgPA-----C---------WLWDYLRRSGASGFLLPLSGGADSssVAAIVGSM-----CQLVVKAIregdeqvkad 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1331740938 402 ---IGCIMPG-FGTSERTLdqARRLVAA--LGCEAREIDIRPSCLRMLEDIG 447
Cdd:PLN02339 390 arrIGNYADGeVPTDSKEF--AKRIFYTvyMGSENSSEETRSRAKQLADEIG 439
|
|
| PRK13980 |
PRK13980 |
NAD synthetase; Provisional |
363-501 |
2.39e-21 |
|
NAD synthetase; Provisional
Pssm-ID: 184435 [Multi-domain] Cd Length: 265 Bit Score: 94.12 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 363 RAARASRLVIGVSGGLDSTqalLVCMHAVQALqlPTTAVIGCIMPGFGTSERTLDQARRLVAALGCEAREIDIRPsclrm 442
Cdd:PRK13980 26 EKAGAKGVVLGLSGGIDSA---VVAYLAVKAL--GKENVLALLMPSSVSPPEDLEDAELVAEDLGIEYKVIEITP----- 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331740938 443 ledIGHPYANGEPVHD-ITFENVQAGERTSHLFRMANQSGALVVGTGDLSELALGWCT-YG 501
Cdd:PRK13980 96 ---IVDAFFSAIPDADrLRVGNIMARTRMVLLYDYANRENRLVLGTGNKSELLLGYFTkYG 153
|
|
| NAD_synthase |
pfam02540 |
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ... |
367-547 |
8.08e-19 |
|
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: 86.28 E-value: 8.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 367 ASRLVIGVSGGLDSTQALLVCMHAVQALQlpttaVIGCIMPGFGTSERTLDQARRLVAALGCEAREIDIRPSCLRMLEDI 446
Cdd:pfam02540 18 FKGVVLGLSGGIDSSLVAYLAVKALGKEN-----VLALIMPSSQSSEEDVQDALALAENLGIEYKTIDIKPIVRAFSQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 447 GHpyaNGEpvhDITFENVQAGERTSHLFRMANQSGALVVGTGDLSELALGWCT-YGVG--DQMSHYGVNASVPKTLIQYL 523
Cdd:pfam02540 93 QD---ASE---DFAKGNLKARIRMAILYYIANKFNYLVLGTGNKSELAVGYFTkYGDGacDIAPIGDLYKTQVYELARYL 166
|
170 180 190
....*....|....*....|....*....|....
gi 1331740938 524 ------IRRSAQAGPFSAQASAVLL----DVLDT 547
Cdd:pfam02540 167 nvperiIKKPPSADLWPGQTDEEELgipyDELDD 200
|
|
| nitrilase |
cd07197 |
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ... |
18-289 |
3.47e-17 |
|
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: 81.60 E-value: 3.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 18 IAVAVPRAHVADPASNARETIALMREADADHAAVTLFPELGLSAYSCDDLFHQRALLDASLAALNDVVAA-SRDIGSIVV 96
Cdd:cd07197 1 IAAVQLAPKIGDVEANLAKALRLIKEAAEQGADLIVLPELFLTGYSFESAKEDLDLAEELDGPTLEALAElAKELGIYIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 97 VGLPLEIDALLFNCAAVVHR-GAIIGVVPKTYLPNyreFYEPRQFARGDRLlrdsisllgqsdvpcgnaLLFRFgqqPLL 175
Cdd:cd07197 81 AGIAEKDGDKLYNTAVVIDPdGEIIGKYRKIHLFD---FGERRYFSPGDEF------------------PVFDT---PGG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 176 TFHIEICEDLWVPvPPSSFAALAGATVLLNLSASnvTVGKADFRRELVggqSARCLaayaysaagygEST---------- 245
Cdd:cd07197 137 KIGLLICYDLRFP-ELARELALKGADIILVPAAW--PTARREHWELLL---RARAI-----------ENGvyvvaanrvg 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1331740938 246 --TDLAWDGHGVIYE-NGNALAETRRFldaPQCIFADVDLDRLISER 289
Cdd:cd07197 200 eeGGLEFAGGSMIVDpDGEVLAEASEE---EGILVAELDLDELREAR 243
|
|
| nitrilase_8 |
cd07586 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
17-218 |
5.29e-17 |
|
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: 81.57 E-value: 5.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 17 RIAVAVPRAHVADPASNARETIALMREADADHAAVTLFPELGLSAYSCDDLFhQRALLDASLAALNDVVAASRDIgSIVV 96
Cdd:cd07586 1 RVAIAQIDPVLGDVEENLEKHLEIIETARERGADLVVFPELSLTGYNLGDLV-YEVAMHADDPRLQALAEASGGI-CVVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 97 VGLPLEIDALLFNCAAVVHRGAIIGVVPKTYLPNYREFYEPRQFARGDRLlrdsisllgqsdvpcgNALLFRFGQqpllt 176
Cdd:cd07586 79 GFVEEGRDGRFYNSAAYLEDGRVVHVHRKVYLPTYGLFEEGRYFAPGSHL----------------RAFDTRFGR----- 137
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1331740938 177 FHIEICEDLWVPVPPsSFAALAGATVLLNLSASNVTVGKADF 218
Cdd:cd07586 138 AGVLICEDAWHPSLP-YLLALDGADVIFIPANSPARGVGGDF 178
|
|
| nadE |
TIGR00552 |
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ... |
367-547 |
5.06e-14 |
|
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: 72.42 E-value: 5.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 367 ASRLVIGVSGGLDStqaLLVCMHAVQALqlPTTAVIGCIMPGFGTSERTLDQARRLVAALGCEAREIDIRPSclrMLEDI 446
Cdd:TIGR00552 22 AKGVVLGLSGGIDS---AVVAALCVEAL--GEQNHALLLPHSVQTPEQDVQDALALAEPLGINYKNIDIAPI---AASFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 447 GHPYANGEPVHDITFENVQAGERTSHLFRMANQSGALVVGTGDLSELALGWCT-YGVG--DQMSHYGVNASVPKTLIQYL 523
Cdd:TIGR00552 94 AQTETGDELSDFLAKGNLKARLRMAALYAIANKHNLLVLGTGNKSELMLGYFTkYGDGgcDIAPIGDLFKTQVYELAKRL 173
|
170 180 190
....*....|....*....|....*....|....
gi 1331740938 524 ------IRRSAQAGPFSAQASAVLL----DVLDT 547
Cdd:TIGR00552 174 nvperiIEKPPTADLFDGQTDETELgityDELDD 207
|
|
| nitrilase_2 |
cd07580 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
17-203 |
2.22e-09 |
|
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: 58.90 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 17 RIAVAVPRAHVADPASNARETIALMREADADHAAVTLFPELGLSAYScddlFHQRALLDASLAALND------VVAASRD 90
Cdd:cd07580 1 RVACVQFDPRVGDLDANLARSIELIREAADAGANLVVLPELANTGYV----FESRDEAFALAEEVPDgastraWAELAAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 91 IGSIVVVGLPLEIDALLFNCAAVVHRGAIIGVVPKTYLPNyrefYEPRQFARGDRLLrdsisllgqsdvPCGNALLFRFG 170
Cdd:cd07580 77 LGLYIVAGFAERDGDRLYNSAVLVGPDGVIGTYRKAHLWN----EEKLLFEPGDLGL------------PVFDTPFGRIG 140
|
170 180 190
....*....|....*....|....*....|...
gi 1331740938 171 qqplltfhIEICEDLWVPVPPSSfAALAGATVL 203
Cdd:cd07580 141 --------VAICYDGWFPETFRL-LALQGADIV 164
|
|
| R-amidase_like |
cd07576 |
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ... |
17-146 |
9.94e-07 |
|
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: 50.66 E-value: 9.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 17 RIAVAVPRAHVADPASNARETIALMREADADHAAVTLFPELGLSAYSCDDLfHQRALLDASLAALNDVVAASRDIGSIVV 96
Cdd:cd07576 1 RLALYQGPARDGDVAANLARLDEAAARAAAAGADLLVFPELFLTGYNIGDA-VARLAEPADGPALQALRAIARRHGIAIV 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1331740938 97 VGLPLEIDALLFNCAAVVHR-GAIIGVVPKTYLPnyrEFYEPRQFARGDRL 146
Cdd:cd07576 80 VGYPERAGGAVYNAAVLIDEdGTVLANYRKTHLF---GDSERAAFTPGDRF 127
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|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
328-458 |
4.39e-05 |
|
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis
Pssm-ID: 440136 [Multi-domain] Cd Length: 558 Bit Score: 46.75 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 328 RKYERFPYVPSDPARRDERCREiydiqvqGLVTRMRAARASRLV----IGV--SGGLDSTqaLLVCMhAVQALQLP-TTA 400
Cdd:COG0367 218 RRYWDLEFVPHERSDSEEEAVE-------ELRELLEDAVRRRLRadvpVGAflSGGLDSS--AIAAL-AARLSKGPlKTF 287
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1331740938 401 VIGciMPGFGTSERtlDQARRLVAALGCEAREIDIRPS-CLRMLEDIghPYANGEPVHD 458
Cdd:COG0367 288 SIG--FEDSAYDES--PYARAVAEHLGTEHHEVTVTPEdLLDALPDL--VWHLDEPFAD 340
|
|
| Ph0642_like |
cd07577 |
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ... |
29-148 |
8.39e-05 |
|
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily (putative class 13 nitrilases); Uncharacterized subgroup of the nitrilase superfamily. This superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. Pyrococcus horikoshii Ph0642 is a hypothetical protein belonging to this subgroup. 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 was classified as belonging to class 13, which represents proteins that at the time were difficult to place in a distinct similarity group. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.
Pssm-ID: 143601 Cd Length: 259 Bit Score: 44.98 E-value: 8.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 29 DPASNARETIALMREADADhaaVTLFPELGLSAYscddLFHQRALLDASLAALNDVVAA------SRDIGSIVVVGLPLE 102
Cdd:cd07577 13 EVEKNLKKVESLIKGVEAD---LIVLPELFNTGY----AFTSKEEVASLAESIPDGPTTrflqelARETGAYIVAGLPER 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1331740938 103 IDALLFNCAAVVHRGAIIGVVPKTYLpnyreFY-EPRQFARGDRLLR 148
Cdd:cd07577 86 DGDKFYNSAVVVGPEGYIGIYRKTHL-----FYeEKLFFEPGDTGFR 127
|
|
| PTZ00323 |
PTZ00323 |
NAD+ synthase; Provisional |
371-492 |
8.77e-04 |
|
NAD+ synthase; Provisional
Pssm-ID: 185554 [Multi-domain] Cd Length: 294 Bit Score: 42.07 E-value: 8.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 371 VIGVSGGLDSTQALLVCMHAVQALQLPTTAVIGCIMPgFGTSERTLDQARRLVAALGCEAREID---IRPSCLRMLEDI- 446
Cdd:PTZ00323 50 VTSVSGGIDSAVVLALCARAMRMPNSPIQKNVGLCQP-IHSSAWALNRGRENIQACGATEVTVDqteIHTQLSSLVEKAv 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1331740938 447 ---GHPYANGepvhditfeNVQAGERTSHLFRMA---NQSG--ALVVGTGDLSE 492
Cdd:PTZ00323 129 gikGGAFARG---------QLRSYMRTPVAFYVAqllSQEGtpAVVMGTGNFDE 173
|
|
| nitrilase_7 |
cd07585 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
17-204 |
3.66e-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: 39.61 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 17 RIAVAVPRAHVADPASNARETIALMREADADHAAVTLFPELGLSAYScddlfHQRALLDASLAALNDVVAA----SRDIG 92
Cdd:cd07585 1 RIALVQFEARVGDKARNLAVIARWTRKAAAQGAELVCFPEMCITGYT-----HVRALSREAEVPDGPSTQAlsdlARRYG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 93 SIVVVGLpLEIDA-LLFNCAAVVHRGAIIGVVPKTYLPNYREFYeprqFARGDRLlrdsiSLLGQSDVPCGnallfrfgq 171
Cdd:cd07585 76 LTILAGL-IEKAGdRPYNTYLVCLPDGLVHRYRKLHLFRREHPY----IAAGDEY-----PVFATPGVRFG--------- 136
|
170 180 190
....*....|....*....|....*....|...
gi 1331740938 172 qplltfhIEICEDLWVPvPPSSFAALAGATVLL 204
Cdd:cd07585 137 -------ILICYDNHFP-ENVRATALLGAEILF 161
|
|
| CPA |
cd07573 |
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ... |
28-144 |
4.01e-03 |
|
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known as N-carbamoylputrescine amidase and carbamoylputrescine hydrolase) converts N-carbamoylputrescine to putrescine, a step in polyamine biosynthesis in plants and bacteria. This subgroup includes Arabidopsis thaliana CPA, also known as nitrilase-like 1 (NLP1), and Pseudomonas aeruginosa AguB. 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), this subgroup corresponds to class 11. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer; P. aeruginosa AugB is a homohexamer, Arabidopsis thaliana NLP1 is a homooctomer.
Pssm-ID: 143597 Cd Length: 284 Bit Score: 39.85 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 28 ADPASNARETIALMREADADHAAVTLFPELGLSAYSCD----DLFhQRALLDASLAALNDVVAASRDIGsiVVVGLPL-E 102
Cdd:cd07573 12 EDPEANLAKAEELVREAAAQGAQIVCLQELFETPYFCQeedeDYF-DLAEPPIPGPTTARFQALAKELG--VVIPVSLfE 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1331740938 103 IDA--LLFNCAAVVHR-GAIIGVVPKTYLPNYREFYEPRQFARGD 144
Cdd:cd07573 89 KRGngLYYNSAVVIDAdGSLLGVYRKMHIPDDPGYYEKFYFTPGD 133
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
372-489 |
9.99e-03 |
|
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or synthetase) B is always associated with an N-terminal amidotransferase domain. Family members that contain this domain catalyze the conversion of aspartate to asparagine. Asparagine synthase B catalyzes the synthesis of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase.
Pssm-ID: 467495 [Multi-domain] Cd Length: 224 Bit Score: 38.02 E-value: 9.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331740938 372 IGV--SGGLDSTqALLVCMHAVQALQLPTTAVIGCimPGFGTSERtlDQARRLVAALGCEAREIDI-RPSCLRMLEDIGH 448
Cdd:cd01991 5 VGVllSGGLDSS-LIAALAARLLPETPIDLFTVGF--EGSPTPDR--AAARRVAEELGTEHHEVEVtIEELLDALPDVIL 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1331740938 449 PYANGEPVHDitfenvQAGERTSHLFRMANQSGALVVGTGD 489
Cdd:cd01991 80 IYPTDTPMDL------SIAIPLYFASRLAGKLGAKVVLSGE 114
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