|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02339 |
PLN02339 |
NAD+ synthase (glutamine-hydrolysing) |
3-695 |
0e+00 |
|
NAD+ synthase (glutamine-hydrolysing)
Pssm-ID: 177973 [Multi-domain] Cd Length: 700 Bit Score: 1025.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 3 RKVTVAVSTLNQWALDFEGNMVRILQSILEAKDMGASYRTGPELEVCGYSCEDHFREPDTFLHSWEVLLEVMMSPMCENM 82
Cdd:PLN02339 2 RLLKVATCNLNQWAMDFDGNLKRIKESIAEAKAAGAVYRVGPELEITGYGCEDHFLELDTVTHSWECLAEILVGDLTDGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 83 LVDVGMPVMHRNVAYNCRVAFFNRQILLIRPKMAMCDDGNYRESRWFTAWTKALQTEEYVLPRMIAQHTGQQTVPFGDAV 162
Cdd:PLN02339 82 LCDIGMPVIHGGVRYNCRVFCLNRKILLIRPKMWLANDGNYRELRWFTAWKHKKKVEDFQLPEEIAEATSQKSVPFGDGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 163 IATRDTCLGYEICEELWNVRSKHIEMSLAGVELIVNSSGSYMELRKAHITSDLIRNASFKAGGAYLFSNLRGCDGQRVYF 242
Cdd:PLN02339 162 LQFLDTAVAAETCEELFTPQAPHIDLALNGVEIISNGSGSHHQLRKLNTRLDLIRSATHKCGGVYLYANQRGCDGGRLYY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 243 NGCSAIALNGEILARSQQFALQDVEVTLATIDLEEIRAYRVSLRSRCTAAASAAEYPRIHCDFEMSTHSDIFKTSTPPLN 322
Cdd:PLN02339 242 DGCACIVVNGEVVAQGSQFSLQDVEVVTACVDLDAVVSFRGSISSFREQASSKKRVPSVAVPFKLCPPFSLSLVPSSPLK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 323 WPMHTPEEEIALGPACWLWDYLRRSGQGGFFLPLSGGVDSSSSATIVHSMCRQIVQAVQQGDAQVLHDIRQLL-ADSDYT 401
Cdd:PLN02339 322 IRYHSPEEEIALGPACWLWDYLRRSGASGFLLPLSGGADSSSVAAIVGSMCQLVVKAIREGDEQVKADARRIGnYADGEV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 402 PDNAAGLCNRLLVTCYMGSVNSSKETRRRAAQLANQLGSYHIEISIDSAVNALLSIFNAVTGLTPRFRTQGGCARQNLAL 481
Cdd:PLN02339 402 PTDSKEFAKRIFYTVYMGSENSSEETRSRAKQLADEIGSSHLDVKIDGVVSAVLSLFQTLTGKRPRYKVDGGSNAENLAL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 482 QNMQSRIRMVLAYIFAQLTLWVRNRPGGLLVLGSANVDESLRGYLTKYDCSSADINPIGGISKMDLRRFLTYAKDKFNLP 561
Cdd:PLN02339 482 QNIQARIRMVLAFMLASLLPWVRGKSGFLLVLGSANVDEGLRGYLTKYDCSSADINPIGGISKQDLRSFLRWAATNLGYP 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 562 VLESIIDAPPTAELEPLQENGElqQTDEADMGMTYAELSQFGRLRKQSFCGPYSMFCHLVATWKSDLSPKEVAEKVKHFF 641
Cdd:PLN02339 562 SLAEVEAAPPTAELEPIRDDYS--QTDEEDMGMTYEELGVYGRLRKIFRCGPVSMFKNLCHEWNGRLSPSEVAAKVKDFF 639
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 24641841 642 LCYAINRHKMTVLTPSVHAESYSPDDNRFDHRPFLYRPNWSWQFKAIDDEAEKL 695
Cdd:PLN02339 640 KYYSINRHKMTTLTPSYHAESYSPDDNRFDLRQFLYNTRWPYQFRKIDELVEEL 693
|
|
| NAD_synthase |
cd00553 |
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ... |
328-651 |
2.21e-93 |
|
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: 292.15 E-value: 2.21e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 328 PEEEIALGPACWLWDYLRRSGQGGFFLPLSGGVDSSSSATIVHSMCRqivqavqqgdaqvlhdirqlladsdytpdnaag 407
Cdd:cd00553 2 DPEEIIEALVCFLRDYLRKSGAKGFVLGLSGGIDSAVVAALAVRALG--------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 408 lCNRLLVTCYMGSvNSSKETRRRAAQLANQLGSYHIEISIDSAVNALLSIFNAVTGLTPrfrtqggcarQNLALQNMQSR 487
Cdd:cd00553 49 -AENVLALIMPSR-YSSKETRDDAKALAENLGIEYRTIDIDPIVDAFLKALEHAGGSEA----------EDLALGNIQAR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 488 IRMVLAYIFAQLTlwvrnrpgGLLVLGSANVDESLRGYLTKYDCSSADINPIGGISKMDLRRFLTYAKdkfnlpVLESII 567
Cdd:cd00553 117 LRMVLLYALANLL--------GGLVLGTGNKSELLLGYFTKYGDGAADINPIGDLYKTQVRELARYLG------VPEEII 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 568 DAPPTAELEPlqengelQQTDEADMGMTYAELSQFGRLRKQSFCGPYsmfchlvatwkSDLSPKEVAEKVKHFFLCYAIN 647
Cdd:cd00553 183 EKPPSAELWP-------GQTDEDELGMPYEELDLILYGLVDGKLGPE-----------EILSPGEDEEKVKRIFRLYRRN 244
|
....
gi 24641841 648 RHKM 651
Cdd:cd00553 245 EHKR 248
|
|
| CN_hydrolase |
pfam00795 |
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ... |
6-282 |
1.46e-47 |
|
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: 169.46 E-value: 1.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 6 TVAVSTLNQWALDFEGNMVRILQSILEAKDMGASYRTGPELEVCGYSCEDHFREPDTFlHSWEVLLEVMMSPMCENMLVD 85
Cdd:pfam00795 1 RVALVQLPQGFWDLEANLQKALELIEEAARYGADLIVLPELFITGYPCWAHFLEAAEV-GDGETLAGLAALARKNGIAIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 86 VGmpVMHRNVaYNCRvaFFNRQILLIRPKMAMcddGNYRESRWFTAWTKALQTEEYVLPRmiaqhtgqqtvpfGDA--VI 163
Cdd:pfam00795 80 IG--LIERWL-TGGR--LYNTAVLLDPDGKLV---GKYRKLHLFPEPRPPGFRERVLFEP-------------GDGgtVF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 164 ATRDTCLGYEICEELWNVRSKHIeMSLAGVELIVN-SSGSYMELRKAHITSDLIRNASFKAGGAY-LFSNLRGCDGQRVY 241
Cdd:pfam00795 139 DTPLGKIGAAICYEIRFPELLRA-LALKGAEILINpSARAPFPGSLGPPQWLLLARARALENGCFvIAANQVGGEEDAPW 217
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 24641841 242 FNGCSAI-ALNGEILARSQQFALqdvEVTLATIDLEEIRAYR 282
Cdd:pfam00795 218 PYGHSMIiDPDGRILAGAGEWEE---GVLIADIDLALVRAWR 256
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
83-670 |
4.97e-42 |
|
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: 161.55 E-value: 4.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 83 LVDVGMPVMHRNVAYNCRVAFFNRQILLIRPKMAMCDDGNYRESRWFTAWTKALQTEEYVLprmiAQHTGQQTVPFGDAV 162
Cdd:COG0171 36 LLLLLLLLLLLLLLLALLLLLAAARLLVAAAALLLLALAAGGGAALAGGGGGAGGGLLNGA----ALVLGGGDLLFFADD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 163 IATRDTCLGYEICEELWNVRSKHIEMSLAGVELIVNSSGSYM--ELRKAHITSDLIRNASFKAGGAYLFSNLRGCDGQRV 240
Cdd:COG0171 112 FLLLLLVVEEEEEEFVGGPPPPPAALGGAGVLLILSSSSSAVgaAAAAAALAAALLSSLSSAAYYAAAGGGESTTDLARG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 241 YFNGCSAIALNGEILARSQQFALQDVEVTLATIDLEEIRAYRVSLRSRCTAAASAAEYPRIHcdfemsthsdifkTSTPP 320
Cdd:COG0171 192 GGGGLLLVVLLLVGGGDDDFFDGGSAAVDDDDLLLLLRRRREEELLLARARDADGGRRVAAE-------------AAPPP 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 321 LNWPMHTPEEEI-ALgpACWLWDYLRRSGQGGFFLPLSGGVDSSSSATIVhsmcrqiVQAVqqGdaqvlhdirqlladsd 399
Cdd:COG0171 259 PEEEEMDLEEVYdAL--VLGLRDYVRKNGFKGVVLGLSGGIDSALVAALA-------VDAL--G---------------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 400 ytPDNaaglcnrllVTC-YMGSVNSSKETRRRAAQLANQLGSYHIEISIDSAVNALLSIFNAVTGLTPrfrtqggcarQN 478
Cdd:COG0171 312 --PEN---------VLGvTMPSRYTSDESLEDAEELAENLGIEYEEIDITPAVEAFLEALPHAFGGEL----------DD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 479 LALQNMQSRIRMVLAYIFAQLTlwvrnrpgGLLVLGSANVDESLRGYLTKYDCSSADINPIGGISKMDLRRFLTYAkDKF 558
Cdd:COG0171 371 VAEENLQARIRMVILMALANKF--------GGLVLGTGNKSELAVGYFTKYGDGAGDLAPIADLYKTQVYALARWL-NRN 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 559 NLPVLESIIDAPPTAELEPLqengelqQTDEADMGmTYAELSQFgrlrkqsfcgpysmfchLVATWKSDLSPKEVA---- 634
Cdd:COG0171 442 GEVIPEDIIDKPPSAELRPG-------QTDEDELG-PYEVLDAI-----------------LYAYVEEGLSPEEIAaagy 496
|
570 580 590
....*....|....*....|....*....|....*....
gi 24641841 635 --EKVKHFFLCYAINRHKMTVLTPSVHAESYSPD-DNRF 670
Cdd:COG0171 497 drEWVERVLRLVRRNEYKRRQPPPGPKVSSRAFGrGRRY 535
|
|
| nadE |
TIGR00552 |
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ... |
339-665 |
4.73e-31 |
|
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the biosynthesis of the essensial cofactor NAD. The member of this family from Bacillus subtilis is a strictly NH(3)-dependent NAD(+) synthetase of 272 amino acids. Proteins consisting only of the domain modeled here may be named as NH3-dependent NAD+ synthetase. Amidotransferase activity may reside in a separate protein, or not be present. Some other members of the family, such as from Mycobacterium tuberculosis, are considerably longer, contain an apparent amidotransferase domain, and show glutamine-dependent as well as NH(3)-dependent activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]
Pssm-ID: 273132 [Multi-domain] Cd Length: 250 Bit Score: 122.11 E-value: 4.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 339 WLWDYLRRSGQGGFFLPLSGGVDSSSSATIvhsmcrqivqAVQQGDAQVLhdirqlladsdytpdnaAGLcnrllvtcYM 418
Cdd:TIGR00552 12 FLRGYVQKSGAKGVVLGLSGGIDSAVVAAL----------CVEALGEQNH-----------------ALL--------LP 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 419 GSVNSSKETRRRAAQLANQLGSYHIEISIDSAVNALLSIFNAVTGLTPRfrtqggcarqnLALQNMQSRIRMVLAYIFAQ 498
Cdd:TIGR00552 57 HSVQTPEQDVQDALALAEPLGINYKNIDIAPIAASFQAQTETGDELSDF-----------LAKGNLKARLRMAALYAIAN 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 499 LTlwvrnrpgGLLVLGSANVDESLRGYLTKYDCSSADINPIGGISKMDLRRFLTYakdkFNLPvlESIIDAPPTAELEPl 578
Cdd:TIGR00552 126 KH--------NLLVLGTGNKSELMLGYFTKYGDGGCDIAPIGDLFKTQVYELAKR----LNVP--ERIIEKPPTADLFD- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 579 qengelQQTDEADMGMTYAELSQFGRLRKQsfcgpysmfchlvatwksdlSPKEVAEKVKHFFLCYAINRHKMTVltPSV 658
Cdd:TIGR00552 191 ------GQTDETELGITYDELDDYLKGIEE--------------------LSQTVQEVVKRIESLVQKSEHKRRL--PAT 242
|
....*..
gi 24641841 659 HAESYSP 665
Cdd:TIGR00552 243 IFDLFWK 249
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02339 |
PLN02339 |
NAD+ synthase (glutamine-hydrolysing) |
3-695 |
0e+00 |
|
NAD+ synthase (glutamine-hydrolysing)
Pssm-ID: 177973 [Multi-domain] Cd Length: 700 Bit Score: 1025.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 3 RKVTVAVSTLNQWALDFEGNMVRILQSILEAKDMGASYRTGPELEVCGYSCEDHFREPDTFLHSWEVLLEVMMSPMCENM 82
Cdd:PLN02339 2 RLLKVATCNLNQWAMDFDGNLKRIKESIAEAKAAGAVYRVGPELEITGYGCEDHFLELDTVTHSWECLAEILVGDLTDGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 83 LVDVGMPVMHRNVAYNCRVAFFNRQILLIRPKMAMCDDGNYRESRWFTAWTKALQTEEYVLPRMIAQHTGQQTVPFGDAV 162
Cdd:PLN02339 82 LCDIGMPVIHGGVRYNCRVFCLNRKILLIRPKMWLANDGNYRELRWFTAWKHKKKVEDFQLPEEIAEATSQKSVPFGDGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 163 IATRDTCLGYEICEELWNVRSKHIEMSLAGVELIVNSSGSYMELRKAHITSDLIRNASFKAGGAYLFSNLRGCDGQRVYF 242
Cdd:PLN02339 162 LQFLDTAVAAETCEELFTPQAPHIDLALNGVEIISNGSGSHHQLRKLNTRLDLIRSATHKCGGVYLYANQRGCDGGRLYY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 243 NGCSAIALNGEILARSQQFALQDVEVTLATIDLEEIRAYRVSLRSRCTAAASAAEYPRIHCDFEMSTHSDIFKTSTPPLN 322
Cdd:PLN02339 242 DGCACIVVNGEVVAQGSQFSLQDVEVVTACVDLDAVVSFRGSISSFREQASSKKRVPSVAVPFKLCPPFSLSLVPSSPLK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 323 WPMHTPEEEIALGPACWLWDYLRRSGQGGFFLPLSGGVDSSSSATIVHSMCRQIVQAVQQGDAQVLHDIRQLL-ADSDYT 401
Cdd:PLN02339 322 IRYHSPEEEIALGPACWLWDYLRRSGASGFLLPLSGGADSSSVAAIVGSMCQLVVKAIREGDEQVKADARRIGnYADGEV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 402 PDNAAGLCNRLLVTCYMGSVNSSKETRRRAAQLANQLGSYHIEISIDSAVNALLSIFNAVTGLTPRFRTQGGCARQNLAL 481
Cdd:PLN02339 402 PTDSKEFAKRIFYTVYMGSENSSEETRSRAKQLADEIGSSHLDVKIDGVVSAVLSLFQTLTGKRPRYKVDGGSNAENLAL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 482 QNMQSRIRMVLAYIFAQLTLWVRNRPGGLLVLGSANVDESLRGYLTKYDCSSADINPIGGISKMDLRRFLTYAKDKFNLP 561
Cdd:PLN02339 482 QNIQARIRMVLAFMLASLLPWVRGKSGFLLVLGSANVDEGLRGYLTKYDCSSADINPIGGISKQDLRSFLRWAATNLGYP 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 562 VLESIIDAPPTAELEPLQENGElqQTDEADMGMTYAELSQFGRLRKQSFCGPYSMFCHLVATWKSDLSPKEVAEKVKHFF 641
Cdd:PLN02339 562 SLAEVEAAPPTAELEPIRDDYS--QTDEEDMGMTYEELGVYGRLRKIFRCGPVSMFKNLCHEWNGRLSPSEVAAKVKDFF 639
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 24641841 642 LCYAINRHKMTVLTPSVHAESYSPDDNRFDHRPFLYRPNWSWQFKAIDDEAEKL 695
Cdd:PLN02339 640 KYYSINRHKMTTLTPSYHAESYSPDDNRFDLRQFLYNTRWPYQFRKIDELVEEL 693
|
|
| NAD_synthase |
cd00553 |
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ... |
328-651 |
2.21e-93 |
|
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: 292.15 E-value: 2.21e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 328 PEEEIALGPACWLWDYLRRSGQGGFFLPLSGGVDSSSSATIVHSMCRqivqavqqgdaqvlhdirqlladsdytpdnaag 407
Cdd:cd00553 2 DPEEIIEALVCFLRDYLRKSGAKGFVLGLSGGIDSAVVAALAVRALG--------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 408 lCNRLLVTCYMGSvNSSKETRRRAAQLANQLGSYHIEISIDSAVNALLSIFNAVTGLTPrfrtqggcarQNLALQNMQSR 487
Cdd:cd00553 49 -AENVLALIMPSR-YSSKETRDDAKALAENLGIEYRTIDIDPIVDAFLKALEHAGGSEA----------EDLALGNIQAR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 488 IRMVLAYIFAQLTlwvrnrpgGLLVLGSANVDESLRGYLTKYDCSSADINPIGGISKMDLRRFLTYAKdkfnlpVLESII 567
Cdd:cd00553 117 LRMVLLYALANLL--------GGLVLGTGNKSELLLGYFTKYGDGAADINPIGDLYKTQVRELARYLG------VPEEII 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 568 DAPPTAELEPlqengelQQTDEADMGMTYAELSQFGRLRKQSFCGPYsmfchlvatwkSDLSPKEVAEKVKHFFLCYAIN 647
Cdd:cd00553 183 EKPPSAELWP-------GQTDEDELGMPYEELDLILYGLVDGKLGPE-----------EILSPGEDEEKVKRIFRLYRRN 244
|
....
gi 24641841 648 RHKM 651
Cdd:cd00553 245 EHKR 248
|
|
| GAT_Gln-NAD-synth |
cd07570 |
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ... |
6-287 |
1.52e-85 |
|
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: 272.04 E-value: 1.52e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 6 TVAVSTLNQWALDFEGNMVRILQSILEAKDMGASYRTGPELEVCGYSCEDHFREPDTFLHSWEVLLEVMMSPMCENMLVD 85
Cdd:cd07570 1 RIALAQLNPTVGDLEGNAEKILEAIREAKAQGADLVVFPELSLTGYPPEDLLLRPDFLEAAEEALEELAAATADLDIAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 86 VGMPVMHRNVAYNCRVAFFNRQILLIRPKMAMCDDGNYRESRWFTAWTKAlqteeyvlprmiaqhtgqqtvpfgdAVIAT 165
Cdd:cd07570 81 VGLPLRHDGKLYNAAAVLQNGKILGVVPKQLLPNYGVFDEKRYFTPGDKP-------------------------DVLFF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 166 RDTCLGYEICEELWNVRSKHIEMSLAGVELIVNSSGSYMELRKAHITSDLIRNASFKAGGAYLFSNLrGCDGQRVYFNGC 245
Cdd:cd07570 136 KGLRIGVEICEDLWVPDPPSAELALAGADLILNLSASPFHLGKQDYRRELVSSRSARTGLPYVYVNQ-VGGQDDLVFDGG 214
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 24641841 246 SAIALN-GEILARSQQFalqdvEVTLATIDLEEIRAYRVSLRS 287
Cdd:cd07570 215 SFIADNdGELLAEAPRF-----EEDLADVDLDRLRSERRRNSS 252
|
|
| CN_hydrolase |
pfam00795 |
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ... |
6-282 |
1.46e-47 |
|
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: 169.46 E-value: 1.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 6 TVAVSTLNQWALDFEGNMVRILQSILEAKDMGASYRTGPELEVCGYSCEDHFREPDTFlHSWEVLLEVMMSPMCENMLVD 85
Cdd:pfam00795 1 RVALVQLPQGFWDLEANLQKALELIEEAARYGADLIVLPELFITGYPCWAHFLEAAEV-GDGETLAGLAALARKNGIAIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 86 VGmpVMHRNVaYNCRvaFFNRQILLIRPKMAMcddGNYRESRWFTAWTKALQTEEYVLPRmiaqhtgqqtvpfGDA--VI 163
Cdd:pfam00795 80 IG--LIERWL-TGGR--LYNTAVLLDPDGKLV---GKYRKLHLFPEPRPPGFRERVLFEP-------------GDGgtVF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 164 ATRDTCLGYEICEELWNVRSKHIeMSLAGVELIVN-SSGSYMELRKAHITSDLIRNASFKAGGAY-LFSNLRGCDGQRVY 241
Cdd:pfam00795 139 DTPLGKIGAAICYEIRFPELLRA-LALKGAEILINpSARAPFPGSLGPPQWLLLARARALENGCFvIAANQVGGEEDAPW 217
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 24641841 242 FNGCSAI-ALNGEILARSQQFALqdvEVTLATIDLEEIRAYR 282
Cdd:pfam00795 218 PYGHSMIiDPDGRILAGAGEWEE---GVLIADIDLALVRAWR 256
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
83-670 |
4.97e-42 |
|
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: 161.55 E-value: 4.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 83 LVDVGMPVMHRNVAYNCRVAFFNRQILLIRPKMAMCDDGNYRESRWFTAWTKALQTEEYVLprmiAQHTGQQTVPFGDAV 162
Cdd:COG0171 36 LLLLLLLLLLLLLLLALLLLLAAARLLVAAAALLLLALAAGGGAALAGGGGGAGGGLLNGA----ALVLGGGDLLFFADD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 163 IATRDTCLGYEICEELWNVRSKHIEMSLAGVELIVNSSGSYM--ELRKAHITSDLIRNASFKAGGAYLFSNLRGCDGQRV 240
Cdd:COG0171 112 FLLLLLVVEEEEEEFVGGPPPPPAALGGAGVLLILSSSSSAVgaAAAAAALAAALLSSLSSAAYYAAAGGGESTTDLARG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 241 YFNGCSAIALNGEILARSQQFALQDVEVTLATIDLEEIRAYRVSLRSRCTAAASAAEYPRIHcdfemsthsdifkTSTPP 320
Cdd:COG0171 192 GGGGLLLVVLLLVGGGDDDFFDGGSAAVDDDDLLLLLRRRREEELLLARARDADGGRRVAAE-------------AAPPP 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 321 LNWPMHTPEEEI-ALgpACWLWDYLRRSGQGGFFLPLSGGVDSSSSATIVhsmcrqiVQAVqqGdaqvlhdirqlladsd 399
Cdd:COG0171 259 PEEEEMDLEEVYdAL--VLGLRDYVRKNGFKGVVLGLSGGIDSALVAALA-------VDAL--G---------------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 400 ytPDNaaglcnrllVTC-YMGSVNSSKETRRRAAQLANQLGSYHIEISIDSAVNALLSIFNAVTGLTPrfrtqggcarQN 478
Cdd:COG0171 312 --PEN---------VLGvTMPSRYTSDESLEDAEELAENLGIEYEEIDITPAVEAFLEALPHAFGGEL----------DD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 479 LALQNMQSRIRMVLAYIFAQLTlwvrnrpgGLLVLGSANVDESLRGYLTKYDCSSADINPIGGISKMDLRRFLTYAkDKF 558
Cdd:COG0171 371 VAEENLQARIRMVILMALANKF--------GGLVLGTGNKSELAVGYFTKYGDGAGDLAPIADLYKTQVYALARWL-NRN 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 559 NLPVLESIIDAPPTAELEPLqengelqQTDEADMGmTYAELSQFgrlrkqsfcgpysmfchLVATWKSDLSPKEVA---- 634
Cdd:COG0171 442 GEVIPEDIIDKPPSAELRPG-------QTDEDELG-PYEVLDAI-----------------LYAYVEEGLSPEEIAaagy 496
|
570 580 590
....*....|....*....|....*....|....*....
gi 24641841 635 --EKVKHFFLCYAINRHKMTVLTPSVHAESYSPD-DNRF 670
Cdd:COG0171 497 drEWVERVLRLVRRNEYKRRQPPPGPKVSSRAFGrGRRY 535
|
|
| NAD_synthase |
pfam02540 |
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ... |
339-602 |
5.35e-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: 127.50 E-value: 5.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 339 WLWDYLRRSGQGGFFLPLSGGVDSSssatIVHSMCrqiVQAVQqgdaqvlhdirqlladsdytPDNAAGLcnrllvtcYM 418
Cdd:pfam02540 8 FLRDYVQKAGFKGVVLGLSGGIDSS----LVAYLA---VKALG--------------------KENVLAL--------IM 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 419 GSVNSSKETRRRAAQLANQLGSYHIEISIDSAVNALLSIFNAvtgltprfrtqggcARQNLALQNMQSRIRMVLAYIFAQ 498
Cdd:pfam02540 53 PSSQSSEEDVQDALALAENLGIEYKTIDIKPIVRAFSQLFQD--------------ASEDFAKGNLKARIRMAILYYIAN 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 499 LTlwvrnrpgGLLVLGSANVDESLRGYLTKYDCSSADINPIGGISKMDLRRFLTYakdkFNLPvlESIIDAPPTAELEPl 578
Cdd:pfam02540 119 KF--------NYLVLGTGNKSELAVGYFTKYGDGACDIAPIGDLYKTQVYELARY----LNVP--ERIIKKPPSADLWP- 183
|
250 260
....*....|....*....|....
gi 24641841 579 qengelQQTDEADMGMTYAELSQF 602
Cdd:pfam02540 184 ------GQTDEEELGIPYDELDDI 201
|
|
| nadE |
TIGR00552 |
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ... |
339-665 |
4.73e-31 |
|
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the biosynthesis of the essensial cofactor NAD. The member of this family from Bacillus subtilis is a strictly NH(3)-dependent NAD(+) synthetase of 272 amino acids. Proteins consisting only of the domain modeled here may be named as NH3-dependent NAD+ synthetase. Amidotransferase activity may reside in a separate protein, or not be present. Some other members of the family, such as from Mycobacterium tuberculosis, are considerably longer, contain an apparent amidotransferase domain, and show glutamine-dependent as well as NH(3)-dependent activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]
Pssm-ID: 273132 [Multi-domain] Cd Length: 250 Bit Score: 122.11 E-value: 4.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 339 WLWDYLRRSGQGGFFLPLSGGVDSSSSATIvhsmcrqivqAVQQGDAQVLhdirqlladsdytpdnaAGLcnrllvtcYM 418
Cdd:TIGR00552 12 FLRGYVQKSGAKGVVLGLSGGIDSAVVAAL----------CVEALGEQNH-----------------ALL--------LP 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 419 GSVNSSKETRRRAAQLANQLGSYHIEISIDSAVNALLSIFNAVTGLTPRfrtqggcarqnLALQNMQSRIRMVLAYIFAQ 498
Cdd:TIGR00552 57 HSVQTPEQDVQDALALAEPLGINYKNIDIAPIAASFQAQTETGDELSDF-----------LAKGNLKARLRMAALYAIAN 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 499 LTlwvrnrpgGLLVLGSANVDESLRGYLTKYDCSSADINPIGGISKMDLRRFLTYakdkFNLPvlESIIDAPPTAELEPl 578
Cdd:TIGR00552 126 KH--------NLLVLGTGNKSELMLGYFTKYGDGGCDIAPIGDLFKTQVYELAKR----LNVP--ERIIEKPPTADLFD- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 579 qengelQQTDEADMGMTYAELSQFGRLRKQsfcgpysmfchlvatwksdlSPKEVAEKVKHFFLCYAINRHKMTVltPSV 658
Cdd:TIGR00552 191 ------GQTDETELGITYDELDDYLKGIEE--------------------LSQTVQEVVKRIESLVQKSEHKRRL--PAT 242
|
....*..
gi 24641841 659 HAESYSP 665
Cdd:TIGR00552 243 IFDLFWK 249
|
|
| nadE |
PRK02628 |
NAD synthetase; Reviewed |
4-287 |
1.23e-29 |
|
NAD synthetase; Reviewed
Pssm-ID: 235057 [Multi-domain] Cd Length: 679 Bit Score: 125.36 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 4 KVTVAvstlnqwalDFEGNMVRILQSILEAKDMGASYRTGPELEVCGYSCEDhfrepdtfLHSWEVLLEVMMSPMCE--- 80
Cdd:PRK02628 21 KVRVA---------DPAFNAARILALARRAADDGVALAVFPELSLSGYSCDD--------LFLQDTLLDAVEDALATlve 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 81 -----NMLVDVGMPVMHRNVAYNCRVAFFNRQILLIRPKMAMCddgNYR---ESRWFTAWTKAlqTEEYVlprmiaqHTG 152
Cdd:PRK02628 84 asadlDPLLVVGAPLRVRHRLYNCAVVIHRGRILGVVPKSYLP---NYRefyEKRWFAPGDGA--RGETI-------RLC 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 153 QQTVPFGD----AVIATRDTCLGYEICEELWNVRSKHIEMSLAGVELIVNSSGSYMELRKAHITSDLIRNASFKAGGAYL 228
Cdd:PRK02628 152 GQEVPFGTdllfEAEDLPGFVFGVEICEDLWVPIPPSSYAALAGATVLANLSASNITVGKADYRRLLVASQSARCLAAYV 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24641841 229 FSNlRGC---------DGQrvyfngcSAIALNGEILARSQQFAlQDVEVTLATIDLEEIRAYRVSLRS 287
Cdd:PRK02628 232 YAA-AGVgesttdlawDGQ-------TLIYENGELLAESERFP-REEQLIVADVDLERLRQERLRNGS 290
|
|
| PRK13981 |
PRK13981 |
NAD synthetase; Provisional |
5-589 |
3.58e-29 |
|
NAD synthetase; Provisional
Pssm-ID: 237577 [Multi-domain] Cd Length: 540 Bit Score: 122.96 E-value: 3.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 5 VTVAVSTLNQWALDFEGNMVRILQSILEAKDMGASYRTGPELEVCGYSCEDHFREPDtFLHSWEVLLEVMMSPMCENMLV 84
Cdd:PRK13981 1 LRIALAQLNPTVGDIAGNAAKILAAAAEAADAGADLLLFPELFLSGYPPEDLLLRPA-FLAACEAALERLAAATAGGPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 85 DVGMPVMHRNVAYNCRVAFFNRQILLIRPKMAMCDDGNYRESRWFTAwtkalqteeyvlprmiaqhtGQQTVPFgdaviA 164
Cdd:PRK13981 80 LVGHPWREGGKLYNAAALLDGGEVLATYRKQDLPNYGVFDEKRYFAP--------------------GPEPGVV-----E 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 165 TRDTCLGYEICEELWNvrSKHIE-MSLAGVELIVNSSGSYMELRKAHITSDLIRNASFKAGGAYLFSNLRGcdGQ-RVYF 242
Cdd:PRK13981 135 LKGVRIGVPICEDIWN--PEPAEtLAEAGAELLLVPNASPYHRGKPDLREAVLRARVRETGLPLVYLNQVG--GQdELVF 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 243 NGCSaIALN--GEILARSQQFalqdvEVTLATIDLEeirayRVSLRSRCTAAASAAEYPRihcdfemsthsdifktstpp 320
Cdd:PRK13981 211 DGAS-FVLNadGELAARLPAF-----EEQIAVVDFD-----RGEDGWRPLPGPIAPPPEG-------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 321 lnwpmhtpEEEI----ALGpacwLWDYLRRSGQGGFFLPLSGGVDSSSSATIvhsmcrqivqAVqqgDAqvlhdirqLLA 396
Cdd:PRK13981 260 --------EAEDyralVLG----LRDYVRKNGFPGVVLGLSGGIDSALVAAI----------AV---DA--------LGA 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 397 DSdytpdnaaglcnrllVTC-YMGSVNSSKETRRRAAQLANQLGSYHIEISIDSAVNALLSIfnavtgLTPRFR-TQGGC 474
Cdd:PRK13981 307 ER---------------VRAvMMPSRYTSEESLDDAAALAKNLGVRYDIIPIEPAFEAFEAA------LAPLFAgTEPDI 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 475 ARQNLalqnmQSRIRMVLayIFAqltlwVRNRPGGLlVLGSANVDESLRGYLTKYdcssADIN----PIGGISKMD---L 547
Cdd:PRK13981 366 TEENL-----QSRIRGTL--LMA-----LSNKFGSL-VLTTGNKSEMAVGYATLY----GDMAggfaPIKDVYKTLvyrL 428
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 24641841 548 RRFLTYAKDKFNLPvlESIIDAPPTAELEPlqengelQQTDE 589
Cdd:PRK13981 429 CRWRNTVSPGEVIP--ERIITKPPSAELRP-------NQTDQ 461
|
|
| PRK13980 |
PRK13980 |
NAD synthetase; Provisional |
342-599 |
1.03e-26 |
|
NAD synthetase; Provisional
Pssm-ID: 184435 [Multi-domain] Cd Length: 265 Bit Score: 110.30 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 342 DYLRRSGQGGFFLPLSGGVDSSSSATIVhsmcrqiVQAVqqgdaqvlhdirqlladsdyTPDNAAGLCnrllvtcyMGSV 421
Cdd:PRK13980 23 EEVEKAGAKGVVLGLSGGIDSAVVAYLA-------VKAL--------------------GKENVLALL--------MPSS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 422 NSSKETRRRAAQLANQLGSYHIEISIDSAVNALLSIFNAVTgltprfrtqggcarqNLALQNMQSRIRMVLAYIFAQLtl 501
Cdd:PRK13980 68 VSPPEDLEDAELVAEDLGIEYKVIEITPIVDAFFSAIPDAD---------------RLRVGNIMARTRMVLLYDYANR-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 502 wvRNRpgglLVLGSANVDESLRGYLTKYDCSSADINPIGGISKMDLRRFLTYakdkfnLPVLESIIDAPPTAELEPlqen 581
Cdd:PRK13980 131 --ENR----LVLGTGNKSELLLGYFTKYGDGAVDLNPIGDLYKTQVRELARH------LGVPEDIIEKPPSADLWE---- 194
|
250
....*....|....*...
gi 24641841 582 GelqQTDEADMGMTYAEL 599
Cdd:PRK13980 195 G---QTDEGELGFSYETI 209
|
|
| Nit2 |
COG0388 |
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]; |
4-282 |
3.32e-25 |
|
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
Pssm-ID: 440157 [Multi-domain] Cd Length: 264 Bit Score: 105.72 E-value: 3.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 4 KVTVAVSTLNQWALDFEGNMVRILQSILEAKDMGASYRTGPELEVCGYSCEDHfrepdTFLHSWEVLLEVMMSPMCE--- 80
Cdd:COG0388 1 TMRIALAQLNPTVGDIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDD-----DLLELAEPLDGPALAALAElar 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 81 --NMLVDVGMPV-MHRNVAYNCrVAFFNR--QILLIRPKMAMCDDGNYRESRWFTAWTKALqteeyvlprmiaqhtgqqt 155
Cdd:COG0388 76 elGIAVVVGLPErDEGGRLYNT-ALVIDPdgEILGRYRKIHLPNYGVFDEKRYFTPGDELV------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 156 vpfgdaVIATRDTCLGYEICEELWN---VRskhiEMSLAGVELIVNSSGSYMELRKAHItSDLIRNASFKAGGAYLFSNL 232
Cdd:COG0388 136 ------VFDTDGGRIGVLICYDLWFpelAR----ALALAGADLLLVPSASPFGRGKDHW-ELLLRARAIENGCYVVAANQ 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 24641841 233 RGCDGQRVyFNGCSAIA-LNGEILARsqqfALQDVEVTLATIDLEEIRAYR 282
Cdd:COG0388 205 VGGEDGLV-FDGGSMIVdPDGEVLAE----AGDEEGLLVADIDLDRLREAR 250
|
|
| nadE |
PRK00768 |
ammonia-dependent NAD(+) synthetase; |
328-602 |
5.97e-09 |
|
ammonia-dependent NAD(+) synthetase;
Pssm-ID: 234831 [Multi-domain] Cd Length: 268 Bit Score: 57.84 E-value: 5.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 328 PEEEIALGPAcWLWDYLRRSGQGGFFLPLSGGVDSSSSATIvhsmCrQIvqAVQQgdaqvlhdIRQLLADSDYT------ 401
Cdd:PRK00768 18 PEEEIRRRVD-FLKDYLKKSGLKSLVLGISGGQDSTLAGRL----A-QL--AVEE--------LRAETGDDDYQfiavrl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 402 PdnaaglcnrllvtcYmGSVNSSKEtrrraAQLANQLgsyhIEISIDSAVNallsIFNAVTGLTPRFRtQGGCARQNLAL 481
Cdd:PRK00768 82 P--------------Y-GVQADEDD-----AQDALAF----IQPDRVLTVN----IKPAVDASVAALE-AAGIELSDFVK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 482 QNMQSRIRMVLAYIFAQLTlwvrnrpgGLLVLGSANVDESLRGYLTKYDCSSADINPIGGISKMDLRRFLTYakdkFNLP 561
Cdd:PRK00768 133 GNIKARERMIAQYAIAGAT--------GGLVVGTDHAAEAVTGFFTKFGDGGADILPLFGLNKRQGRALLAA----LGAP 200
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 24641841 562 vlESIIDAPPTAELEPLQEngelQQTDEADMGMTYAELSQF 602
Cdd:PRK00768 201 --EHLYEKVPTADLEDDRP----GLPDEVALGVTYDQIDDY 235
|
|
| PTZ00323 |
PTZ00323 |
NAD+ synthase; Provisional |
333-596 |
2.03e-08 |
|
NAD+ synthase; Provisional
Pssm-ID: 185554 [Multi-domain] Cd Length: 294 Bit Score: 56.32 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 333 ALGPACW-------LWDYLRRSGQGGFFLPLSGGVDSSssatIVHSMCRQivqavqqgdAQVLHD--IRQLLadsdytpd 403
Cdd:PTZ00323 23 AFNPAAWiekkcakLNEYMRRCGLKGCVTSVSGGIDSA----VVLALCAR---------AMRMPNspIQKNV-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 404 naaGLCNrllvtcymgSVNSSKETRRRAAQLANQLGSyhIEISIDSAvnallSIFnavTGLTPRFRTQGGCARQNLALQN 483
Cdd:PTZ00323 82 ---GLCQ---------PIHSSAWALNRGRENIQACGA--TEVTVDQT-----EIH---TQLSSLVEKAVGIKGGAFARGQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 484 MQSRIRMVLAYIFAQLtLWVRNRPGglLVLGSANVDESlrGYLTkYDCSS----ADINPIGGISKMDLRRFLTYakdkfn 559
Cdd:PTZ00323 140 LRSYMRTPVAFYVAQL-LSQEGTPA--VVMGTGNFDED--GYLG-YFCKAgdgvVDVQLISDLHKSEVFLVARE------ 207
|
250 260 270
....*....|....*....|....*....|....*..
gi 24641841 560 LPVLESIIDAPPTAELEPlqengelQQTDEADMGMTY 596
Cdd:PTZ00323 208 LGVPENTLQAAPSADLWE-------GQTDEDELGFPY 237
|
|
| nitrilase_8 |
cd07586 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
6-282 |
2.08e-07 |
|
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: 53.06 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 6 TVAVSTLNQWALDFEGNMVRILQSILEAKDMGASYRTGPELEVCGYSCEDhfREPDTFLH-SWEVLLEvmMSPMCENMLV 84
Cdd:cd07586 1 RVAIAQIDPVLGDVEENLEKHLEIIETARERGADLVVFPELSLTGYNLGD--LVYEVAMHaDDPRLQA--LAEASGGICV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 85 DVGM-----PVMHRNVAY---NCRVAFFNRQILLirpkmamCDDGNYRESRWFTAwtkalqteeyvlprmiaqhtGQQTV 156
Cdd:cd07586 77 VFGFveegrDGRFYNSAAyleDGRVVHVHRKVYL-------PTYGLFEEGRYFAP--------------------GSHLR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641841 157 PFGdaviaTRDTCLGYEICEELWNVRSKHIeMSLAGVELIV--NSSGSYMELRKAHITSDLIRNASFKA---GGAYLFSN 231
Cdd:cd07586 130 AFD-----TRFGRAGVLICEDAWHPSLPYL-LALDGADVIFipANSPARGVGGDFDNEENWETLLKFYAmmnGVYVVFAN 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 24641841 232 LRGCDGQRVYFNGCSAIALNGEILARSQQFalqDVEVTLATIDLEEIRAYR 282
Cdd:cd07586 204 RVGVEDGVYFWGGSRVVDPDGEVVAEAPLF---EEDLLVAELDRSAIRRAR 251
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| |
