|
Name |
Accession |
Description |
Interval |
E-value |
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-555 |
0e+00 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 547.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 1 MCGIWALFGSD---DCLSVQCLSAMK-IAHRGPDAfrfENVNGYTNCCFGFHRLAVVDPLFGMQPI--RVKKypyLWLCY 74
Cdd:PRK09431 1 MCGIFGILDIKtdaDELRKKALEMSRlMRHRGPDW---SGIYASDNAILGHERLSIVDVNGGAQPLynEDGT---HVLAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 75 NGEIYNHKKMQQHFE--FEYQTKVDGEIILHLYDKGGIEqTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTED 152
Cdd:PRK09431 75 NGEIYNHQELRAELGdkYAFQTGSDCEVILALYQEKGPD-FLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 153 GFLAVCSEAKGLVtlkhsatPFLK-VEPFLPGHYevldLKPngkvASVEMVKYHHcRDVPLhalYDNVEklfpgfEIETV 231
Cdd:PRK09431 154 GNLYFASEMKALV-------PVCKtIKEFPPGHY----YWS----KDGEFVRYYQ-RDWFD---YDAVK------DNVTD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 232 KNNLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAA--------TLLKQLKEAQVQYPLQTFAIGMEDSPDLLAARKVA 303
Cdd:PRK09431 209 KNELRDALEAAVKKRLMSDVPYGVLLSGGLDSSLISAiakkyaarRIEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 304 DHIGSEHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIrKNTDSVVIFSGEGSDELTQGYIYFHKAPSP 383
Cdd:PRK09431 289 DHLGTVHHEIHFTVQEGLDALRDVIYHLETYDVTTIRASTPMYLMARKI-KAMGIKMVLSGEGADELFGGYLYFHKAPNA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 384 EKAEEESERLLRELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRIPKNG-IEKHLLRETFEDsnLIPKEI 462
Cdd:PRK09431 368 KEFHEETVRKLRALHMYDCLRANKAMMAWGVEARVPFLDKEFLDVAMRINPEDKMCGNGkMEKHILREAFEG--YLPESI 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 463 LWRPKEAFSDGitsVKNSWFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQVFERHYPGRA--------DWLS 534
Cdd:PRK09431 446 LWRQKEQFSDG---VGYSWIDTLKEVAAEQVSDQQLATARFRFPYNTPTTKEAYLYREIFEELFPLPSaaecvpggPSVA 522
|
570 580
....*....|....*....|....*..
gi 168229248 535 HYWMP------KWINATDPSARTLTHY 555
Cdd:PRK09431 523 CSSAKaiewdeAFKNMDDPSGRAVSGV 549
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-470 |
0e+00 |
|
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 535.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 4 IWALFGSDDCLSVQ---CLS-AMKIAHRGPDAFRFENvnGYTNCCFGFHRLAVVDPLFGMQPIRVKKyPYLWLCYNGEIY 79
Cdd:TIGR01536 1 IAGFFDLDDKAVEEdeaIKRmSDTIAHRGPDASGIEY--KDGNAILGHRRLAIIDLSGGAQPMSNEG-KTYVIVFNGEIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 80 NHKKMQQHFE---FEYQTKVDGEIILHLYDKGGiEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMtEDGFLA 156
Cdd:TIGR01536 78 NHEELREELEakgYTFQTDSDTEVILHLYEEWG-EECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAY-DGGQLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 157 VCSEAKGLVTLKhSATPFLKVEPFLPGHYEVLDlkPNGKVASVEMVKYHHCRDVPLHALYDNVEKL------FPGFEIET 230
Cdd:TIGR01536 156 FASEIKALLAHP-NIKPFPDGAALAPGFGFVRV--PPPSTFFRGVFELEPGHDLPLDDDGLNIERYywerrdEHTDSEED 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 231 VKNNLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEaqvqYPLQTFAIGMEDSPDLL---AARKVADHIG 307
Cdd:TIGR01536 233 LVDELRSLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPR----GPVHTFSIGFEGSPDFDeskYARKVADHLG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 308 SEHYEVLFNSEEGIQALDEVIFSLEtyDITTVRASVGMYLISKYIRKNTdSVVIFSGEGSDELTQGYIYFHKAPSPEKAE 387
Cdd:TIGR01536 309 TEHHEVLFSVEEGLDALPEVIYHLE--EPTTIRASIPLYLLSKLAREDG-VKVVLSGEGADELFGGYLYFHEAPAAEALR 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 388 EESERLLRELYLFDVLRA-DRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRIpKNGIEKHLLRETFEDsnLIPKEILWRP 466
Cdd:TIGR01536 386 EELQYLDLELYMPGLLRRkDRMSMAHSLEVRVPFLDHELVEYALSIPPEMKL-RDGKEKYLLREAFEG--YLPEEILWRP 462
|
....
gi 168229248 467 KEAF 470
Cdd:TIGR01536 463 KEGF 466
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-561 |
2.13e-157 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 461.93 E-value: 2.13e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 1 MCGIWALFGSDDCLS-----VQCLSAmKIAHRGPDAFRFEnvnGYTNCCFGFHRLAVVDPLFGMQPIRVKKYPYLwLCYN 75
Cdd:PLN02549 1 MCGILAVLGCSDDSQakrsrVLELSR-RLRHRGPDWSGLY---GNEDCYLAHERLAIMDPESGDQPLYNEDKTIV-VTAN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 76 GEIYNHKKMQQHFE-FEYQTKVDGEIILHLYDKGGiEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGF 154
Cdd:PLN02549 76 GEIYNHKELREKLKlHKFRTGSDCEVIAHLYEEHG-EEFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGLDGS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 155 LAVCSEAKGLVtlKHSAtpflKVEPFLPGHYEVLdlKPNGkvasveMVKYHHCR---DVPLHALYDNVEklfpgfeietv 231
Cdd:PLN02549 155 VWFASEMKALC--DDCE----RFEEFPPGHYYSS--KAGG------FRRWYNPPwfsESIPSTPYDPLV----------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 232 knnLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQY----PLQTFAIGMEDSPDLLAARKVADHIG 307
Cdd:PLN02549 210 ---LREAFEKAVIKRLMTDVPFGVLLSGGLDSSLVASIAARHLAETKAARqwgqQLHSFCVGLEGSPDLKAAREVADYLG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 308 SEHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIRKNTDSVVIfSGEGSDELTQGYIYFHKAPSPEKAE 387
Cdd:PLN02549 287 TVHHEFHFTVQEGIDAIEDVIYHLETYDVTTIRASTPMFLMSRKIKSLGVKMVL-SGEGSDEIFGGYLYFHKAPNKEEFH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 388 EESERLLRELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRIPKNG---IEKHLLRETF--EDSNLIPKEI 462
Cdd:PLN02549 366 KETCRKIKALHQYDCLRANKSTSAWGLEARVPFLDKEFIDVAMSIDPEWKMIRPGegrIEKWVLRKAFddEEDPYLPKHI 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 463 LWRPKEAFSDGitsVKNSWFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQVFERHYPGR------------- 529
Cdd:PLN02549 446 LWRQKEQFSDG---VGYSWIDGLKAHAEKHVSDEMFANASFRYPHNTPTTKEAYYYRMIFEKHFPQDaarltvpggpsva 522
|
570 580 590
....*....|....*....|....*....|....*...
gi 168229248 530 -ADWLSHYWMPKWINATDPSARTLT--H---YKSAVKA 561
Cdd:PLN02549 523 cSTAKAVEWDAAWSKNLDPSGRAALgvHvaaYEEDVAA 560
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-560 |
1.58e-152 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 449.93 E-value: 1.58e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 1 MCGIWALFGSDDCLS-----VQCLSAmKIAHRGPDAFR---FENVNGYTNCcFGFHRLAVVDPLFGMQPIRVKKYPyLWL 72
Cdd:PTZ00077 1 MCGILAIFNSKGERHelrrkALELSK-RLRHRGPDWSGiivLENSPGTYNI-LAHERLAIVDLSDGKQPLLDDDET-VAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 73 CYNGEIYNHKKMQQHFE---FEYQTKVDGEIILHLYDKGGIEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAM 149
Cdd:PTZ00077 78 MQNGEIYNHWEIRPELEkegYKFSSNSDCEIIGHLYKEYGPKDFWNHLDGMFATVIYDMKTNTFFAARDHIGIIPLYIGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 150 TEDGFLAVCSEAKGLvtlkHSATpfLKVEPFLPGHYeVLDLKPNGkvasvEMVKYHHcrdvplhALYDNVEKLFPGFEIE 229
Cdd:PTZ00077 158 AKDGSIWFSSELKAL----HDQC--VEVKQFPPGHY-YDQTKEKG-----EFVRYYN-------PNWHDFDHPIPTGEID 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 230 TVKnnLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQYP------LQTFAIGMEDSPDLLAARKVA 303
Cdd:PTZ00077 219 LEE--IREALEAAVRKRLMGDVPFGLFLSGGLDSSIVAAIVAKLIKNGEIDLSkrgmpkLHSFCIGLEGSPDLKAARKVA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 304 DHIGSEHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIrKNTDSVVIFSGEGSDELTQGYIYFHKAPSP 383
Cdd:PTZ00077 297 EYLGTEHHEFTFTVEEGIDALPDVIYHTETYDVTTIRASTPMYLLSRRI-KALGIKMVLSGEGSDELFGGYLYFHKAPNR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 384 EKAEEESERLLRELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRIPKNG---IEKHLLRETFED--SNLI 458
Cdd:PTZ00077 376 EEFHRELVRKLHDLHKYDCLRANKATMAWGIEARVPFLDKDFLEYVMNIDPKYKMCNAFegqMEKYILRKAFEGleKPYL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 459 PKEILWRPKEAFSDGitsVKNSWFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQVFERHYPGRADWLS-HY- 536
Cdd:PTZ00077 456 PDEILWRQKEQFSDG---VGYSWIDGLKEYAEKKISDQEFSQASFLFPYNTPRTKEAYLYRQIFSKHFPSDSAALTvPYg 532
|
570 580 590
....*....|....*....|....*....|....*..
gi 168229248 537 ------------WMPKWINATDPSART-LTHYKSAVK 560
Cdd:PTZ00077 533 psiacstekaleWDESFKKNTDESGRAvLSVHNDAKQ 569
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-538 |
6.07e-128 |
|
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: 385.73 E-value: 6.07e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 1 MCGIWALFGSDDCLSVQCLSAM--KIAHRGPDAFRFEnVNGytNCCFGFHRLAVVDP-LFGMQPIRVKKYPYlWLCYNGE 77
Cdd:COG0367 1 MCGIAGIIDFDGGADREVLERMldALAHRGPDGSGIW-VDG--GVALGHRRLSIIDLsEGGHQPMVSEDGRY-VLVFNGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 78 IYNHKKMQQHFE---FEYQTKVDGEIILHLYDKGGiEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGF 154
Cdd:COG0367 77 IYNYRELRAELEalgHRFRTHSDTEVILHAYEEWG-EDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDGGGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 155 lAVCSEAKGLVTLKH---------------------SATPFLKVEPFLPGHYevLDLKPNGKVasvEMVKYHHCRDVPLH 213
Cdd:COG0367 156 -AFASELKALLAHPGvdreldpealaeyltlgyvpaPRTIFKGIRKLPPGHY--LTVDAGGEL---EIRRYWDLEFVPHE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 214 ALYDnveklfpgfeIETVKNNLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEaqvqyPLQTFAIGMEDS 293
Cdd:COG0367 230 RSDS----------EEEAVEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKG-----PLKTFSIGFEDS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 294 P--DLLAARKVADHIGSEHYEVLFNSEEGIQALDEVIFSLEtyDITTVRASVGMYLISKYIRKntDSVVIFSGEGSDELT 371
Cdd:COG0367 295 AydESPYARAVAEHLGTEHHEVTVTPEDLLDALPDLVWHLD--EPFADPSAVPTYLLSRLARE--HVKVVLSGEGADELF 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 372 QGYIYFHKAP---SPEKAEEESERLLREL--------------------YLFDVL--RADRTTAAHGLELRVPFLDHRFS 426
Cdd:COG0367 371 GGYPRYREAAlllSPDFAEALGGELVPRLyaesgaedplrrmlyldlktYLPGDLlvKVDRMSMAHSLEVRVPFLDHRLV 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 427 SYYLSLPPEMRIpKNGIEKHLLRETFEDsnLIPKEILWRPKEAFSDGItsvkNSWFK-ILQEYVEHQVDDAMManAAQKF 505
Cdd:COG0367 451 EFALSLPPELKL-RGGRGKYLLRKALEG--LLPDEVLDRPKQGFPVPL----GPWLRgPLREWLEDLLSDESL--AARGL 521
|
570 580 590
....*....|....*....|....*....|...
gi 168229248 506 pFNTpktkegYYYRQVFERHYPGRADWLSHYWM 538
Cdd:COG0367 522 -FDP------DAVRRLLEEHLAGRRDHSRKLWS 547
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
234-538 |
1.13e-92 |
|
Asparagine synthase; This family is always found associated with pfam00310. Members of this family catalyze the conversion of aspartate to asparagine.
Pssm-ID: 395594 [Multi-domain] Cd Length: 279 Bit Score: 285.28 E-value: 1.13e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 234 NLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEaqvqyPLQTFAIGME--DSPDLLAARKVADHIGSEHY 311
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSPS-----PLHTFSIGFEgrGYDEAPYAREVAEHLGTDHH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 312 EVLFNSEEGIQALDEVIFSLETydITTVRASVGMYLISKYIRKnTDSVVIFSGEGSDELTQGYIYFHKAPSPEKAEEESE 391
Cdd:pfam00733 76 ELVVTPEDLLDALPDVIWHLDE--PFADPSAIPLYLLSRLARR-KGVKVVLSGEGADELFGGYPFYKGEDPLRRMLYLDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 392 RLLrelYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRIpKNGIEKHLLRETFEDsnLIPKEILWRPKEAFS 471
Cdd:pfam00733 153 KTL---LPGDLLRADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKL-RGGIEKYILREALEG--ILPDEILERPKEGFS 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 168229248 472 DGitsVKNSWFKI-LQEYVEHQVDDAmmanaaqkfpfntPKTKEGYYYRQVFERHYPGRADWLSHYWM 538
Cdd:pfam00733 227 AP---VGDWKLRGpLRELAEDLLSDS-------------RLAKEGLLDREAVRELLDEHLAGMLELWL 278
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
249-473 |
3.20e-75 |
|
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: 237.94 E-value: 3.20e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 249 TDRRIGCLLSGGLDSSLVAATLLKQLKEAqvqyPLQTFAIGMEDS--PDLLAARKVADHIGSEHYEVLFNSEEGIQALDE 326
Cdd:cd01991 1 SDVPVGVLLSGGLDSSLIAALAARLLPET----PIDLFTVGFEGSptPDRAAARRVAEELGTEHHEVEVTIEELLDALPD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 327 VIFSLETYDITTVRASVGMYLISKYIRKNTDSVVIfSGEGSDELTQGYIYFHKAPSPEKAEEESERLLREL--YLFDVLR 404
Cdd:cd01991 77 VILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVL-SGEGADELFGGYSRHRDAPLRGWEALEEELLRDLDrlWTRNLGR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 405 ADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRI-PKNGIEKHLLRETFEDsnLIPKEILWRPKEAFSDG 473
Cdd:cd01991 156 DDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIdPRGGGEKYILREAARD--LLPDEIAWRPKRAIQFG 223
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-206 |
1.30e-59 |
|
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia.
Pssm-ID: 238364 [Multi-domain] Cd Length: 220 Bit Score: 197.01 E-value: 1.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 2 CGIWALFGSD---DCLSVQCLSAMKIAHRGPDAFRFENVNGytnCCFGFHRLAVVDPLFGMQPIRVKKyPYLWLCYNGEI 78
Cdd:cd00712 1 CGIAGIIGLDgasVDRATLERMLDALAHRGPDGSGIWIDEG---VALGHRRLSIIDLSGGAQPMVSED-GRLVLVFNGEI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 79 YNHKKMQQHFEFEY---QTKVDGEIILHLYDKGGiEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTeDGFL 155
Cdd:cd00712 77 YNYRELRAELEALGhrfRTHSDTEVILHLYEEWG-EDCLERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGRD-GGGL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 168229248 156 AVCSEAKGLVTLKH---------------------SATPFLKVEPFLPGHYEVLDLKPngkvasVEMVKYHH 206
Cdd:cd00712 155 AFASELKALLALPGvpreldeaalaeylafqyvpaPRTIFKGIRKLPPGHYLTVDPGG------VEIRRYWD 220
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-185 |
1.43e-36 |
|
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.
Pssm-ID: 238212 [Multi-domain] Cd Length: 220 Bit Score: 135.65 E-value: 1.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 2 CGIWALFGSDDCLSVQCL----SAMKIAHRGPDAF------------------------RFENVNGYTNCCFGFHRLAVV 53
Cdd:cd00352 1 CGIFGIVGADGAASLLLLlllrGLAALEHRGPDGAgiavydgdglfvekragpvsdvalDLLDEPLKSGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 54 DP--LFGMQPIRVKKYPYlWLCYNGEIYNHKKMQQHFE---FEYQTKVDGEIILHLYDKGG--------IEQTICMLDGV 120
Cdd:cd00352 81 GLpsEANAQPFRSEDGRI-ALVHNGEIYNYRELREELEargYRFEGESDSEVILHLLERLGregglfeaVEDALKRLDGP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 168229248 121 FAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVtlkhsATPFLKVEPFLPGHY 185
Cdd:cd00352 160 FAFALWDGKPDRLFAARDRFGIRPLYYGITKDGGLVFASEPKALL-----ALPFKGVRRLPPGEL 219
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
49-164 |
7.53e-31 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes such as asparagine synthetase and glutamine-fructose-6-phosphate transaminase.
Pssm-ID: 433289 [Multi-domain] Cd Length: 123 Bit Score: 116.46 E-value: 7.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 49 RLAVVDPLFGMQPIRVKKYPYLWLCYNGEIYNHKKMQQHFE---FEYQTKVDGEIILHLYDKGGIEQTICMLDGVFAFVL 125
Cdd:pfam13537 3 RLSIIDLEGGAQPMVSSEDGRYVIVFNGEIYNYRELRAELEakgYRFRTHSDTEVILHLYEAEWGEDCVDRLNGMFAFAI 82
|
90 100 110
....*....|....*....|....*....|....*....
gi 168229248 126 LDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGL 164
Cdd:pfam13537 83 WDRRRQRLFLARDRFGIKPLYYGRDDGGRLLFASELKAL 121
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
29-155 |
2.03e-17 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.
Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 78.50 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 29 PDAFRFEnvngYTNCC-FGFHRLAVVD-PLFGMQPIRVkkyPY--LWLCYNGEIYNHKKMQQHFE---FEYQTKVDGEII 101
Cdd:pfam13522 1 PDFSGIW----VEGGVaLGHVRLAIVDlPDAGNQPMLS---RDgrLVLVHNGEIYNYGELREELAdlgHAFRSRSDTEVL 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 168229248 102 LHLYDKGGiEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFL 155
Cdd:pfam13522 74 LALYEEWG-EDCLERLRGMFAFAIWDRRRRTLFLARDRLGIKPLYYGILGGGFV 126
|
|
| Gn_AT_II_novel |
cd03766 |
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its ... |
1-179 |
4.69e-17 |
|
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its function has not yet been determined. The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.
Pssm-ID: 239735 [Multi-domain] Cd Length: 181 Bit Score: 79.25 E-value: 4.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 1 MCGIWALFG--SDDCLSVQCLSAMK--IAHRGPDAFRFENVN-GYTNCCFGFHRLAVVDPLFGMQPIRVKKYPYLwLCYN 75
Cdd:cd03766 1 MCGILCSVSpsGPHINSSLLSEELLpnLRNRGPDYLSTRQLSvTNWTLLFTSSVLSLRGDHVTRQPLVDQSTGNV-LQWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 76 GEIYNHKKMQQhfefeyqTKVDGEIILHL-----YDKGGIEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPL-FKAM 149
Cdd:cd03766 80 GELYNIDGVED-------EENDTEVIFELlancsSESQDILDVLSSIEGPFAFIYYDASENKLYFGRDCLGRRSLlYKLD 152
|
170 180 190
....*....|....*....|....*....|
gi 168229248 150 TEDGFLAVCSeakglVTLKHSATPFLKVEP 179
Cdd:cd03766 153 PNGFELSISS-----VSGSSSGSGFQEVLA 177
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
56-167 |
8.19e-08 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 54.65 E-value: 8.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 56 LFGMQPIRVK-KYPYLWLCYNGEIYNHKKMQQHFEFE---YQTKVDGEIILHL---YDKGGIEQ----TICMLDGVFAFV 124
Cdd:PRK05793 97 LDNAQPLVANyKLGSIAIAHNGNLVNADVIRELLEDGgriFQTSIDSEVILNLiarSAKKGLEKalvdAIQAIKGSYALV 176
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 168229248 125 LLdTANKkvFLG-RDTYGVRPLFKAMTEDGFLaVCSEAKGLVTL 167
Cdd:PRK05793 177 IL-TEDK--LIGvRDPHGIRPLCLGKLGDDYI-LSSESCALDTI 216
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
60-160 |
3.99e-07 |
|
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; Glutamine phosphoribosylpyrophosphate amidotransferase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439804 [Multi-domain] Cd Length: 464 Bit Score: 52.72 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 60 QPIRVKkYPYLW--LCYNGEIYNHKKMQQHFE---FEYQTKVDGEIILHL----YDKGGIEQTIC----MLDGVFAFVLL 126
Cdd:COG0034 92 QPFYVN-SPFGSiaLAHNGNLTNAEELREELEeegAIFQTTSDTEVILHLiareLTKEDLEEAIKealrRVKGAYSLVIL 170
|
90 100 110
....*....|....*....|....*....|....
gi 168229248 127 DtaNKKVFLGRDTYGVRPLFKAMTEDGFlAVCSE 160
Cdd:COG0034 171 T--GDGLIAARDPNGIRPLVLGKLEDGY-VVASE 201
|
|
| DUF3700 |
pfam12481 |
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ... |
111-174 |
6.36e-05 |
|
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 amino acids in length. There are two conserved sequence motifs: YGL and LRDR. This family is related to GATase enzyme domains.
Pssm-ID: 403619 [Multi-domain] Cd Length: 228 Bit Score: 44.66 E-value: 6.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 168229248 111 EQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLaVCSEAKGLVT--LKHSATPF 174
Cdd:pfam12481 123 DQVVRDLEGKFAFVLYDSSTSTVFVASDADGSVPLYWGIDADGSL-VFSDDIEIVKkgCGKSFAPF 187
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
60-160 |
8.88e-05 |
|
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the N-terminus of glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase) . The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. GPATase crystalizes as a homotetramer, but can also exist as a homdimer.
Pssm-ID: 238367 [Multi-domain] Cd Length: 252 Bit Score: 44.37 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 60 QPIRVKkYP--YLWLCYNGEIYNHKKMQQ-------HFefeyQTKVDGEIILHL----YDKGGIEQTIC----MLDGVFA 122
Cdd:cd00715 85 QPFVVN-SPlgGIALAHNGNLVNAKELREeleeegrIF----QTTSDSEVILHLiarsLAKDDLFEAIIdaleRVKGAYS 159
|
90 100 110
....*....|....*....|....*....|....*...
gi 168229248 123 FVLLDtaNKKVFLGRDTYGVRPLFKAMTEDGFLAVCSE 160
Cdd:cd00715 160 LVIMT--ADGLIAVRDPHGIRPLVLGKLEGDGYVVASE 195
|
|
| Wali7 |
cd01910 |
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ... |
111-161 |
1.00e-04 |
|
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced by aluminum. Wali7 has a single domain similar to the glutamine amidotransferase domain of glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The Wali7 domain is also somewhat similar to the Ntn hydrolase fold of the proteasomal alph and beta subunits.
Pssm-ID: 238891 [Multi-domain] Cd Length: 224 Bit Score: 43.84 E-value: 1.00e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 168229248 111 EQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEA 161
Cdd:cd01910 119 DQVVKDLEGSFAFVLYDKKTSTVFVASDADGSVPLYWGIAADGSVVFSDDV 169
|
|
| MnmA_TRMU-like |
cd01998 |
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
252-318 |
1.26e-04 |
|
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.
Pssm-ID: 467502 [Multi-domain] Cd Length: 349 Bit Score: 44.42 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 252 RIGCLLSGGLDSSlVAATLLKqlkEAQVQYplqtFAIGM-----EDSP--------DLLAARKVADHIGSEHYEVLFNSE 318
Cdd:cd01998 1 KVAVAMSGGVDSS-VAAALLK---EQGYDV----IGVFMknwddEDNEkggccseeDIEDARRVADQLGIPLYVVDFSEE 72
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-160 |
1.36e-04 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 44.67 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 1 MCGIWALFGSDDCLSVQCLSAMKIAHRGPDA--------FRFENV--NGYTNCCFGFHRLAVVDPLFGMQPIR------- 63
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGagivtvdgNRLQSItgNGLVSDVFDESKLDQLPGDIAIGHVRystagas 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 64 --------VKKYPY--LWLCYNGEIYNHKKMQQHFEFE---YQTKVDGEIILHLYDKG-------GIEQTICMLDGVFAF 123
Cdd:PLN02440 81 slknvqpfVANYRFgsIGVAHNGNLVNYEELRAKLEENgsiFNTSSDTEVLLHLIAISkarpffsRIVDACEKLKGAYSM 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 168229248 124 VLLdtANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSE 160
Cdd:PLN02440 161 VFL--TEDKLVAVRDPHGFRPLVMGRRSNGAVVFASE 195
|
|
| QueC |
pfam06508 |
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ... |
255-313 |
3.32e-04 |
|
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis of 7-carboxy-7-deazaguanine. They catalyze the conversion of 7-deaza-7-carboxyguanine to preQ0.
Pssm-ID: 428982 [Multi-domain] Cd Length: 210 Bit Score: 42.22 E-value: 3.32e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 168229248 255 CLLSGGLDSSLVAATLLKQLKEAqvqYPLqTFAIGMEDSPDLLAARKVADHIGSEHYEV 313
Cdd:pfam06508 4 VLLSGGLDSTTCLAWAKKEGYEV---YAL-SFDYGQRHRKELECAKKIAKALGVEHKIL 58
|
|
| tRNA_Me_trans |
pfam03054 |
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ... |
251-315 |
1.29e-03 |
|
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.
Pssm-ID: 460787 [Multi-domain] Cd Length: 202 Bit Score: 40.31 E-value: 1.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 168229248 251 RRIGCLLSGGLDSSlVAATLLK----QLKEAQVQYPLQTFAIGMEDSP----DLLAARKVADHIGSEHYEVLF 315
Cdd:pfam03054 1 MKVVVAMSGGVDSS-VAAYLLKeqghNVIGVFMKNWDEEQSLDEEGKCcseeDLADAQRVCEQLGIPLYVVNF 72
|
|
| NAD_synthase |
cd00553 |
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ... |
257-313 |
1.71e-03 |
|
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: 40.23 E-value: 1.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 168229248 257 LSGGLDSSLVAATLLKQLKEAQVqyplqtFAIGM--EDSP--DLLAARKVADHIGSEHYEV 313
Cdd:cd00553 30 LSGGIDSAVVAALAVRALGAENV------LALIMpsRYSSkeTRDDAKALAENLGIEYRTI 84
|
|
| QueC |
COG0603 |
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ... |
255-313 |
7.92e-03 |
|
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; 7-cyano-7-deazaguanine synthase (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440368 [Multi-domain] Cd Length: 223 Bit Score: 38.22 E-value: 7.92e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 168229248 255 CLLSGGLDSSLVAATLLKQLKEAqvqYPLqTFAIG----MEdspdLLAARKVADHIGS-EHYEV 313
Cdd:COG0603 7 VLLSGGLDSTTCLAWALARGYEV---YAL-SFDYGqrhrKE----LEAARRIAKALGVgEHKVI 62
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
257-347 |
8.79e-03 |
|
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: 38.67 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 257 LSGGLDSSLVAATLLKQLKEAQVqyplqtFAIGM--EDSPD--LLAARKVADHIGSEHYEVlfNSEEGIQALDEVI---F 329
Cdd:COG0171 293 LSGGIDSALVAALAVDALGPENV------LGVTMpsRYTSDesLEDAEELAENLGIEYEEI--DITPAVEAFLEALphaF 364
|
90 100
....*....|....*....|....
gi 168229248 330 SLETYDITT------VRASVGMYL 347
Cdd:COG0171 365 GGELDDVAEenlqarIRMVILMAL 388
|
|
| CTU1-like |
cd01713 |
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ... |
252-328 |
9.65e-03 |
|
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human cytoplasmic tRNA 2-thiolation protein 1, also called cytosolic thiouridylase subunit 1 (CTU1), ATP-binding domain-containing protein 3 (ATPBD3), cancer-associated gene protein, or cytoplasmic tRNA adenylyltransferase 1. CTU1 plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). It directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. The CTU1-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.
Pssm-ID: 467486 Cd Length: 208 Bit Score: 37.57 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168229248 252 RIGCLLSGGLDSSlVAATLLKQLKEaQVQYPLQTFAI-------GMEDSpDLLAARKVADHIGSEHYEVLFNSEEGIqAL 324
Cdd:cd01713 20 RVAVGLSGGKDST-VLLYVLKELNK-RHDYGVELIAVtidegikGYRDD-SLEAARKLAEEYGIPLEIVSFEDEFGF-TL 95
|
....
gi 168229248 325 DEVI 328
Cdd:cd01713 96 DELI 99
|
|
| |
