|
Name |
Accession |
Description |
Interval |
E-value |
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-560 |
0e+00 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 534.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 1 MCGIWALFGSD---DCLSVQCLSAMK-IAHRGPDAfrfENVNGYTNCCFGFHRLAVVDPLFGMQPI--RVKKypyLWLCY 74
Cdd:PRK09431 1 MCGIFGILDIKtdaDELRKKALEMSRlMRHRGPDW---SGIYASDNAILGHERLSIVDVNGGAQPLynEDGT---HVLAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 75 NGEIYNYKKMQRHFE--FEYQTNVDGEIILHLYDKGGIEqTVCMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTED 152
Cdd:PRK09431 75 NGEIYNHQELRAELGdkYAFQTGSDCEVILALYQEKGPD-FLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 153 GFLAVCSEAKGLVtlkhsttPFLK-VEPFLPGHYevldLKPngkvASVEMVKYHHcRDEPLhalYDNVDklfpgfEIETV 231
Cdd:PRK09431 154 GNLYFASEMKALV-------PVCKtIKEFPPGHY----YWS----KDGEFVRYYQ-RDWFD---YDAVK------DNVTD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 232 KNNLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAA--------TLLKQLKEAQVQYPLQTFAIGMEDSPDLLAARKVA 303
Cdd:PRK09431 209 KNELRDALEAAVKKRLMSDVPYGVLLSGGLDSSLISAiakkyaarRIEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 304 NHIGSEHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIrKNTDNVVIFSGEGSDELTQGYIYFHKAPSP 383
Cdd:PRK09431 289 DHLGTVHHEIHFTVQEGLDALRDVIYHLETYDVTTIRASTPMYLMARKI-KAMGIKMVLSGEGADELFGGYLYFHKAPNA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 384 EEAEEESERLLRELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRTPKNG-IEKHLLRETFEesNLIPKEI 462
Cdd:PRK09431 368 KEFHEETVRKLRALHMYDCLRANKAMMAWGVEARVPFLDKEFLDVAMRINPEDKMCGNGkMEKHILREAFE--GYLPESI 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 463 LWRPKEAFSDGitsVKNSWFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQIFERHYPGRA--------DWLS 534
Cdd:PRK09431 446 LWRQKEQFSDG---VGYSWIDTLKEVAAEQVSDQQLATARFRFPYNTPTTKEAYLYREIFEELFPLPSaaecvpggPSVA 522
|
570 580 590
....*....|....*....|....*....|..
gi 1622925219 535 HYWMP------KWINATDPSARTLTHYKSAAK 560
Cdd:PRK09431 523 CSSAKaiewdeAFKNMDDPSGRAVSGVHQSAY 554
|
|
| 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: 520.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 4 IWALFGSDDCLSVQ---CLS-AMKIAHRGPDAFRFENvnGYTNCCFGFHRLAVVDPLFGMQPIRVKKyPYLWLCYNGEIY 79
Cdd:TIGR01536 1 IAGFFDLDDKAVEEdeaIKRmSDTIAHRGPDASGIEY--KDGNAILGHRRLAIIDLSGGAQPMSNEG-KTYVIVFNGEIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 80 NYKKMQRHFE---FEYQTNVDGEIILHLYDKGGiEQTVCMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMtEDGFLA 156
Cdd:TIGR01536 78 NHEELREELEakgYTFQTDSDTEVILHLYEEWG-EECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAY-DGGQLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 157 VCSEAKGLVTLKhSTTPFLKVEPFLPGHYEVLDlkPNGKVASVEMVKYHHCRDEPLHALYDNVDKL------FPGFEIET 230
Cdd:TIGR01536 156 FASEIKALLAHP-NIKPFPDGAALAPGFGFVRV--PPPSTFFRGVFELEPGHDLPLDDDGLNIERYywerrdEHTDSEED 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 231 VKNNLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEaqvqYPLQTFAIGMEDSPDLL---AARKVANHIG 307
Cdd:TIGR01536 233 LVDELRSLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPR----GPVHTFSIGFEGSPDFDeskYARKVADHLG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 308 SEHYEVLFNSEEGIQALDEVIFSLEtyDITTVRASVGMYLISKYIRKNTdNVVIFSGEGSDELTQGYIYFHKAPSPEEAE 387
Cdd:TIGR01536 309 TEHHEVLFSVEEGLDALPEVIYHLE--EPTTIRASIPLYLLSKLAREDG-VKVVLSGEGADELFGGYLYFHEAPAAEALR 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 388 EESERLLRELYLFDVLRA-DRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRTpKNGIEKHLLRETFEEsnLIPKEILWRP 466
Cdd:TIGR01536 386 EELQYLDLELYMPGLLRRkDRMSMAHSLEVRVPFLDHELVEYALSIPPEMKL-RDGKEKYLLREAFEG--YLPEEILWRP 462
|
....
gi 1622925219 467 KEAF 470
Cdd:TIGR01536 463 KEGF 466
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-559 |
1.48e-153 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 452.30 E-value: 1.48e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 1 MCGIWALFGSDDCLS-----VQCLSAmKIAHRGPDAFRFEnvnGYTNCCFGFHRLAVVDPLFGMQPIRVKKYPYLwLCYN 75
Cdd:PLN02549 1 MCGILAVLGCSDDSQakrsrVLELSR-RLRHRGPDWSGLY---GNEDCYLAHERLAIMDPESGDQPLYNEDKTIV-VTAN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 76 GEIYNYKKMQRHFE-FEYQTNVDGEIILHLYDKGGiEQTVCMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGF 154
Cdd:PLN02549 76 GEIYNHKELREKLKlHKFRTGSDCEVIAHLYEEHG-EEFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGLDGS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 155 LAVCSEAKGLVTlkhsttPFLKVEPFLPGHYEVLdlKPNGkvasveMVKYHhcrdEPlhalydnvdKLFPGFEIETVKN- 233
Cdd:PLN02549 155 VWFASEMKALCD------DCERFEEFPPGHYYSS--KAGG------FRRWY----NP---------PWFSESIPSTPYDp 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 234 -NLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQY----PLQTFAIGMEDSPDLLAARKVANHIGS 308
Cdd:PLN02549 208 lVLREAFEKAVIKRLMTDVPFGVLLSGGLDSSLVASIAARHLAETKAARqwgqQLHSFCVGLEGSPDLKAAREVADYLGT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 309 EHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIRKNTDNVVIfSGEGSDELTQGYIYFHKAPSPEEAEE 388
Cdd:PLN02549 288 VHHEFHFTVQEGIDAIEDVIYHLETYDVTTIRASTPMFLMSRKIKSLGVKMVL-SGEGSDEIFGGYLYFHKAPNKEEFHK 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 389 ESERLLRELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRTPKNG---IEKHLLRETF--EESNLIPKEIL 463
Cdd:PLN02549 367 ETCRKIKALHQYDCLRANKSTSAWGLEARVPFLDKEFIDVAMSIDPEWKMIRPGegrIEKWVLRKAFddEEDPYLPKHIL 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 464 WRPKEAFSDGitsVKNSWFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQIFERHYPGR-------------- 529
Cdd:PLN02549 447 WRQKEQFSDG---VGYSWIDGLKAHAEKHVSDEMFANASFRYPHNTPTTKEAYYYRMIFEKHFPQDaarltvpggpsvac 523
|
570 580 590
....*....|....*....|....*....|
gi 1622925219 530 ADWLSHYWMPKWINATDPSARTLTHYKSAA 559
Cdd:PLN02549 524 STAKAVEWDAAWSKNLDPSGRAALGVHVAA 553
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-560 |
1.63e-150 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 444.54 E-value: 1.63e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 1 MCGIWALFGSDDCLS-----VQCLSAmKIAHRGPDAFR---FENVNGYTNCcFGFHRLAVVDPLFGMQPIRVKKYPyLWL 72
Cdd:PTZ00077 1 MCGILAIFNSKGERHelrrkALELSK-RLRHRGPDWSGiivLENSPGTYNI-LAHERLAIVDLSDGKQPLLDDDET-VAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 73 CYNGEIYNYKKMQRHFE---FEYQTNVDGEIILHLYDKGGIEQTVCMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAM 149
Cdd:PTZ00077 78 MQNGEIYNHWEIRPELEkegYKFSSNSDCEIIGHLYKEYGPKDFWNHLDGMFATVIYDMKTNTFFAARDHIGIIPLYIGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 150 TEDGFLAVCSEAKGLvtlkhsTTPFLKVEPFLPGHYeVLDLKPNGkvasvEMVKYHHcrdeplhALYDNVDKLFPGFEIE 229
Cdd:PTZ00077 158 AKDGSIWFSSELKAL------HDQCVEVKQFPPGHY-YDQTKEKG-----EFVRYYN-------PNWHDFDHPIPTGEID 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 230 TVKnnLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQYP------LQTFAIGMEDSPDLLAARKVA 303
Cdd:PTZ00077 219 LEE--IREALEAAVRKRLMGDVPFGLFLSGGLDSSIVAAIVAKLIKNGEIDLSkrgmpkLHSFCIGLEGSPDLKAARKVA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 304 NHIGSEHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIrKNTDNVVIFSGEGSDELTQGYIYFHKAPSP 383
Cdd:PTZ00077 297 EYLGTEHHEFTFTVEEGIDALPDVIYHTETYDVTTIRASTPMYLLSRRI-KALGIKMVLSGEGSDELFGGYLYFHKAPNR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 384 EEAEEESERLLRELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRTPKNG---IEKHLLRETFE--ESNLI 458
Cdd:PTZ00077 376 EEFHRELVRKLHDLHKYDCLRANKATMAWGIEARVPFLDKDFLEYVMNIDPKYKMCNAFegqMEKYILRKAFEglEKPYL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 459 PKEILWRPKEAFSDGitsVKNSWFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQIFERHYPGRADWLS-HY- 536
Cdd:PTZ00077 456 PDEILWRQKEQFSDG---VGYSWIDGLKEYAEKKISDQEFSQASFLFPYNTPRTKEAYLYRQIFSKHFPSDSAALTvPYg 532
|
570 580 590
....*....|....*....|....*....|....*..
gi 1622925219 537 ------------WMPKWINATDPSART-LTHYKSAAK 560
Cdd:PTZ00077 533 psiacstekaleWDESFKKNTDESGRAvLSVHNDAKQ 569
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-538 |
3.80e-127 |
|
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: 383.80 E-value: 3.80e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 1 MCGIWALFGSDDCLSVQCLSAM--KIAHRGPDAFRFEnVNGytNCCFGFHRLAVVDP-LFGMQPIRVKKYPYlWLCYNGE 77
Cdd:COG0367 1 MCGIAGIIDFDGGADREVLERMldALAHRGPDGSGIW-VDG--GVALGHRRLSIIDLsEGGHQPMVSEDGRY-VLVFNGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 78 IYNYKK-----MQRHFEFeyQTNVDGEIILHLYDKGGiEQTVCMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTED 152
Cdd:COG0367 77 IYNYRElraelEALGHRF--RTHSDTEVILHAYEEWG-EDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 153 GFlAVCSEAKGLVTLKH---------------------STTPFLKVEPFLPGHYevLDLKPNGKVasvEMVKYHHCRDEP 211
Cdd:COG0367 154 GL-AFASELKALLAHPGvdreldpealaeyltlgyvpaPRTIFKGIRKLPPGHY--LTVDAGGEL---EIRRYWDLEFVP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 212 LHALYDnvdklfpgfeIETVKNNLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEaqvqyPLQTFAIGME 291
Cdd:COG0367 228 HERSDS----------EEEAVEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKG-----PLKTFSIGFE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 292 DSP--DLLAARKVANHIGSEHYEVLFNSEEGIQALDEVIFSLEtyDITTVRASVGMYLISKYIRKNtdnV-VIFSGEGSD 368
Cdd:COG0367 293 DSAydESPYARAVAEHLGTEHHEVTVTPEDLLDALPDLVWHLD--EPFADPSAVPTYLLSRLAREH---VkVVLSGEGAD 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 369 ELTQGYIYFHKAPSPEEAEEESERLLRE-----------------------LYLFDVL--RADRTTAAHGLELRVPFLDH 423
Cdd:COG0367 368 ELFGGYPRYREAALLLSPDFAEALGGELvprlyaesgaedplrrmlyldlkTYLPGDLlvKVDRMSMAHSLEVRVPFLDH 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 424 RFSSYYLSLPPEMRTpKNGIEKHLLRETFEesNLIPKEILWRPKEAFSDGItsvkNSWFK-ILQEYVEHQVDDAMManAA 502
Cdd:COG0367 448 RLVEFALSLPPELKL-RGGRGKYLLRKALE--GLLPDEVLDRPKQGFPVPL----GPWLRgPLREWLEDLLSDESL--AA 518
|
570 580 590
....*....|....*....|....*....|....*.
gi 1622925219 503 QKFpFNTpktkegYYYRQIFERHYPGRADWLSHYWM 538
Cdd:COG0367 519 RGL-FDP------DAVRRLLEEHLAGRRDHSRKLWS 547
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
234-538 |
2.01e-89 |
|
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: 276.81 E-value: 2.01e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 234 NLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEaqvqyPLQTFAIGME--DSPDLLAARKVANHIGSEHY 311
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSPS-----PLHTFSIGFEgrGYDEAPYAREVAEHLGTDHH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 312 EVLFNSEEGIQALDEVIFSLETydITTVRASVGMYLISKYIRKnTDNVVIFSGEGSDELTQGYIYFHKAPSPEEAEEESE 391
Cdd:pfam00733 76 ELVVTPEDLLDALPDVIWHLDE--PFADPSAIPLYLLSRLARR-KGVKVVLSGEGADELFGGYPFYKGEDPLRRMLYLDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 392 RLLrelYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRTpKNGIEKHLLRETFEesNLIPKEILWRPKEAFS 471
Cdd:pfam00733 153 KTL---LPGDLLRADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKL-RGGIEKYILREALE--GILPDEILERPKEGFS 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622925219 472 DGitsVKNSWFKI-LQEYVEHQVDDAmmanaaqkfpfntPKTKEGYYYRQIFERHYPGRADWLSHYWM 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 |
2.78e-72 |
|
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: 230.24 E-value: 2.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 249 TDRRIGCLLSGGLDSSLVAATLLKQLKEAqvqyPLQTFAIGMEDS--PDLLAARKVANHIGSEHYEVLFNSEEGIQALDE 326
Cdd:cd01991 1 SDVPVGVLLSGGLDSSLIAALAARLLPET----PIDLFTVGFEGSptPDRAAARRVAEELGTEHHEVEVTIEELLDALPD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 327 VIFSLETYDITTVRASVGMYLISKYIRKNTDNVVIfSGEGSDELTQGYIYFHKAPSPEEAEEESERLLREL--YLFDVLR 404
Cdd:cd01991 77 VILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVL-SGEGADELFGGYSRHRDAPLRGWEALEEELLRDLDrlWTRNLGR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 405 ADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRT-PKNGIEKHLLRETFEesNLIPKEILWRPKEAFSDG 473
Cdd:cd01991 156 DDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIdPRGGGEKYILREAAR--DLLPDEIAWRPKRAIQFG 223
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-206 |
6.18e-61 |
|
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: 200.48 E-value: 6.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 2 CGIWALFGSD---DCLSVQCLSAMKIAHRGPDAFRFENVNGytnCCFGFHRLAVVDPLFGMQPIRVKKyPYLWLCYNGEI 78
Cdd:cd00712 1 CGIAGIIGLDgasVDRATLERMLDALAHRGPDGSGIWIDEG---VALGHRRLSIIDLSGGAQPMVSED-GRLVLVFNGEI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 79 YNYKKMQRHFEFEY---QTNVDGEIILHLYDKGGiEQTVCMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTeDGFL 155
Cdd:cd00712 77 YNYRELRAELEALGhrfRTHSDTEVILHLYEEWG-EDCLERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGRD-GGGL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622925219 156 AVCSEAKGLVTLKHST---------------------TPFLKVEPFLPGHYEVLDLKPngkvasVEMVKYHH 206
Cdd:cd00712 155 AFASELKALLALPGVPreldeaalaeylafqyvpaprTIFKGIRKLPPGHYLTVDPGG------VEIRRYWD 220
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-185 |
1.44e-37 |
|
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: 138.35 E-value: 1.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 2 CGIWALFGSDDCLSVQCL----SAMKIAHRGPDAF------------------------RFENVNGYTNCCFGFHRLAVV 53
Cdd:cd00352 1 CGIFGIVGADGAASLLLLlllrGLAALEHRGPDGAgiavydgdglfvekragpvsdvalDLLDEPLKSGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 54 DP--LFGMQPIRVKKYPYlWLCYNGEIYNYKKMQRHFE---FEYQTNVDGEIILHLYDKGG--------IEQTVCMLDGV 120
Cdd:cd00352 81 GLpsEANAQPFRSEDGRI-ALVHNGEIYNYRELREELEargYRFEGESDSEVILHLLERLGregglfeaVEDALKRLDGP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622925219 121 FAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVTLkhsttPFLKVEPFLPGHY 185
Cdd:cd00352 160 FAFALWDGKPDRLFAARDRFGIRPLYYGITKDGGLVFASEPKALLAL-----PFKGVRRLPPGEL 219
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
49-164 |
1.21e-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: 118.39 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 49 RLAVVDPLFGMQPIRVKKYPYLWLCYNGEIYNYKKMQRHFE---FEYQTNVDGEIILHLYDKGGIEQTVCMLDGVFAFVL 125
Cdd:pfam13537 3 RLSIIDLEGGAQPMVSSEDGRYVIVFNGEIYNYRELRAELEakgYRFRTHSDTEVILHLYEAEWGEDCVDRLNGMFAFAI 82
|
90 100 110
....*....|....*....|....*....|....*....
gi 1622925219 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 |
1.52e-18 |
|
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: 81.97 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 29 PDAFRFEnvngYTNCC-FGFHRLAVVD-PLFGMQPIRVkkyPY--LWLCYNGEIYNYKKMQRHFE---FEYQTNVDGEII 101
Cdd:pfam13522 1 PDFSGIW----VEGGVaLGHVRLAIVDlPDAGNQPMLS---RDgrLVLVHNGEIYNYGELREELAdlgHAFRSRSDTEVL 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622925219 102 LHLYDKGGiEQTVCMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFL 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 |
1.61e-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: 80.41 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 1 MCGIWALFG--SDDCLSVQCLSAMK--IAHRGPDAFRFENVN-GYTNCCFGFHRLAVVDPLFGMQPIRVKKYPYLwLCYN 75
Cdd:cd03766 1 MCGILCSVSpsGPHINSSLLSEELLpnLRNRGPDYLSTRQLSvTNWTLLFTSSVLSLRGDHVTRQPLVDQSTGNV-LQWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 76 GEIYNYKKMqrhfefEYQTNvDGEIILHL-----YDKGGIEQTVCMLDGVFAFVLLDTANKKVFLGRDTYGVRPL-FKAM 149
Cdd:cd03766 80 GELYNIDGV------EDEEN-DTEVIFELlancsSESQDILDVLSSIEGPFAFIYYDASENKLYFGRDCLGRRSLlYKLD 152
|
170 180 190
....*....|....*....|....*....|
gi 1622925219 150 TEDGFLAVCSeakglVTLKHSTTPFLKVEP 179
Cdd:cd03766 153 PNGFELSISS-----VSGSSSGSGFQEVLA 177
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
60-160 |
1.90e-08 |
|
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: 56.95 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 60 QPIRVKkYPYLW--LCYNGEIYNYKKMQRHFE---FEYQTNVDGEIILHL----YDKGGIEQTVC----MLDGVFAFVLL 126
Cdd:COG0034 92 QPFYVN-SPFGSiaLAHNGNLTNAEELREELEeegAIFQTTSDTEVILHLiareLTKEDLEEAIKealrRVKGAYSLVIL 170
|
90 100 110
....*....|....*....|....*....|....
gi 1622925219 127 DtaNKKVFLGRDTYGVRPLFKAMTEDGFlAVCSE 160
Cdd:COG0034 171 T--GDGLIAARDPNGIRPLVLGKLEDGY-VVASE 201
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
56-167 |
7.98e-08 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 55.04 E-value: 7.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 56 LFGMQPIRVK-KYPYLWLCYNGEIYNYKKMQRHFEFE---YQTNVDGEIILHL---YDKGGIEQTV--CMLD--GVFAFV 124
Cdd:PRK05793 97 LDNAQPLVANyKLGSIAIAHNGNLVNADVIRELLEDGgriFQTSIDSEVILNLiarSAKKGLEKALvdAIQAikGSYALV 176
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622925219 125 LLdTANKkvFLG-RDTYGVRPLFKAMTEDGFLaVCSEAKGLVTL 167
Cdd:PRK05793 177 IL-TEDK--LIGvRDPHGIRPLCLGKLGDDYI-LSSESCALDTI 216
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
60-160 |
1.63e-06 |
|
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: 49.77 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 60 QPIRVKkYP--YLWLCYNGEIYNYKKMQ-------RHFefeyQTNVDGEIILHL----YDKG----GIEQTVCMLDGVFA 122
Cdd:cd00715 85 QPFVVN-SPlgGIALAHNGNLVNAKELReeleeegRIF----QTTSDSEVILHLiarsLAKDdlfeAIIDALERVKGAYS 159
|
90 100 110
....*....|....*....|....*....|....*...
gi 1622925219 123 FVLLDtaNKKVFLGRDTYGVRPLFKAMTEDGFLAVCSE 160
Cdd:cd00715 160 LVIMT--ADGLIAVRDPHGIRPLVLGKLEGDGYVVASE 195
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-160 |
9.20e-06 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 48.14 E-value: 9.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 1 MCGIWALFGSDDCLSVQCLSAMKIAHRGPDA--------FRFENV--NGYTNCCFGFHRLAVVDPLFGMQPIR------- 63
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGagivtvdgNRLQSItgNGLVSDVFDESKLDQLPGDIAIGHVRystagas 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 64 --------VKKYPY--LWLCYNGEIYNYKKMQ-------RHFefeyQTNVDGEIILHLYDKG-------GIEQTVCMLDG 119
Cdd:PLN02440 81 slknvqpfVANYRFgsIGVAHNGNLVNYEELRakleengSIF----NTSSDTEVLLHLIAISkarpffsRIVDACEKLKG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622925219 120 VFAFVLLdtANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSE 160
Cdd:PLN02440 157 AYSMVFL--TEDKLVAVRDPHGFRPLVMGRRSNGAVVFASE 195
|
|
| DUF3700 |
pfam12481 |
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ... |
48-174 |
2.24e-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: 45.82 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 48 HRL-AVVDPLFGMqpirvkkypylwlcYNGEIYNYKKMQRHFEFEYQTNvdgEIIL------HLYDKG--GIEQTVCMLD 118
Cdd:pfam12481 68 PRLfAVVDDIFCL--------------FQGHLENLASLKQQYGLSKGAN---EAMIvieayrTLRDRGpyPADQVVRDLE 130
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622925219 119 GVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLaVCSEAKGLVT--LKHSTTPF 174
Cdd:pfam12481 131 GKFAFVLYDSSTSTVFVASDADGSVPLYWGIDADGSL-VFSDDIEIVKkgCGKSFAPF 187
|
|
| Wali7 |
cd01910 |
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ... |
111-161 |
4.24e-05 |
|
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: 44.99 E-value: 4.24e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1622925219 111 EQTVCMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEA 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 |
2.26e-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: 43.65 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925219 252 RIGCLLSGGLDSSlVAATLLKqlkEAQVQYplqtFAIGM-----EDSP--------DLLAARKVANHIGSEHYEVLFNSE 318
Cdd:cd01998 1 KVAVAMSGGVDSS-VAAALLK---EQGYDV----IGVFMknwddEDNEkggccseeDIEDARRVADQLGIPLYVVDFSEE 72
|
|
| QueC |
pfam06508 |
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ... |
255-313 |
6.21e-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: 41.45 E-value: 6.21e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622925219 255 CLLSGGLDSSLVAATLLKQLKEAqvqYPLqTFAIGMEDSPDLLAARKVANHIGSEHYEV 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 |
1.27e-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: 1.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622925219 251 RRIGCLLSGGLDSSlVAATLLK----QLKEAQVQYPLQTFAIGMEDSP----DLLAARKVANHIGSEHYEVLF 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 |
2.11e-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: 2.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622925219 257 LSGGLDSSLVAATLLKQLKEAQVqyplqtFAIGM--EDSP--DLLAARKVANHIGSEHYEV 313
Cdd:cd00553 30 LSGGIDSAVVAALAVRALGAENV------LALIMpsRYSSkeTRDDAKALAENLGIEYRTI 84
|
|
| |
