|
Name |
Accession |
Description |
Interval |
E-value |
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-554 |
0e+00 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 1148.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 1 MCSVFGILDIKSDAAALRPIALEMSKKLRHRGPDWSGIYSSERAILAHERLAIVGLNSGAQPLYSPDKKLILAVNGEIYN 80
Cdd:PRK09431 1 MCGIFGILDIKTDADELRKKALEMSRLMRHRGPDWSGIYASDNAILGHERLSIVDVNGGAQPLYNEDGTHVLAVNGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 81 HKEIRARYEGKYEFQTDSDCEVILALYQDMGADLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYQGYDEHGNYYVAS 160
Cdd:PRK09431 81 HQELRAELGDKYAFQTGSDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGNLYFAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 161 EMKALVPVCKTVSEFPPGSHYSSKDAEPQRYYIRDWNEYAAVQGNSTSKEELTEALEAAVKRQLMTDVPYGVLLSGGLDS 240
Cdd:PRK09431 161 EMKALVPVCKTIKEFPPGHYYWSKDGEFVRYYQRDWFDYDAVKDNVTDKNELRDALEAAVKKRLMSDVPYGVLLSGGLDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 241 SITSAVAKRYAAMRIEDDEKSEAWWPQLHSFAVGLEGAPDLKAAREVAEKIGTVHHEMTYTIQEGLDAIRDVIYHIETYD 320
Cdd:PRK09431 241 SLISAIAKKYAARRIEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVADHLGTVHHEIHFTVQEGLDALRDVIYHLETYD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 321 VTTIRASTPMFLMGRKIKAMGIKMVLSGEGADEIFGGYLYFHKAPNAKEFHEETVRKLLALNMFDCARANKSLAAWGVEG 400
Cdd:PRK09431 321 VTTIRASTPMYLMARKIKAMGIKMVLSGEGADELFGGYLYFHKAPNAKEFHEETVRKLRALHMYDCLRANKAMMAWGVEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 401 RVPFLDKEFIDVAMRLNPADKMCGNGKMEKHILRECFEHYLPDSIAWRQKEQFSDGVGYSWIDTLKAVAEEKVTDQQMET 480
Cdd:PRK09431 401 RVPFLDKEFLDVAMRINPEDKMCGNGKMEKHILREAFEGYLPESILWRQKEQFSDGVGYSWIDTLKEVAAEQVSDQQLAT 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1796992097 481 AQYRFPYNTPTTKEGYVYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDESFKNCVDPSGRAVQTVHNDAY 554
Cdd:PRK09431 481 ARFRFPYNTPTTKEAYLYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDEAFKNMDDPSGRAVSGVHQSAY 554
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-453 |
3.48e-177 |
|
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: 508.03 E-value: 3.48e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 4 VFGILDIKSDAAALRPIALEMSKKLRHRGPDWSGI-YSSERAILAHERLAIVGLNSGAQPLYSPDKKLILAVNGEIYNHK 82
Cdd:TIGR01536 1 IAGFFDLDDKAVEEDEAIKRMSDTIAHRGPDASGIeYKDGNAILGHRRLAIIDLSGGAQPMSNEGKTYVIVFNGEIYNHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 83 EIRARYEGK-YEFQTDSDCEVILALYQDMGADLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYQGYDeHGNYYVASE 161
Cdd:TIGR01536 81 ELREELEAKgYTFQTDSDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYD-GGQLYFASE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 162 MKALVPVCkTVSEFPPGSHYSSKDAE----PQRYYIRDWNEYAAVQGNS------------------------TSKEELT 213
Cdd:TIGR01536 160 IKALLAHP-NIKPFPDGAALAPGFGFvrvpPPSTFFRGVFELEPGHDLPldddglnieryywerrdehtdseeDLVDELR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 214 EALEAAVKRQLMTDVPYGVLLSGGLDSSITSAVAKRYAAMrieddekseawwPQLHSFAVGLEGAPDL---KAAREVAEK 290
Cdd:TIGR01536 239 SLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPR------------GPVHTFSIGFEGSPDFdesKYARKVADH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 291 IGTVHHEMTYTIQEGLDAIRDVIYHIEtyDVTTIRASTPMFLMGRKIKAMGIKMVLSGEGADEIFGGYLYFHKAPNAKEF 370
Cdd:TIGR01536 307 LGTEHHEVLFSVEEGLDALPEVIYHLE--EPTTIRASIPLYLLSKLAREDGVKVVLSGEGADELFGGYLYFHEAPAAEAL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 371 HEETVRKLLALNMFDCARAN-KSLAAWGVEGRVPFLDKEFIDVAMRLNPADKMcgNGKMEKHILRECFEHYLPDSIAWRQ 449
Cdd:TIGR01536 385 REELQYLDLELYMPGLLRRKdRMSMAHSLEVRVPFLDHELVEYALSIPPEMKL--RDGKEKYLLREAFEGYLPEEILWRP 462
|
....
gi 1796992097 450 KEQF 453
Cdd:TIGR01536 463 KEGF 466
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-507 |
1.93e-175 |
|
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: 507.07 E-value: 1.93e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 1 MCSVFGILDIksDAAALRPIALEMSKKLRHRGPDWSGIYSSERAILAHERLAIVGL-NSGAQPLYSPDKKLILAVNGEIY 79
Cdd:COG0367 1 MCGIAGIIDF--DGGADREVLERMLDALAHRGPDGSGIWVDGGVALGHRRLSIIDLsEGGHQPMVSEDGRYVLVFNGEIY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 80 NHKEIRARYEGK-YEFQTDSDCEVILALYQDMGADLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYQGYDEhGNYYV 158
Cdd:COG0367 79 NYRELRAELEALgHRFRTHSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDG-GGLAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 159 ASEMKALVP---------------------------VCKTVSEFPPGSHYSSKD---AEPQRYYIRDWNEYAAVQGNSTS 208
Cdd:COG0367 158 ASELKALLAhpgvdreldpealaeyltlgyvpaprtIFKGIRKLPPGHYLTVDAggeLEIRRYWDLEFVPHERSDSEEEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 209 KEELTEALEAAVKRQLMTDVPYGVLLSGGLDSSITSAVAKRYAAmrieddekseawwPQLHSFAVGLEGAP--DLKAARE 286
Cdd:COG0367 238 VEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSK-------------GPLKTFSIGFEDSAydESPYARA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 287 VAEKIGTVHHEMTYTIQEGLDAIRDVIYHIEtyDVTTIRASTPMFLMGRKIKAMgIKMVLSGEGADEIFGGYLYFHKAPN 366
Cdd:COG0367 305 VAEHLGTEHHEVTVTPEDLLDALPDLVWHLD--EPFADPSAVPTYLLSRLAREH-VKVVLSGEGADELFGGYPRYREAAL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 367 AKE-------------------FHEETVRKLLALNMF------DCARANKSLAAWGVEGRVPFLDKEFIDVAMRLNPADK 421
Cdd:COG0367 382 LLSpdfaealggelvprlyaesGAEDPLRRMLYLDLKtylpgdLLVKVDRMSMAHSLEVRVPFLDHRLVEFALSLPPELK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 422 McgNGKMEKHILRECFEHYLPDSIAWRQKEQFSDGVGySWID-TLKAVAEEKVTDQQMETAQYrfpYNTpttkegYVYRE 500
Cdd:COG0367 462 L--RGGRGKYLLRKALEGLLPDEVLDRPKQGFPVPLG-PWLRgPLREWLEDLLSDESLAARGL---FDP------DAVRR 529
|
....*..
gi 1796992097 501 IFEELFP 507
Cdd:COG0367 530 LLEEHLA 536
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
211-512 |
6.91e-108 |
|
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: 324.18 E-value: 6.91e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 211 ELTEALEAAVKRQLMTDVPYGVLLSGGLDSSITSAVAKRYAAmrieddekseawwPQLHSFAVGLEGA--PDLKAAREVA 288
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSP-------------SPLHTFSIGFEGRgyDEAPYAREVA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 289 EKIGTVHHEMTYTIQEGLDAIRDVIYHIETydVTTIRASTPMFLMGRKIKAMGIKMVLSGEGADEIFGGYLYFHkapNAK 368
Cdd:pfam00733 68 EHLGTDHHELVVTPEDLLDALPDVIWHLDE--PFADPSAIPLYLLSRLARRKGVKVVLSGEGADELFGGYPFYK---GED 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 369 EFHEETVRKLLALNMFDCARANKSLAAWGVEGRVPFLDKEFIDVAMRLNPADKMCGNgkMEKHILRECFEHYLPDSIAWR 448
Cdd:pfam00733 143 PLRRMLYLDLKTLLPGDLLRADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKLRGG--IEKYILREALEGILPDEILER 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1796992097 449 QKEQFSDGVGYSWID-TLKAVAEEKVTDQqmetaqyrfpyntPTTKEGYVYREIFEELFPLPSAA 512
Cdd:pfam00733 221 PKEGFSAPVGDWKLRgPLRELAEDLLSDS-------------RLAKEGLLDREAVRELLDEHLAG 272
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
226-457 |
1.09e-88 |
|
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: 272.61 E-value: 1.09e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 226 TDVPYGVLLSGGLDSSITSAVAKRYAAMrieddekseawwPQLHSFAVGLEG--APDLKAAREVAEKIGTVHHEMTYTIQ 303
Cdd:cd01991 1 SDVPVGVLLSGGLDSSLIAALAARLLPE------------TPIDLFTVGFEGspTPDRAAARRVAEELGTEHHEVEVTIE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 304 EGLDAIRDVIYHIETYDVTTIRASTPMFLMGRKIKAMGIKMVLSGEGADEIFGGYLYFHKAPNA--KEFHEETVRKLLAL 381
Cdd:cd01991 69 ELLDALPDVILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVLSGEGADELFGGYSRHRDAPLRgwEALEEELLRDLDRL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1796992097 382 NMFDCARANKSLAAWGVEGRVPFLDKEFIDVAMRLNPADKMCGNGKMEKHILRECFEHYLPDSIAWRQKEQFSDGV 457
Cdd:cd01991 149 WTRNLGRDDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIDPRGGGEKYILREAARDLLPDEIAWRPKRAIQFGS 224
|
|
| lass_lactam_cya |
NF033535 |
lasso peptide isopeptide bond-forming cyclase; Members of this family are the isopeptide ... |
1-271 |
9.82e-25 |
|
lasso peptide isopeptide bond-forming cyclase; Members of this family are the isopeptide bond-forming cyclase of lasso peptide biosynthesis systems, from a subgroup that contains primarily cyanobacterial examples. These proteins resemble the glutamine-hydrolyzing asparagine synthase AsnB (EC 6.3.5.4).
Pssm-ID: 468066 [Multi-domain] Cd Length: 668 Bit Score: 108.54 E-value: 9.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 1 MCSVFGILDIKS---DAAALRPialeMSKKLRHRGPDWSGIYSSERAILAH-------ERLaivglnSGAQPLYSPDKKL 70
Cdd:NF033535 1 MSGIVGIYYLDGrpvDREDLQQ----MVDILAHRGPDGADIWCEGSVGLGHrmlwttpESL------LEKLPLVNQTGDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 71 ILAVNGEIYNHKEIRARYEGKY---EFQTDSdcEVILALYQDMGADLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLY 147
Cdd:NF033535 71 VITADARIDNRDELISALQLNNcppEKITDS--QLILAAYEKWGEQCPEHLLGDFAFAIWDKRKQQLFCARDHFGVKPFY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 148 qgYDEHGN-YYVASEMKAL-----VPVC----------------KTVSEF------PPGsHY---SSKDAEPQRYYIRDW 196
Cdd:NF033535 149 --YYQSDKrFAFASEIKALlclpeVPRRlnevriadylalmledKVITFYqdifrlPPA-HSmtvSQSGLQIRSYWSLDP 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1796992097 197 NEYAAVQGNSTSKEELTEALEAAVKRQLMTDVPYGVLLSGGLDSSITSAVAKryaamRIEDDEKSeawwPQLHSF 271
Cdd:NF033535 226 SRELRLDSDEEYAEAFREIFTEAVRCRLRSAFPVGSHLSGGLDSSSITCVAR-----QLLAEEKK----APLHTF 291
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-554 |
0e+00 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 1148.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 1 MCSVFGILDIKSDAAALRPIALEMSKKLRHRGPDWSGIYSSERAILAHERLAIVGLNSGAQPLYSPDKKLILAVNGEIYN 80
Cdd:PRK09431 1 MCGIFGILDIKTDADELRKKALEMSRLMRHRGPDWSGIYASDNAILGHERLSIVDVNGGAQPLYNEDGTHVLAVNGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 81 HKEIRARYEGKYEFQTDSDCEVILALYQDMGADLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYQGYDEHGNYYVAS 160
Cdd:PRK09431 81 HQELRAELGDKYAFQTGSDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGNLYFAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 161 EMKALVPVCKTVSEFPPGSHYSSKDAEPQRYYIRDWNEYAAVQGNSTSKEELTEALEAAVKRQLMTDVPYGVLLSGGLDS 240
Cdd:PRK09431 161 EMKALVPVCKTIKEFPPGHYYWSKDGEFVRYYQRDWFDYDAVKDNVTDKNELRDALEAAVKKRLMSDVPYGVLLSGGLDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 241 SITSAVAKRYAAMRIEDDEKSEAWWPQLHSFAVGLEGAPDLKAAREVAEKIGTVHHEMTYTIQEGLDAIRDVIYHIETYD 320
Cdd:PRK09431 241 SLISAIAKKYAARRIEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVADHLGTVHHEIHFTVQEGLDALRDVIYHLETYD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 321 VTTIRASTPMFLMGRKIKAMGIKMVLSGEGADEIFGGYLYFHKAPNAKEFHEETVRKLLALNMFDCARANKSLAAWGVEG 400
Cdd:PRK09431 321 VTTIRASTPMYLMARKIKAMGIKMVLSGEGADELFGGYLYFHKAPNAKEFHEETVRKLRALHMYDCLRANKAMMAWGVEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 401 RVPFLDKEFIDVAMRLNPADKMCGNGKMEKHILRECFEHYLPDSIAWRQKEQFSDGVGYSWIDTLKAVAEEKVTDQQMET 480
Cdd:PRK09431 401 RVPFLDKEFLDVAMRINPEDKMCGNGKMEKHILREAFEGYLPESILWRQKEQFSDGVGYSWIDTLKEVAAEQVSDQQLAT 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1796992097 481 AQYRFPYNTPTTKEGYVYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDESFKNCVDPSGRAVQTVHNDAY 554
Cdd:PRK09431 481 ARFRFPYNTPTTKEAYLYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDEAFKNMDDPSGRAVSGVHQSAY 554
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-554 |
0e+00 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 821.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 1 MCSVFGILDIKSDAAALRPIALEMSKKLRHRGPDWSGIYSSERA-----ILAHERLAIVGLNSGAQPLYSPDKKLILAVN 75
Cdd:PTZ00077 1 MCGILAIFNSKGERHELRRKALELSKRLRHRGPDWSGIIVLENSpgtynILAHERLAIVDLSDGKQPLLDDDETVALMQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 76 GEIYNHKEIRARYEGK-YEFQTDSDCEVILALYQDMGA-DLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYQGYDEH 153
Cdd:PTZ00077 81 GEIYNHWEIRPELEKEgYKFSSNSDCEIIGHLYKEYGPkDFWNHLDGMFATVIYDMKTNTFFAARDHIGIIPLYIGYAKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 154 GNYYVASEMKALVPVCKTVSEFPPGSHYSS--KDAEPQRYYIRDW-NEYAAVQGNSTSKEELTEALEAAVKRQLMTDVPY 230
Cdd:PTZ00077 161 GSIWFSSELKALHDQCVEVKQFPPGHYYDQtkEKGEFVRYYNPNWhDFDHPIPTGEIDLEEIREALEAAVRKRLMGDVPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 231 GVLLSGGLDSSITSAVAKRYAamRIEDDEKSEAWWPQLHSFAVGLEGAPDLKAAREVAEKIGTVHHEMTYTIQEGLDAIR 310
Cdd:PTZ00077 241 GLFLSGGLDSSIVAAIVAKLI--KNGEIDLSKRGMPKLHSFCIGLEGSPDLKAARKVAEYLGTEHHEFTFTVEEGIDALP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 311 DVIYHIETYDVTTIRASTPMFLMGRKIKAMGIKMVLSGEGADEIFGGYLYFHKAPNAKEFHEETVRKLLALNMFDCARAN 390
Cdd:PTZ00077 319 DVIYHTETYDVTTIRASTPMYLLSRRIKALGIKMVLSGEGSDELFGGYLYFHKAPNREEFHRELVRKLHDLHKYDCLRAN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 391 KSLAAWGVEGRVPFLDKEFIDVAMRLNPADKMC--GNGKMEKHILRECFE----HYLPDSIAWRQKEQFSDGVGYSWIDT 464
Cdd:PTZ00077 399 KATMAWGIEARVPFLDKDFLEYVMNIDPKYKMCnaFEGQMEKYILRKAFEglekPYLPDEILWRQKEQFSDGVGYSWIDG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 465 LKAVAEEKVTDQQMETAQYRFPYNTPTTKEGYVYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDESFKNCVDPSGR 544
Cdd:PTZ00077 479 LKEYAEKKISDQEFSQASFLFPYNTPRTKEAYLYRQIFSKHFPSDSAALTVPYGPSIACSTEKALEWDESFKKNTDESGR 558
|
570
....*....|
gi 1796992097 545 AVQTVHNDAY 554
Cdd:PTZ00077 559 AVLSVHNDAK 568
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-554 |
0e+00 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 815.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 1 MCSVFGILDIKSDAAALRPIALEMSKKLRHRGPDWSGIYSSERAILAHERLAIVGLNSGAQPLYSPDKKLILAVNGEIYN 80
Cdd:PLN02549 1 MCGILAVLGCSDDSQAKRSRVLELSRRLRHRGPDWSGLYGNEDCYLAHERLAIMDPESGDQPLYNEDKTIVVTANGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 81 HKEIRARYeGKYEFQTDSDCEVILALYQDMGADLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYQGYDEHGNYYVAS 160
Cdd:PLN02549 81 HKELREKL-KLHKFRTGSDCEVIAHLYEEHGEEFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGLDGSVWFAS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 161 EMKALVPVCKTVSEFPPGSHYSSKDAEPQRYYIRDW-NEYAAVQGNSTSkeELTEALEAAVKRQLMTDVPYGVLLSGGLD 239
Cdd:PLN02549 160 EMKALCDDCERFEEFPPGHYYSSKAGGFRRWYNPPWfSESIPSTPYDPL--VLREAFEKAVIKRLMTDVPFGVLLSGGLD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 240 SSITSAVAKRYaamrIEDDEKSEAWWPQLHSFAVGLEGAPDLKAAREVAEKIGTVHHEMTYTIQEGLDAIRDVIYHIETY 319
Cdd:PLN02549 238 SSLVASIAARH----LAETKAARQWGQQLHSFCVGLEGSPDLKAAREVADYLGTVHHEFHFTVQEGIDAIEDVIYHLETY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 320 DVTTIRASTPMFLMGRKIKAMGIKMVLSGEGADEIFGGYLYFHKAPNAKEFHEETVRKLLALNMFDCARANKSLAAWGVE 399
Cdd:PLN02549 314 DVTTIRASTPMFLMSRKIKSLGVKMVLSGEGSDEIFGGYLYFHKAPNKEEFHKETCRKIKALHQYDCLRANKSTSAWGLE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 400 GRVPFLDKEFIDVAMRLNPADKMC--GNGKMEKHILRECFE----HYLPDSIAWRQKEQFSDGVGYSWIDTLKAVAEEKV 473
Cdd:PLN02549 394 ARVPFLDKEFIDVAMSIDPEWKMIrpGEGRIEKWVLRKAFDdeedPYLPKHILWRQKEQFSDGVGYSWIDGLKAHAEKHV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 474 TDQQMETAQYRFPYNTPTTKEGYVYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDESFKNCVDPSGRAVQTVHNDA 553
Cdd:PLN02549 474 SDEMFANASFRYPHNTPTTKEAYYYRMIFEKHFPQDAARLTVPGGPSVACSTAKAVEWDAAWSKNLDPSGRAALGVHVAA 553
|
.
gi 1796992097 554 Y 554
Cdd:PLN02549 554 Y 554
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-453 |
3.48e-177 |
|
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: 508.03 E-value: 3.48e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 4 VFGILDIKSDAAALRPIALEMSKKLRHRGPDWSGI-YSSERAILAHERLAIVGLNSGAQPLYSPDKKLILAVNGEIYNHK 82
Cdd:TIGR01536 1 IAGFFDLDDKAVEEDEAIKRMSDTIAHRGPDASGIeYKDGNAILGHRRLAIIDLSGGAQPMSNEGKTYVIVFNGEIYNHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 83 EIRARYEGK-YEFQTDSDCEVILALYQDMGADLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYQGYDeHGNYYVASE 161
Cdd:TIGR01536 81 ELREELEAKgYTFQTDSDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYD-GGQLYFASE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 162 MKALVPVCkTVSEFPPGSHYSSKDAE----PQRYYIRDWNEYAAVQGNS------------------------TSKEELT 213
Cdd:TIGR01536 160 IKALLAHP-NIKPFPDGAALAPGFGFvrvpPPSTFFRGVFELEPGHDLPldddglnieryywerrdehtdseeDLVDELR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 214 EALEAAVKRQLMTDVPYGVLLSGGLDSSITSAVAKRYAAMrieddekseawwPQLHSFAVGLEGAPDL---KAAREVAEK 290
Cdd:TIGR01536 239 SLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPR------------GPVHTFSIGFEGSPDFdesKYARKVADH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 291 IGTVHHEMTYTIQEGLDAIRDVIYHIEtyDVTTIRASTPMFLMGRKIKAMGIKMVLSGEGADEIFGGYLYFHKAPNAKEF 370
Cdd:TIGR01536 307 LGTEHHEVLFSVEEGLDALPEVIYHLE--EPTTIRASIPLYLLSKLAREDGVKVVLSGEGADELFGGYLYFHEAPAAEAL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 371 HEETVRKLLALNMFDCARAN-KSLAAWGVEGRVPFLDKEFIDVAMRLNPADKMcgNGKMEKHILRECFEHYLPDSIAWRQ 449
Cdd:TIGR01536 385 REELQYLDLELYMPGLLRRKdRMSMAHSLEVRVPFLDHELVEYALSIPPEMKL--RDGKEKYLLREAFEGYLPEEILWRP 462
|
....
gi 1796992097 450 KEQF 453
Cdd:TIGR01536 463 KEGF 466
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-507 |
1.93e-175 |
|
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: 507.07 E-value: 1.93e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 1 MCSVFGILDIksDAAALRPIALEMSKKLRHRGPDWSGIYSSERAILAHERLAIVGL-NSGAQPLYSPDKKLILAVNGEIY 79
Cdd:COG0367 1 MCGIAGIIDF--DGGADREVLERMLDALAHRGPDGSGIWVDGGVALGHRRLSIIDLsEGGHQPMVSEDGRYVLVFNGEIY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 80 NHKEIRARYEGK-YEFQTDSDCEVILALYQDMGADLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYQGYDEhGNYYV 158
Cdd:COG0367 79 NYRELRAELEALgHRFRTHSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDG-GGLAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 159 ASEMKALVP---------------------------VCKTVSEFPPGSHYSSKD---AEPQRYYIRDWNEYAAVQGNSTS 208
Cdd:COG0367 158 ASELKALLAhpgvdreldpealaeyltlgyvpaprtIFKGIRKLPPGHYLTVDAggeLEIRRYWDLEFVPHERSDSEEEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 209 KEELTEALEAAVKRQLMTDVPYGVLLSGGLDSSITSAVAKRYAAmrieddekseawwPQLHSFAVGLEGAP--DLKAARE 286
Cdd:COG0367 238 VEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSK-------------GPLKTFSIGFEDSAydESPYARA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 287 VAEKIGTVHHEMTYTIQEGLDAIRDVIYHIEtyDVTTIRASTPMFLMGRKIKAMgIKMVLSGEGADEIFGGYLYFHKAPN 366
Cdd:COG0367 305 VAEHLGTEHHEVTVTPEDLLDALPDLVWHLD--EPFADPSAVPTYLLSRLAREH-VKVVLSGEGADELFGGYPRYREAAL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 367 AKE-------------------FHEETVRKLLALNMF------DCARANKSLAAWGVEGRVPFLDKEFIDVAMRLNPADK 421
Cdd:COG0367 382 LLSpdfaealggelvprlyaesGAEDPLRRMLYLDLKtylpgdLLVKVDRMSMAHSLEVRVPFLDHRLVEFALSLPPELK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 422 McgNGKMEKHILRECFEHYLPDSIAWRQKEQFSDGVGySWID-TLKAVAEEKVTDQQMETAQYrfpYNTpttkegYVYRE 500
Cdd:COG0367 462 L--RGGRGKYLLRKALEGLLPDEVLDRPKQGFPVPLG-PWLRgPLREWLEDLLSDESLAARGL---FDP------DAVRR 529
|
....*..
gi 1796992097 501 IFEELFP 507
Cdd:COG0367 530 LLEEHLA 536
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
211-512 |
6.91e-108 |
|
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: 324.18 E-value: 6.91e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 211 ELTEALEAAVKRQLMTDVPYGVLLSGGLDSSITSAVAKRYAAmrieddekseawwPQLHSFAVGLEGA--PDLKAAREVA 288
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSP-------------SPLHTFSIGFEGRgyDEAPYAREVA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 289 EKIGTVHHEMTYTIQEGLDAIRDVIYHIETydVTTIRASTPMFLMGRKIKAMGIKMVLSGEGADEIFGGYLYFHkapNAK 368
Cdd:pfam00733 68 EHLGTDHHELVVTPEDLLDALPDVIWHLDE--PFADPSAIPLYLLSRLARRKGVKVVLSGEGADELFGGYPFYK---GED 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 369 EFHEETVRKLLALNMFDCARANKSLAAWGVEGRVPFLDKEFIDVAMRLNPADKMCGNgkMEKHILRECFEHYLPDSIAWR 448
Cdd:pfam00733 143 PLRRMLYLDLKTLLPGDLLRADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKLRGG--IEKYILREALEGILPDEILER 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1796992097 449 QKEQFSDGVGYSWID-TLKAVAEEKVTDQqmetaqyrfpyntPTTKEGYVYREIFEELFPLPSAA 512
Cdd:pfam00733 221 PKEGFSAPVGDWKLRgPLRELAEDLLSDS-------------RLAKEGLLDREAVRELLDEHLAG 272
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
226-457 |
1.09e-88 |
|
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: 272.61 E-value: 1.09e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 226 TDVPYGVLLSGGLDSSITSAVAKRYAAMrieddekseawwPQLHSFAVGLEG--APDLKAAREVAEKIGTVHHEMTYTIQ 303
Cdd:cd01991 1 SDVPVGVLLSGGLDSSLIAALAARLLPE------------TPIDLFTVGFEGspTPDRAAARRVAEELGTEHHEVEVTIE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 304 EGLDAIRDVIYHIETYDVTTIRASTPMFLMGRKIKAMGIKMVLSGEGADEIFGGYLYFHKAPNA--KEFHEETVRKLLAL 381
Cdd:cd01991 69 ELLDALPDVILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVLSGEGADELFGGYSRHRDAPLRgwEALEEELLRDLDRL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1796992097 382 NMFDCARANKSLAAWGVEGRVPFLDKEFIDVAMRLNPADKMCGNGKMEKHILRECFEHYLPDSIAWRQKEQFSDGV 457
Cdd:cd01991 149 WTRNLGRDDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIDPRGGGEKYILREAARDLLPDEIAWRPKRAIQFGS 224
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-192 |
1.95e-80 |
|
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: 251.32 E-value: 1.95e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 2 CSVFGILDIKsDAAALRPIALEMSKKLRHRGPDWSGIYSSERAILAHERLAIVGLNSGAQPLYSPDKKLILAVNGEIYNH 81
Cdd:cd00712 1 CGIAGIIGLD-GASVDRATLERMLDALAHRGPDGSGIWIDEGVALGHRRLSIIDLSGGAQPMVSEDGRLVLVFNGEIYNY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 82 KEIRARYEGK-YEFQTDSDCEVILALYQDMGADLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYQGYDEhGNYYVAS 160
Cdd:cd00712 80 RELRAELEALgHRFRTHSDTEVILHLYEEWGEDCLERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGRDG-GGLAFAS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1796992097 161 EMKALVPVC---------------------------KTVSEFPPGSHYSSKD--AEPQRYY 192
Cdd:cd00712 159 ELKALLALPgvpreldeaalaeylafqyvpaprtifKGIRKLPPGHYLTVDPggVEIRRYW 219
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-179 |
1.47e-52 |
|
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: 178.41 E-value: 1.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 2 CSVFGILDIKSDAAALRPIALEMSKKLRHRGPDWSGIYSSE---------------------------RAILAHERLAIV 54
Cdd:cd00352 1 CGIFGIVGADGAASLLLLLLLRGLAALEHRGPDGAGIAVYDgdglfvekragpvsdvaldlldeplksGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 55 GLNS--GAQPLYSPDKKLILAVNGEIYNHKEIRARYEGK-YEFQTDSDCEVILALYQDMGA---------DLLEELNGIF 122
Cdd:cd00352 81 GLPSeaNAQPFRSEDGRIALVHNGEIYNYRELREELEARgYRFEGESDSEVILHLLERLGRegglfeaveDALKRLDGPF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1796992097 123 AFVLYDEEKDEYLVGRDHIGIIPLYQGYDEHGNYYVASEMKALVPVC-KTVSEFPPGS 179
Cdd:cd00352 161 AFALWDGKPDRLFAARDRFGIRPLYYGITKDGGLVFASEPKALLALPfKGVRRLPPGE 218
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
48-167 |
2.59e-52 |
|
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: 174.24 E-value: 2.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 48 HERLAIVGLNSGAQPLY-SPDKKLILAVNGEIYNHKEIRARYEGK-YEFQTDSDCEVILALYQDM-GADLLEELNGIFAF 124
Cdd:pfam13537 1 HRRLSIIDLEGGAQPMVsSEDGRYVIVFNGEIYNYRELRAELEAKgYRFRTHSDTEVILHLYEAEwGEDCVDRLNGMFAF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1796992097 125 VLYDEEKDEYLVGRDHIGIIPLYQGYDEHGNYYVASEMKALVP 167
Cdd:pfam13537 81 AIWDRRRQRLFLARDRFGIKPLYYGRDDGGRLLFASELKALLA 123
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
33-161 |
4.72e-49 |
|
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: 165.94 E-value: 4.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 33 PDWSGIYSSERAILAHERLAIVGL-NSGAQPLYSPDKKLILAVNGEIYNHKEIRARYEGK-YEFQTDSDCEVILALYQDM 110
Cdd:pfam13522 1 PDFSGIWVEGGVALGHVRLAIVDLpDAGNQPMLSRDGRLVLVHNGEIYNYGELREELADLgHAFRSRSDTEVLLALYEEW 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1796992097 111 GADLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYQGYDeHGNYYVASE 161
Cdd:pfam13522 81 GEDCLERLRGMFAFAIWDRRRRTLFLARDRLGIKPLYYGIL-GGGFVFASE 130
|
|
| lass_lactam_cya |
NF033535 |
lasso peptide isopeptide bond-forming cyclase; Members of this family are the isopeptide ... |
1-271 |
9.82e-25 |
|
lasso peptide isopeptide bond-forming cyclase; Members of this family are the isopeptide bond-forming cyclase of lasso peptide biosynthesis systems, from a subgroup that contains primarily cyanobacterial examples. These proteins resemble the glutamine-hydrolyzing asparagine synthase AsnB (EC 6.3.5.4).
Pssm-ID: 468066 [Multi-domain] Cd Length: 668 Bit Score: 108.54 E-value: 9.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 1 MCSVFGILDIKS---DAAALRPialeMSKKLRHRGPDWSGIYSSERAILAH-------ERLaivglnSGAQPLYSPDKKL 70
Cdd:NF033535 1 MSGIVGIYYLDGrpvDREDLQQ----MVDILAHRGPDGADIWCEGSVGLGHrmlwttpESL------LEKLPLVNQTGDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 71 ILAVNGEIYNHKEIRARYEGKY---EFQTDSdcEVILALYQDMGADLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLY 147
Cdd:NF033535 71 VITADARIDNRDELISALQLNNcppEKITDS--QLILAAYEKWGEQCPEHLLGDFAFAIWDKRKQQLFCARDHFGVKPFY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 148 qgYDEHGN-YYVASEMKAL-----VPVC----------------KTVSEF------PPGsHY---SSKDAEPQRYYIRDW 196
Cdd:NF033535 149 --YYQSDKrFAFASEIKALlclpeVPRRlnevriadylalmledKVITFYqdifrlPPA-HSmtvSQSGLQIRSYWSLDP 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1796992097 197 NEYAAVQGNSTSKEELTEALEAAVKRQLMTDVPYGVLLSGGLDSSITSAVAKryaamRIEDDEKSeawwPQLHSF 271
Cdd:NF033535 226 SRELRLDSDEEYAEAFREIFTEAVRCRLRSAFPVGSHLSGGLDSSSITCVAR-----QLLAEEKK----APLHTF 291
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-161 |
8.90e-14 |
|
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: 73.52 E-value: 8.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 1 MCSVFGILDiKSDAAALRPIALEMskkLRHRGPDWSGI-YSSERAILAHERLaivGL---------------NSG----- 59
Cdd:COG0034 7 ECGVFGIYG-HEDVAQLTYYGLYA---LQHRGQESAGIaTSDGGRFHLHKGM---GLvsdvfdeedlerlkgNIAighvr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 60 -----------AQPLY--SPDKKLILAVNGEIYNHKEIRARYEGK-YEFQTDSDCEVILAL------YQDMG---ADLLE 116
Cdd:COG0034 80 ysttgssslenAQPFYvnSPFGSIALAHNGNLTNAEELREELEEEgAIFQTTSDTEVILHLiareltKEDLEeaiKEALR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1796992097 117 ELNGIFAFVLYDEEKdeyLVG-RDHIGIIPLYQGYDEHGnYYVASE 161
Cdd:COG0034 160 RVKGAYSLVILTGDG---LIAaRDPNGIRPLVLGKLEDG-YVVASE 201
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-165 |
3.04e-13 |
|
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: 69.80 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 2 CSVFGILDiKSDAAALRPIALEMskkLRHRGPDWSGIYSSE-RAILAH------------ERLAIVGLNSG--------- 59
Cdd:cd00715 1 CGVFGIYG-AEDAARLTYLGLYA---LQHRGQESAGIATSDgKRFHTHkgmglvsdvfdeEKLRRLPGNIAighvrysta 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 60 -------AQPLY--SPDKKLILAVNGEIYNHKEIRARYEGKY-EFQTDSDCEVILAL------YQDMG---ADLLEELNG 120
Cdd:cd00715 77 gssslenAQPFVvnSPLGGIALAHNGNLVNAKELREELEEEGrIFQTTSDSEVILHLiarslaKDDLFeaiIDALERVKG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1796992097 121 IFAFVLYDEEKdeyLVG-RDHIGIIPLYQGYDEHGNYYVASEMKAL 165
Cdd:cd00715 157 AYSLVIMTADG---LIAvRDPHGIRPLVLGKLEGDGYVVASESCAL 199
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-178 |
9.93e-13 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 70.48 E-value: 9.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 1 MCSVFGILDiKSDAAALRPIALEMskkLRHRGPDWSGIYSSERAIL---------------------------AHERLAI 53
Cdd:PLN02440 1 ECGVVGIFG-DPEASRLCYLGLHA---LQHRGQEGAGIVTVDGNRLqsitgnglvsdvfdeskldqlpgdiaiGHVRYST 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 54 VGLNS--GAQPLY--SPDKKLILAVNGEIYNHKEIRARYEGKYE-FQTDSDCEVILALYQDMGA--------DLLEELNG 120
Cdd:PLN02440 77 AGASSlkNVQPFVanYRFGSIGVAHNGNLVNYEELRAKLEENGSiFNTSSDTEVLLHLIAISKArpffsrivDACEKLKG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 121 IFAFVLYDEEKdeyLVG-RDHIGIIPLYQGYDEHGNYYVASEMKALVPV-CKTVSEFPPG 178
Cdd:PLN02440 157 AYSMVFLTEDK---LVAvRDPHGFRPLVMGRRSNGAVVFASETCALDLIgATYEREVNPG 213
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
60-172 |
6.37e-10 |
|
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus of glucosamine-6P synthase (GlmS, or GFAT in humans). The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. In humans, GFAT catalyzes the first and rate-limiting step of hexosamine metabolism, the conversion of D-fructose-6P (Fru6P) into D-glucosamine-6P using L-glutamine as a nitrogen source. The end product of this pathway, UDP-N-acetyl glucosamine, is a major building block of the bacterial peptidoglycan and fungal chitin.
Pssm-ID: 238366 [Multi-domain] Cd Length: 215 Bit Score: 59.38 E-value: 6.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 60 AQPLYSPDKKLILAVNGEIYNHKEIRARYEGK-YEFQTDSDCEVI---LALYQDMGADLLE-------ELNGIFAFVLYD 128
Cdd:cd00714 84 AHPHRSCDGEIAVVHNGIIENYAELKEELEAKgYKFESETDTEVIahlIEYYYDGGLDLLEavkkalkRLEGAYALAVIS 163
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1796992097 129 EEKDEYLVG--RD---HIGIiplyqGYDEhgnYYVASEMKALVPVCKTV 172
Cdd:cd00714 164 KDEPDEIVAarNGsplVIGI-----GDGE---NFVASDAPALLEHTRRV 204
|
|
| Gn_AT_II_novel |
cd03766 |
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its ... |
1-181 |
8.27e-10 |
|
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: 58.07 E-value: 8.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 1 MCSVFGILDIKSDAAALRPIALEMSKKLRHRGPDWSG-IYSSERAILAHER---LAIVGLNSGAQPLYSPDKKLILAVNG 76
Cdd:cd03766 1 MCGILCSVSPSGPHINSSLLSEELLPNLRNRGPDYLStRQLSVTNWTLLFTssvLSLRGDHVTRQPLVDQSTGNVLQWNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 77 EIYN--HKEIRaryegkyefqtDSDCEVILAL-------YQDMgADLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLY 147
Cdd:cd03766 81 ELYNidGVEDE-----------ENDTEVIFELlancsseSQDI-LDVLSSIEGPFAFIYYDASENKLYFGRDCLGRRSLL 148
|
170 180 190
....*....|....*....|....*....|....*
gi 1796992097 148 QGYDEHG-NYYVASemkalvpvcktVSEFPPGSHY 181
Cdd:cd03766 149 YKLDPNGfELSISS-----------VSGSSSGSGF 172
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
60-172 |
2.56e-09 |
|
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440218 [Multi-domain] Cd Length: 610 Bit Score: 60.03 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 60 AQPLYSPDKKLILAVNGEIYNHKEIRARYEGK-YEFQTDSDCEVI---LALYQDMGADLLE-------ELNGIFAFVLYD 128
Cdd:COG0449 85 AHPHTSCSGRIAVVHNGIIENYAELREELEAKgHTFKSETDTEVIahlIEEYLKGGGDLLEavrkalkRLEGAYALAVIS 164
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1796992097 129 EEKDEYLVG--RDHigiiPLYQGYDEHGNyYVASEMKALVPVCKTV 172
Cdd:COG0449 165 ADEPDRIVAarKGS----PLVIGLGEGEN-FLASDVPALLPYTRRV 205
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-165 |
6.48e-09 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 58.12 E-value: 6.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 2 CSVFGI-LDIKSDAAALRPIALEmskKLRHRGPDWSGI-YSSERAILAHERLAIV------------------------- 54
Cdd:PRK05793 15 CGVFGVfSKNNIDVASLTYYGLY---ALQHRGQESAGIaVSDGEKIKVHKGMGLVsevfskeklkglkgnsaighvryst 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 55 ---GLNSGAQPLYSPDKK--LILAVNGEIYNHKEIRARYE-GKYEFQTDSDCEVILAL--------YQDMGADLLEELNG 120
Cdd:PRK05793 92 tgaSDLDNAQPLVANYKLgsIAIAHNGNLVNADVIRELLEdGGRIFQTSIDSEVILNLiarsakkgLEKALVDAIQAIKG 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1796992097 121 IFAFVLYDEEKdeyLVG-RDHIGIIPLYQGYDEhGNYYVASEMKAL 165
Cdd:PRK05793 172 SYALVILTEDK---LIGvRDPHGIRPLCLGKLG-DDYILSSESCAL 213
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
60-174 |
7.13e-08 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 55.05 E-value: 7.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 60 AQPLYSPDKKLILAVNGEIYNHKEIRARYEGK-YEFQTDSDCEVI---LALYQDMGADLLE-------ELNGIFAFVLYD 128
Cdd:PRK00331 85 AHPHTDCSGRIAVVHNGIIENYAELKEELLAKgHVFKSETDTEVIahlIEEELKEGGDLLEavrkalkRLEGAYALAVID 164
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1796992097 129 EEKDEYLVG--RDHigiiPLYQGYDEHGNyYVASEMKALVPVCKTVSE 174
Cdd:PRK00331 165 KDEPDTIVAarNGS----PLVIGLGEGEN-FLASDALALLPYTRRVIY 207
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
46-165 |
1.32e-06 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 51.18 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 46 LAHERLAIVG--LNSGAQPLYSPDKKLILAVNGEIYNHKEIRARYEGK-YEFQTDSDCEVI---LALYQDMGADLLE--- 116
Cdd:PTZ00295 99 IAHTRWATHGgkTDENAHPHCDYKKRIALVHNGTIENYVELKSELIAKgIKFRSETDSEVIanlIGLELDQGEDFQEavk 178
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1796992097 117 ----ELNGIFAFVLYDEE-KDEYLVGRDHigiIPLYQGYDEHGnYYVASEMKAL 165
Cdd:PTZ00295 179 saisRLQGTWGLCIIHKDnPDSLIVARNG---SPLLVGIGDDS-IYVASEPSAF 228
|
|
| DUF3700 |
pfam12481 |
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ... |
115-183 |
4.02e-06 |
|
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: 48.13 E-value: 4.02e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 115 LEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYQGYDEHGNYYVASEMKALVPVC-KTVSEFPPGSHYSS 183
Cdd:pfam12481 126 VRDLEGKFAFVLYDSSTSTVFVASDADGSVPLYWGIDADGSLVFSDDIEIVKKGCgKSFAPFPKGCFFTS 195
|
|
| Wali7 |
cd01910 |
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ... |
115-183 |
6.80e-06 |
|
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: 47.30 E-value: 6.80e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 115 LEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYQGYDEHGNYYVASEMKALVPVC-KTVSEFPPGSHYSS 183
Cdd:cd01910 122 VKDLEGSFAFVLYDKKTSTVFVASDADGSVPLYWGIAADGSVVFSDDVELVKASCgKSFAPFPKGCFFHS 191
|
|
| AANH_superfamily |
cd01984 |
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ... |
230-275 |
4.06e-05 |
|
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase (AANH) superfamily includes N-type ATP PPases, ATP sulfurylases, universal stress response proteins (USPs), and electron transfer flavoproteins (ETFs). The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.
Pssm-ID: 467489 [Multi-domain] Cd Length: 56 Bit Score: 41.31 E-value: 4.06e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1796992097 230 YGVLLSGGLDSSITSAVAKRYAamrieddeksEAWWPQLHSFAVGL 275
Cdd:cd01984 1 ILVPLSGGEDSSIALKHAKKFK----------TSKAEEVVVVHVGE 36
|
|
| betaLS_CarA_N |
cd01909 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_betaLS-type. Carbapenam ... |
76-186 |
1.93e-04 |
|
Glutamine amidotransferases class-II (GATase) asparagine synthase_betaLS-type. Carbapenam synthetase (CarA) is an ATP/Mg2+-dependent enzyme that catalyzes the formation of the beta-lactam ring in (5R)-carbapenem-3-carboxylic acid biosynthesis. CarA is homologous to beta-lactam synthetase (beta-LS), which is involved in the biosynthesis of clavulanic acid, a clinically important beta-lactamase inhibitor. CarA and beta-LS each have two distinct domains, an N-terminal Ntn hydrolase domain and a C-terminal synthetase domain, a domain architecture similar to that of the class-B asparagine synthetases (AS-B's). The N-terminal domain of these enzymes hydrolyzes glutamine to glutamate and ammonia. CarA forms a homotetramer while betaLS forms a heterodimer. The N-terminal folds of CarA and beta-LS are similar to those of other class II glutamine amidotransferases including lucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), and glutamate synthase (GltS). This fold is also somwhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238890 [Multi-domain] Cd Length: 199 Bit Score: 42.87 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796992097 76 GEIYNHKEIR-ARYEGKYEFQTDSDCEVILALYQDMGADLLEELNGIFAFVLyDEEKDEYLVGRDHIGIIPLYQGYDehG 154
Cdd:cd01909 58 GELYNRDELRsLLGAGEGRSAVLGDAELLLLLLTRLGLHAFRLAEGDFCFFI-EDGNGRLTLATDHAGSVPVYLVQA--G 134
|
90 100 110
....*....|....*....|....*....|..
gi 1796992097 155 NYYVASEMKALvpvckTVSEFPPGSHYSSKDA 186
Cdd:cd01909 135 EVWATTELKLL-----AAHEGPKAFPFKSAGA 161
|
|
| |
