|
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: 1151.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 1 MCSVFGILDIKSDAAALRPIALEMSKKLRHRGPDWSGIYAGEKAILAHERLAIVGLNSGAQPLYSQDKKHILAVNGEIYN 80
Cdd:PRK09431 1 MCGIFGILDIKTDADELRKKALEMSRLMRHRGPDWSGIYASDNAILGHERLSIVDVNGGAQPLYNEDGTHVLAVNGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 81 HKELRARYEDKYQFQTDSDCEVILALYQEMGADLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYQGYDEHGNYYVAS 160
Cdd:PRK09431 81 HQELRAELGDKYAFQTGSDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGNLYFAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 161 EMKALVEVCKTISEFPPGSFYSSKDAEPQRYYIRDWNEYAAVQGNSTSKEELTEALEAAVKRQLMTDVPYGVLLSGGLDS 240
Cdd:PRK09431 161 EMKALVPVCKTIKEFPPGHYYWSKDGEFVRYYQRDWFDYDAVKDNVTDKNELRDALEAAVKKRLMSDVPYGVLLSGGLDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 241 SITSAVAKRFAAMRIEDDEQSEAWWPQLHSFAVGLEGAPDLIAAREVADKIGTVHHEMTYTIQEGLDAIRDVIYHIETYD 320
Cdd:PRK09431 241 SLISAIAKKYAARRIEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVADHLGTVHHEIHFTVQEGLDALRDVIYHLETYD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 321 VTTIRASTPMYLLARKIKAMGIKMVLSGEGADEIFGGYLYFHKAPNAKEFHEETVRKLLALSMFDCARANKSLAAWGVEG 400
Cdd:PRK09431 321 VTTIRASTPMYLMARKIKAMGIKMVLSGEGADELFGGYLYFHKAPNAKEFHEETVRKLRALHMYDCLRANKAMMAWGVEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 401 RVPFLDKEFIDVAMRLNPEDKMCGNGKMEKHILRECFEDYLPDSIAWRQKEQFSDGVGYDWIDTLKATAEAKVTDQQMEA 480
Cdd:PRK09431 401 RVPFLDKEFLDVAMRINPEDKMCGNGKMEKHILREAFEGYLPESILWRQKEQFSDGVGYSWIDTLKEVAAEQVSDQQLAT 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515633407 481 AKFRFPYNTPTTKEGYVYREIFEELFPLESAAECVPGGPSVACSSAKAIEWDESFKNCVDPSGRAVQAVHNDAY 554
Cdd:PRK09431 481 ARFRFPYNTPTTKEAYLYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDEAFKNMDDPSGRAVSGVHQSAY 554
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-453 |
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: 521.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 4 VFGILDIKSDAAALRPIALEMSKKLRHRGPDWSGI-YAGEKAILAHERLAIVGLNSGAQPLYSQDKKHILAVNGEIYNHK 82
Cdd:TIGR01536 1 IAGFFDLDDKAVEEDEAIKRMSDTIAHRGPDASGIeYKDGNAILGHRRLAIIDLSGGAQPMSNEGKTYVIVFNGEIYNHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 83 ELRARYEDK-YQFQTDSDCEVILALYQEMGADLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYQGYDeHGNYYVASE 161
Cdd:TIGR01536 81 ELREELEAKgYTFQTDSDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYD-GGQLYFASE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 162 MKALVEVCkTISEFPPGSFYSSKDAE----PQRYYIRDWNEYAAVQGNS------------------------TSKEELT 213
Cdd:TIGR01536 160 IKALLAHP-NIKPFPDGAALAPGFGFvrvpPPSTFFRGVFELEPGHDLPldddglnieryywerrdehtdseeDLVDELR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 214 EALEAAVKRQLMTDVPYGVLLSGGLDSSITSAVAKRFAAMrieddeqseawwPQLHSFAVGLEGAPDLI---AAREVADK 290
Cdd:TIGR01536 239 SLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPR------------GPVHTFSIGFEGSPDFDeskYARKVADH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 291 IGTVHHEMTYTIQEGLDAIRDVIYHIEtyDVTTIRASTPMYLLARKIKAMGIKMVLSGEGADEIFGGYLYFHKAPNAKEF 370
Cdd:TIGR01536 307 LGTEHHEVLFSVEEGLDALPEVIYHLE--EPTTIRASIPLYLLSKLAREDGVKVVLSGEGADELFGGYLYFHEAPAAEAL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 371 HEETVRKLLALSMFDCARAN-KSLAAWGVEGRVPFLDKEFIDVAMRLNPEDKMcgNGKMEKHILRECFEDYLPDSIAWRQ 449
Cdd:TIGR01536 385 REELQYLDLELYMPGLLRRKdRMSMAHSLEVRVPFLDHELVEYALSIPPEMKL--RDGKEKYLLREAFEGYLPEEILWRP 462
|
....
gi 515633407 450 KEQF 453
Cdd:TIGR01536 463 KEGF 466
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-507 |
9.47e-176 |
|
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: 507.84 E-value: 9.47e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 1 MCSVFGILDIksDAAALRPIALEMSKKLRHRGPDWSGIYAGEKAILAHERLAIVGL-NSGAQPLYSQDKKHILAVNGEIY 79
Cdd:COG0367 1 MCGIAGIIDF--DGGADREVLERMLDALAHRGPDGSGIWVDGGVALGHRRLSIIDLsEGGHQPMVSEDGRYVLVFNGEIY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 80 NHKELRARYEDK-YQFQTDSDCEVILALYQEMGADLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYQGYDEhGNYYV 158
Cdd:COG0367 79 NYRELRAELEALgHRFRTHSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDG-GGLAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 159 ASEMKALVE---------------------------VCKTISEFPPGSFYSSKD---AEPQRYYIRDWNEYAAVQGNSTS 208
Cdd:COG0367 158 ASELKALLAhpgvdreldpealaeyltlgyvpaprtIFKGIRKLPPGHYLTVDAggeLEIRRYWDLEFVPHERSDSEEEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 209 KEELTEALEAAVKRQLMTDVPYGVLLSGGLDSSITSAVAKRFAAmrieddeqseawwPQLHSFAVGLEGAP--DLIAARE 286
Cdd:COG0367 238 VEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSK-------------GPLKTFSIGFEDSAydESPYARA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 287 VADKIGTVHHEMTYTIQEGLDAIRDVIYHIEtyDVTTIRASTPMYLLARKIKAMgIKMVLSGEGADEIFGGYLYFHKAPN 366
Cdd:COG0367 305 VAEHLGTEHHEVTVTPEDLLDALPDLVWHLD--EPFADPSAVPTYLLSRLAREH-VKVVLSGEGADELFGGYPRYREAAL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 367 AKE-------------------FHEETVRKLLALSMF------DCARANKSLAAWGVEGRVPFLDKEFIDVAMRLNPEDK 421
Cdd:COG0367 382 LLSpdfaealggelvprlyaesGAEDPLRRMLYLDLKtylpgdLLVKVDRMSMAHSLEVRVPFLDHRLVEFALSLPPELK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 422 McgNGKMEKHILRECFEDYLPDSIAWRQKEQFSDGVGyDWID-TLKATAEAKVTDQQMEAAKFrfpYNTpttkegYVYRE 500
Cdd:COG0367 462 L--RGGRGKYLLRKALEGLLPDEVLDRPKQGFPVPLG-PWLRgPLREWLEDLLSDESLAARGL---FDP------DAVRR 529
|
....*..
gi 515633407 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 |
2.46e-106 |
|
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: 319.95 E-value: 2.46e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 211 ELTEALEAAVKRQLMTDVPYGVLLSGGLDSSITSAVAKRFAAmrieddeqseawwPQLHSFAVGLEGA--PDLIAAREVA 288
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSP-------------SPLHTFSIGFEGRgyDEAPYAREVA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 289 DKIGTVHHEMTYTIQEGLDAIRDVIYHIETydVTTIRASTPMYLLARKIKAMGIKMVLSGEGADEIFGGYLYFHkapNAK 368
Cdd:pfam00733 68 EHLGTDHHELVVTPEDLLDALPDVIWHLDE--PFADPSAIPLYLLSRLARRKGVKVVLSGEGADELFGGYPFYK---GED 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 369 EFHEETVRKLLALSMFDCARANKSLAAWGVEGRVPFLDKEFIDVAMRLNPEDKMCGNgkMEKHILRECFEDYLPDSIAWR 448
Cdd:pfam00733 143 PLRRMLYLDLKTLLPGDLLRADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKLRGG--IEKYILREALEGILPDEILER 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515633407 449 QKEQFSDGVGYDWID-TLKATAEAKVTDQqmeaakfrfpyntPTTKEGYVYREIFEELFPLESAA 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 |
2.46e-91 |
|
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: 279.54 E-value: 2.46e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 226 TDVPYGVLLSGGLDSSITSAVAKRFAAMrieddeqseawwPQLHSFAVGLEG--APDLIAAREVADKIGTVHHEMTYTIQ 303
Cdd:cd01991 1 SDVPVGVLLSGGLDSSLIAALAARLLPE------------TPIDLFTVGFEGspTPDRAAARRVAEELGTEHHEVEVTIE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 304 EGLDAIRDVIYHIETYDVTTIRASTPMYLLARKIKAMGIKMVLSGEGADEIFGGYLYFHKAPNA--KEFHEETVRKLLAL 381
Cdd:cd01991 69 ELLDALPDVILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVLSGEGADELFGGYSRHRDAPLRgwEALEEELLRDLDRL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515633407 382 SMFDCARANKSLAAWGVEGRVPFLDKEFIDVAMRLNPEDKMCGNGKMEKHILRECFEDYLPDSIAWRQKEQFSDGV 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 |
1.52e-24 |
|
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: 108.16 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 1 MCSVFGILDIKS---DAAALRPialeMSKKLRHRGPDWSGIYAGEKAILAH-------ERLaivglnSGAQPLYSQDKKH 70
Cdd:NF033535 1 MSGIVGIYYLDGrpvDREDLQQ----MVDILAHRGPDGADIWCEGSVGLGHrmlwttpESL------LEKLPLVNQTGDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 71 ILAVNGEIYNHKELRARYE-DKYQFQTDSDCEVILALYQEMGADLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYqg 149
Cdd:NF033535 71 VITADARIDNRDELISALQlNNCPPEKITDSQLILAAYEKWGEQCPEHLLGDFAFAIWDKRKQQLFCARDHFGVKPFY-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 150 YDEHGN-YYVASEMKALV---EVCKTISE------------------------FPPGSFY--SSKDAEPQRYYIRDWNEY 199
Cdd:NF033535 149 YYQSDKrFAFASEIKALLclpEVPRRLNEvriadylalmledkvitfyqdifrLPPAHSMtvSQSGLQIRSYWSLDPSRE 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515633407 200 AAVQGNSTSKEELTEALEAAVKRQLMTDVPYGVLLSGGLDSSITSAVAKrfaamriedDEQSEAWWPQLHSF 271
Cdd:NF033535 229 LRLDSDEEYAEAFREIFTEAVRCRLRSAFPVGSHLSGGLDSSSITCVAR---------QLLAEEKKAPLHTF 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: 1151.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 1 MCSVFGILDIKSDAAALRPIALEMSKKLRHRGPDWSGIYAGEKAILAHERLAIVGLNSGAQPLYSQDKKHILAVNGEIYN 80
Cdd:PRK09431 1 MCGIFGILDIKTDADELRKKALEMSRLMRHRGPDWSGIYASDNAILGHERLSIVDVNGGAQPLYNEDGTHVLAVNGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 81 HKELRARYEDKYQFQTDSDCEVILALYQEMGADLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYQGYDEHGNYYVAS 160
Cdd:PRK09431 81 HQELRAELGDKYAFQTGSDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGNLYFAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 161 EMKALVEVCKTISEFPPGSFYSSKDAEPQRYYIRDWNEYAAVQGNSTSKEELTEALEAAVKRQLMTDVPYGVLLSGGLDS 240
Cdd:PRK09431 161 EMKALVPVCKTIKEFPPGHYYWSKDGEFVRYYQRDWFDYDAVKDNVTDKNELRDALEAAVKKRLMSDVPYGVLLSGGLDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 241 SITSAVAKRFAAMRIEDDEQSEAWWPQLHSFAVGLEGAPDLIAAREVADKIGTVHHEMTYTIQEGLDAIRDVIYHIETYD 320
Cdd:PRK09431 241 SLISAIAKKYAARRIEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVADHLGTVHHEIHFTVQEGLDALRDVIYHLETYD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 321 VTTIRASTPMYLLARKIKAMGIKMVLSGEGADEIFGGYLYFHKAPNAKEFHEETVRKLLALSMFDCARANKSLAAWGVEG 400
Cdd:PRK09431 321 VTTIRASTPMYLMARKIKAMGIKMVLSGEGADELFGGYLYFHKAPNAKEFHEETVRKLRALHMYDCLRANKAMMAWGVEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 401 RVPFLDKEFIDVAMRLNPEDKMCGNGKMEKHILRECFEDYLPDSIAWRQKEQFSDGVGYDWIDTLKATAEAKVTDQQMEA 480
Cdd:PRK09431 401 RVPFLDKEFLDVAMRINPEDKMCGNGKMEKHILREAFEGYLPESILWRQKEQFSDGVGYSWIDTLKEVAAEQVSDQQLAT 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515633407 481 AKFRFPYNTPTTKEGYVYREIFEELFPLESAAECVPGGPSVACSSAKAIEWDESFKNCVDPSGRAVQAVHNDAY 554
Cdd:PRK09431 481 ARFRFPYNTPTTKEAYLYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDEAFKNMDDPSGRAVSGVHQSAY 554
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-554 |
0e+00 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 828.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 1 MCSVFGILDIKSDAAALRPIALEMSKKLRHRGPDWSGIYAGEKAILAHERLAIVGLNSGAQPLYSQDKKHILAVNGEIYN 80
Cdd:PLN02549 1 MCGILAVLGCSDDSQAKRSRVLELSRRLRHRGPDWSGLYGNEDCYLAHERLAIMDPESGDQPLYNEDKTIVVTANGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 81 HKELRARYEDkYQFQTDSDCEVILALYQEMGADLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYQGYDEHGNYYVAS 160
Cdd:PLN02549 81 HKELREKLKL-HKFRTGSDCEVIAHLYEEHGEEFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGLDGSVWFAS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 161 EMKALVEVCKTISEFPPGSFYSSKDAEPQRYYIRDW-NEYAAVQGNSTSkeELTEALEAAVKRQLMTDVPYGVLLSGGLD 239
Cdd:PLN02549 160 EMKALCDDCERFEEFPPGHYYSSKAGGFRRWYNPPWfSESIPSTPYDPL--VLREAFEKAVIKRLMTDVPFGVLLSGGLD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 240 SSITSAVAKRFaamrIEDDEQSEAWWPQLHSFAVGLEGAPDLIAAREVADKIGTVHHEMTYTIQEGLDAIRDVIYHIETY 319
Cdd:PLN02549 238 SSLVASIAARH----LAETKAARQWGQQLHSFCVGLEGSPDLKAAREVADYLGTVHHEFHFTVQEGIDAIEDVIYHLETY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 320 DVTTIRASTPMYLLARKIKAMGIKMVLSGEGADEIFGGYLYFHKAPNAKEFHEETVRKLLALSMFDCARANKSLAAWGVE 399
Cdd:PLN02549 314 DVTTIRASTPMFLMSRKIKSLGVKMVLSGEGSDEIFGGYLYFHKAPNKEEFHKETCRKIKALHQYDCLRANKSTSAWGLE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 400 GRVPFLDKEFIDVAMRLNPEDKMC--GNGKMEKHILRECFED----YLPDSIAWRQKEQFSDGVGYDWIDTLKATAEAKV 473
Cdd:PLN02549 394 ARVPFLDKEFIDVAMSIDPEWKMIrpGEGRIEKWVLRKAFDDeedpYLPKHILWRQKEQFSDGVGYSWIDGLKAHAEKHV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 474 TDQQMEAAKFRFPYNTPTTKEGYVYREIFEELFPLESAAECVPGGPSVACSSAKAIEWDESFKNCVDPSGRAVQAVHNDA 553
Cdd:PLN02549 474 SDEMFANASFRYPHNTPTTKEAYYYRMIFEKHFPQDAARLTVPGGPSVACSTAKAVEWDAAWSKNLDPSGRAALGVHVAA 553
|
.
gi 515633407 554 Y 554
Cdd:PLN02549 554 Y 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: 827.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 1 MCSVFGILDIKSDAAALRPIALEMSKKLRHRGPDWSGIYAGEKA-----ILAHERLAIVGLNSGAQPLYSQDKKHILAVN 75
Cdd:PTZ00077 1 MCGILAIFNSKGERHELRRKALELSKRLRHRGPDWSGIIVLENSpgtynILAHERLAIVDLSDGKQPLLDDDETVALMQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 76 GEIYNHKELRARYEDK-YQFQTDSDCEVILALYQEMGA-DLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYQGYDEH 153
Cdd:PTZ00077 81 GEIYNHWEIRPELEKEgYKFSSNSDCEIIGHLYKEYGPkDFWNHLDGMFATVIYDMKTNTFFAARDHIGIIPLYIGYAKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 154 GNYYVASEMKALVEVCKTISEFPPGSFYSS--KDAEPQRYYIRDW-NEYAAVQGNSTSKEELTEALEAAVKRQLMTDVPY 230
Cdd:PTZ00077 161 GSIWFSSELKALHDQCVEVKQFPPGHYYDQtkEKGEFVRYYNPNWhDFDHPIPTGEIDLEEIREALEAAVRKRLMGDVPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 231 GVLLSGGLDSSITSAVAKRFAamRIEDDEQSEAWWPQLHSFAVGLEGAPDLIAAREVADKIGTVHHEMTYTIQEGLDAIR 310
Cdd:PTZ00077 241 GLFLSGGLDSSIVAAIVAKLI--KNGEIDLSKRGMPKLHSFCIGLEGSPDLKAARKVAEYLGTEHHEFTFTVEEGIDALP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 311 DVIYHIETYDVTTIRASTPMYLLARKIKAMGIKMVLSGEGADEIFGGYLYFHKAPNAKEFHEETVRKLLALSMFDCARAN 390
Cdd:PTZ00077 319 DVIYHTETYDVTTIRASTPMYLLSRRIKALGIKMVLSGEGSDELFGGYLYFHKAPNREEFHRELVRKLHDLHKYDCLRAN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 391 KSLAAWGVEGRVPFLDKEFIDVAMRLNPEDKMC--GNGKMEKHILRECFED----YLPDSIAWRQKEQFSDGVGYDWIDT 464
Cdd:PTZ00077 399 KATMAWGIEARVPFLDKDFLEYVMNIDPKYKMCnaFEGQMEKYILRKAFEGlekpYLPDEILWRQKEQFSDGVGYSWIDG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 465 LKATAEAKVTDQQMEAAKFRFPYNTPTTKEGYVYREIFEELFPLESAAECVPGGPSVACSSAKAIEWDESFKNCVDPSGR 544
Cdd:PTZ00077 479 LKEYAEKKISDQEFSQASFLFPYNTPRTKEAYLYRQIFSKHFPSDSAALTVPYGPSIACSTEKALEWDESFKKNTDESGR 558
|
570
....*....|
gi 515633407 545 AVQAVHNDAY 554
Cdd:PTZ00077 559 AVLSVHNDAK 568
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-453 |
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: 521.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 4 VFGILDIKSDAAALRPIALEMSKKLRHRGPDWSGI-YAGEKAILAHERLAIVGLNSGAQPLYSQDKKHILAVNGEIYNHK 82
Cdd:TIGR01536 1 IAGFFDLDDKAVEEDEAIKRMSDTIAHRGPDASGIeYKDGNAILGHRRLAIIDLSGGAQPMSNEGKTYVIVFNGEIYNHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 83 ELRARYEDK-YQFQTDSDCEVILALYQEMGADLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYQGYDeHGNYYVASE 161
Cdd:TIGR01536 81 ELREELEAKgYTFQTDSDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYD-GGQLYFASE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 162 MKALVEVCkTISEFPPGSFYSSKDAE----PQRYYIRDWNEYAAVQGNS------------------------TSKEELT 213
Cdd:TIGR01536 160 IKALLAHP-NIKPFPDGAALAPGFGFvrvpPPSTFFRGVFELEPGHDLPldddglnieryywerrdehtdseeDLVDELR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 214 EALEAAVKRQLMTDVPYGVLLSGGLDSSITSAVAKRFAAMrieddeqseawwPQLHSFAVGLEGAPDLI---AAREVADK 290
Cdd:TIGR01536 239 SLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPR------------GPVHTFSIGFEGSPDFDeskYARKVADH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 291 IGTVHHEMTYTIQEGLDAIRDVIYHIEtyDVTTIRASTPMYLLARKIKAMGIKMVLSGEGADEIFGGYLYFHKAPNAKEF 370
Cdd:TIGR01536 307 LGTEHHEVLFSVEEGLDALPEVIYHLE--EPTTIRASIPLYLLSKLAREDGVKVVLSGEGADELFGGYLYFHEAPAAEAL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 371 HEETVRKLLALSMFDCARAN-KSLAAWGVEGRVPFLDKEFIDVAMRLNPEDKMcgNGKMEKHILRECFEDYLPDSIAWRQ 449
Cdd:TIGR01536 385 REELQYLDLELYMPGLLRRKdRMSMAHSLEVRVPFLDHELVEYALSIPPEMKL--RDGKEKYLLREAFEGYLPEEILWRP 462
|
....
gi 515633407 450 KEQF 453
Cdd:TIGR01536 463 KEGF 466
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-507 |
9.47e-176 |
|
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: 507.84 E-value: 9.47e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 1 MCSVFGILDIksDAAALRPIALEMSKKLRHRGPDWSGIYAGEKAILAHERLAIVGL-NSGAQPLYSQDKKHILAVNGEIY 79
Cdd:COG0367 1 MCGIAGIIDF--DGGADREVLERMLDALAHRGPDGSGIWVDGGVALGHRRLSIIDLsEGGHQPMVSEDGRYVLVFNGEIY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 80 NHKELRARYEDK-YQFQTDSDCEVILALYQEMGADLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYQGYDEhGNYYV 158
Cdd:COG0367 79 NYRELRAELEALgHRFRTHSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDG-GGLAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 159 ASEMKALVE---------------------------VCKTISEFPPGSFYSSKD---AEPQRYYIRDWNEYAAVQGNSTS 208
Cdd:COG0367 158 ASELKALLAhpgvdreldpealaeyltlgyvpaprtIFKGIRKLPPGHYLTVDAggeLEIRRYWDLEFVPHERSDSEEEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 209 KEELTEALEAAVKRQLMTDVPYGVLLSGGLDSSITSAVAKRFAAmrieddeqseawwPQLHSFAVGLEGAP--DLIAARE 286
Cdd:COG0367 238 VEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSK-------------GPLKTFSIGFEDSAydESPYARA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 287 VADKIGTVHHEMTYTIQEGLDAIRDVIYHIEtyDVTTIRASTPMYLLARKIKAMgIKMVLSGEGADEIFGGYLYFHKAPN 366
Cdd:COG0367 305 VAEHLGTEHHEVTVTPEDLLDALPDLVWHLD--EPFADPSAVPTYLLSRLAREH-VKVVLSGEGADELFGGYPRYREAAL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 367 AKE-------------------FHEETVRKLLALSMF------DCARANKSLAAWGVEGRVPFLDKEFIDVAMRLNPEDK 421
Cdd:COG0367 382 LLSpdfaealggelvprlyaesGAEDPLRRMLYLDLKtylpgdLLVKVDRMSMAHSLEVRVPFLDHRLVEFALSLPPELK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 422 McgNGKMEKHILRECFEDYLPDSIAWRQKEQFSDGVGyDWID-TLKATAEAKVTDQQMEAAKFrfpYNTpttkegYVYRE 500
Cdd:COG0367 462 L--RGGRGKYLLRKALEGLLPDEVLDRPKQGFPVPLG-PWLRgPLREWLEDLLSDESLAARGL---FDP------DAVRR 529
|
....*..
gi 515633407 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 |
2.46e-106 |
|
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: 319.95 E-value: 2.46e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 211 ELTEALEAAVKRQLMTDVPYGVLLSGGLDSSITSAVAKRFAAmrieddeqseawwPQLHSFAVGLEGA--PDLIAAREVA 288
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSP-------------SPLHTFSIGFEGRgyDEAPYAREVA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 289 DKIGTVHHEMTYTIQEGLDAIRDVIYHIETydVTTIRASTPMYLLARKIKAMGIKMVLSGEGADEIFGGYLYFHkapNAK 368
Cdd:pfam00733 68 EHLGTDHHELVVTPEDLLDALPDVIWHLDE--PFADPSAIPLYLLSRLARRKGVKVVLSGEGADELFGGYPFYK---GED 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 369 EFHEETVRKLLALSMFDCARANKSLAAWGVEGRVPFLDKEFIDVAMRLNPEDKMCGNgkMEKHILRECFEDYLPDSIAWR 448
Cdd:pfam00733 143 PLRRMLYLDLKTLLPGDLLRADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKLRGG--IEKYILREALEGILPDEILER 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515633407 449 QKEQFSDGVGYDWID-TLKATAEAKVTDQqmeaakfrfpyntPTTKEGYVYREIFEELFPLESAA 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 |
2.46e-91 |
|
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: 279.54 E-value: 2.46e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 226 TDVPYGVLLSGGLDSSITSAVAKRFAAMrieddeqseawwPQLHSFAVGLEG--APDLIAAREVADKIGTVHHEMTYTIQ 303
Cdd:cd01991 1 SDVPVGVLLSGGLDSSLIAALAARLLPE------------TPIDLFTVGFEGspTPDRAAARRVAEELGTEHHEVEVTIE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 304 EGLDAIRDVIYHIETYDVTTIRASTPMYLLARKIKAMGIKMVLSGEGADEIFGGYLYFHKAPNA--KEFHEETVRKLLAL 381
Cdd:cd01991 69 ELLDALPDVILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVLSGEGADELFGGYSRHRDAPLRgwEALEEELLRDLDRL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515633407 382 SMFDCARANKSLAAWGVEGRVPFLDKEFIDVAMRLNPEDKMCGNGKMEKHILRECFEDYLPDSIAWRQKEQFSDGV 457
Cdd:cd01991 149 WTRNLGRDDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIDPRGGGEKYILREAARDLLPDEIAWRPKRAIQFGS 224
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-192 |
5.09e-81 |
|
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: 252.86 E-value: 5.09e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 2 CSVFGILDIKsDAAALRPIALEMSKKLRHRGPDWSGIYAGEKAILAHERLAIVGLNSGAQPLYSQDKKHILAVNGEIYNH 81
Cdd:cd00712 1 CGIAGIIGLD-GASVDRATLERMLDALAHRGPDGSGIWIDEGVALGHRRLSIIDLSGGAQPMVSEDGRLVLVFNGEIYNY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 82 KELRARYEDK-YQFQTDSDCEVILALYQEMGADLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYQGYDEhGNYYVAS 160
Cdd:cd00712 80 RELRAELEALgHRFRTHSDTEVILHLYEEWGEDCLERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGRDG-GGLAFAS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515633407 161 EMKALVEVC---------------------------KTISEFPPGSFYSSKD--AEPQRYY 192
Cdd:cd00712 159 ELKALLALPgvpreldeaalaeylafqyvpaprtifKGIRKLPPGHYLTVDPggVEIRRYW 219
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-181 |
2.40e-53 |
|
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: 180.72 E-value: 2.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 2 CSVFGILDIKSDAAALRPIALEMSKKLRHRGPDWSGIYAGE---------------------------KAILAHERLAIV 54
Cdd:cd00352 1 CGIFGIVGADGAASLLLLLLLRGLAALEHRGPDGAGIAVYDgdglfvekragpvsdvaldlldeplksGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 55 GLNS--GAQPLYSQDKKHILAVNGEIYNHKELRARYEDK-YQFQTDSDCEVILALYQEMGA---------DLLEELNGIF 122
Cdd:cd00352 81 GLPSeaNAQPFRSEDGRIALVHNGEIYNYRELREELEARgYRFEGESDSEVILHLLERLGRegglfeaveDALKRLDGPF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 123 AFVLYDEEKDEYLVGRDHIGIIPLYQGYDEHGNYYVASEMKALVEVC-KTISEFPPGSFY 181
Cdd:cd00352 161 AFALWDGKPDRLFAARDRFGIRPLYYGITKDGGLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
48-165 |
5.64e-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: 173.47 E-value: 5.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 48 HERLAIVGLNSGAQPLY-SQDKKHILAVNGEIYNHKELRARYEDK-YQFQTDSDCEVILALYQEM-GADLLEELNGIFAF 124
Cdd:pfam13537 1 HRRLSIIDLEGGAQPMVsSEDGRYVIVFNGEIYNYRELRAELEAKgYRFRTHSDTEVILHLYEAEwGEDCVDRLNGMFAF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 515633407 125 VLYDEEKDEYLVGRDHIGIIPLYQGYDEHGNYYVASEMKAL 165
Cdd:pfam13537 81 AIWDRRRQRLFLARDRFGIKPLYYGRDDGGRLLFASELKAL 121
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
33-161 |
3.02e-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: 166.33 E-value: 3.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 33 PDWSGIYAGEKAILAHERLAIVGL-NSGAQPLYSQDKKHILAVNGEIYNHKELRARYEDK-YQFQTDSDCEVILALYQEM 110
Cdd:pfam13522 1 PDFSGIWVEGGVALGHVRLAIVDLpDAGNQPMLSRDGRLVLVHNGEIYNYGELREELADLgHAFRSRSDTEVLLALYEEW 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 515633407 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 |
1.52e-24 |
|
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: 108.16 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 1 MCSVFGILDIKS---DAAALRPialeMSKKLRHRGPDWSGIYAGEKAILAH-------ERLaivglnSGAQPLYSQDKKH 70
Cdd:NF033535 1 MSGIVGIYYLDGrpvDREDLQQ----MVDILAHRGPDGADIWCEGSVGLGHrmlwttpESL------LEKLPLVNQTGDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 71 ILAVNGEIYNHKELRARYE-DKYQFQTDSDCEVILALYQEMGADLLEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYqg 149
Cdd:NF033535 71 VITADARIDNRDELISALQlNNCPPEKITDSQLILAAYEKWGEQCPEHLLGDFAFAIWDKRKQQLFCARDHFGVKPFY-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 150 YDEHGN-YYVASEMKALV---EVCKTISE------------------------FPPGSFY--SSKDAEPQRYYIRDWNEY 199
Cdd:NF033535 149 YYQSDKrFAFASEIKALLclpEVPRRLNEvriadylalmledkvitfyqdifrLPPAHSMtvSQSGLQIRSYWSLDPSRE 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515633407 200 AAVQGNSTSKEELTEALEAAVKRQLMTDVPYGVLLSGGLDSSITSAVAKrfaamriedDEQSEAWWPQLHSF 271
Cdd:NF033535 229 LRLDSDEEYAEAFREIFTEAVRCRLRSAFPVGSHLSGGLDSSSITCVAR---------QLLAEEKKAPLHTF 291
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-165 |
9.57e-14 |
|
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: 71.34 E-value: 9.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 2 CSVFGILDiKSDAAALRPIALEMskkLRHRGPDWSGI----------------------------YAGEKAIlAHERLAI 53
Cdd:cd00715 1 CGVFGIYG-AEDAARLTYLGLYA---LQHRGQESAGIatsdgkrfhthkgmglvsdvfdeeklrrLPGNIAI-GHVRYST 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 54 VG--LNSGAQPLYSQDKKHILAV--NGEIYNHKELRARYEDKYQ-FQTDSDCEVILAL----YQEMG-----ADLLEELN 119
Cdd:cd00715 76 AGssSLENAQPFVVNSPLGGIALahNGNLVNAKELREELEEEGRiFQTTSDSEVILHLiarsLAKDDlfeaiIDALERVK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515633407 120 GIFAFVLYDEEKdeyLVG-RDHIGIIPLYQGYDEHGNYYVASEMKAL 165
Cdd:cd00715 156 GAYSLVIMTADG---LIAvRDPHGIRPLVLGKLEGDGYVVASESCAL 199
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-161 |
5.75e-13 |
|
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: 71.21 E-value: 5.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 1 MCSVFGILDiKSDAAALRPIALEMskkLRHRGPDWSGI----------------------------YAGEKAIlAHERLA 52
Cdd:COG0034 7 ECGVFGIYG-HEDVAQLTYYGLYA---LQHRGQESAGIatsdggrfhlhkgmglvsdvfdeedlerLKGNIAI-GHVRYS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 53 IVGLNS--GAQPLYSQDKKHILAV--NGEIYNHKELRARYEDKYQ-FQTDSDCEVILAL-YQEMG--------ADLLEEL 118
Cdd:COG0034 82 TTGSSSleNAQPFYVNSPFGSIALahNGNLTNAEELREELEEEGAiFQTTSDTEVILHLiARELTkedleeaiKEALRRV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515633407 119 NGIFAFVLYDEEKdeyLVG-RDHIGIIPLYQGYDEHGnYYVASE 161
Cdd:COG0034 162 KGAYSLVILTGDG---LIAaRDPNGIRPLVLGKLEDG-YVVASE 201
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-165 |
4.35e-12 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 68.55 E-value: 4.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 1 MCSVFGILDiKSDAAALRPIALEMskkLRHRGPDWSGIYAGEKAIL---------------------------AHERLAI 53
Cdd:PLN02440 1 ECGVVGIFG-DPEASRLCYLGLHA---LQHRGQEGAGIVTVDGNRLqsitgnglvsdvfdeskldqlpgdiaiGHVRYST 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 54 VGLNS--GAQPLYSQDKKHILAV--NGEIYNHKELRARYEDKYQ-FQTDSDCEVILALYQEMGA--------DLLEELNG 120
Cdd:PLN02440 77 AGASSlkNVQPFVANYRFGSIGVahNGNLVNYEELRAKLEENGSiFNTSSDTEVLLHLIAISKArpffsrivDACEKLKG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515633407 121 IFAFVLYDEEKdeyLVG-RDHIGIIPLYQGYDEHGNYYVASEMKAL 165
Cdd:PLN02440 157 AYSMVFLTEDK---LVAvRDPHGFRPLVMGRRSNGAVVFASETCAL 199
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-165 |
5.03e-11 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 65.06 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 2 CSVFGI-LDIKSDAAALRPIALEmskKLRHRGPDWSGI--YAGEK--------------------------AIlAHERLA 52
Cdd:PRK05793 15 CGVFGVfSKNNIDVASLTYYGLY---ALQHRGQESAGIavSDGEKikvhkgmglvsevfskeklkglkgnsAI-GHVRYS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 53 IVGLNS--GAQPLYSQDKKHILAV--NGEIYNHKELRARYEDK-YQFQTDSDCEVILAL--------YQEMGADLLEELN 119
Cdd:PRK05793 91 TTGASDldNAQPLVANYKLGSIAIahNGNLVNADVIRELLEDGgRIFQTSIDSEVILNLiarsakkgLEKALVDAIQAIK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515633407 120 GIFAFVLYDEEKdeyLVG-RDHIGIIPLYQGYDEhGNYYVASEMKAL 165
Cdd:PRK05793 171 GSYALVILTEDK---LIGvRDPHGIRPLCLGKLG-DDYILSSESCAL 213
|
|
| Gn_AT_II_novel |
cd03766 |
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its ... |
1-142 |
4.26e-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: 59.22 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 1 MCSVFGILDIKSDAAALRPIALEMSKKLRHRGPDWSG-----IYAGEKAILAHErLAIVGLNSGAQPLYSQDKKHILAVN 75
Cdd:cd03766 1 MCGILCSVSPSGPHINSSLLSEELLPNLRNRGPDYLStrqlsVTNWTLLFTSSV-LSLRGDHVTRQPLVDQSTGNVLQWN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515633407 76 GEIYNhkelraryEDKYQFQtDSDCEVILALYQEMGA------DLLEELNGIFAFVLYDEEKDEYLVGRDHIG 142
Cdd:cd03766 80 GELYN--------IDGVEDE-ENDTEVIFELLANCSSesqdilDVLSSIEGPFAFIYYDASENKLYFGRDCLG 143
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-172 |
6.00e-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: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 2 CSVFGILDiKSDAAalrPIALEMSKKLRHRGPDWSGI------------YAG-----EKAILAHERLAIVGL-------- 56
Cdd:cd00714 1 CGIVGYIG-KREAV---DILLEGLKRLEYRGYDSAGIavigdgslevvkAVGkvanlEEKLAEKPLSGHVGIghtrwath 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 57 ------NsgAQPLYSQDKKhiLAV--NGEIYNHKELRARYEDK-YQFQTDSDCEVI---LALYQEMGADLLE-------E 117
Cdd:cd00714 77 geptdvN--AHPHRSCDGE--IAVvhNGIIENYAELKEELEAKgYKFESETDTEVIahlIEYYYDGGLDLLEavkkalkR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 118 LNGIFAFVLYDEEKDEYLVG--RD---HIGIiplyqGYDEhgnYYVASEMKALVEVCKTI 172
Cdd:cd00714 153 LEGAYALAVISKDEPDEIVAarNGsplVIGI-----GDGE---NFVASDAPALLEHTRRV 204
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
60-172 |
5.20e-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: 58.87 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 60 AQPLYSQDKKhiLAV--NGEIYNHKELRARYEDK-YQFQTDSDCEVI---LALYQEMGADLLE-------ELNGIFAFVL 126
Cdd:COG0449 85 AHPHTSCSGR--IAVvhNGIIENYAELREELEAKgHTFKSETDTEVIahlIEEYLKGGGDLLEavrkalkRLEGAYALAV 162
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 515633407 127 YDEEKDEYLVG--RDHigiiPLYQGYDEHGNyYVASEMKALVEVCKTI 172
Cdd:COG0449 163 ISADEPDRIVAarKGS----PLVIGLGEGEN-FLASDVPALLPYTRRV 205
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-181 |
3.75e-08 |
|
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including 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 GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238888 [Multi-domain] Cd Length: 249 Bit Score: 54.58 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 2 CSVFGILDiKSDAAALRPIALEMSKKLRHRGPDWSG---IYAGEKA---------------------------------- 44
Cdd:cd01907 1 CGIFGIMS-KDGEPFVGALLVEMLDAMQERGPGDGAgfaLYGDPDAfvyssgkdmevfkgvgypediarrydleeykgyh 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 45 ILAHERLAIvglNS-----GAQPLYSQDkkhILAV-NGEIYNHKELRARYEDK-YQFQTDSDCEVILALYQEMGADL--- 114
Cdd:cd01907 80 WIAHTRQPT---NSavwwyGAHPFSIGD---IAVVhNGEISNYGSNREYLERFgYKFETETDTEVIAYYLDLLLRKGglp 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 115 --------------------------LEELNGIFAFVLYDeeKDEYLVGRDHIGIIPLYQGYDEhGNYYVASEMKALVEV 168
Cdd:cd01907 154 leyykhiirmpeeerelllalrltyrLADLDGPFTIIVGT--PDGFIVIRDRIKLRPAVVAETD-DYVAIASEECAIREI 230
|
250
....*....|....*..
gi 515633407 169 C----KTISEFPPGSFY 181
Cdd:cd01907 231 PdrdnAKVWEPRPGEYV 247
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-174 |
5.93e-08 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 55.43 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 1 MCSVFGILDiKSDAAalrPIALEMSKKLRHRGPDWSGIY------------AGEKAILAhERLAIVGLNSG--------- 59
Cdd:PRK00331 1 MCGIVGYVG-QRNAA---EILLEGLKRLEYRGYDSAGIAvlddgglevrkaVGKVANLE-AKLEEEPLPGTtgightrwa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 60 ---------AQPLYSQDKKhiLAV--NGEIYNHKELRARYEDK-YQFQTDSDCEVI---LALYQEMGADLLE-------E 117
Cdd:PRK00331 76 thgkpternAHPHTDCSGR--IAVvhNGIIENYAELKEELLAKgHVFKSETDTEVIahlIEEELKEGGDLLEavrkalkR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515633407 118 LNGIFAFVLYDEEKDEYLVG--RDHigiiPLYQGYDEHGNyYVASEMKALVEVCKTISE 174
Cdd:PRK00331 154 LEGAYALAVIDKDEPDTIVAarNGS----PLVIGLGEGEN-FLASDALALLPYTRRVIY 207
|
|
| DUF3700 |
pfam12481 |
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ... |
115-183 |
1.32e-07 |
|
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: 52.75 E-value: 1.32e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 115 LEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYQGYDEHGNYYVASEMKALVEVC-KTISEFPPGSFYSS 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 |
1.48e-07 |
|
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: 52.31 E-value: 1.48e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 115 LEELNGIFAFVLYDEEKDEYLVGRDHIGIIPLYQGYDEHGNYYVASEMKALVEVC-KTISEFPPGSFYSS 183
Cdd:cd01910 122 VKDLEGSFAFVLYDKKTSTVFVASDADGSVPLYWGIAADGSVVFSDDVELVKASCgKSFAPFPKGCFFHS 191
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
46-165 |
3.03e-06 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 50.02 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515633407 46 LAHERLAIVG--LNSGAQPLYSQDKKHILAVNGEIYNHKELRARYEDK-YQFQTDSDCEVI---LALYQEMGADLLE--- 116
Cdd:PTZ00295 99 IAHTRWATHGgkTDENAHPHCDYKKRIALVHNGTIENYVELKSELIAKgIKFRSETDSEVIanlIGLELDQGEDFQEavk 178
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 515633407 117 ----ELNGIFAFVLYDEE-KDEYLVGRDHigiIPLYQGYDEHGnYYVASEMKAL 165
Cdd:PTZ00295 179 saisRLQGTWGLCIIHKDnPDSLIVARNG---SPLLVGIGDDS-IYVASEPSAF 228
|
|
| AANH_superfamily |
cd01984 |
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ... |
230-275 |
4.72e-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: 4.72e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 515633407 230 YGVLLSGGLDSSITSAVAKRFAamrieddeqsEAWWPQLHSFAVGL 275
Cdd:cd01984 1 ILVPLSGGEDSSIALKHAKKFK----------TSKAEEVVVVHVGE 36
|
|
| betaLS_CarA_N |
cd01909 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_betaLS-type. Carbapenam ... |
76-147 |
8.52e-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: 40.94 E-value: 8.52e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515633407 76 GEIYNHKELR-ARYEDKYQFQTDSDCEVILALYQEMGADLLEELNGIFAFVLyDEEKDEYLVGRDHIGIIPLY 147
Cdd:cd01909 58 GELYNRDELRsLLGAGEGRSAVLGDAELLLLLLTRLGLHAFRLAEGDFCFFI-EDGNGRLTLATDHAGSVPVY 129
|
|
| |
