|
Name |
Accession |
Description |
Interval |
E-value |
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-602 |
0e+00 |
|
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: 651.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 1 MCGITGWVDWKKDLSNEhvILEKMANRIQHRGPDAEGFWFSPRAAFAHRRLIVIDP-EGGTQPktFRTGDYTYALTYNGE 79
Cdd:COG0367 1 MCGIAGIIDFDGGADRE--VLERMLDALAHRGPDGSGIWVDGGVALGHRRLSIIDLsEGGHQP--MVSEDGRYVLVFNGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 80 IYNFRELREQLRKCGHAFETHSDTEVLLHAYLEWKEDCVQHLNGIFAFALWDDQKQQLFLARDHLGVKPLFYTERNDSII 159
Cdd:COG0367 77 IYNYRELRAELEALGHRFRTHSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDGGGLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 160 FGSEIKALLAHPSVPAEIDADGLNEIFGLGlFRTPGCGVFKHIQEVRAGHCITFTRDKKV-VTKYWNLESKVHTDCT--E 236
Cdd:COG0367 157 FASELKALLAHPGVDRELDPEALAEYLTLG-YVPAPRTIFKGIRKLPPGHYLTVDAGGELeIRRYWDLEFVPHERSDseE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 237 DTSSHILSILQDTVKRQLIADVPLVCMLSGGLDSSGITALAGKEFaaeNKTLHTYSVDFVNSAKDfeltfartglDAPWV 316
Cdd:COG0367 236 EAVEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLS---KGPLKTFSIGFEDSAYD----------ESPYA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 317 KRVSEHVGTSHHDIILNAEELANHLFVPLRAKDLPSAGEMETSLYLLFCEMKKDATVALSGESADEVFGGYPWFHQEELL 396
Cdd:COG0367 303 RAVAEHLGTEHHEVTVTPEDLLDALPDLVWHLDEPFADPSAVPTYLLSRLAREHVKVVLSGEGADELFGGYPRYREAALL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 397 YvdkfpwltnwkntSPLLLNEINNEcnlenyidtrfqeailEVPTLEGESKKSAKQRQMFYLFLTRFLP-FLLDRKDRMS 475
Cdd:COG0367 383 L-------------SPDFAEALGGE----------------LVPRLYAESGAEDPLRRMLYLDLKTYLPgDLLVKVDRMS 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 476 MAVGFEVRVPFCDYRLVEYLWNVPFNIKSIDNIEKGILRRALQPALPDDVRNRRKSAYPTSQDPHYLQTIRHLSLDMCSN 555
Cdd:COG0367 434 MAHSLEVRVPFLDHRLVEFALSLPPELKLRGGRGKYLLRKALEGLLPDEVLDRPKQGFPVPLGPWLRGPLREWLEDLLSD 513
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 872543463 556 KNNPIFSLINHSILLSIADESNKEINNFeaRSAMEYMLQVNEWLKTY 602
Cdd:COG0367 514 ESLAARGLFDPDAVRRLLEEHLAGRRDH--SRKLWSLLMLELWLRRF 558
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-533 |
8.26e-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: 509.18 E-value: 8.26e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 4 ITGWVDWKKDLSNEHVILEKMANRIQHRGPDAEGF-WFSPRAAFAHRRLIVIDPEGGTQPktFRTGDYTYALTYNGEIYN 82
Cdd:TIGR01536 1 IAGFFDLDDKAVEEDEAIKRMSDTIAHRGPDASGIeYKDGNAILGHRRLAIIDLSGGAQP--MSNEGKTYVIVFNGEIYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 83 FRELREQLRKCGHAFETHSDTEVLLHAYLEWKEDCVQHLNGIFAFALWDDQKQQLFLARDHLGVKPLFYTERNDSIIFGS 162
Cdd:TIGR01536 79 HEELREELEAKGYTFQTDSDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYDGGQLYFAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 163 EIKALLAHPSVPAEIDADGLNEIFGLGLFRTPGCgVFKHIQEVRAGHCITFTRDKKVVTKYWNLESKVHTDCTEDTSSHI 242
Cdd:TIGR01536 159 EIKALLAHPNIKPFPDGAALAPGFGFVRVPPPST-FFRGVFELEPGHDLPLDDDGLNIERYYWERRDEHTDSEEDLVDEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 243 LSILQDTVKRQLIADVPLVCMLSGGLDSSGITALAGKEfaAENKTLHTYSVDFVNSaKDFEltfartglDAPWVKRVSEH 322
Cdd:TIGR01536 238 RSLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARRE--APRGPVHTFSIGFEGS-PDFD--------ESKYARKVADH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 323 VGTSHHDIILNAEELANHLFVPLRAKDLPSAGEMETSLYLLFCEMKKDA-TVALSGESADEVFGGYPWFHqeellyvdKF 401
Cdd:TIGR01536 307 LGTEHHEVLFSVEEGLDALPEVIYHLEEPTTIRASIPLYLLSKLAREDGvKVVLSGEGADELFGGYLYFH--------EA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 402 PWLTNWkntsplllneinnecnlenyidtrfqeailevptlegeskksakQRQMFYLFLTRFLPFLLDRKDRMSMAVGFE 481
Cdd:TIGR01536 379 PAAEAL--------------------------------------------REELQYLDLELYMPGLLRRKDRMSMAHSLE 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 872543463 482 VRVPFCDYRLVEYLWNVPFNIKSIDNIEKGILRRALQPALPDDVRNRRKSAY 533
Cdd:TIGR01536 415 VRVPFLDHELVEYALSIPPEMKLRDGKEKYLLREAFEGYLPEEILWRPKEGF 466
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-225 |
9.13e-114 |
|
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: 338.38 E-value: 9.13e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 2 CGITGWVDWKKDLSNEHViLEKMANRIQHRGPDAEGFWFSPRAAFAHRRLIVIDPEGGTQPktFRTGDYTYALTYNGEIY 81
Cdd:cd00712 1 CGIAGIIGLDGASVDRAT-LERMLDALAHRGPDGSGIWIDEGVALGHRRLSIIDLSGGAQP--MVSEDGRLVLVFNGEIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 82 NFRELREQLRKCGHAFETHSDTEVLLHAYLEWKEDCVQHLNGIFAFALWDDQKQQLFLARDHLGVKPLFYTERNDSIIFG 161
Cdd:cd00712 78 NYRELRAELEALGHRFRTHSDTEVILHLYEEWGEDCLERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGRDGGGLAFA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872543463 162 SEIKALLAHPSVPAEIDADGLNEIFgLGLFRTPGCGVFKHIQEVRAGHCITFTRDKKVVTKYWN 225
Cdd:cd00712 158 SELKALLALPGVPRELDEAALAEYL-AFQYVPAPRTIFKGIRKLPPGHYLTVDPGGVEIRRYWD 220
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-533 |
6.89e-95 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 301.83 E-value: 6.89e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 1 MCGITGWVDWKKDLSNEHVILEKMANRIQHRGPDAEGFWFSPRAAFAHRRLIVIDPEGGTQPktFRTGDYTYALTYNGEI 80
Cdd:PRK09431 1 MCGIFGILDIKTDADELRKKALEMSRLMRHRGPDWSGIYASDNAILGHERLSIVDVNGGAQP--LYNEDGTHVLAVNGEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 81 YNFRELREQLrKCGHAFETHSDTEVLLHAYLEWKEDCVQHLNGIFAFALWDDQKQQLFLARDHLGVKPLFYTER-NDSII 159
Cdd:PRK09431 79 YNHQELRAEL-GDKYAFQTGSDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDeHGNLY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 160 FGSEIKALlahpsvpaeidadglneifglglfrTPGCgvfKHIQEVRAGHciTFTRDKKVVTKYWNLESKVHTDCTEDTS 239
Cdd:PRK09431 158 FASEMKAL-------------------------VPVC---KTIKEFPPGH--YYWSKDGEFVRYYQRDWFDYDAVKDNVT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 240 S--HILSILQDTVKRQLIADVPLVCMLSGGLDSSGITALAGKEFAAENKT----------LHTYSVDFVNSAkdfELTFA 307
Cdd:PRK09431 208 DknELRDALEAAVKKRLMSDVPYGVLLSGGLDSSLISAIAKKYAARRIEDderseawwpqLHSFAVGLEGSP---DLKAA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 308 RtgldapwvkRVSEHVGTSHHDIILNAEE-------LANHL--FVP--LRAkdlpsagemETSLYLLfCEMKK--DATVA 374
Cdd:PRK09431 285 R---------EVADHLGTVHHEIHFTVQEgldalrdVIYHLetYDVttIRA---------STPMYLM-ARKIKamGIKMV 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 375 LSGESADEVFGGYpwfhqeelLYVDKFPwltnwkntsplllneiNNEcnlenyidtRFQEailevptlegESKKSAKQRQ 454
Cdd:PRK09431 346 LSGEGADELFGGY--------LYFHKAP----------------NAK---------EFHE----------ETVRKLRALH 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 455 MFYLFltrflpflldRKDRMSMAVGFEVRVPFCDYRLVEYLWNVPFNIKSI--DNIEKGILRRALQPALPDDVRNRRKSA 532
Cdd:PRK09431 383 MYDCL----------RANKAMMAWGVEARVPFLDKEFLDVAMRINPEDKMCgnGKMEKHILREAFEGYLPESILWRQKEQ 452
|
.
gi 872543463 533 Y 533
Cdd:PRK09431 453 F 453
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
241-575 |
1.59e-90 |
|
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: 281.04 E-value: 1.59e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 241 HILSILQDTVKRQLIADVPLVCMLSGGLDSSGITALAGKEFAAEnktLHTYSVDFVNSAKDfeltfartglDAPWVKRVS 320
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSPSP---LHTFSIGFEGRGYD----------EAPYAREVA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 321 EHVGTSHHDIILNAEELANHLFVPLRAKDLPSAGEMETSLYLLFCEMKKD-ATVALSGESADEVFGGYPWFHQEEllyvd 399
Cdd:pfam00733 68 EHLGTDHHELVVTPEDLLDALPDVIWHLDEPFADPSAIPLYLLSRLARRKgVKVVLSGEGADELFGGYPFYKGED----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 400 kfpwltnwkntsplllneinnecnlenyidtrfqeailevptlegeskksaKQRQMFYLFLTRFLPFLLDRKDRMSMAVG 479
Cdd:pfam00733 143 ---------------------------------------------------PLRRMLYLDLKTLLPGDLLRADRMSMAHG 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 480 FEVRVPFCDYRLVEYLWNVPFNIKSIDNIEKGILRRALQPALPDDVRNRRKSAYPT-SQDPHYLQTIRHLSLDMCSNKNN 558
Cdd:pfam00733 172 LEVRVPFLDHRLVEYALRLPPELKLRGGIEKYILREALEGILPDEILERPKEGFSApVGDWKLRGPLRELAEDLLSDSRL 251
|
330
....*....|....*..
gi 872543463 559 PIFSLINHSILLSIADE 575
Cdd:pfam00733 252 AKEGLLDREAVRELLDE 268
|
|
| lass_lactam_cya |
NF033535 |
lasso peptide isopeptide bond-forming cyclase; Members of this family are the isopeptide ... |
21-529 |
2.64e-55 |
|
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: 198.68 E-value: 2.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 21 LEKMANRIQHRGPDAEGFWFSPRAAFAHRRLIVIdPEG--GTQPKTFRTGDYtyALTYNGEIYNFREL--REQLRKCghA 96
Cdd:NF033535 20 LQQMVDILAHRGPDGADIWCEGSVGLGHRMLWTT-PESllEKLPLVNQTGDL--VITADARIDNRDELisALQLNNC--P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 97 FETHSDTEVLLHAYLEWKEDCVQHLNGIFAFALWDDQKQQLFLARDHLGVKPLFYTERNDSIIFGSEIKALLAHPSVPAE 176
Cdd:NF033535 95 PEKITDSQLILAAYEKWGEQCPEHLLGDFAFAIWDKRKQQLFCARDHFGVKPFYYYQSDKRFAFASEIKALLCLPEVPRR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 177 IdadglNEI----FGLGLFRTPGCGVFKHIQEVRAGHCITFTRDKKVVTKYWNLESK--VHTDCTEDTSSHILSILQDTV 250
Cdd:NF033535 175 L-----NEVriadYLALMLEDKVITFYQDIFRLPPAHSMTVSQSGLQIRSYWSLDPSreLRLDSDEEYAEAFREIFTEAV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 251 KRQLIADVPLVCMLSGGLDSSGITALAGKEFAAENKT-LHTYSVDF--------------VNSAKDFELTFARTGLDAPW 315
Cdd:NF033535 250 RCRLRSAFPVGSHLSGGLDSSSITCVARQLLAEEKKApLHTFSNIFdkvtecderpfinaVLEQGGLIPHYVHADQFGPL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 316 --VKRVSEH-----VGTSHH--------------DIILN---AEELANHLFVPLRakDLPSAGEMETslylLFCEMKkdA 371
Cdd:NF033535 330 sdLEQIFEYedepfLGPNHFlpwglnraaqkegvRILLDgfdGDSTVSHGHGYLT--ELANQGKWLT----FAQEIR--A 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 372 TVALSGESADEVFGGYPWFHQEELlyVDKFPWLTNWK--NTSPLLLNEINNECNLENYIDTRFQEAILEV-PTLEGESKK 448
Cdd:NF033535 402 LSKNYGTSPWGLLRQYGLPYLEKL--ARQFKWLTFLKpaNQIHKHFGISRRQLFLQHGIKPLVPRALLKLwRKLRGQAQP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 449 SAKQRQMFYL-------FLTRF--------------------------LPFLLDRKDRMSMAVGFEVRVPFCDYRLVEYL 495
Cdd:NF033535 480 GNSWRPIINPdfaerigLKERIqrldpppssspltvreehwqsltsgiLPFVLEVLDKYAAAFSLEARHPFMDKRLVEFC 559
|
570 580 590
....*....|....*....|....*....|....*...
gi 872543463 496 WNVPFNIKsidnIEKG----ILRRALQPALPDDVRNRR 529
Cdd:NF033535 560 LALPPEQK----LRQGwsrmVMRRAMEGILPPQVQWRG 593
|
|
| macrolact_Ik_Al |
NF033561 |
albusnodin/ikarugamycin family macrolactam cyclase; Members of this family show homology ... |
166-354 |
2.78e-03 |
|
albusnodin/ikarugamycin family macrolactam cyclase; Members of this family show homology enzymes known to form the lactam bond of the isopeptide linkage of lasso peptides. This family includes the peptide cyclase involved in biosynthesis of the lasso peptide albusnodin. However, another member of this family belongs to the biosynthesis cassette for ikarugamycin, a macrolactam whose biosynthesis relies on a hybrid PKS/NRPS system, not a ribosomally produced peptide.
Pssm-ID: 468087 [Multi-domain] Cd Length: 561 Bit Score: 40.67 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 166 ALLAhPSVPAEIdadglneifglglfrtPGCGVFKHIQEVRAGHCITFTRDKKV-VTKYWnleSKVHTDCTEDTSSHILS 244
Cdd:NF033561 138 ALLA-PSVPALA----------------AGRSAFAGVEQVPPGHRLTLPADGGApRTPWW---WRPDPRPGPDAVARLRA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 245 ILQDTVKRQLIADVPLVCMLSGGLDSSGITALAGkEFAAENKTLH--TYSVDFVNSAKDfeLTFARTgldapwvkrVSEH 322
Cdd:NF033561 198 ALAAAVALRVDGAPPLSSDLSGGLDSTTLALLAA-RCLPVGRRLTgvTVHPEGRTEGGD--LDYARL---------AARA 265
|
170 180 190
....*....|....*....|....*....|..
gi 872543463 323 VGTSHHdiilnaeelanhlFVPLRAKDLPSAG 354
Cdd:NF033561 266 PRIRHR-------------LLPLGAEHPPYTA 284
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-602 |
0e+00 |
|
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: 651.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 1 MCGITGWVDWKKDLSNEhvILEKMANRIQHRGPDAEGFWFSPRAAFAHRRLIVIDP-EGGTQPktFRTGDYTYALTYNGE 79
Cdd:COG0367 1 MCGIAGIIDFDGGADRE--VLERMLDALAHRGPDGSGIWVDGGVALGHRRLSIIDLsEGGHQP--MVSEDGRYVLVFNGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 80 IYNFRELREQLRKCGHAFETHSDTEVLLHAYLEWKEDCVQHLNGIFAFALWDDQKQQLFLARDHLGVKPLFYTERNDSII 159
Cdd:COG0367 77 IYNYRELRAELEALGHRFRTHSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDGGGLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 160 FGSEIKALLAHPSVPAEIDADGLNEIFGLGlFRTPGCGVFKHIQEVRAGHCITFTRDKKV-VTKYWNLESKVHTDCT--E 236
Cdd:COG0367 157 FASELKALLAHPGVDRELDPEALAEYLTLG-YVPAPRTIFKGIRKLPPGHYLTVDAGGELeIRRYWDLEFVPHERSDseE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 237 DTSSHILSILQDTVKRQLIADVPLVCMLSGGLDSSGITALAGKEFaaeNKTLHTYSVDFVNSAKDfeltfartglDAPWV 316
Cdd:COG0367 236 EAVEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLS---KGPLKTFSIGFEDSAYD----------ESPYA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 317 KRVSEHVGTSHHDIILNAEELANHLFVPLRAKDLPSAGEMETSLYLLFCEMKKDATVALSGESADEVFGGYPWFHQEELL 396
Cdd:COG0367 303 RAVAEHLGTEHHEVTVTPEDLLDALPDLVWHLDEPFADPSAVPTYLLSRLAREHVKVVLSGEGADELFGGYPRYREAALL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 397 YvdkfpwltnwkntSPLLLNEINNEcnlenyidtrfqeailEVPTLEGESKKSAKQRQMFYLFLTRFLP-FLLDRKDRMS 475
Cdd:COG0367 383 L-------------SPDFAEALGGE----------------LVPRLYAESGAEDPLRRMLYLDLKTYLPgDLLVKVDRMS 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 476 MAVGFEVRVPFCDYRLVEYLWNVPFNIKSIDNIEKGILRRALQPALPDDVRNRRKSAYPTSQDPHYLQTIRHLSLDMCSN 555
Cdd:COG0367 434 MAHSLEVRVPFLDHRLVEFALSLPPELKLRGGRGKYLLRKALEGLLPDEVLDRPKQGFPVPLGPWLRGPLREWLEDLLSD 513
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 872543463 556 KNNPIFSLINHSILLSIADESNKEINNFeaRSAMEYMLQVNEWLKTY 602
Cdd:COG0367 514 ESLAARGLFDPDAVRRLLEEHLAGRRDH--SRKLWSLLMLELWLRRF 558
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-533 |
8.26e-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: 509.18 E-value: 8.26e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 4 ITGWVDWKKDLSNEHVILEKMANRIQHRGPDAEGF-WFSPRAAFAHRRLIVIDPEGGTQPktFRTGDYTYALTYNGEIYN 82
Cdd:TIGR01536 1 IAGFFDLDDKAVEEDEAIKRMSDTIAHRGPDASGIeYKDGNAILGHRRLAIIDLSGGAQP--MSNEGKTYVIVFNGEIYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 83 FRELREQLRKCGHAFETHSDTEVLLHAYLEWKEDCVQHLNGIFAFALWDDQKQQLFLARDHLGVKPLFYTERNDSIIFGS 162
Cdd:TIGR01536 79 HEELREELEAKGYTFQTDSDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYDGGQLYFAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 163 EIKALLAHPSVPAEIDADGLNEIFGLGLFRTPGCgVFKHIQEVRAGHCITFTRDKKVVTKYWNLESKVHTDCTEDTSSHI 242
Cdd:TIGR01536 159 EIKALLAHPNIKPFPDGAALAPGFGFVRVPPPST-FFRGVFELEPGHDLPLDDDGLNIERYYWERRDEHTDSEEDLVDEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 243 LSILQDTVKRQLIADVPLVCMLSGGLDSSGITALAGKEfaAENKTLHTYSVDFVNSaKDFEltfartglDAPWVKRVSEH 322
Cdd:TIGR01536 238 RSLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARRE--APRGPVHTFSIGFEGS-PDFD--------ESKYARKVADH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 323 VGTSHHDIILNAEELANHLFVPLRAKDLPSAGEMETSLYLLFCEMKKDA-TVALSGESADEVFGGYPWFHqeellyvdKF 401
Cdd:TIGR01536 307 LGTEHHEVLFSVEEGLDALPEVIYHLEEPTTIRASIPLYLLSKLAREDGvKVVLSGEGADELFGGYLYFH--------EA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 402 PWLTNWkntsplllneinnecnlenyidtrfqeailevptlegeskksakQRQMFYLFLTRFLPFLLDRKDRMSMAVGFE 481
Cdd:TIGR01536 379 PAAEAL--------------------------------------------REELQYLDLELYMPGLLRRKDRMSMAHSLE 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 872543463 482 VRVPFCDYRLVEYLWNVPFNIKSIDNIEKGILRRALQPALPDDVRNRRKSAY 533
Cdd:TIGR01536 415 VRVPFLDHELVEYALSIPPEMKLRDGKEKYLLREAFEGYLPEEILWRPKEGF 466
|
|
| eps_aminotran_1 |
TIGR03108 |
exosortase A system-associated amidotransferase 1; The predicted protein-sorting ... |
1-530 |
7.88e-120 |
|
exosortase A system-associated amidotransferase 1; The predicted protein-sorting transpeptidase that we call exosortase (see TIGR02602) has distinct subclasses that associated with different types of exopolysaccharide production loci. This model represents a distinct clade among a set of amidotransferases largely annotated (not necessarily accurately) as glutatime-hydrolyzing asparagine synthases. Members of this clade are essentially restricted to the characteristic exopolysaccharide (EPS) regions that contain the exosortase 1 genome (xrtA), in genomes that also have numbers of PEP-CTERM domain (TIGR02595) proteins.
Pssm-ID: 132152 [Multi-domain] Cd Length: 628 Bit Score: 368.68 E-value: 7.88e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 1 MCGITGWVDW--KKDLSNEhvILEKMANRIQHRGPDAEGFWFSPRAAFAHRRLIVIDPEGGTQPKTFRTGDytYALTYNG 78
Cdd:TIGR03108 1 MCGITGIFDLtgQRPIDRD--LLRRMNDAQAHRGPDGGGVHVEPGIGLGHRRLSIIDLSGGQQPLFNEDGS--VVVVFNG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 79 EIYNFRELREQLRKCGHAFETHSDTEVLLHAYLEWKEDCVQHLNGIFAFALWDDQKQQLFLARDHLGVKPLFYTERND-S 157
Cdd:TIGR03108 77 EIYNFQELVAELQALGHVFRTRSDTEVIVHAWEEWGEACVERFRGMFAFALWDRNQETLFLARDRLGIKPLYYALLADgW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 158 IIFGSEIKALLAHPSVPAEIDADGLNEIFGLGLFRTPGcGVFKHIQEVRAGHCITFTRDKKVVT--KYWNLESKVHTDCT 235
Cdd:TIGR03108 157 FIFGSELKALTAHPSLPRELDPLAVEDYFAYGYVPDPR-TIFKGVKKLEPGHTLTLRRGAPPARprCYWDVSFAPAAPLS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 236 E-DTSSHILSILQDTVKRQLIADVPLVCMLSGGLDSSGITALAGKefaAENKTLHTYSVDFVNSAKDfeltfartglDAP 314
Cdd:TIGR03108 236 EaDALAELIERLREAVRSRMVADVPLGAFLSGGVDSSAVVALMAG---LSDTPVNTCSIAFDDPAFD----------ESA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 315 WVKRVSEHVGTSHHDIILNAEELAnhLFVPLRA-KDLPSAGEMETSLYLLfCEM-KKDATVALSGESADEVFGGYP---W 389
Cdd:TIGR03108 303 YARQVAERYGTNHRVETVDPDDFS--LVDRLAGlYDEPFADSSALPTYRV-CELaRKRVTVALSGDGGDELFAGYRryrW 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 390 FHQEE-------------------LLYvDKFPWLTNW---KNTSPLLlneinNECNLENY------IDTRFQEAILEvPT 441
Cdd:TIGR03108 380 HMAEErvrgilplglrrplfgtlgRLY-PKADWAPRMlraKTTFQAL-----ARDPLEGYfhsvsvLDNALRRQLFS-PD 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 442 LEGE-------------SKKSAKQR---QMFYLFLTRFLPF-LLDRKDRMSMAVGFEVRVPFCDYRLVEYLWNVPFNIKS 504
Cdd:TIGR03108 453 FRRElqgyraievlrrhAARAPTDDalsLAQYLDLKTYLPGdILTKVDRASMAHGLEVRVPLLDHRLVEWAAGLPPDLKL 532
|
570 580
....*....|....*....|....*.
gi 872543463 505 IDNIEKGILRRALQPALPDDVRNRRK 530
Cdd:TIGR03108 533 RGGEGKYLLKKAMRPYLPDDVLYRPK 558
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-225 |
9.13e-114 |
|
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: 338.38 E-value: 9.13e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 2 CGITGWVDWKKDLSNEHViLEKMANRIQHRGPDAEGFWFSPRAAFAHRRLIVIDPEGGTQPktFRTGDYTYALTYNGEIY 81
Cdd:cd00712 1 CGIAGIIGLDGASVDRAT-LERMLDALAHRGPDGSGIWIDEGVALGHRRLSIIDLSGGAQP--MVSEDGRLVLVFNGEIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 82 NFRELREQLRKCGHAFETHSDTEVLLHAYLEWKEDCVQHLNGIFAFALWDDQKQQLFLARDHLGVKPLFYTERNDSIIFG 161
Cdd:cd00712 78 NYRELRAELEALGHRFRTHSDTEVILHLYEEWGEDCLERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGRDGGGLAFA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872543463 162 SEIKALLAHPSVPAEIDADGLNEIFgLGLFRTPGCGVFKHIQEVRAGHCITFTRDKKVVTKYWN 225
Cdd:cd00712 158 SELKALLALPGVPRELDEAALAEYL-AFQYVPAPRTIFKGIRKLPPGHYLTVDPGGVEIRRYWD 220
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-533 |
6.89e-95 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 301.83 E-value: 6.89e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 1 MCGITGWVDWKKDLSNEHVILEKMANRIQHRGPDAEGFWFSPRAAFAHRRLIVIDPEGGTQPktFRTGDYTYALTYNGEI 80
Cdd:PRK09431 1 MCGIFGILDIKTDADELRKKALEMSRLMRHRGPDWSGIYASDNAILGHERLSIVDVNGGAQP--LYNEDGTHVLAVNGEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 81 YNFRELREQLrKCGHAFETHSDTEVLLHAYLEWKEDCVQHLNGIFAFALWDDQKQQLFLARDHLGVKPLFYTER-NDSII 159
Cdd:PRK09431 79 YNHQELRAEL-GDKYAFQTGSDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDeHGNLY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 160 FGSEIKALlahpsvpaeidadglneifglglfrTPGCgvfKHIQEVRAGHciTFTRDKKVVTKYWNLESKVHTDCTEDTS 239
Cdd:PRK09431 158 FASEMKAL-------------------------VPVC---KTIKEFPPGH--YYWSKDGEFVRYYQRDWFDYDAVKDNVT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 240 S--HILSILQDTVKRQLIADVPLVCMLSGGLDSSGITALAGKEFAAENKT----------LHTYSVDFVNSAkdfELTFA 307
Cdd:PRK09431 208 DknELRDALEAAVKKRLMSDVPYGVLLSGGLDSSLISAIAKKYAARRIEDderseawwpqLHSFAVGLEGSP---DLKAA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 308 RtgldapwvkRVSEHVGTSHHDIILNAEE-------LANHL--FVP--LRAkdlpsagemETSLYLLfCEMKK--DATVA 374
Cdd:PRK09431 285 R---------EVADHLGTVHHEIHFTVQEgldalrdVIYHLetYDVttIRA---------STPMYLM-ARKIKamGIKMV 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 375 LSGESADEVFGGYpwfhqeelLYVDKFPwltnwkntsplllneiNNEcnlenyidtRFQEailevptlegESKKSAKQRQ 454
Cdd:PRK09431 346 LSGEGADELFGGY--------LYFHKAP----------------NAK---------EFHE----------ETVRKLRALH 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 455 MFYLFltrflpflldRKDRMSMAVGFEVRVPFCDYRLVEYLWNVPFNIKSI--DNIEKGILRRALQPALPDDVRNRRKSA 532
Cdd:PRK09431 383 MYDCL----------RANKAMMAWGVEARVPFLDKEFLDVAMRINPEDKMCgnGKMEKHILREAFEGYLPESILWRQKEQ 452
|
.
gi 872543463 533 Y 533
Cdd:PRK09431 453 F 453
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
241-575 |
1.59e-90 |
|
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: 281.04 E-value: 1.59e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 241 HILSILQDTVKRQLIADVPLVCMLSGGLDSSGITALAGKEFAAEnktLHTYSVDFVNSAKDfeltfartglDAPWVKRVS 320
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSPSP---LHTFSIGFEGRGYD----------EAPYAREVA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 321 EHVGTSHHDIILNAEELANHLFVPLRAKDLPSAGEMETSLYLLFCEMKKD-ATVALSGESADEVFGGYPWFHQEEllyvd 399
Cdd:pfam00733 68 EHLGTDHHELVVTPEDLLDALPDVIWHLDEPFADPSAIPLYLLSRLARRKgVKVVLSGEGADELFGGYPFYKGED----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 400 kfpwltnwkntsplllneinnecnlenyidtrfqeailevptlegeskksaKQRQMFYLFLTRFLPFLLDRKDRMSMAVG 479
Cdd:pfam00733 143 ---------------------------------------------------PLRRMLYLDLKTLLPGDLLRADRMSMAHG 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 480 FEVRVPFCDYRLVEYLWNVPFNIKSIDNIEKGILRRALQPALPDDVRNRRKSAYPT-SQDPHYLQTIRHLSLDMCSNKNN 558
Cdd:pfam00733 172 LEVRVPFLDHRLVEYALRLPPELKLRGGIEKYILREALEGILPDEILERPKEGFSApVGDWKLRGPLRELAEDLLSDSRL 251
|
330
....*....|....*..
gi 872543463 559 PIFSLINHSILLSIADE 575
Cdd:pfam00733 252 AKEGLLDREAVRELLDE 268
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-530 |
4.62e-72 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 242.36 E-value: 4.62e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 1 MCGITGWVDWKKDLSNEHVILEKMANRIQHRGPDAEGFWFSPRAAFAHRRLIVIDPEGGTQPktFRTGDYTYALTYNGEI 80
Cdd:PLN02549 1 MCGILAVLGCSDDSQAKRSRVLELSRRLRHRGPDWSGLYGNEDCYLAHERLAIMDPESGDQP--LYNEDKTIVVTANGEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 81 YNFRELREQLRKcgHAFETHSDTEVLLHAYLEWKEDCVQHLNGIFAFALWDDQKQQLFLARDHLGVKPLFYTERND-SII 159
Cdd:PLN02549 79 YNHKELREKLKL--HKFRTGSDCEVIAHLYEEHGEEFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGLDgSVW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 160 FGSEIKALlahpsvpaeidadglneifglglfrtpgCGVFKHIQEVRAGHCitFTRDKKVVTKYWNLE--SKVHTDCTED 237
Cdd:PLN02549 157 FASEMKAL----------------------------CDDCERFEEFPPGHY--YSSKAGGFRRWYNPPwfSESIPSTPYD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 238 TsSHILSILQDTVKRQLIADVPLVCMLSGGLDSSGITALAGKEFAAENKT------LHTYSVDFVNSAkdfELTFARtgl 311
Cdd:PLN02549 207 P-LVLREAFEKAVIKRLMTDVPFGVLLSGGLDSSLVASIAARHLAETKAArqwgqqLHSFCVGLEGSP---DLKAAR--- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 312 dapwvkRVSEHVGTSHH-------DIILNAEELANHL----FVPLRAkdlpsagemETSLYLLFCEMK-KDATVALSGES 379
Cdd:PLN02549 280 ------EVADYLGTVHHefhftvqEGIDAIEDVIYHLetydVTTIRA---------STPMFLMSRKIKsLGVKMVLSGEG 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 380 ADEVFGGYPWFHqeellyvdKFPwltnwkNTsplllNEINNECnlenyidtrfqeailevptlegeskksakQRQMFYLF 459
Cdd:PLN02549 345 SDEIFGGYLYFH--------KAP------NK-----EEFHKET-----------------------------CRKIKALH 376
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872543463 460 LTRFLpflldRKDRMSMAVGFEVRVPFCDYRLVEYLWNVPFNIKSIDN----IEKGILRRAL----QPALPDDVRNRRK 530
Cdd:PLN02549 377 QYDCL-----RANKSTSAWGLEARVPFLDKEFIDVAMSIDPEWKMIRPgegrIEKWVLRKAFddeeDPYLPKHILWRQK 450
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
48-169 |
1.87e-66 |
|
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: 212.38 E-value: 1.87e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 48 HRRLIVIDPEGGTQPkTFRTGDYTYALTYNGEIYNFRELREQLRKCGHAFETHSDTEVLLHAY-LEWKEDCVQHLNGIFA 126
Cdd:pfam13537 1 HRRLSIIDLEGGAQP-MVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYeAEWGEDCVDRLNGMFA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 872543463 127 FALWDDQKQQLFLARDHLGVKPLFYTERND-SIIFGSEIKALLA 169
Cdd:pfam13537 80 FAIWDRRRQRLFLARDRFGIKPLYYGRDDGgRLLFASELKALLA 123
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-530 |
3.34e-64 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 221.51 E-value: 3.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 1 MCGITGWVDwkkdLSNEHVILEKMA----NRIQHRGPDAEGFWFSPRA-----AFAHRRLIVIDPEGGTQPktFRTGDYT 71
Cdd:PTZ00077 1 MCGILAIFN----SKGERHELRRKAlelsKRLRHRGPDWSGIIVLENSpgtynILAHERLAIVDLSDGKQP--LLDDDET 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 72 YALTYNGEIYNFRELREQLRKCGHAFETHSDTEVLLHAYLEWKE-DCVQHLNGIFAFALWDDQKQQLFLARDHLGVKPLF 150
Cdd:PTZ00077 75 VALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKEYGPkDFWNHLDGMFATVIYDMKTNTFFAARDHIGIIPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 151 Y-TERNDSIIFGSEIKALlaHPSVpaeidadglneifglglfrtpgcgvfKHIQEVRAGHCITFTRDKKVVTKY-----W 224
Cdd:PTZ00077 155 IgYAKDGSIWFSSELKAL--HDQC--------------------------VEVKQFPPGHYYDQTKEKGEFVRYynpnwH 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 225 NLESKVHTDctEDTSSHILSILQDTVKRQLIADVPLVCMLSGGLDSSGITALAGKEFAAEN--------KTLHTYSVDFV 296
Cdd:PTZ00077 207 DFDHPIPTG--EIDLEEIREALEAAVRKRLMGDVPFGLFLSGGLDSSIVAAIVAKLIKNGEidlskrgmPKLHSFCIGLE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 297 NSAkdfELTFARtgldapwvkRVSEHVGTSHHDIILNAEELANHL-----------FVPLRAkdlpsagemETSLYLLfC 365
Cdd:PTZ00077 285 GSP---DLKAAR---------KVAEYLGTEHHEFTFTVEEGIDALpdviyhtetydVTTIRA---------STPMYLL-S 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 366 EMKKDATV--ALSGESADEVFGGYPWFHqeellyvdkfpwltNWKNTsplllNEINNECnlenyidtrfqeailevptle 443
Cdd:PTZ00077 343 RRIKALGIkmVLSGEGSDELFGGYLYFH--------------KAPNR-----EEFHREL--------------------- 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 444 geskksakQRQMFYLFLTRFLpflldRKDRMSMAVGFEVRVPFCDYRLVEYLWNVPFNIKSIDN----IEKGILRRALQ- 518
Cdd:PTZ00077 383 --------VRKLHDLHKYDCL-----RANKATMAWGIEARVPFLDKDFLEYVMNIDPKYKMCNAfegqMEKYILRKAFEg 449
|
570
....*....|....*
gi 872543463 519 ---PALPDDVRNRRK 530
Cdd:PTZ00077 450 lekPYLPDEILWRQK 464
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-171 |
7.24e-57 |
|
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: 190.74 E-value: 7.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 2 CGITGWVDWKKDLSNEHVILEKMANRIQHRGPDAEGFWFSP---------------------------RAAFAHRRLIVI 54
Cdd:cd00352 1 CGIFGIVGADGAASLLLLLLLRGLAALEHRGPDGAGIAVYDgdglfvekragpvsdvaldlldeplksGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 55 DP--EGGTQPktFRTGDYTYALTYNGEIYNFRELREQLRKCGHAFETHSDTEVLLHAYLEWK---------EDCVQHLNG 123
Cdd:cd00352 81 GLpsEANAQP--FRSEDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGregglfeavEDALKRLDG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 872543463 124 IFAFALWDDQKQQLFLARDHLGVKPLFYTERND-SIIFGSEIKALLAHP 171
Cdd:cd00352 159 PFAFALWDGKPDRLFAARDRFGIRPLYYGITKDgGLVFASEPKALLALP 207
|
|
| lass_lactam_cya |
NF033535 |
lasso peptide isopeptide bond-forming cyclase; Members of this family are the isopeptide ... |
21-529 |
2.64e-55 |
|
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: 198.68 E-value: 2.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 21 LEKMANRIQHRGPDAEGFWFSPRAAFAHRRLIVIdPEG--GTQPKTFRTGDYtyALTYNGEIYNFREL--REQLRKCghA 96
Cdd:NF033535 20 LQQMVDILAHRGPDGADIWCEGSVGLGHRMLWTT-PESllEKLPLVNQTGDL--VITADARIDNRDELisALQLNNC--P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 97 FETHSDTEVLLHAYLEWKEDCVQHLNGIFAFALWDDQKQQLFLARDHLGVKPLFYTERNDSIIFGSEIKALLAHPSVPAE 176
Cdd:NF033535 95 PEKITDSQLILAAYEKWGEQCPEHLLGDFAFAIWDKRKQQLFCARDHFGVKPFYYYQSDKRFAFASEIKALLCLPEVPRR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 177 IdadglNEI----FGLGLFRTPGCGVFKHIQEVRAGHCITFTRDKKVVTKYWNLESK--VHTDCTEDTSSHILSILQDTV 250
Cdd:NF033535 175 L-----NEVriadYLALMLEDKVITFYQDIFRLPPAHSMTVSQSGLQIRSYWSLDPSreLRLDSDEEYAEAFREIFTEAV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 251 KRQLIADVPLVCMLSGGLDSSGITALAGKEFAAENKT-LHTYSVDF--------------VNSAKDFELTFARTGLDAPW 315
Cdd:NF033535 250 RCRLRSAFPVGSHLSGGLDSSSITCVARQLLAEEKKApLHTFSNIFdkvtecderpfinaVLEQGGLIPHYVHADQFGPL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 316 --VKRVSEH-----VGTSHH--------------DIILN---AEELANHLFVPLRakDLPSAGEMETslylLFCEMKkdA 371
Cdd:NF033535 330 sdLEQIFEYedepfLGPNHFlpwglnraaqkegvRILLDgfdGDSTVSHGHGYLT--ELANQGKWLT----FAQEIR--A 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 372 TVALSGESADEVFGGYPWFHQEELlyVDKFPWLTNWK--NTSPLLLNEINNECNLENYIDTRFQEAILEV-PTLEGESKK 448
Cdd:NF033535 402 LSKNYGTSPWGLLRQYGLPYLEKL--ARQFKWLTFLKpaNQIHKHFGISRRQLFLQHGIKPLVPRALLKLwRKLRGQAQP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 449 SAKQRQMFYL-------FLTRF--------------------------LPFLLDRKDRMSMAVGFEVRVPFCDYRLVEYL 495
Cdd:NF033535 480 GNSWRPIINPdfaerigLKERIqrldpppssspltvreehwqsltsgiLPFVLEVLDKYAAAFSLEARHPFMDKRLVEFC 559
|
570 580 590
....*....|....*....|....*....|....*...
gi 872543463 496 WNVPFNIKsidnIEKG----ILRRALQPALPDDVRNRR 529
Cdd:NF033535 560 LALPPEQK----LRQGwsrmVMRRAMEGILPPQVQWRG 593
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
33-163 |
1.65e-54 |
|
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: 181.35 E-value: 1.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 33 PDAEGFWFSPRAAFAHRRLIVID-PEGGTQPKTFRTGdyTYALTYNGEIYNFRELREQLRKCGHAFETHSDTEVLLHAYL 111
Cdd:pfam13522 1 PDFSGIWVEGGVALGHVRLAIVDlPDAGNQPMLSRDG--RLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYE 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 872543463 112 EWKEDCVQHLNGIFAFALWDDQKQQLFLARDHLGVKPLFYTERNDSIIFGSE 163
Cdd:pfam13522 79 EWGEDCLERLRGMFAFAIWDRRRRTLFLARDRLGIKPLYYGILGGGFVFASE 130
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
256-534 |
3.39e-52 |
|
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: 178.62 E-value: 3.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 256 ADVPLVCMLSGGLDSSGITALAGKEFAAENktLHTYSVDFVNSAKDfeltfartglDAPWVKRVSEHVGTSHHDIILNAE 335
Cdd:cd01991 1 SDVPVGVLLSGGLDSSLIAALAARLLPETP--IDLFTVGFEGSPTP----------DRAAARRVAEELGTEHHEVEVTIE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 336 ELANHL--FVPLRAKDLPSAGEMETSLYLLFCEMKKD-ATVALSGESADEVFGGYPWFHQeellyvdkfPWLTNWKNTSP 412
Cdd:cd01991 69 ELLDALpdVILIYPTDTPMDLSIAIPLYFASRLAGKLgAKVVLSGEGADELFGGYSRHRD---------APLRGWEALEE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 413 LLLNEINNecnlenyIDTRfqeailevptlegeskksakqrqmfylfltrflpfLLDRKDRMSMAVGFEVRVPFCDYRLV 492
Cdd:cd01991 140 ELLRDLDR-------LWTR-----------------------------------NLGRDDRVAMAHGLEARVPFLDEELV 177
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 872543463 493 EYLWNVPFNIK--SIDNIEKGILRRALQPALPDDVRNRRKSAYP 534
Cdd:cd01991 178 EFALSLPPSLKidPRGGGEKYILREAARDLLPDEIAWRPKRAIQ 221
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-216 |
7.72e-16 |
|
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: 80.07 E-value: 7.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 1 MCGITGwvdwkkdlsnehVILEKMANRI--------QHRGPDAEGF-WFSPRAAFAHRR--LI--VIDPE---------- 57
Cdd:COG0034 7 ECGVFG------------IYGHEDVAQLtyyglyalQHRGQESAGIaTSDGGRFHLHKGmgLVsdVFDEEdlerlkgnia 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 58 ---------GGT-----QPKTFRTGDYTYALTYNGEIYNFRELREQLRKCGHAFETHSDTEVLLH------AYLEWKE-- 115
Cdd:COG0034 75 ighvrysttGSSslenaQPFYVNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHliarelTKEDLEEai 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 116 -DCVQHLNGIFAFALWDDQKqqLFLARDHLGVKPLFYTERNDSIIFGSEIKALlahpsvpaeiDADGlneifglglfrtp 194
Cdd:COG0034 155 kEALRRVKGAYSLVILTGDG--LIAARDPNGIRPLVLGKLEDGYVVASESCAL----------DILG------------- 209
|
250 260
....*....|....*....|..
gi 872543463 195 gcgvFKHIQEVRAGHCITFTRD 216
Cdd:COG0034 210 ----AEFVRDVEPGEIVVIDED 227
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
61-216 |
6.98e-15 |
|
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: 74.80 E-value: 6.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 61 QPKTFRTGDYTYALTYNGEIYNFRELREQLRKCGHAFETHSDTEVLLH------AYLEWKE---DCVQHLNGIFAFALWD 131
Cdd:cd00715 85 QPFVVNSPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHliarslAKDDLFEaiiDALERVKGAYSLVIMT 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 132 DQKqqLFLARDHLGVKPLFYTER-NDSIIFGSEIKALLAhpsvpaeIDAdglneifglglfrtpgcgvfKHIQEVRAGHC 210
Cdd:cd00715 165 ADG--LIAVRDPHGIRPLVLGKLeGDGYVVASESCALDI-------IGA--------------------EFVRDVEPGEI 215
|
....*.
gi 872543463 211 ITFTRD 216
Cdd:cd00715 216 VVIDDD 221
|
|
| Gn_AT_II_novel |
cd03766 |
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its ... |
1-151 |
7.22e-12 |
|
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: 64.23 E-value: 7.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 1 MCGITGWVDWKKDLSNEHVILEKMANRIQHRGPDA---------------EGFWFSPRAAFAHRrlividpeggtQPKTF 65
Cdd:cd03766 1 MCGILCSVSPSGPHINSSLLSEELLPNLRNRGPDYlstrqlsvtnwtllfTSSVLSLRGDHVTR-----------QPLVD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 66 RTGDYTyaLTYNGEIYNFRELREQlrkcghafetHSDTEVLLHAYLEWKE------DCVQHLNGIFAFALWDDQKQQLFL 139
Cdd:cd03766 70 QSTGNV--LQWNGELYNIDGVEDE----------ENDTEVIFELLANCSSesqdilDVLSSIEGPFAFIYYDASENKLYF 137
|
170
....*....|..
gi 872543463 140 ARDHLGVKPLFY 151
Cdd:cd03766 138 GRDCLGRRSLLY 149
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
73-170 |
4.34e-11 |
|
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: 62.85 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 73 ALTYNGEIYNFRELREQLRKCGHAFETHSDTEV---LLHAYLEWKED-------CVQHLNGIFAFALWD-DQKQQLFLAR 141
Cdd:cd00714 95 AVVHNGIIENYAELKEELEAKGYKFESETDTEViahLIEYYYDGGLDlleavkkALKRLEGAYALAVISkDEPDEIVAAR 174
|
90 100 110
....*....|....*....|....*....|...
gi 872543463 142 D----HLGVKplfyterNDSIIFGSEIKALLAH 170
Cdd:cd00714 175 NgsplVIGIG-------DGENFVASDAPALLEH 200
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-167 |
5.33e-10 |
|
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: 60.36 E-value: 5.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 2 CGITGWVDwKKDLSNEHVILEKMANRIQHRGP-DAEGFwfsprAAFAHRRLIVI-------------DPE---------- 57
Cdd:cd01907 1 CGIFGIMS-KDGEPFVGALLVEMLDAMQERGPgDGAGF-----ALYGDPDAFVYssgkdmevfkgvgYPEdiarrydlee 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 58 --------------------GGTQPktFRTGDYtyALTYNGEIYNFRELREQLRKCGHAFETHSDTEV------LLHAYL 111
Cdd:cd01907 75 ykgyhwiahtrqptnsavwwYGAHP--FSIGDI--AVVHNGEISNYGSNREYLERFGYKFETETDTEViayyldLLLRKG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872543463 112 EWKEDCVQH-----------------------LNGIFAFALwdDQKQQLFLARDHLGVKPLFYTERNDSIIFGSEIKAL 167
Cdd:cd01907 151 GLPLEYYKHiirmpeeerelllalrltyrladLDGPFTIIV--GTPDGFIVIRDRIKLRPAVVAETDDYVAIASEECAI 227
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
73-219 |
1.81e-09 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 60.46 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 73 ALTYNGEIYNFRELREQLRKCGHAFETHSDTEVLLHAYLEWK--------EDCVQHLNGifAFALWDDQKQQLFLARDHL 144
Cdd:PLN02440 98 GVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKarpffsriVDACEKLKG--AYSMVFLTEDKLVAVRDPH 175
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872543463 145 GVKPLFYTER-NDSIIFGSEIKALlahpsvpaeidadGLNEifglglfrtpgcgvFKHIQEVRAGHCITFTRDKKV 219
Cdd:PLN02440 176 GFRPLVMGRRsNGAVVFASETCAL-------------DLIG--------------ATYEREVNPGEVIVVDKDKGV 224
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
77-141 |
2.18e-08 |
|
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: 56.94 E-value: 2.18e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872543463 77 NGEIYNFRELREQLRKCGHAFETHSDTEV---LLHAYLEWKED-------CVQHLNGIFAFA-LWDDQKQQLFLAR 141
Cdd:COG0449 100 NGIIENYAELREELEAKGHTFKSETDTEViahLIEEYLKGGGDlleavrkALKRLEGAYALAvISADEPDRIVAAR 175
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
73-141 |
1.56e-07 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 54.28 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 73 ALTYNGEIYNFRELREQLRKCGHAFETHSDTEV---LLHAYLEWKEDC-------VQHLNGIFAFAL-WDDQKQQLFLAR 141
Cdd:PRK00331 96 AVVHNGIIENYAELKEELLAKGHVFKSETDTEViahLIEEELKEGGDLleavrkaLKRLEGAYALAViDKDEPDTIVAAR 175
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
61-202 |
1.73e-07 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 53.88 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 61 QPKTFRTGDYTYALTYNGEIYNFRELREQLRKCGHAFETHSDTEVLLH--AYLEWKE------DCVQHLNGIFAFALWDD 132
Cdd:PRK05793 101 QPLVANYKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNliARSAKKGlekalvDAIQAIKGSYALVILTE 180
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872543463 133 QKqqLFLARDHLGVKPLFYTERNDSIIFGSE------IKALLAHPSVPAEI---DADGLNEIFGLGLFRTPGCgVFKHI 202
Cdd:PRK05793 181 DK--LIGVRDPHGIRPLCLGKLGDDYILSSEscaldtIGAEFIRDVEPGEIviiDEDGIKSIKFAEKTKCQTC-AFEYI 256
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
73-186 |
2.10e-06 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 50.79 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 73 ALTYNGEIYNFRELREQLRKCGHAFETHSDTEV---LLHAYLEWKED-------CVQHLNGIFAFALWD-DQKQQLFLAR 141
Cdd:PTZ00295 126 ALVHNGTIENYVELKSELIAKGIKFRSETDSEVianLIGLELDQGEDfqeavksAISRLQGTWGLCIIHkDNPDSLIVAR 205
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 872543463 142 DHlgvKPLFYTERNDSIIFGSEIKALLAHPSV--------PAEIDADGLNEIF 186
Cdd:PTZ00295 206 NG---SPLLVGIGDDSIYVASEPSAFAKYTNEyislkdgeIAELSLENVNDLY 255
|
|
| betaLS_CarA_N |
cd01909 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_betaLS-type. Carbapenam ... |
23-213 |
5.60e-06 |
|
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: 47.49 E-value: 5.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 23 KMANRIQHRgPDAEGFWFSPRAAFAHRRlividpeGGTQPKTFRTGDYTYALTynGEIYNFRELREQLRKCGHAFETHSD 102
Cdd:cd01909 13 KDINLFAHR-GSHTGEALPNGAGTIVHA-------GSVDVQVARSETGTAYLI--GELYNRDELRSLLGAGEGRSAVLGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 103 TEVLLHAYLEWKEDCVQHLNGIFAFALwDDQKQQLFLARDHLGVKPLfYTERNDSIIFGSEIKALLAHPSVPAeidadGL 182
Cdd:cd01909 83 AELLLLLLTRLGLHAFRLAEGDFCFFI-EDGNGRLTLATDHAGSVPV-YLVQAGEVWATTELKLLAAHEGPKA-----FP 155
|
170 180 190
....*....|....*....|....*....|...
gi 872543463 183 NEIFGLGLFrTPGCGVfkhiQEVRAG--HCITF 213
Cdd:cd01909 156 FKSAGADTV-SGLTGV----QRVPPGtvNVLTF 183
|
|
| macrolact_Ik_Al |
NF033561 |
albusnodin/ikarugamycin family macrolactam cyclase; Members of this family show homology ... |
166-354 |
2.78e-03 |
|
albusnodin/ikarugamycin family macrolactam cyclase; Members of this family show homology enzymes known to form the lactam bond of the isopeptide linkage of lasso peptides. This family includes the peptide cyclase involved in biosynthesis of the lasso peptide albusnodin. However, another member of this family belongs to the biosynthesis cassette for ikarugamycin, a macrolactam whose biosynthesis relies on a hybrid PKS/NRPS system, not a ribosomally produced peptide.
Pssm-ID: 468087 [Multi-domain] Cd Length: 561 Bit Score: 40.67 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 166 ALLAhPSVPAEIdadglneifglglfrtPGCGVFKHIQEVRAGHCITFTRDKKV-VTKYWnleSKVHTDCTEDTSSHILS 244
Cdd:NF033561 138 ALLA-PSVPALA----------------AGRSAFAGVEQVPPGHRLTLPADGGApRTPWW---WRPDPRPGPDAVARLRA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 245 ILQDTVKRQLIADVPLVCMLSGGLDSSGITALAGkEFAAENKTLH--TYSVDFVNSAKDfeLTFARTgldapwvkrVSEH 322
Cdd:NF033561 198 ALAAAVALRVDGAPPLSSDLSGGLDSTTLALLAA-RCLPVGRRLTgvTVHPEGRTEGGD--LDYARL---------AARA 265
|
170 180 190
....*....|....*....|....*....|..
gi 872543463 323 VGTSHHdiilnaeelanhlFVPLRAKDLPSAG 354
Cdd:NF033561 266 PRIRHR-------------LLPLGAEHPPYTA 284
|
|
| DUF3700 |
pfam12481 |
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ... |
118-164 |
6.40e-03 |
|
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: 38.50 E-value: 6.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 872543463 118 VQHLNGIFAFALWDDQKQQLFLARDHLGVKPLFY-TERNDSIIFGSEI 164
Cdd:pfam12481 126 VRDLEGKFAFVLYDSSTSTVFVASDADGSVPLYWgIDADGSLVFSDDI 173
|
|
| Wali7 |
cd01910 |
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ... |
61-151 |
6.86e-03 |
|
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: 38.44 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872543463 61 QPKTFRTGDYTYALtYNGEIYNFRELREQ--LRKCGhafethsdTEVLL--HAYLEWK-------EDCVQHLNGIFAFAL 129
Cdd:cd01910 63 HPRLFAVKDDIFCL-FQGHLDNLGSLKQQygLSKTA--------NEAMLviEAYRTLRdrgpypaDQVVKDLEGSFAFVL 133
|
90 100
....*....|....*....|..
gi 872543463 130 WDDQKQQLFLARDHLGVKPLFY 151
Cdd:cd01910 134 YDKKTSTVFVASDADGSVPLYW 155
|
|
| |
