|
Name |
Accession |
Description |
Interval |
E-value |
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-553 |
0e+00 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 1187.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 1 MCSIFGVFDIKTDAVELRKKALELSRLMRHRGPDWSGIYASDNAILAHERLSIVDVNAGAQPLYNQQKTHVLAVNGEIYN 80
Cdd:PRK09431 1 MCGIFGILDIKTDADELRKKALEMSRLMRHRGPDWSGIYASDNAILGHERLSIVDVNGGAQPLYNEDGTHVLAVNGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 81 HQALRAEYGDRYQFQTGSDCEVILALYQEKGPEFLDDLQGMFAFALYDSEKDAYLIGRDHLGIIPLYMGYDEHGQLYVAS 160
Cdd:PRK09431 81 HQELRAELGDKYAFQTGSDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGNLYFAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 161 EMKALVPVCRTIKEFPAGSYLWSQDGEIRSYYHRDWFDYDAVKDNVTDKNELRQALEDSVKSHLMSDVPYGVLLSGGLDS 240
Cdd:PRK09431 161 EMKALVPVCKTIKEFPPGHYYWSKDGEFVRYYQRDWFDYDAVKDNVTDKNELRDALEAAVKKRLMSDVPYGVLLSGGLDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 241 SIISAITKKYAARRVEDQERSEAWWPQLHSFAVGLPGSPDLKAAQEVANHLGTVHHEIHFTVQEGLDAIRDVIYHIETYD 320
Cdd:PRK09431 241 SLISAIAKKYAARRIEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVADHLGTVHHEIHFTVQEGLDALRDVIYHLETYD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 321 VTTIRASTPMYLMSRKIKAMGIKMVLSGEGSDEVFGGYLYFHKAPNAKELHEETVRKLLALHMYDCARANKAMSAWGVEA 400
Cdd:PRK09431 321 VTTIRASTPMYLMARKIKAMGIKMVLSGEGADELFGGYLYFHKAPNAKEFHEETVRKLRALHMYDCLRANKAMMAWGVEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 401 RVPFLDKKFLDVAMRINPQDKMCGNGKMEKHILRECFESYLPASVAWRQKEQFSDGVGYSWIDTLKEVAAQQVSDQQLET 480
Cdd:PRK09431 401 RVPFLDKEFLDVAMRINPEDKMCGNGKMEKHILREAFEGYLPESILWRQKEQFSDGVGYSWIDTLKEVAAEQVSDQQLAT 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446259226 481 ARFRFPYNTPTSKEAYLYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDEAFKKMDDPSGRAV-GVHQSAY 553
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: 578.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 4 IFGVFDIKTDAVELRKKALELSRLMRHRGPDWSGI-YASDNAILAHERLSIVDVNAGAQPLYNQQKTHVLAVNGEIYNHQ 82
Cdd:TIGR01536 1 IAGFFDLDDKAVEEDEAIKRMSDTIAHRGPDASGIeYKDGNAILGHRRLAIIDLSGGAQPMSNEGKTYVIVFNGEIYNHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 83 ALRAEYGDR-YQFQTGSDCEVILALYQEKGPEFLDDLQGMFAFALYDSEKDAYLIGRDHLGIIPLYMGYDeHGQLYVASE 161
Cdd:TIGR01536 81 ELREELEAKgYTFQTDSDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYD-GGQLYFASE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 162 MKALVPVCrTIKEFPAGSYLWSQDGEIRS----YYHRDWFDYDAVKDNVTD------------------------KNELR 213
Cdd:TIGR01536 160 IKALLAHP-NIKPFPDGAALAPGFGFVRVpppsTFFRGVFELEPGHDLPLDddglnieryywerrdehtdseedlVDELR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 214 QALEDSVKSHLMSDVPYGVLLSGGLDSSIISAITKKYAARrvedqerseawwPQLHSFAVGLPGSPDL---KAAQEVANH 290
Cdd:TIGR01536 239 SLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPR------------GPVHTFSIGFEGSPDFdesKYARKVADH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 291 LGTVHHEIHFTVQEGLDAIRDVIYHIEtyDVTTIRASTPMYLMSRKIKAMGIKMVLSGEGSDEVFGGYLYFHKAPNAKEL 370
Cdd:TIGR01536 307 LGTEHHEVLFSVEEGLDALPEVIYHLE--EPTTIRASIPLYLLSKLAREDGVKVVLSGEGADELFGGYLYFHEAPAAEAL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 371 HEETVRKLLALHMYDCARANKAMS-AWGVEARVPFLDKKFLDVAMRINPQDKMcgNGKMEKHILRECFESYLPASVAWRQ 449
Cdd:TIGR01536 385 REELQYLDLELYMPGLLRRKDRMSmAHSLEVRVPFLDHELVEYALSIPPEMKL--RDGKEKYLLREAFEGYLPEEILWRP 462
|
....
gi 446259226 450 KEQF 453
Cdd:TIGR01536 463 KEGF 466
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-507 |
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: 524.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 1 MCSIFGVFDIKTDAveLRKKALELSRLMRHRGPDWSGIYASDNAILAHERLSIVDV-NAGAQPLYNQQKTHVLAVNGEIY 79
Cdd:COG0367 1 MCGIAGIIDFDGGA--DREVLERMLDALAHRGPDGSGIWVDGGVALGHRRLSIIDLsEGGHQPMVSEDGRYVLVFNGEIY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 80 NHQALRAEYGDR-YQFQTGSDCEVILALYQEKGPEFLDDLQGMFAFALYDSEKDAYLIGRDHLGIIPLYMGYDEhGQLYV 158
Cdd:COG0367 79 NYRELRAELEALgHRFRTHSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDG-GGLAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 159 ASEMKALVP---------------------------VCRTIKEFPAGSYLWSQDG---EIRSYYHRDWFDYDAVKDNVTD 208
Cdd:COG0367 158 ASELKALLAhpgvdreldpealaeyltlgyvpaprtIFKGIRKLPPGHYLTVDAGgelEIRRYWDLEFVPHERSDSEEEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 209 KNELRQALEDSVKSHLMSDVPYGVLLSGGLDSSIISAITKKYAARRvedqerseawwpqLHSFAVGLPGSP--DLKAAQE 286
Cdd:COG0367 238 VEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKGP-------------LKTFSIGFEDSAydESPYARA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 287 VANHLGTVHHEIHFTVQEGLDAIRDVIYHIEtyDVTTIRASTPMYLMSRKIKAMgIKMVLSGEGSDEVFGGYLYFHKAPN 366
Cdd:COG0367 305 VAEHLGTEHHEVTVTPEDLLDALPDLVWHLD--EPFADPSAVPTYLLSRLAREH-VKVVLSGEGADELFGGYPRYREAAL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 367 ------AKELHEETVRKLLA-------------------LHMYDCARANKAMSAWGVEARVPFLDKKFLDVAMRINPQDK 421
Cdd:COG0367 382 llspdfAEALGGELVPRLYAesgaedplrrmlyldlktyLPGDLLVKVDRMSMAHSLEVRVPFLDHRLVEFALSLPPELK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 422 McgNGKMEKHILRECFESYLPASVAWRQKEQFSDGVGySWID-TLKEVAAQQVSDQQLETARFrfpYNtptskeAYLYRE 500
Cdd:COG0367 462 L--RGGRGKYLLRKALEGLLPDEVLDRPKQGFPVPLG-PWLRgPLREWLEDLLSDESLAARGL---FD------PDAVRR 529
|
....*..
gi 446259226 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 |
1.07e-110 |
|
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: 331.12 E-value: 1.07e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 211 ELRQALEDSVKSHLMSDVPYGVLLSGGLDSSIISAITKKYAArrvedqerseawwPQLHSFAVGL--PGSPDLKAAQEVA 288
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSP-------------SPLHTFSIGFegRGYDEAPYAREVA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 289 NHLGTVHHEIHFTVQEGLDAIRDVIYHIETydVTTIRASTPMYLMSRKIKAMGIKMVLSGEGSDEVFGGYLYFHkapNAK 368
Cdd:pfam00733 68 EHLGTDHHELVVTPEDLLDALPDVIWHLDE--PFADPSAIPLYLLSRLARRKGVKVVLSGEGADELFGGYPFYK---GED 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 369 ELHEETVRKLLALHMYDCARANKAMSAWGVEARVPFLDKKFLDVAMRINPQDKMCGNgkMEKHILRECFESYLPASVAWR 448
Cdd:pfam00733 143 PLRRMLYLDLKTLLPGDLLRADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKLRGG--IEKYILREALEGILPDEILER 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446259226 449 QKEQFSDGVGYSWID-TLKEVAAQQVSDQqletarfrfpyntPTSKEAYLYREIFEELFPLPSAA 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 |
4.14e-93 |
|
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: 284.17 E-value: 4.14e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 226 SDVPYGVLLSGGLDSSIISAITKKYAARrvedqerseawwPQLHSFAVGLPGS--PDLKAAQEVANHLGTVHHEIHFTVQ 303
Cdd:cd01991 1 SDVPVGVLLSGGLDSSLIAALAARLLPE------------TPIDLFTVGFEGSptPDRAAARRVAEELGTEHHEVEVTIE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 304 EGLDAIRDVIYHIETYDVTTIRASTPMYLMSRKIKAMGIKMVLSGEGSDEVFGGYLYFHKAPNA--KELHEETVRKLLAL 381
Cdd:cd01991 69 ELLDALPDVILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVLSGEGADELFGGYSRHRDAPLRgwEALEEELLRDLDRL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446259226 382 HMYDCARANKAMSAWGVEARVPFLDKKFLDVAMRINPQDKMCGNGKMEKHILRECFESYLPASVAWRQKEQFSDGV 457
Cdd:cd01991 149 WTRNLGRDDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIDPRGGGEKYILREAARDLLPDEIAWRPKRAIQFGS 224
|
|
| lass_lactam_cya |
NF033535 |
lasso peptide isopeptide bond-forming cyclase; Members of this family are the isopeptide ... |
1-362 |
9.78e-26 |
|
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: 111.62 E-value: 9.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 1 MCSIFGVFDIKTDAVELRKKALELSRLMrHRGPDWSGIYASDNAILAH-------ERLSivdvnaGAQPLYNQQKTHVLA 73
Cdd:NF033535 1 MSGIVGIYYLDGRPVDREDLQQMVDILA-HRGPDGADIWCEGSVGLGHrmlwttpESLL------EKLPLVNQTGDLVIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 74 VNGEIYNhqalRAEYGDRYQF-----QTGSDCEVILALYQEKGPEFLDDLQGMFAFALYDSEKDAYLIGRDHLGIIPLYm 148
Cdd:NF033535 74 ADARIDN----RDELISALQLnncppEKITDSQLILAAYEKWGEQCPEHLLGDFAFAIWDKRKQQLFCARDHFGVKPFY- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 149 gYDEHGQLYV-ASEMKAL-----VPVC----------------------RTIKEFPAGSYLW-SQDG-EIRSYyhrdWfD 198
Cdd:NF033535 149 -YYQSDKRFAfASEIKALlclpeVPRRlnevriadylalmledkvitfyQDIFRLPPAHSMTvSQSGlQIRSY----W-S 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 199 YDAVKDNVTDKNE-----LRQALEDSVKSHLMSDVPYGVLLSGGLDSSIISAItkkyaARRVEDQERSeawwPQLHSFAV 273
Cdd:NF033535 223 LDPSRELRLDSDEeyaeaFREIFTEAVRCRLRSAFPVGSHLSGGLDSSSITCV-----ARQLLAEEKK----APLHTFSN 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 274 ---GLPGSPDLKAAQEVANHLGTVHHEIH---FTVQEGLDAIrdVIYHIETYdvttiraSTPMYLMSRKI----KAMGIK 343
Cdd:NF033535 294 ifdKVTECDERPFINAVLEQGGLIPHYVHadqFGPLSDLEQI--FEYEDEPF-------LGPNHFLPWGLnraaQKEGVR 364
|
410 420
....*....|....*....|
gi 446259226 344 MVLSGEGSDE-VFGGYLYFH 362
Cdd:NF033535 365 ILLDGFDGDStVSHGHGYLT 384
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-553 |
0e+00 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 1187.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 1 MCSIFGVFDIKTDAVELRKKALELSRLMRHRGPDWSGIYASDNAILAHERLSIVDVNAGAQPLYNQQKTHVLAVNGEIYN 80
Cdd:PRK09431 1 MCGIFGILDIKTDADELRKKALEMSRLMRHRGPDWSGIYASDNAILGHERLSIVDVNGGAQPLYNEDGTHVLAVNGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 81 HQALRAEYGDRYQFQTGSDCEVILALYQEKGPEFLDDLQGMFAFALYDSEKDAYLIGRDHLGIIPLYMGYDEHGQLYVAS 160
Cdd:PRK09431 81 HQELRAELGDKYAFQTGSDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGNLYFAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 161 EMKALVPVCRTIKEFPAGSYLWSQDGEIRSYYHRDWFDYDAVKDNVTDKNELRQALEDSVKSHLMSDVPYGVLLSGGLDS 240
Cdd:PRK09431 161 EMKALVPVCKTIKEFPPGHYYWSKDGEFVRYYQRDWFDYDAVKDNVTDKNELRDALEAAVKKRLMSDVPYGVLLSGGLDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 241 SIISAITKKYAARRVEDQERSEAWWPQLHSFAVGLPGSPDLKAAQEVANHLGTVHHEIHFTVQEGLDAIRDVIYHIETYD 320
Cdd:PRK09431 241 SLISAIAKKYAARRIEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVADHLGTVHHEIHFTVQEGLDALRDVIYHLETYD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 321 VTTIRASTPMYLMSRKIKAMGIKMVLSGEGSDEVFGGYLYFHKAPNAKELHEETVRKLLALHMYDCARANKAMSAWGVEA 400
Cdd:PRK09431 321 VTTIRASTPMYLMARKIKAMGIKMVLSGEGADELFGGYLYFHKAPNAKEFHEETVRKLRALHMYDCLRANKAMMAWGVEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 401 RVPFLDKKFLDVAMRINPQDKMCGNGKMEKHILRECFESYLPASVAWRQKEQFSDGVGYSWIDTLKEVAAQQVSDQQLET 480
Cdd:PRK09431 401 RVPFLDKEFLDVAMRINPEDKMCGNGKMEKHILREAFEGYLPESILWRQKEQFSDGVGYSWIDTLKEVAAEQVSDQQLAT 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446259226 481 ARFRFPYNTPTSKEAYLYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDEAFKKMDDPSGRAV-GVHQSAY 553
Cdd:PRK09431 481 ARFRFPYNTPTTKEAYLYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDEAFKNMDDPSGRAVsGVHQSAY 554
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-554 |
0e+00 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 854.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 1 MCSIFGVFDIKTDAVELRKKALELSRLMRHRGPDWSGIYASDNA-----ILAHERLSIVDVNAGAQPLYNQQKTHVLAVN 75
Cdd:PTZ00077 1 MCGILAIFNSKGERHELRRKALELSKRLRHRGPDWSGIIVLENSpgtynILAHERLAIVDLSDGKQPLLDDDETVALMQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 76 GEIYNHQALRAEY-GDRYQFQTGSDCEVILALYQEKGP-EFLDDLQGMFAFALYDSEKDAYLIGRDHLGIIPLYMGYDEH 153
Cdd:PTZ00077 81 GEIYNHWEIRPELeKEGYKFSSNSDCEIIGHLYKEYGPkDFWNHLDGMFATVIYDMKTNTFFAARDHIGIIPLYIGYAKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 154 GQLYVASEMKALVPVCRTIKEFPAGSYLWS--QDGEIRSYYHRDWFDYDA-VKDNVTDKNELRQALEDSVKSHLMSDVPY 230
Cdd:PTZ00077 161 GSIWFSSELKALHDQCVEVKQFPPGHYYDQtkEKGEFVRYYNPNWHDFDHpIPTGEIDLEEIREALEAAVRKRLMGDVPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 231 GVLLSGGLDSSIISAITKKYaaRRVEDQERSEAWWPQLHSFAVGLPGSPDLKAAQEVANHLGTVHHEIHFTVQEGLDAIR 310
Cdd:PTZ00077 241 GLFLSGGLDSSIVAAIVAKL--IKNGEIDLSKRGMPKLHSFCIGLEGSPDLKAARKVAEYLGTEHHEFTFTVEEGIDALP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 311 DVIYHIETYDVTTIRASTPMYLMSRKIKAMGIKMVLSGEGSDEVFGGYLYFHKAPNAKELHEETVRKLLALHMYDCARAN 390
Cdd:PTZ00077 319 DVIYHTETYDVTTIRASTPMYLLSRRIKALGIKMVLSGEGSDELFGGYLYFHKAPNREEFHRELVRKLHDLHKYDCLRAN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 391 KAMSAWGVEARVPFLDKKFLDVAMRINPQDKMC--GNGKMEKHILRECFE----SYLPASVAWRQKEQFSDGVGYSWIDT 464
Cdd:PTZ00077 399 KATMAWGIEARVPFLDKDFLEYVMNIDPKYKMCnaFEGQMEKYILRKAFEglekPYLPDEILWRQKEQFSDGVGYSWIDG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 465 LKEVAAQQVSDQQLETARFRFPYNTPTSKEAYLYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDEAFKKMDDPSGR 544
Cdd:PTZ00077 479 LKEYAEKKISDQEFSQASFLFPYNTPRTKEAYLYRQIFSKHFPSDSAALTVPYGPSIACSTEKALEWDESFKKNTDESGR 558
|
570
....*....|.
gi 446259226 545 AV-GVHQSAYK 554
Cdd:PTZ00077 559 AVlSVHNDAKQ 569
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-554 |
0e+00 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 840.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 1 MCSIFGVFDIKTDAVELRKKALELSRLMRHRGPDWSGIYASDNAILAHERLSIVDVNAGAQPLYNQQKTHVLAVNGEIYN 80
Cdd:PLN02549 1 MCGILAVLGCSDDSQAKRSRVLELSRRLRHRGPDWSGLYGNEDCYLAHERLAIMDPESGDQPLYNEDKTIVVTANGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 81 HQALRAEYGDrYQFQTGSDCEVILALYQEKGPEFLDDLQGMFAFALYDSEKDAYLIGRDHLGIIPLYMGYDEHGQLYVAS 160
Cdd:PLN02549 81 HKELREKLKL-HKFRTGSDCEVIAHLYEEHGEEFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGLDGSVWFAS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 161 EMKALVPVCRTIKEFPAGSYLWSQDGEIRSYYHRDWF-DYDAVKDnvTDKNELRQALEDSVKSHLMSDVPYGVLLSGGLD 239
Cdd:PLN02549 160 EMKALCDDCERFEEFPPGHYYSSKAGGFRRWYNPPWFsESIPSTP--YDPLVLREAFEKAVIKRLMTDVPFGVLLSGGLD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 240 SSIISAItkkyAARRVEDQERSEAWWPQLHSFAVGLPGSPDLKAAQEVANHLGTVHHEIHFTVQEGLDAIRDVIYHIETY 319
Cdd:PLN02549 238 SSLVASI----AARHLAETKAARQWGQQLHSFCVGLEGSPDLKAAREVADYLGTVHHEFHFTVQEGIDAIEDVIYHLETY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 320 DVTTIRASTPMYLMSRKIKAMGIKMVLSGEGSDEVFGGYLYFHKAPNAKELHEETVRKLLALHMYDCARANKAMSAWGVE 399
Cdd:PLN02549 314 DVTTIRASTPMFLMSRKIKSLGVKMVLSGEGSDEIFGGYLYFHKAPNKEEFHKETCRKIKALHQYDCLRANKSTSAWGLE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 400 ARVPFLDKKFLDVAMRINPQDKMC--GNGKMEKHILRECFE----SYLPASVAWRQKEQFSDGVGYSWIDTLKEVAAQQV 473
Cdd:PLN02549 394 ARVPFLDKEFIDVAMSIDPEWKMIrpGEGRIEKWVLRKAFDdeedPYLPKHILWRQKEQFSDGVGYSWIDGLKAHAEKHV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 474 SDQQLETARFRFPYNTPTSKEAYLYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDEAFKKMDDPSGRAV-GVHQSA 552
Cdd:PLN02549 474 SDEMFANASFRYPHNTPTTKEAYYYRMIFEKHFPQDAARLTVPGGPSVACSTAKAVEWDAAWSKNLDPSGRAAlGVHVAA 553
|
..
gi 446259226 553 YK 554
Cdd:PLN02549 554 YE 555
|
|
| 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: 578.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 4 IFGVFDIKTDAVELRKKALELSRLMRHRGPDWSGI-YASDNAILAHERLSIVDVNAGAQPLYNQQKTHVLAVNGEIYNHQ 82
Cdd:TIGR01536 1 IAGFFDLDDKAVEEDEAIKRMSDTIAHRGPDASGIeYKDGNAILGHRRLAIIDLSGGAQPMSNEGKTYVIVFNGEIYNHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 83 ALRAEYGDR-YQFQTGSDCEVILALYQEKGPEFLDDLQGMFAFALYDSEKDAYLIGRDHLGIIPLYMGYDeHGQLYVASE 161
Cdd:TIGR01536 81 ELREELEAKgYTFQTDSDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYD-GGQLYFASE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 162 MKALVPVCrTIKEFPAGSYLWSQDGEIRS----YYHRDWFDYDAVKDNVTD------------------------KNELR 213
Cdd:TIGR01536 160 IKALLAHP-NIKPFPDGAALAPGFGFVRVpppsTFFRGVFELEPGHDLPLDddglnieryywerrdehtdseedlVDELR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 214 QALEDSVKSHLMSDVPYGVLLSGGLDSSIISAITKKYAARrvedqerseawwPQLHSFAVGLPGSPDL---KAAQEVANH 290
Cdd:TIGR01536 239 SLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPR------------GPVHTFSIGFEGSPDFdesKYARKVADH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 291 LGTVHHEIHFTVQEGLDAIRDVIYHIEtyDVTTIRASTPMYLMSRKIKAMGIKMVLSGEGSDEVFGGYLYFHKAPNAKEL 370
Cdd:TIGR01536 307 LGTEHHEVLFSVEEGLDALPEVIYHLE--EPTTIRASIPLYLLSKLAREDGVKVVLSGEGADELFGGYLYFHEAPAAEAL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 371 HEETVRKLLALHMYDCARANKAMS-AWGVEARVPFLDKKFLDVAMRINPQDKMcgNGKMEKHILRECFESYLPASVAWRQ 449
Cdd:TIGR01536 385 REELQYLDLELYMPGLLRRKDRMSmAHSLEVRVPFLDHELVEYALSIPPEMKL--RDGKEKYLLREAFEGYLPEEILWRP 462
|
....
gi 446259226 450 KEQF 453
Cdd:TIGR01536 463 KEGF 466
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-507 |
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: 524.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 1 MCSIFGVFDIKTDAveLRKKALELSRLMRHRGPDWSGIYASDNAILAHERLSIVDV-NAGAQPLYNQQKTHVLAVNGEIY 79
Cdd:COG0367 1 MCGIAGIIDFDGGA--DREVLERMLDALAHRGPDGSGIWVDGGVALGHRRLSIIDLsEGGHQPMVSEDGRYVLVFNGEIY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 80 NHQALRAEYGDR-YQFQTGSDCEVILALYQEKGPEFLDDLQGMFAFALYDSEKDAYLIGRDHLGIIPLYMGYDEhGQLYV 158
Cdd:COG0367 79 NYRELRAELEALgHRFRTHSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDG-GGLAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 159 ASEMKALVP---------------------------VCRTIKEFPAGSYLWSQDG---EIRSYYHRDWFDYDAVKDNVTD 208
Cdd:COG0367 158 ASELKALLAhpgvdreldpealaeyltlgyvpaprtIFKGIRKLPPGHYLTVDAGgelEIRRYWDLEFVPHERSDSEEEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 209 KNELRQALEDSVKSHLMSDVPYGVLLSGGLDSSIISAITKKYAARRvedqerseawwpqLHSFAVGLPGSP--DLKAAQE 286
Cdd:COG0367 238 VEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKGP-------------LKTFSIGFEDSAydESPYARA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 287 VANHLGTVHHEIHFTVQEGLDAIRDVIYHIEtyDVTTIRASTPMYLMSRKIKAMgIKMVLSGEGSDEVFGGYLYFHKAPN 366
Cdd:COG0367 305 VAEHLGTEHHEVTVTPEDLLDALPDLVWHLD--EPFADPSAVPTYLLSRLAREH-VKVVLSGEGADELFGGYPRYREAAL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 367 ------AKELHEETVRKLLA-------------------LHMYDCARANKAMSAWGVEARVPFLDKKFLDVAMRINPQDK 421
Cdd:COG0367 382 llspdfAEALGGELVPRLYAesgaedplrrmlyldlktyLPGDLLVKVDRMSMAHSLEVRVPFLDHRLVEFALSLPPELK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 422 McgNGKMEKHILRECFESYLPASVAWRQKEQFSDGVGySWID-TLKEVAAQQVSDQQLETARFrfpYNtptskeAYLYRE 500
Cdd:COG0367 462 L--RGGRGKYLLRKALEGLLPDEVLDRPKQGFPVPLG-PWLRgPLREWLEDLLSDESLAARGL---FD------PDAVRR 529
|
....*..
gi 446259226 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 |
1.07e-110 |
|
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: 331.12 E-value: 1.07e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 211 ELRQALEDSVKSHLMSDVPYGVLLSGGLDSSIISAITKKYAArrvedqerseawwPQLHSFAVGL--PGSPDLKAAQEVA 288
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSP-------------SPLHTFSIGFegRGYDEAPYAREVA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 289 NHLGTVHHEIHFTVQEGLDAIRDVIYHIETydVTTIRASTPMYLMSRKIKAMGIKMVLSGEGSDEVFGGYLYFHkapNAK 368
Cdd:pfam00733 68 EHLGTDHHELVVTPEDLLDALPDVIWHLDE--PFADPSAIPLYLLSRLARRKGVKVVLSGEGADELFGGYPFYK---GED 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 369 ELHEETVRKLLALHMYDCARANKAMSAWGVEARVPFLDKKFLDVAMRINPQDKMCGNgkMEKHILRECFESYLPASVAWR 448
Cdd:pfam00733 143 PLRRMLYLDLKTLLPGDLLRADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKLRGG--IEKYILREALEGILPDEILER 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446259226 449 QKEQFSDGVGYSWID-TLKEVAAQQVSDQqletarfrfpyntPTSKEAYLYREIFEELFPLPSAA 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 |
4.14e-93 |
|
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: 284.17 E-value: 4.14e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 226 SDVPYGVLLSGGLDSSIISAITKKYAARrvedqerseawwPQLHSFAVGLPGS--PDLKAAQEVANHLGTVHHEIHFTVQ 303
Cdd:cd01991 1 SDVPVGVLLSGGLDSSLIAALAARLLPE------------TPIDLFTVGFEGSptPDRAAARRVAEELGTEHHEVEVTIE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 304 EGLDAIRDVIYHIETYDVTTIRASTPMYLMSRKIKAMGIKMVLSGEGSDEVFGGYLYFHKAPNA--KELHEETVRKLLAL 381
Cdd:cd01991 69 ELLDALPDVILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVLSGEGADELFGGYSRHRDAPLRgwEALEEELLRDLDRL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446259226 382 HMYDCARANKAMSAWGVEARVPFLDKKFLDVAMRINPQDKMCGNGKMEKHILRECFESYLPASVAWRQKEQFSDGV 457
Cdd:cd01991 149 WTRNLGRDDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIDPRGGGEKYILREAARDLLPDEIAWRPKRAIQFGS 224
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-193 |
6.55e-83 |
|
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: 257.49 E-value: 6.55e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 2 CSIFGVFDIKtDAVELRKKALELSRLMRHRGPDWSGIYASDNAILAHERLSIVDVNAGAQPLYNQQKTHVLAVNGEIYNH 81
Cdd:cd00712 1 CGIAGIIGLD-GASVDRATLERMLDALAHRGPDGSGIWIDEGVALGHRRLSIIDLSGGAQPMVSEDGRLVLVFNGEIYNY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 82 QALRAEYGDR-YQFQTGSDCEVILALYQEKGPEFLDDLQGMFAFALYDSEKDAYLIGRDHLGIIPLYMGYDEHGqLYVAS 160
Cdd:cd00712 80 RELRAELEALgHRFRTHSDTEVILHLYEEWGEDCLERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGRDGGG-LAFAS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446259226 161 EMKALVPVC---------------------------RTIKEFPAGSYLWSQDG--EIRSYYH 193
Cdd:cd00712 159 ELKALLALPgvpreldeaalaeylafqyvpaprtifKGIRKLPPGHYLTVDPGgvEIRRYWD 220
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
48-167 |
1.94e-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: 433289 [Multi-domain] Cd Length: 123 Bit Score: 179.64 E-value: 1.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 48 HERLSIVDVNAGAQPLYNQQ-KTHVLAVNGEIYNHQALRAEYGDR-YQFQTGSDCEVILALYQ-EKGPEFLDDLQGMFAF 124
Cdd:pfam13537 1 HRRLSIIDLEGGAQPMVSSEdGRYVIVFNGEIYNYRELRAELEAKgYRFRTHSDTEVILHLYEaEWGEDCVDRLNGMFAF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446259226 125 ALYDSEKDAYLIGRDHLGIIPLYMGYDEHGQLYVASEMKALVP 167
Cdd:pfam13537 81 AIWDRRRQRLFLARDRFGIKPLYYGRDDGGRLLFASELKALLA 123
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-181 |
2.91e-49 |
|
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: 169.55 E-value: 2.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 2 CSIFGVFDIKTDAVELRKKALELSRLMRHRGPDWSGIYASD---------------------------NAILAHERLSIV 54
Cdd:cd00352 1 CGIFGIVGADGAASLLLLLLLRGLAALEHRGPDGAGIAVYDgdglfvekragpvsdvaldlldeplksGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 55 DV--NAGAQPLYNQQKTHVLAVNGEIYNHQALRAEYGDR-YQFQTGSDCEVILALYQEKG---------PEFLDDLQGMF 122
Cdd:cd00352 81 GLpsEANAQPFRSEDGRIALVHNGEIYNYRELREELEARgYRFEGESDSEVILHLLERLGregglfeavEDALKRLDGPF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 123 AFALYDSEKDAYLIGRDHLGIIPLYMGYDEHGQLYVASEMKALVPVC-RTIKEFPAGSYL 181
Cdd:cd00352 161 AFALWDGKPDRLFAARDRFGIRPLYYGITKDGGLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
33-161 |
2.15e-46 |
|
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: 158.62 E-value: 2.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 33 PDWSGIYASDNAILAHERLSIVDV-NAGAQPLYNQQKTHVLAVNGEIYNHQALRAEYGDR-YQFQTGSDCEVILALYQEK 110
Cdd:pfam13522 1 PDFSGIWVEGGVALGHVRLAIVDLpDAGNQPMLSRDGRLVLVHNGEIYNYGELREELADLgHAFRSRSDTEVLLALYEEW 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446259226 111 GPEFLDDLQGMFAFALYDSEKDAYLIGRDHLGIIPLYMGYDeHGQLYVASE 161
Cdd:pfam13522 81 GEDCLERLRGMFAFAIWDRRRRTLFLARDRLGIKPLYYGIL-GGGFVFASE 130
|
|
| lass_lactam_cya |
NF033535 |
lasso peptide isopeptide bond-forming cyclase; Members of this family are the isopeptide ... |
1-362 |
9.78e-26 |
|
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: 111.62 E-value: 9.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 1 MCSIFGVFDIKTDAVELRKKALELSRLMrHRGPDWSGIYASDNAILAH-------ERLSivdvnaGAQPLYNQQKTHVLA 73
Cdd:NF033535 1 MSGIVGIYYLDGRPVDREDLQQMVDILA-HRGPDGADIWCEGSVGLGHrmlwttpESLL------EKLPLVNQTGDLVIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 74 VNGEIYNhqalRAEYGDRYQF-----QTGSDCEVILALYQEKGPEFLDDLQGMFAFALYDSEKDAYLIGRDHLGIIPLYm 148
Cdd:NF033535 74 ADARIDN----RDELISALQLnncppEKITDSQLILAAYEKWGEQCPEHLLGDFAFAIWDKRKQQLFCARDHFGVKPFY- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 149 gYDEHGQLYV-ASEMKAL-----VPVC----------------------RTIKEFPAGSYLW-SQDG-EIRSYyhrdWfD 198
Cdd:NF033535 149 -YYQSDKRFAfASEIKALlclpeVPRRlnevriadylalmledkvitfyQDIFRLPPAHSMTvSQSGlQIRSY----W-S 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 199 YDAVKDNVTDKNE-----LRQALEDSVKSHLMSDVPYGVLLSGGLDSSIISAItkkyaARRVEDQERSeawwPQLHSFAV 273
Cdd:NF033535 223 LDPSRELRLDSDEeyaeaFREIFTEAVRCRLRSAFPVGSHLSGGLDSSSITCV-----ARQLLAEEKK----APLHTFSN 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 274 ---GLPGSPDLKAAQEVANHLGTVHHEIH---FTVQEGLDAIrdVIYHIETYdvttiraSTPMYLMSRKI----KAMGIK 343
Cdd:NF033535 294 ifdKVTECDERPFINAVLEQGGLIPHYVHadqFGPLSDLEQI--FEYEDEPF-------LGPNHFLPWGLnraaQKEGVR 364
|
410 420
....*....|....*....|
gi 446259226 344 MVLSGEGSDE-VFGGYLYFH 362
Cdd:NF033535 365 ILLDGFDGDStVSHGHGYLT 384
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-161 |
2.18e-10 |
|
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: 62.73 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 1 MCSIFGVFDiKTDAVELRKKALelsRLMRHRGPDWSGIYASD-NAILAHERLSIV-DV-----------NAG-------- 59
Cdd:COG0034 7 ECGVFGIYG-HEDVAQLTYYGL---YALQHRGQESAGIATSDgGRFHLHKGMGLVsDVfdeedlerlkgNIAighvryst 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 60 --------AQPLYNQQKTHVLAV--NGEIYNHQALRAEYGDRYQ-FQTGSDCEVILAL---YQEKGPEF------LDDLQ 119
Cdd:COG0034 83 tgssslenAQPFYVNSPFGSIALahNGNLTNAEELREELEEEGAiFQTTSDTEVILHLiarELTKEDLEeaikeaLRRVK 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446259226 120 GMFAFALYDSEKdayLIG-RDHLGIIPLYMGYDEHGqLYVASE 161
Cdd:COG0034 163 GAYSLVILTGDG---LIAaRDPNGIRPLVLGKLEDG-YVVASE 201
|
|
| Gn_AT_II_novel |
cd03766 |
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its ... |
1-160 |
1.67e-08 |
|
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: 54.22 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 1 MCSIFGVFDIKTDAVELRKKALELSRLMRHRGPDWSGI----YASDNAILAHERLSIVDVNAGAQPLYNQQKTHVLAVNG 76
Cdd:cd03766 1 MCGILCSVSPSGPHINSSLLSEELLPNLRNRGPDYLSTrqlsVTNWTLLFTSSVLSLRGDHVTRQPLVDQSTGNVLQWNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 77 EIYNhqalraeygDRYQFQTGSDCEVILALYQE---KGPEFLD---DLQGMFAFALYD-SEKDAYLiGRDHLGIIPLYMG 149
Cdd:cd03766 81 ELYN---------IDGVEDEENDTEVIFELLANcssESQDILDvlsSIEGPFAFIYYDaSENKLYF-GRDCLGRRSLLYK 150
|
170
....*....|..
gi 446259226 150 YDEHG-QLYVAS 160
Cdd:cd03766 151 LDPNGfELSISS 162
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-165 |
2.67e-08 |
|
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: 55.16 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 2 CSIFGVFDiKTDAVELRKKALelsRLMRHRGPDWSGIYASD---------------------------NAILAHERLSiv 54
Cdd:cd00715 1 CGVFGIYG-AEDAARLTYLGL---YALQHRGQESAGIATSDgkrfhthkgmglvsdvfdeeklrrlpgNIAIGHVRYS-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 55 dvNAG------AQPLYNQQKTHVLAV--NGEIYNHQALRAEYGDRYQ-FQTGSDCEVILAL----YQEKGPE-----FLD 116
Cdd:cd00715 75 --TAGssslenAQPFVVNSPLGGIALahNGNLVNAKELREELEEEGRiFQTTSDSEVILHLiarsLAKDDLFeaiidALE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446259226 117 DLQGMFAFALYDSEKdayLIG-RDHLGIIPLYMGYDEHGQLYVASEMKAL 165
Cdd:cd00715 153 RVKGAYSLVIMTADG---LIAvRDPHGIRPLVLGKLEGDGYVVASESCAL 199
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-168 |
4.58e-08 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 55.45 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 1 MCSIFGVFDiktDAVELRKKALELSRLmRHRGPDWSGIYASDNAILaHER--LSIV-DV--------------------- 56
Cdd:PLN02440 1 ECGVVGIFG---DPEASRLCYLGLHAL-QHRGQEGAGIVTVDGNRL-QSItgNGLVsDVfdeskldqlpgdiaighvrys 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 57 NAG------AQPLYNQQKTHVLAV--NGEIYNHQALRAEYGDRYQ-FQTGSDCEVILALYQE-KGPEFLD-------DLQ 119
Cdd:PLN02440 76 TAGasslknVQPFVANYRFGSIGVahNGNLVNYEELRAKLEENGSiFNTSSDTEVLLHLIAIsKARPFFSrivdaceKLK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446259226 120 GmfAFALYDSEKDAYLIGRDHLGIIPLYMGYDEHGQLYVASEMKALVPV 168
Cdd:PLN02440 156 G--AYSMVFLTEDKLVAVRDPHGFRPLVMGRRSNGAVVFASETCALDLI 202
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-165 |
6.68e-08 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 55.04 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 2 CSIFGVFDiktdavelrKKALELSRL-------MRHRGPDWSGIYASD-NAILAHERLSIV-DV-----------NAG-- 59
Cdd:PRK05793 15 CGVFGVFS---------KNNIDVASLtyyglyaLQHRGQESAGIAVSDgEKIKVHKGMGLVsEVfskeklkglkgNSAig 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 60 --------------AQPLYNQQKTHVLAV--NGEIYNHQALRAEYGDR-YQFQTGSDCEVILAL---YQEKGPEF----- 114
Cdd:PRK05793 86 hvrysttgasdldnAQPLVANYKLGSIAIahNGNLVNADVIRELLEDGgRIFQTSIDSEVILNLiarSAKKGLEKalvda 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446259226 115 LDDLQGMFAFALYDSEKdayLIG-RDHLGIIPLYMGYDEHGqLYVASEMKAL 165
Cdd:PRK05793 166 IQAIKGSYALVILTEDK---LIGvRDPHGIRPLCLGKLGDD-YILSSESCAL 213
|
|
| Wali7 |
cd01910 |
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ... |
76-193 |
1.93e-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: 51.93 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 76 GEIYNHQALRAEYGdryqfQTGSDCEVILAL--YQ---EKGP----EFLDDLQGMFAFALYDSEKDAYLIGRDHLGIIPL 146
Cdd:cd01910 79 GHLDNLGSLKQQYG-----LSKTANEAMLVIeaYRtlrDRGPypadQVVKDLEGSFAFVLYDKKTSTVFVASDADGSVPL 153
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 446259226 147 YMGYDEHGQLYVASEMKALVPVC-RTIKEFPAGSYLWSqDGEIRSYYH 193
Cdd:cd01910 154 YWGIAADGSVVFSDDVELVKASCgKSFAPFPKGCFFHS-EGGLRSFEH 200
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
75-188 |
6.01e-07 |
|
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: 50.52 E-value: 6.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 75 NGEIYNHQALRAEYGDR-YQFQTGSDCEVI---LALYQEKGPEFLD-------DLQGMFAFALYDSEKDAYLIG--RDHl 141
Cdd:cd00714 99 NGIIENYAELKEELEAKgYKFESETDTEVIahlIEYYYDGGLDLLEavkkalkRLEGAYALAVISKDEPDEIVAarNGS- 177
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 446259226 142 giiPLYMGYDEhGQLYVASEMKALVPVCRTIkefpagSYLwsQDGEI 188
Cdd:cd00714 178 ---PLVIGIGD-GENFVASDAPALLEHTRRV------IYL--EDGDI 212
|
|
| DUF3700 |
pfam12481 |
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ... |
76-193 |
1.25e-06 |
|
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 amino acids in length. There are two conserved sequence motifs: YGL and LRDR. This family is related to GATase enzyme domains.
Pssm-ID: 403619 [Multi-domain] Cd Length: 228 Bit Score: 49.67 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 76 GEIYNHQALRAEYGdryqFQTGSDcEVILAL--YQ---EKGP----EFLDDLQGMFAFALYDSEKDAYLIGRDHLGIIPL 146
Cdd:pfam12481 83 GHLENLASLKQQYG----LSKGAN-EAMIVIeaYRtlrDRGPypadQVVRDLEGKFAFVLYDSSTSTVFVASDADGSVPL 157
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 446259226 147 YMGYDEHGQLYVASEMKALVPVC-RTIKEFPAGSYlWSQDGEIRSYYH 193
Cdd:pfam12481 158 YWGIDADGSLVFSDDIEIVKKGCgKSFAPFPKGCF-FTSSGGLRSFEH 204
|
|
| AANH_superfamily |
cd01984 |
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ... |
230-275 |
3.52e-06 |
|
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: 44.39 E-value: 3.52e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 446259226 230 YGVLLSGGLDSSIISAITKKYAARrvedqerseaWWPQLHSFAVGL 275
Cdd:cd01984 1 ILVPLSGGEDSSIALKHAKKFKTS----------KAEEVVVVHVGE 36
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
72-188 |
3.56e-06 |
|
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: 49.63 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 72 LAV--NGEIYNHQALRAEYGDR-YQFQTGSDCEVI---LALYQEKGPEFLD-------DLQGMFAFAlydsekdayLIGR 138
Cdd:COG0449 95 IAVvhNGIIENYAELREELEAKgHTFKSETDTEVIahlIEEYLKGGGDLLEavrkalkRLEGAYALA---------VISA 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 446259226 139 DHLGII-------PLYMGYDEhGQLYVASEMKALVPVCRTIkefpagSYLwsQDGEI 188
Cdd:COG0449 166 DEPDRIvaarkgsPLVIGLGE-GENFLASDVPALLPYTRRV------IYL--EDGEI 213
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
72-188 |
2.95e-05 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 46.96 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 72 LAV--NGEIYNHQALRAEYGDR-YQFQTGSDCEVI---LALYQEKGPEFLD-------DLQGMFAFAlydsekdayLIGR 138
Cdd:PRK00331 95 IAVvhNGIIENYAELKEELLAKgHVFKSETDTEVIahlIEEELKEGGDLLEavrkalkRLEGAYALA---------VIDK 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 446259226 139 DHLGII-------PLYMGYDEhGQLYVASEMKALVPVCRTIkefpagSYLwsQDGEI 188
Cdd:PRK00331 166 DEPDTIvaarngsPLVIGLGE-GENFLASDALALLPYTRRV------IYL--EDGEI 213
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-169 |
1.77e-04 |
|
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: 43.41 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 2 CSIFGVFDiKTDAVELRKKALELSRLMRHRGPDWSG---IYASDNA---------------------------------- 44
Cdd:cd01907 1 CGIFGIMS-KDGEPFVGALLVEMLDAMQERGPGDGAgfaLYGDPDAfvyssgkdmevfkgvgypediarrydleeykgyh 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 45 ILAHERL---SIVDVnAGAQP--LYNQQKTHvlavNGEIYNHQALRaEY--GDRYQFQTGSDCEVILALYQEKGPEF--- 114
Cdd:cd01907 80 WIAHTRQptnSAVWW-YGAHPfsIGDIAVVH----NGEISNYGSNR-EYleRFGYKFETETDTEVIAYYLDLLLRKGglp 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446259226 115 --------------------------LDDLQGMFAFALydSEKDAYLIGRDHLGIIPLYMGYDEhGQLYVASEMKALVPV 168
Cdd:cd01907 154 leyykhiirmpeeerelllalrltyrLADLDGPFTIIV--GTPDGFIVIRDRIKLRPAVVAETD-DYVAIASEECAIREI 230
|
.
gi 446259226 169 C 169
Cdd:cd01907 231 P 231
|
|
| |
