|
Name |
Accession |
Description |
Interval |
E-value |
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-611 |
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: 728.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 1 MCGFAGCLTdrtkADNAAYDQTIHEMTKMIVHRGPDDDGYFADDNITMGFRRLSIIDL-AGGHQPLSYDNERYWMTFNGE 79
Cdd:COG0367 1 MCGIAGIID----FDGGADREVLERMLDALAHRGPDGSGIWVDGGVALGHRRLSIIDLsEGGHQPMVSEDGRYVLVFNGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 80 IYNYVELREQLKQEGYEFKTSSDSEVILAMYAKYHADATKYLRGMFAFVIWDKQEKTLFAARDQFGIKPFYYAISGDDFY 159
Cdd:COG0367 77 IYNYRELRAELEALGHRFRTHSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDGGGLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 160 YASESKAIYKI-LKDKTFDKNALQDYMTFQFVPEPETLTKEIKMLAPGCSLTKKLGSAPRIDRYYHREF--HPVQRSEDE 236
Cdd:COG0367 157 FASELKALLAHpGVDRELDPEALAEYLTLGYVPAPRTIFKGIRKLPPGHYLTVDAGGELEIRRYWDLEFvpHERSDSEEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 237 YAKKIKDALIDSVKIHMRSDVPVGSFLSGGIDSSIIVAIA-KNFNPNLETISVGFEREGYSELDVAQETAEKLGVKNYSM 315
Cdd:COG0367 237 AVEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAaRLSKGPLKTFSIGFEDSAYDESPYARAVAEHLGTEHHEV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 316 TITPEAFMKAFPHFVWSMDDPLADPAAVPQYFLAKEAVKHVKVCLTGEGADELFGGYTIYHEPESLkpfrytkpingalk 395
Cdd:COG0367 317 TVTPEDLLDALPDLVWHLDEPFADPSAVPTYLLSRLAREHVKVVLSGEGADELFGGYPRYREAALL-------------- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 396 rialmmpegmrgrsfllrgttplenryvgnafifgeqekqafFKNYNQNHPFQSITQPLYDESVDYDPISRMQFIDMHTW 475
Cdd:COG0367 383 ------------------------------------------LSPDFAEALGGELVPRLYAESGAEDPLRRMLYLDLKTY 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 476 LNGDLLHNADRTTMAHSLELRTPFVDREVYNLAAEIPADLRISHGTTKYILRKAVEDIVPAHVLHRKKLGFPVPIRFWLK 555
Cdd:COG0367 421 LPGDLLVKVDRMSMAHSLEVRVPFLDHRLVEFALSLPPELKLRGGRGKYLLRKALEGLLPDEVLDRPKQGFPVPLGPWLR 500
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 489741667 556 DEMYDWAKQIINDS--QTDQYFNKDYFLKLLDDHKAGVRDNSRKLWTVLTFMMWHRLY 611
Cdd:COG0367 501 GPLREWLEDLLSDEslAARGLFDPDAVRRLLEEHLAGRRDHSRKLWSLLMLELWLRRF 558
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-546 |
6.57e-170 |
|
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: 492.62 E-value: 6.57e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 4 FAGCLTDRTKADNAayDQTIHEMTKMIVHRGPDDDGY-FADDNITMGFRRLSIIDLAGGHQPLSYDNERYWMTFNGEIYN 82
Cdd:TIGR01536 1 IAGFFDLDDKAVEE--DEAIKRMSDTIAHRGPDASGIeYKDGNAILGHRRLAIIDLSGGAQPMSNEGKTYVIVFNGEIYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 83 YVELREQLKQEGYEFKTSSDSEVILAMYAKYHADATKYLRGMFAFVIWDKQEKTLFAARDQFGIKPFYYAISGDDFYYAS 162
Cdd:TIGR01536 79 HEELREELEAKGYTFQTDSDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYDGGQLYFAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 163 ESKAIYKILKDKTF-DKNALQDYMTFQFVPEPETLTKEIKMLAPGCSLTKKLGSApRIDRYYHREFHPVQRSEDEYAKKI 241
Cdd:TIGR01536 159 EIKALLAHPNIKPFpDGAALAPGFGFVRVPPPSTFFRGVFELEPGHDLPLDDDGL-NIERYYWERRDEHTDSEEDLVDEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 242 KDALIDSVKIHMRSDVPVGSFLSGGIDSSIIVAIAKNFNPN--LETISVGFERE-GYSELDVAQETAEKLGVKNYSMTIT 318
Cdd:TIGR01536 238 RSLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPRgpVHTFSIGFEGSpDFDESKYARKVADHLGTEHHEVLFS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 319 PEAFMKAFPHFVWSMDDPLADPAAVPQYFLAKEAVKH-VKVCLTGEGADELFGGYTIYHEPESLKPFRytkpingalkri 397
Cdd:TIGR01536 318 VEEGLDALPEVIYHLEEPTTIRASIPLYLLSKLAREDgVKVVLSGEGADELFGGYLYFHEAPAAEALR------------ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 398 almmpegmrgrsfllrgttplenryvgnafifgeqekqaffknynqnhpfqsitqplydesvdydpiSRMQFIDMHTWLN 477
Cdd:TIGR01536 386 -------------------------------------------------------------------EELQYLDLELYMP 398
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489741667 478 GDLLHNaDRTTMAHSLELRTPFVDREVYNLAAEIPADLRISHGTTKYILRKAVEDIVPAHVLHRKKLGF 546
Cdd:TIGR01536 399 GLLRRK-DRMSMAHSLEVRVPFLDHELVEYALSIPPEMKLRDGKEKYLLREAFEGYLPEEILWRPKEGF 466
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-546 |
1.24e-111 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 346.13 E-value: 1.24e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 1 MCGFAGCLtdRTKADNAAYDQTIHEMTKMIVHRGPDDDGYFADDNITMGFRRLSIIDLAGGHQPLSYDNERYWMTFNGEI 80
Cdd:PRK09431 1 MCGIFGIL--DIKTDADELRKKALEMSRLMRHRGPDWSGIYASDNAILGHERLSIVDVNGGAQPLYNEDGTHVLAVNGEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 81 YNYVELREQLKqEGYEFKTSSDSEVILAMYAKYHADATKYLRGMFAFVIWDKQEKTLFAARDQFGIKPFYYAISGDD-FY 159
Cdd:PRK09431 79 YNHQELRAELG-DKYAFQTGSDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGnLY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 160 YASESKAIykilkdktfdknalqdymtfqfvpepETLTKEIKMLAPGCSLTKKLGsapRIDRYYHR---EFHPVQrSEDE 236
Cdd:PRK09431 158 FASEMKAL--------------------------VPVCKTIKEFPPGHYYWSKDG---EFVRYYQRdwfDYDAVK-DNVT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 237 YAKKIKDALIDSVKIHMRSDVPVGSFLSGGIDSSIIVAIAKNFN--------------PNLETISVGFerEGYSELDVAQ 302
Cdd:PRK09431 208 DKNELRDALEAAVKKRLMSDVPYGVLLSGGLDSSLISAIAKKYAarriedderseawwPQLHSFAVGL--EGSPDLKAAR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 303 ETAEKLGVKNYSMTITPEAFMKAFPHFVWSMD--DPLADPAAVPQYFLAK-EAVKHVKVCLTGEGADELFGGYTIYHE-P 378
Cdd:PRK09431 286 EVADHLGTVHHEIHFTVQEGLDALRDVIYHLEtyDVTTIRASTPMYLMARkIKAMGIKMVLSGEGADELFGGYLYFHKaP 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 379 eslkpfrytkpingalkrialmmpegmrgrsfllrgttplenryvgNAFIFGEQekqaffknynqnhpFQSITQPLYdes 458
Cdd:PRK09431 366 ----------------------------------------------NAKEFHEE--------------TVRKLRALH--- 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 459 vdydpisrmqfidmhtwlNGDLLHnADRTTMAHSLELRTPFVDREVYNLAAEIPADLRISHGT--TKYILRKAVEDIVPA 536
Cdd:PRK09431 383 ------------------MYDCLR-ANKAMMAWGVEARVPFLDKEFLDVAMRINPEDKMCGNGkmEKHILREAFEGYLPE 443
|
570
....*....|
gi 489741667 537 HVLHRKKLGF 546
Cdd:PRK09431 444 SILWRQKEQF 453
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-224 |
4.93e-100 |
|
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: 304.10 E-value: 4.93e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 2 CGFAGCLTDRTKADNAAydqTIHEMTKMIVHRGPDDDGYFADDNITMGFRRLSIIDLAGGHQPLSYDNERYWMTFNGEIY 81
Cdd:cd00712 1 CGIAGIIGLDGASVDRA---TLERMLDALAHRGPDGSGIWIDEGVALGHRRLSIIDLSGGAQPMVSEDGRLVLVFNGEIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 82 NYVELREQLKQEGYEFKTSSDSEVILAMYAKYHADATKYLRGMFAFVIWDKQEKTLFAARDQFGIKPFYYAISGDDFYYA 161
Cdd:cd00712 78 NYRELRAELEALGHRFRTHSDTEVILHLYEEWGEDCLERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGRDGGGLAFA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489741667 162 SESKAIYKILK-DKTFDKNALQDYMTFQFVPEPETLTKEIKMLAPGCSLTKKLGsAPRIDRYYH 224
Cdd:cd00712 158 SELKALLALPGvPRELDEAALAEYLAFQYVPAPRTIFKGIRKLPPGHYLTVDPG-GVEIRRYWD 220
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
240-609 |
7.61e-100 |
|
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: 305.70 E-value: 7.61e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 240 KIKDALIDSVKIHMRSDVPVGSFLSGGIDSSIIVAIAKNFNPN-LETISVGFEREGYSELDVAQETAEKLGVKNYSMTIT 318
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSPSpLHTFSIGFEGRGYDEAPYAREVAEHLGTDHHELVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 319 PEAFMKAFPHFVWSMDDPLADPAAVPQYFLAKEAVKH-VKVCLTGEGADELFGGYTIYHepeslkpfrytkpingalkri 397
Cdd:pfam00733 81 PEDLLDALPDVIWHLDEPFADPSAIPLYLLSRLARRKgVKVVLSGEGADELFGGYPFYK--------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 398 almmpegmrgrsfllrgttplenryvgnafifgeqekqaffknynqnhpfqsitqplydesvDYDPISRMQFIDMHTWLN 477
Cdd:pfam00733 140 --------------------------------------------------------------GEDPLRRMLYLDLKTLLP 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 478 GDLLHnADRTTMAHSLELRTPFVDREVYNLAAEIPADLRISHGTTKYILRKAVEDIVPAHVLHRKKLGFPVPIRFW-LKD 556
Cdd:pfam00733 158 GDLLR-ADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKLRGGIEKYILREALEGILPDEILERPKEGFSAPVGDWkLRG 236
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 489741667 557 EMYDWAKQIINDSQTDQ--YFNKDYFLKLLDDHKAGvrdnsrklwtvlTFMMWHR 609
Cdd:pfam00733 237 PLRELAEDLLSDSRLAKegLLDREAVRELLDEHLAG------------MLELWLR 279
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-573 |
1.55e-78 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 260.42 E-value: 1.55e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 1 MCGFAGCLtdRTKADNAAYDQTIHEMTKMIVHRGPDDDGYFADDNIT-----MGFRRLSIIDLAGGHQPLSYDNERYWMT 75
Cdd:PTZ00077 1 MCGILAIF--NSKGERHELRRKALELSKRLRHRGPDWSGIIVLENSPgtyniLAHERLAIVDLSDGKQPLLDDDETVALM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 76 FNGEIYNYVELREQLKQEGYEFKTSSDSEVILAMYAKYHA-DATKYLRGMFAFVIWDKQEKTLFAARDQFGIKPFYYAIS 154
Cdd:PTZ00077 79 QNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKEYGPkDFWNHLDGMFATVIYDMKTNTFFAARDHIGIIPLYIGYA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 155 GDD-FYYASESKAIykilKDKTFdknalqdymtfqfvpepetltkEIKMLAPGCSL--TKKLGsapRIDRYY----HREF 227
Cdd:PTZ00077 159 KDGsIWFSSELKAL----HDQCV----------------------EVKQFPPGHYYdqTKEKG---EFVRYYnpnwHDFD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 228 HPVQRSEDEYaKKIKDALIDSVKIHMRSDVPVGSFLSGGIDSSIIVAI-AKNFN-----------PNLETISVGFerEGY 295
Cdd:PTZ00077 210 HPIPTGEIDL-EEIREALEAAVRKRLMGDVPFGLFLSGGLDSSIVAAIvAKLIKngeidlskrgmPKLHSFCIGL--EGS 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 296 SELDVAQETAEKLGVKNYSMTITPEAFMKAFPHFVWSMD--DPLADPAAVPQYFLAKE-AVKHVKVCLTGEGADELFGGY 372
Cdd:PTZ00077 287 PDLKAARKVAEYLGTEHHEFTFTVEEGIDALPDVIYHTEtyDVTTIRASTPMYLLSRRiKALGIKMVLSGEGSDELFGGY 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 373 TIYHEPeslkpfrytkpingalkrialmmpegmrgrsfllrgttplenryvgnafifgeqekqaffKNYNQNHpfqsitq 452
Cdd:PTZ00077 367 LYFHKA------------------------------------------------------------PNREEFH------- 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 453 plyDESVDydpisrmQFIDMHTWlngDLLHnADRTTMAHSLELRTPFVDREVYNLAAEIPADLRISHGTT----KYILRK 528
Cdd:PTZ00077 380 ---RELVR-------KLHDLHKY---DCLR-ANKATMAWGIEARVPFLDKDFLEYVMNIDPKYKMCNAFEgqmeKYILRK 445
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 489741667 529 AVEDI----VPAHVLHRKKLGFPVPIRFWLKDEMYDWAKQIINDSQTDQ 573
Cdd:PTZ00077 446 AFEGLekpyLPDEILWRQKEQFSDGVGYSWIDGLKEYAEKKISDQEFSQ 494
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-570 |
8.09e-77 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 255.46 E-value: 8.09e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 1 MCGFAGCLtdRTKADNAAYDQTIHEMTKMIVHRGPDDDGYFADDNITMGFRRLSIIDLAGGHQPLSYDNERYWMTFNGEI 80
Cdd:PLN02549 1 MCGILAVL--GCSDDSQAKRSRVLELSRRLRHRGPDWSGLYGNEDCYLAHERLAIMDPESGDQPLYNEDKTIVVTANGEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 81 YNYVELREQLKQegYEFKTSSDSEVILAMYAKYHADATKYLRGMFAFVIWDKQEKTLFAARDQFGIKPFYYAISGD-DFY 159
Cdd:PLN02549 79 YNHKELREKLKL--HKFRTGSDCEVIAHLYEEHGEEFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGLDgSVW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 160 YASESKAiykiLKDktfdknalqDYMTFQFVPepetltkeikmlaPGCSLTKKLGSaprIDRYYHREFHPVQRSEDEY-A 238
Cdd:PLN02549 157 FASEMKA----LCD---------DCERFEEFP-------------PGHYYSSKAGG---FRRWYNPPWFSESIPSTPYdP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 239 KKIKDALIDSVKIHMRSDVPVGSFLSGGIDSSIIVAIAKNF----------NPNLETISVGFerEGYSELDVAQETAEKL 308
Cdd:PLN02549 208 LVLREAFEKAVIKRLMTDVPFGVLLSGGLDSSLVASIAARHlaetkaarqwGQQLHSFCVGL--EGSPDLKAAREVADYL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 309 GVKNYSMTITPEAFMKAFPHFVWSMD--DPLADPAAVPQYFLAKE-AVKHVKVCLTGEGADELFGGYTIYHEPESlkpfr 385
Cdd:PLN02549 286 GTVHHEFHFTVQEGIDAIEDVIYHLEtyDVTTIRASTPMFLMSRKiKSLGVKMVLSGEGSDEIFGGYLYFHKAPN----- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 386 ytkpingalkrialmmpegmrgrsfllrgttplenryvgnafifgeqeKQAFFKNynqnhpfqsitqplydesvdydpiS 465
Cdd:PLN02549 361 ------------------------------------------------KEEFHKE------------------------T 368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 466 RMQFIDMHTWlngDLLHnADRTTMAHSLELRTPFVDREVYNLAAEI-PADLRISHGTT---KYILRKAVED----IVPAH 537
Cdd:PLN02549 369 CRKIKALHQY---DCLR-ANKSTSAWGLEARVPFLDKEFIDVAMSIdPEWKMIRPGEGrieKWVLRKAFDDeedpYLPKH 444
|
570 580 590
....*....|....*....|....*....|...
gi 489741667 538 VLHRKKLGFPVPIRFWLKDEMYDWAKQIINDSQ 570
Cdd:PLN02549 445 ILWRQKEQFSDGVGYSWIDGLKAHAEKHVSDEM 477
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
255-549 |
9.18e-58 |
|
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: 194.03 E-value: 9.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 255 SDVPVGSFLSGGIDSSIIVAIAKNFNPN--LETISVGFEREGYSELDVAQETAEKLGVKNYSMTITPEAFMKAFPHFV-- 330
Cdd:cd01991 1 SDVPVGVLLSGGLDSSLIAALAARLLPEtpIDLFTVGFEGSPTPDRAAARRVAEELGTEHHEVEVTIEELLDALPDVIli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 331 WSMDDPLADPAAVPQYFLAKEAVKHV-KVCLTGEGADELFGGYTIYHEPESLKPFRYTKPINGALKRIalmmpegmrgrs 409
Cdd:cd01991 81 YPTDTPMDLSIAIPLYFASRLAGKLGaKVVLSGEGADELFGGYSRHRDAPLRGWEALEEELLRDLDRL------------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 410 fllrgttplenryvgnafifgeqekqaffknynqnhpfqsitqplydesvdydpisrmqfidmHTWlngdLLHNADRTTM 489
Cdd:cd01991 149 ---------------------------------------------------------------WTR----NLGRDDRVAM 161
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489741667 490 AHSLELRTPFVDREVYNLAAEIPADLRIS--HGTTKYILRKAVEDIVPAHVLHRKKLGFPVP 549
Cdd:cd01991 162 AHGLEARVPFLDEELVEFALSLPPSLKIDprGGGEKYILREAARDLLPDEIAWRPKRAIQFG 223
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
51-167 |
4.50e-57 |
|
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: 188.50 E-value: 4.50e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 51 RRLSIIDLAGGHQPLSYDNE-RYWMTFNGEIYNYVELREQLKQEGYEFKTSSDSEVILAMYAKYH-ADATKYLRGMFAFV 128
Cdd:pfam13537 2 RRLSIIDLEGGAQPMVSSEDgRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAEWgEDCVDRLNGMFAFA 81
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489741667 129 IWDKQEKTLFAARDQFGIKPFYYA-ISGDDFYYASESKAI 167
Cdd:pfam13537 82 IWDRRRQRLFLARDRFGIKPLYYGrDDGGRLLFASELKAL 121
|
|
| lass_lactam_cya |
NF033535 |
lasso peptide isopeptide bond-forming cyclase; Members of this family are the isopeptide ... |
23-538 |
7.19e-53 |
|
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: 192.51 E-value: 7.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 23 IHEMTKMIVHRGPDDDGYFADDNITMGFRRLSIIDLAG-GHQPLSYDNERYWMTFNGEIYNYVELREQLKQEGYEFKTSS 101
Cdd:NF033535 20 LQQMVDILAHRGPDGADIWCEGSVGLGHRMLWTTPESLlEKLPLVNQTGDLVITADARIDNRDELISALQLNNCPPEKIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 102 DSEVILAMYAKYHADATKYLRGMFAFVIWDKQEKTLFAARDQFGIKPFYYAISGDDFYYASESKAIYkILKD--KTFDKN 179
Cdd:NF033535 100 DSQLILAAYEKWGEQCPEHLLGDFAFAIWDKRKQQLFCARDHFGVKPFYYYQSDKRFAFASEIKALL-CLPEvpRRLNEV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 180 ALQDYMTFQFVPEPETLTKEIKMLAPGCSLT---KKLgsapRIDRYY----HREFHpvQRSEDEYAKKIKDALIDSVKIH 252
Cdd:NF033535 179 RIADYLALMLEDKVITFYQDIFRLPPAHSMTvsqSGL----QIRSYWsldpSRELR--LDSDEEYAEAFREIFTEAVRCR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 253 MRSDVPVGSFLSGGIDSSIIVAIAKNFN-----PNLETISVGFERegYSELDVAQETAEKLGVKNYSmtitpeafmkafP 327
Cdd:NF033535 253 LRSAFPVGSHLSGGLDSSSITCVARQLLaeekkAPLHTFSNIFDK--VTECDERPFINAVLEQGGLI------------P 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 328 HFV---------------WSMDDPLADPAAVPQYFLAKEAVKH-VKVCLTGEGADE------------------------ 367
Cdd:NF033535 319 HYVhadqfgplsdleqifEYEDEPFLGPNHFLPWGLNRAAQKEgVRILLDGFDGDStvshghgyltelanqgkwltfaqe 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 368 --------------LFGGYTIYHEPESLKPFRYTKPInGALKRIALMMpEGMRGRSFLLRGTTPLENRYVGNAFIFGEQE 433
Cdd:NF033535 399 iralsknygtspwgLLRQYGLPYLEKLARQFKWLTFL-KPANQIHKHF-GISRRQLFLQHGIKPLVPRALLKLWRKLRGQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 434 KQaffknyNQNHPFQSITQPLYDESVDYDPISRMQFIDM---------HTW-LNGDL----LHNADRTTMAHSLELRTPF 499
Cdd:NF033535 477 AQ------PGNSWRPIINPDFAERIGLKERIQRLDPPPSsspltvreeHWQsLTSGIlpfvLEVLDKYAAAFSLEARHPF 550
|
570 580 590
....*....|....*....|....*....|....*....
gi 489741667 500 VDREVYNLAAEIPADLRISHGTTKYILRKAVEDIVPAHV 538
Cdd:NF033535 551 MDKRLVEFCLALPPEQKLRQGWSRMVMRRAMEGILPPQV 589
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
35-163 |
6.65e-52 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.
Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 174.80 E-value: 6.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 35 PDDDGYFADDNITMGFRRLSIIDLA-GGHQPLSYDNERYWMTFNGEIYNYVELREQLKQEGYEFKTSSDSEVILAMYAKY 113
Cdd:pfam13522 1 PDFSGIWVEGGVALGHVRLAIVDLPdAGNQPMLSRDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYEEW 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 489741667 114 HADATKYLRGMFAFVIWDKQEKTLFAARDQFGIKPFYYAISGDDFYYASE 163
Cdd:pfam13522 81 GEDCLERLRGMFAFAIWDRRRRTLFLARDRLGIKPLYYGILGGGFVFASE 130
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-170 |
2.40e-50 |
|
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: 173.79 E-value: 2.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 2 CGFAGCLTDRTKADNAAYDQtiHEMTKMIVHRGPDDDGYFADD---------------------------NITMGFRRLS 54
Cdd:cd00352 1 CGIFGIVGADGAASLLLLLL--LRGLAALEHRGPDGAGIAVYDgdglfvekragpvsdvaldlldeplksGVALGHVRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 55 IIDL--AGGHQPLSYDNERYWMTFNGEIYNYVELREQLKQEGYEFKTSSDSEVILAMYAKYHA---------DATKYLRG 123
Cdd:cd00352 79 TNGLpsEANAQPFRSEDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGRegglfeaveDALKRLDG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489741667 124 MFAFVIWDKQEKTLFAARDQFGIKPFYYAISGDDFYY-ASESKAIYKI 170
Cdd:cd00352 159 PFAFALWDGKPDRLFAARDRFGIRPLYYGITKDGGLVfASEPKALLAL 206
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
63-167 |
8.96e-18 |
|
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: 86.23 E-value: 8.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 63 QPLSYDNERYWMTF--NGEIYNYVELREQLKQEGYEFKTSSDSEVILAMYAKYH---------ADATKYLRGMFAFVIWD 131
Cdd:COG0034 92 QPFYVNSPFGSIALahNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIARELtkedleeaiKEALRRVKGAYSLVILT 171
|
90 100 110
....*....|....*....|....*....|....*.
gi 489741667 132 kqEKTLFAARDQFGIKPFYYAISGDDFYYASESKAI 167
Cdd:COG0034 172 --GDGLIAARDPNGIRPLVLGKLEDGYVVASESCAL 205
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
63-167 |
1.32e-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: 77.12 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 63 QPLSYDNERYWMTF--NGEIYNYVELREQLKQEGYEFKTSSDSEVILAMYAKYHADAT---------KYLRGMFAFVIWD 131
Cdd:cd00715 85 QPFVVNSPLGGIALahNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAKDDlfeaiidalERVKGAYSLVIMT 164
|
90 100 110
....*....|....*....|....*....|....*..
gi 489741667 132 kqEKTLFAARDQFGIKPFYYA-ISGDDFYYASESKAI 167
Cdd:cd00715 165 --ADGLIAVRDPHGIRPLVLGkLEGDGYVVASESCAL 199
|
|
| Gn_AT_II_novel |
cd03766 |
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its ... |
1-145 |
1.41e-14 |
|
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: 72.32 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 1 MCGFAGCLTdrTKADNAAYDQTIHEMTKMIVHRGPDDDGY--FADDNITMGFRrLSIIDLAGGH---QPLSYDNERYWMT 75
Cdd:cd03766 1 MCGILCSVS--PSGPHINSSLLSEELLPNLRNRGPDYLSTrqLSVTNWTLLFT-SSVLSLRGDHvtrQPLVDQSTGNVLQ 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489741667 76 FNGEIYNyvelreQLKQEGYEfktsSDSEVILAMYAKYHA------DATKYLRGMFAFVIWDKQEKTLFAARDQFG 145
Cdd:cd03766 78 WNGELYN------IDGVEDEE----NDTEVIFELLANCSSesqdilDVLSSIEGPFAFIYYDASENKLYFGRDCLG 143
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
63-167 |
4.63e-14 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 74.69 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 63 QPL--SYDNERYWMTFNGEIYNYVELREQLKQEGYEFKTSSDSEVILAMYAKYH--------ADATKYLRGMFAFVIWdk 132
Cdd:PRK05793 101 QPLvaNYKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAkkglekalVDAIQAIKGSYALVIL-- 178
|
90 100 110
....*....|....*....|....*....|....*
gi 489741667 133 QEKTLFAARDQFGIKPFYYAISGDDFYYASESKAI 167
Cdd:PRK05793 179 TEDKLIGVRDPHGIRPLCLGKLGDDYILSSESCAL 213
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-167 |
4.98e-13 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 71.63 E-value: 4.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 1 MCGFAGCLTDrtkadnAAYDQTIHEMTKMIVHRGPDDDGYFADDNIT------MG-----FRRLSIIDLAG----GH--- 62
Cdd:PLN02440 1 ECGVVGIFGD------PEASRLCYLGLHALQHRGQEGAGIVTVDGNRlqsitgNGlvsdvFDESKLDQLPGdiaiGHvry 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 63 -----------QPLsYDNERY---WMTFNGEIYNYVELREQLKQEGYEFKTSSDSEVILAMYAKYHA--------DATKY 120
Cdd:PLN02440 75 stagasslknvQPF-VANYRFgsiGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKArpffsrivDACEK 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489741667 121 LRGMFA--FVIWDKqektLFAARDQFGIKPFYYAI-SGDDFYYASESKAI 167
Cdd:PLN02440 154 LKGAYSmvFLTEDK----LVAVRDPHGFRPLVMGRrSNGAVVFASETCAL 199
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
77-167 |
1.21e-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: 64.39 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 77 NGEIYNYVELREQLKQEGYEFKTSSDSEVI---LAMYAKYHAD-------ATKYLRGMFAFVIWDKQEK-TLFAARDQfg 145
Cdd:cd00714 99 NGIIENYAELKEELEAKGYKFESETDTEVIahlIEYYYDGGLDlleavkkALKRLEGAYALAVISKDEPdEIVAARNG-- 176
|
90 100
....*....|....*....|..
gi 489741667 146 iKPFYYAISGDDFYYASESKAI 167
Cdd:cd00714 177 -SPLVIGIGDGENFVASDAPAL 197
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-175 |
1.61e-11 |
|
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: 64.98 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 2 CGFAGcLTDRTKADNAAYDQT--IHEMTkmivHRGPDDDGYFA----DDNITMGF-----------------RRLSIIDL 58
Cdd:cd01907 1 CGIFG-IMSKDGEPFVGALLVemLDAMQ----ERGPGDGAGFAlygdPDAFVYSSgkdmevfkgvgypediaRRYDLEEY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 59 AG----GH--QPLSYDNERYW----MTF------NGEIYNYVELREQLKQEGYEFKTSSDSEVI--------------LA 108
Cdd:cd01907 76 KGyhwiAHtrQPTNSAVWWYGahpfSIGdiavvhNGEISNYGSNREYLERFGYKFETETDTEVIayyldlllrkgglpLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 109 MYAK-----------YHADATKY----LRGMFAFVIWDKQEktLFAARDQFGIKPFYYAISGDDFYYASESKAIYKILKD 173
Cdd:cd01907 156 YYKHiirmpeeerelLLALRLTYrladLDGPFTIIVGTPDG--FIVIRDRIKLRPAVVAETDDYVAIASEECAIREIPDR 233
|
..
gi 489741667 174 KT 175
Cdd:cd01907 234 DN 235
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
77-141 |
8.79e-11 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 64.68 E-value: 8.79e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489741667 77 NGEIYNYVELREQLKQEGYEFKTSSDSEVI---LAMYAKYHAD-------ATKYLRGMFAF-VIWDKQEKTLFAAR 141
Cdd:PRK00331 100 NGIIENYAELKEELLAKGHVFKSETDTEVIahlIEEELKEGGDlleavrkALKRLEGAYALaVIDKDEPDTIVAAR 175
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
77-141 |
4.89e-10 |
|
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: 62.34 E-value: 4.89e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489741667 77 NGEIYNYVELREQLKQEGYEFKTSSDSEVI---LAMYAKYHAD-------ATKYLRGMFAFVIWDKQEK-TLFAAR 141
Cdd:COG0449 100 NGIIENYAELREELEAKGHTFKSETDTEVIahlIEEYLKGGGDlleavrkALKRLEGAYALAVISADEPdRIVAAR 175
|
|
| DUF3700 |
pfam12481 |
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ... |
76-156 |
3.08e-07 |
|
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 amino acids in length. There are two conserved sequence motifs: YGL and LRDR. This family is related to GATase enzyme domains.
Pssm-ID: 403619 [Multi-domain] Cd Length: 228 Bit Score: 51.60 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 76 FNGEIYNYVELREQlkqegYEF-KTSSDSEVILAMY------AKYHAD-ATKYLRGMFAFVIWDKQEKTLFAARDQFGIK 147
Cdd:pfam12481 81 FQGHLENLASLKQQ-----YGLsKGANEAMIVIEAYrtlrdrGPYPADqVVRDLEGKFAFVLYDSSTSTVFVASDADGSV 155
|
....*....
gi 489741667 148 PFYYAISGD 156
Cdd:pfam12481 156 PLYWGIDAD 164
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
77-173 |
4.31e-07 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 53.10 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 77 NGEIYNYVELREQLKQEGYEFKTSSDSEVILAMYAKYHAD----------ATKYLRGMFAFVIWDKQEK-TLFAARDQfg 145
Cdd:PTZ00295 130 NGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQgedfqeavksAISRLQGTWGLCIIHKDNPdSLIVARNG-- 207
|
90 100
....*....|....*....|....*...
gi 489741667 146 iKPFYYAISGDDFYYASESKAIYKILKD 173
Cdd:PTZ00295 208 -SPLLVGIGDDSIYVASEPSAFAKYTNE 234
|
|
| Wali7 |
cd01910 |
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ... |
76-156 |
1.20e-06 |
|
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced by aluminum. Wali7 has a single domain similar to the glutamine amidotransferase domain of glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The Wali7 domain is also somewhat similar to the Ntn hydrolase fold of the proteasomal alph and beta subunits.
Pssm-ID: 238891 [Multi-domain] Cd Length: 224 Bit Score: 50.00 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 76 FNGEIYNYVELReqlKQEGYEfKTSSDSEVILAMY------AKYHAD-ATKYLRGMFAFVIWDKQEKTLFAARDQFGIKP 148
Cdd:cd01910 77 FQGHLDNLGSLK---QQYGLS-KTANEAMLVIEAYrtlrdrGPYPADqVVKDLEGSFAFVLYDKKTSTVFVASDADGSVP 152
|
....*...
gi 489741667 149 FYYAISGD 156
Cdd:cd01910 153 LYWGIAAD 160
|
|
| betaLS_CarA_N |
cd01909 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_betaLS-type. Carbapenam ... |
30-177 |
6.47e-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: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 30 IVHRGPDDDG----YFADDNITMgFRRLSIIDLAGGHQP-LSYDNERYWMTFNGEIYNYVELREQLKQEGYEFKTSSDSE 104
Cdd:cd01909 6 VVAGTGGKDInlfaHRGSHTGEA-LPNGAGTIVHAGSVDvQVARSETGTAYLIGELYNRDELRSLLGAGEGRSAVLGDAE 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489741667 105 VILAMYAKYHADATKYLRGMFAFVIWDKQEKTLfAARDQFGIKPFyYAISGDDFYYASESKAIYKILKDKTFD 177
Cdd:cd01909 85 LLLLLLTRLGLHAFRLAEGDFCFFIEDGNGRLT-LATDHAGSVPV-YLVQAGEVWATTELKLLAAHEGPKAFP 155
|
|
| QueC |
pfam06508 |
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ... |
263-402 |
2.34e-05 |
|
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis of 7-carboxy-7-deazaguanine. They catalyze the conversion of 7-deaza-7-carboxyguanine to preQ0.
Pssm-ID: 428982 [Multi-domain] Cd Length: 210 Bit Score: 45.69 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 263 LSGGIDSSIIVAIAKNFNPNLETISVGFEREGYSELDVAQETAEKLGVKNYSMTITpeaFMKAFPHFVWsmddpLADPAA 342
Cdd:pfam06508 6 LSGGLDSTTCLAWAKKEGYEVYALSFDYGQRHRKELECAKKIAKALGVEHKILDLD---FLKQIGGSAL-----TDDSIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 343 VPQYFLAKEAVKHVKV------CLT-------GEGADELFGG-----YTIY--HEPESLKPFRYTKPINGALKRIALMMP 402
Cdd:pfam06508 78 VPKAELESEEIPNTYVpgrnliFLSiaaslaeALGAEAIFIGvneedYSGYpdCRPEFVKAFNVALNLGTMGKPIEIHTP 157
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
225-338 |
9.00e-04 |
|
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 439941 [Multi-domain] Cd Length: 542 Bit Score: 42.14 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 225 REFHPVQRSEDEYAKKIKDALIDSV-----KIHMRSDVpVGsfLSGGIDSSIIVAIAKNfnpnletiSVGFER------- 292
Cdd:COG0171 253 EAAPPPPEEEEMDLEEVYDALVLGLrdyvrKNGFKGVV-LG--LSGGIDSALVAALAVD--------ALGPENvlgvtmp 321
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 489741667 293 -EGYSELDV--AQETAEKLGVKNYSMTITP--EAFMKAFPHFVWSMDDPLA 338
Cdd:COG0171 322 sRYTSDESLedAEELAENLGIEYEEIDITPavEAFLEALPHAFGGELDDVA 372
|
|
| NAD_synthase |
cd00553 |
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ... |
263-339 |
1.78e-03 |
|
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de novo nicotinamide adenine dinucleotide (NAD(+)) biosynthesis, an amide transfer from either ammonia or glutamine to nicotinic acid adenine dinucleotide (NaAD). The conversion of NaAD to NAD(+) occurs via a NAD-adenylate intermediate and requires ATP and Mg(2+). The intermediate is subsequently cleaved into NAD(+) and AMP. In many prokaryotes, such as Escherichia coli, NAD synthase consists of a single domain and is strictly ammonia dependent. In contrast, eukaryotes and other prokaryotes have an additional N-terminal amidohydrolase domain that prefer glutamine. Interestingly, NAD(+) synthases in these prokaryotes, can also utilize ammonia as an amide source.
Pssm-ID: 467484 [Multi-domain] Cd Length: 248 Bit Score: 40.62 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 263 LSGGIDSSIIVAIAKNfnpnletiSVGFER-------EGYS---ELDVAQETAEKLGVKNYSMTITP--EAFMKAFPHFV 330
Cdd:cd00553 30 LSGGIDSAVVAALAVR--------ALGAENvlalimpSRYSskeTRDDAKALAENLGIEYRTIDIDPivDAFLKALEHAG 101
|
....*....
gi 489741667 331 WSMDDPLAD 339
Cdd:cd00553 102 GSEAEDLAL 110
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
64-106 |
3.71e-03 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 40.25 E-value: 3.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 489741667 64 PLSYDNERYWMTFNGEIYNYVELREQLKQEGYEFKTSSDSEVI 106
Cdd:PTZ00394 119 PQQSNNGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEVI 161
|
|
| QueC |
COG0603 |
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ... |
263-311 |
4.87e-03 |
|
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; 7-cyano-7-deazaguanine synthase (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440368 [Multi-domain] Cd Length: 223 Bit Score: 38.99 E-value: 4.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 489741667 263 LSGGIDSSIIVAIAKNFNPNLETISVGF-EREGySELDVAQETAEKLGVK 311
Cdd:COG0603 9 LSGGLDSTTCLAWALARGYEVYALSFDYgQRHR-KELEAARRIAKALGVG 57
|
|
| AANH_WbpG-like |
cd01996 |
Rhizobium leguminosarum WbpG protein and similar proteins; This subfamily includes Rhizobium ... |
263-371 |
6.32e-03 |
|
Rhizobium leguminosarum WbpG protein and similar proteins; This subfamily includes Rhizobium leguminosarum WbpG and Campylobacter jejuni PseA proteins. They belong to the of adenine nucleotide alpha hydrolase (AANH) superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus.
Pssm-ID: 467500 [Multi-domain] Cd Length: 158 Bit Score: 37.73 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489741667 263 LSGGIDSSIIVAIAKNfNPNLETISVGFEREGYSELDVA--QETAEKLGVKNYSMTITPEAFMKAFPHFVWSMDDPLAdP 340
Cdd:cd01996 12 VSGGKDSTYAAHKAKE-KYGLRPLLVTVDAGWNSPEAVKniEKLVRALGVDLITFVPNWKEMRDLQRLAFKSNGDQDW-P 89
|
90 100 110
....*....|....*....|....*....|...
gi 489741667 341 AAVPQY-FLAKEAVKH-VKVCLTGEGADELFGG 371
Cdd:cd01996 90 QDHGIFtSLYKMAVKFgIPLIIWGENPAEELGG 122
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
61-106 |
8.94e-03 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 38.96 E-value: 8.94e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 489741667 61 GHQPLSYDNERYWMTFNGEIYNYVELREQLKQEGYEFKTSSDSEVI 106
Cdd:PLN02981 106 SHPQSSGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVI 151
|
|
| |
