|
Name |
Accession |
Description |
Interval |
E-value |
| trio_amidotrans |
TIGR03104 |
asparagine synthase family amidotransferase; Members of this protein family are closely ... |
1-588 |
0e+00 |
|
asparagine synthase family amidotransferase; Members of this protein family are closely related to several isoforms of asparagine synthetase (glutamine amidotransferase) and typically have been given this name in genome annotation to date. Each is part of a conserved three-gene cassette sparsely distributed across at least twenty different species known so far, including alpha, beta, and gamma Proteobacteria, Mycobacterium, and Prosthecochloris, which is a member of the Chlorobi. The other two members of the cassette are a probable protease and a member of the GNAT family of acetyltransferases.
Pssm-ID: 274430 [Multi-domain] Cd Length: 589 Bit Score: 1038.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 1 MCGLAGELRFDHQPADLAAVERITHELAPRGPDAWGFHSQGPVALGHRRLKIMDLSDGSAQPMIDSNLGLSLAFNGAIYN 80
Cdd:TIGR03104 1 MCGICGEIRFDGQAPDVAAVVRMLAVLAPRGPDAGGVHAQGPVALGHRRLKIIDLSEASQQPMVDAELGLALVFNGCIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 81 FPELRAELESLGYQFHSGGDTEVLLKGYHAWGADMLPKLNGMFAFAIWERDSKQLFIARDRLGVKPLYLSKTDKRLRFAS 160
Cdd:TIGR03104 81 YRELRAELEALGYRFFSDGDTEVILKAYHAWGRDCVSRFNGMFAFAIWERDSGRLLLARDRLGIKPLYYAEDAGRLRFAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 161 SLPALLKGGDISGMLDPVALNHYLNFHAVVPAPRTLLAGVEKLPPASWMRIDASGKVEQKVWWTLPYGPHEDEKNLTLED 240
Cdd:TIGR03104 161 SLPALLAAGGVDTDIDPVALHHYLTFHAVVPAPHTILKGVRKLPPATWMTVEPDGSRTQRSYWSLDAGRPADDAARTEAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 241 WRDRVLDSTREAVAIRQRAAVDVGVLLSGGVDSSMLVGLLREVGVEDLSTFSIGFQDAGGERGDEFQYSDLIAKHYGTRH 320
Cdd:TIGR03104 241 WQDAILEALRLAVKRRLVADVPVGVLLSGGLDSSLIVGLLAEAGVDGLRTFSIGFEDVGGEKGDEFEYSDIIAERFHTRH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 321 HQLRIQEREIIEQLPAAFRAMSEPMVSHDCIAFYLLSREVSKHCKVVQSGQGADELFAGYHWYPQVD-GASDPVAAYRDA 399
Cdd:TIGR03104 321 HKIRIPNHRVLPALPEAVAAMSEPMVSHDCVAFYLLSEEVSKHVKVVQSGQGADEVFGGYHWYPPLAaGAGDPVAAYRRA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 400 FVDRSYAEYAETVQPKWRtANDAAGDFVRDHFAQPGASAAVDKALRLDSTVMLVDDPVKRVDNMTMAWGLEARTPFLDYR 479
Cdd:TIGR03104 401 FFDRDHAEYLEMVGPRFH-AEDVSGEFVADHFARPGADTAVDQALRLDTTVMLVDDPVKRVDNMTMAWGLEARVPFLDHE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 480 LVELSARIPGKFKLPDGGKQVLKEAARMVIPSEVIDRKKGYFPVPGLKHLQGDTLNWVRELLTD-SSQDRGLFNPAMVDK 558
Cdd:TIGR03104 480 LVELAARIPPELKLADGGKGVLKEAARGVIPSEVIDRPKGYFPVPALKYLRGPFLEWVRDALTSpAARERGLFQRAYVDR 559
|
570 580 590
....*....|....*....|....*....|
gi 489497627 559 LLTNPEGQLTPLRGSKLWQLAALNLWLSEQ 588
Cdd:TIGR03104 560 LLADPDGHLTPLRGSKLWQLALLELWLQRH 589
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-585 |
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: 689.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 1 MCGLAGELRFDHqPADLAAVERITHELAPRGPDAWGFHSQGPVALGHRRLKIMDLSDGSAQPMIDSNLGLSLAFNGAIYN 80
Cdd:COG0367 1 MCGIAGIIDFDG-GADREVLERMLDALAHRGPDGSGIWVDGGVALGHRRLSIIDLSEGGHQPMVSEDGRYVLVFNGEIYN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 81 FPELRAELESLGYQFHSGGDTEVLLKGYHAWGADMLPKLNGMFAFAIWERDSKQLFIARDRLGVKPLYLSKTDKRLRFAS 160
Cdd:COG0367 80 YRELRAELEALGHRFRTHSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDGGGLAFAS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 161 SLPALLKGGDISGMLDPVALNHYLNFHaVVPAPRTLLAGVEKLPPASWMRIDASGKVEQKVWWTLPYGPHEDEKnlTLED 240
Cdd:COG0367 160 ELKALLAHPGVDRELDPEALAEYLTLG-YVPAPRTIFKGIRKLPPGHYLTVDAGGELEIRRYWDLEFVPHERSD--SEEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 241 WRDRVLDSTREAVAIRQRAAVDVGVLLSGGVDSSMLVGLLREVGVEDLSTFSIGFQDAGgerGDEFQYSDLIAKHYGTRH 320
Cdd:COG0367 237 AVEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKGPLKTFSIGFEDSA---YDESPYARAVAEHLGTEH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 321 HQLRIQEREIIEQLPAAFRAMSEPMVSHDCIAFYLLSREVSKHCKVVQSGQGADELFAGYHWYPqvdgasDPVAAYRDAF 400
Cdd:COG0367 314 HEVTVTPEDLLDALPDLVWHLDEPFADPSAVPTYLLSRLAREHVKVVLSGEGADELFGGYPRYR------EAALLLSPDF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 401 VDRsyaeyaetvqpkwrtandAAGDFVRDHFAQPGASAAVDKALRLDSTVMLVDDPVKRVDNMTMAWGLEARTPFLDYRL 480
Cdd:COG0367 388 AEA------------------LGGELVPRLYAESGAEDPLRRMLYLDLKTYLPGDLLVKVDRMSMAHSLEVRVPFLDHRL 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 481 VELSARIPGKFKLPDG-GKQVLKEAARMVIPSEVIDRKKGYFPVPGLKHLQGDTLNWVRELLTDSS-QDRGLFNPAMVDK 558
Cdd:COG0367 450 VEFALSLPPELKLRGGrGKYLLRKALEGLLPDEVLDRPKQGFPVPLGPWLRGPLREWLEDLLSDESlAARGLFDPDAVRR 529
|
570 580
....*....|....*....|....*...
gi 489497627 559 LLTN-PEGQLtpLRGSKLWQLAALNLWL 585
Cdd:COG0367 530 LLEEhLAGRR--DHSRKLWSLLMLELWL 555
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-224 |
2.18e-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: 303.71 E-value: 2.18e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 2 CGLAGELRFDHQPADLAAVERITHELAPRGPDAWGFHSQGPVALGHRRLKIMDLSDGsAQPMIDSNLGLSLAFNGAIYNF 81
Cdd:cd00712 1 CGIAGIIGLDGASVDRATLERMLDALAHRGPDGSGIWIDEGVALGHRRLSIIDLSGG-AQPMVSEDGRLVLVFNGEIYNY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 82 PELRAELESLGYQFHSGGDTEVLLKGYHAWGADMLPKLNGMFAFAIWERDSKQLFIARDRLGVKPLYLSKTDKRLRFASS 161
Cdd:cd00712 80 RELRAELEALGHRFRTHSDTEVILHLYEEWGEDCLERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGRDGGGLAFASE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489497627 162 LPALLKGGDISGMLDPVALNHYLnFHAVVPAPRTLLAGVEKLPPASWMRIDAsGKVEQKVWWT 224
Cdd:cd00712 160 LKALLALPGVPRELDEAALAEYL-AFQYVPAPRTIFKGIRKLPPGHYLTVDP-GGVEIRRYWD 220
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-529 |
1.66e-83 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 271.40 E-value: 1.66e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 1 MCGLAGELRFDHQPAD-----LAAVERITHelapRGPDAWGFHSQGPVALGHRRLKIMDLSDGsAQPMIDSNLGLSLAFN 75
Cdd:PRK09431 1 MCGIFGILDIKTDADElrkkaLEMSRLMRH----RGPDWSGIYASDNAILGHERLSIVDVNGG-AQPLYNEDGTHVLAVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 76 GAIYNFPELRAELESlGYQFHSGGDTEVLLKGYHAWGADMLPKLNGMFAFAIWERDSKQLFIARDRLGVKPLYLSKTDK- 154
Cdd:PRK09431 76 GEIYNHQELRAELGD-KYAFQTGSDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 155 RLRFASSLPALlkggdisgmldpvalnhylnfhavVPAPRTllagVEKLPPASWMRiDASGKVEQkvWWTLPYGPHEDEK 234
Cdd:PRK09431 155 NLYFASEMKAL------------------------VPVCKT----IKEFPPGHYYW-SKDGEFVR--YYQRDWFDYDAVK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 235 N--LTLEDWRDRVldstREAVAIRQRAAVDVGVLLSGGVDSSM-------------LVGLLREVGVEDLSTFSIGFQDAg 299
Cdd:PRK09431 204 DnvTDKNELRDAL----EAAVKKRLMSDVPYGVLLSGGLDSSLisaiakkyaarriEDDERSEAWWPQLHSFAVGLEGS- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 300 gergDEFQYSDLIAKHYGTRHHQLRIQEREIIEQLP-----------AAFRAmSEPMvshdciafYLLSREV-SKHCKVV 367
Cdd:PRK09431 279 ----PDLKAAREVADHLGTVHHEIHFTVQEGLDALRdviyhletydvTTIRA-STPM--------YLMARKIkAMGIKMV 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 368 QSGQGADELFAGYHWYpqvdgasdpvaayrdafvdrsyaeyaetvqpkwrtandaagdfvrdHFAqPGASAAVDKALRLD 447
Cdd:PRK09431 346 LSGEGADELFGGYLYF----------------------------------------------HKA-PNAKEFHEETVRKL 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 448 STVMLVDdpVKRVDNMTMAWGLEARTPFLDYRLVELSARIPGKFKLPDGG---KQVLKEAARMVIPSEVIDRKK------ 518
Cdd:PRK09431 379 RALHMYD--CLRANKAMMAWGVEARVPFLDKEFLDVAMRINPEDKMCGNGkmeKHILREAFEGYLPESILWRQKeqfsdg 456
|
570
....*....|..
gi 489497627 519 -GYFPVPGLKHL 529
Cdd:PRK09431 457 vGYSWIDTLKEV 468
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
244-586 |
1.65e-80 |
|
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: 254.46 E-value: 1.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 244 RVLDSTREAVAIRQRAAVDVGVLLSGGVDSSMLVGLLREVGVEDLSTFSIGFQdagGERGDEFQYSDLIAKHYGTRHHQL 323
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSPSPLHTFSIGFE---GRGYDEAPYAREVAEHLGTDHHEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 324 RIQEREIIEQLPAAFRAMSEPMVSHDCIAFYLLSREV-SKHCKVVQSGQGADELFAGYHWYPQVDgasdpvaayrdafvd 402
Cdd:pfam00733 78 VVTPEDLLDALPDVIWHLDEPFADPSAIPLYLLSRLArRKGVKVVLSGEGADELFGGYPFYKGED--------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 403 rsyaeyaetvqpkwrtandaagdfvrdhfaqpgasaAVDKALRLDSTVMLVDDPVkRVDNMTMAWGLEARTPFLDYRLVE 482
Cdd:pfam00733 143 ------------------------------------PLRRMLYLDLKTLLPGDLL-RADRMSMAHGLEVRVPFLDHRLVE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 483 LSARIPGKFKLPDG-GKQVLKEAARMVIPSEVIDRKKGYFPVP-GLKHLQGDTLNWVRELLTDS-SQDRGLFNPAMVDKL 559
Cdd:pfam00733 186 YALRLPPELKLRGGiEKYILREALEGILPDEILERPKEGFSAPvGDWKLRGPLRELAEDLLSDSrLAKEGLLDREAVREL 265
|
330 340
....*....|....*....|....*..
gi 489497627 560 LTNPEGqltplrgsklwqlAALNLWLS 586
Cdd:pfam00733 266 LDEHLA-------------GMLELWLR 279
|
|
| lass_lactam_cya |
NF033535 |
lasso peptide isopeptide bond-forming cyclase; Members of this family are the isopeptide ... |
1-321 |
1.51e-38 |
|
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: 150.91 E-value: 1.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 1 MCGLAGELRFDHQPADLAAVERITHELAPRGPDAWGFHSQGPVALGHRRLKIMDLSDGSAQPMIDSNLGLSLAFNGAIYN 80
Cdd:NF033535 1 MSGIVGIYYLDGRPVDREDLQQMVDILAHRGPDGADIWCEGSVGLGHRMLWTTPESLLEKLPLVNQTGDLVITADARIDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 81 FPELRAELESLGYQFHSGGDTEVLLKGYHAWGADMLPKLNGMFAFAIWERDSKQLFIARDRLGVKPLYLSKTDKRLRFAS 160
Cdd:NF033535 81 RDELISALQLNNCPPEKITDSQLILAAYEKWGEQCPEHLLGDFAFAIWDKRKQQLFCARDHFGVKPFYYYQSDKRFAFAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 161 SLPALLKGGDISGMLDPVALNHYLnfhAVVPAPR--TLLAGVEKLPPASWMRIDASGkVEQKVWWTLpygphEDEKNLTL 238
Cdd:NF033535 161 EIKALLCLPEVPRRLNEVRIADYL---ALMLEDKviTFYQDIFRLPPAHSMTVSQSG-LQIRSYWSL-----DPSRELRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 239 ---EDWRDRVLDSTREAVAIRQRAAVDVGVLLSGGVDSS----MLVGLLREVGVEDLSTFSIGFqDAGGErGDEFQYSDL 311
Cdd:NF033535 232 dsdEEYAEAFREIFTEAVRCRLRSAFPVGSHLSGGLDSSsitcVARQLLAEEKKAPLHTFSNIF-DKVTE-CDERPFINA 309
|
330
....*....|
gi 489497627 312 IAKHYGTRHH 321
Cdd:NF033535 310 VLEQGGLIPH 319
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| trio_amidotrans |
TIGR03104 |
asparagine synthase family amidotransferase; Members of this protein family are closely ... |
1-588 |
0e+00 |
|
asparagine synthase family amidotransferase; Members of this protein family are closely related to several isoforms of asparagine synthetase (glutamine amidotransferase) and typically have been given this name in genome annotation to date. Each is part of a conserved three-gene cassette sparsely distributed across at least twenty different species known so far, including alpha, beta, and gamma Proteobacteria, Mycobacterium, and Prosthecochloris, which is a member of the Chlorobi. The other two members of the cassette are a probable protease and a member of the GNAT family of acetyltransferases.
Pssm-ID: 274430 [Multi-domain] Cd Length: 589 Bit Score: 1038.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 1 MCGLAGELRFDHQPADLAAVERITHELAPRGPDAWGFHSQGPVALGHRRLKIMDLSDGSAQPMIDSNLGLSLAFNGAIYN 80
Cdd:TIGR03104 1 MCGICGEIRFDGQAPDVAAVVRMLAVLAPRGPDAGGVHAQGPVALGHRRLKIIDLSEASQQPMVDAELGLALVFNGCIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 81 FPELRAELESLGYQFHSGGDTEVLLKGYHAWGADMLPKLNGMFAFAIWERDSKQLFIARDRLGVKPLYLSKTDKRLRFAS 160
Cdd:TIGR03104 81 YRELRAELEALGYRFFSDGDTEVILKAYHAWGRDCVSRFNGMFAFAIWERDSGRLLLARDRLGIKPLYYAEDAGRLRFAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 161 SLPALLKGGDISGMLDPVALNHYLNFHAVVPAPRTLLAGVEKLPPASWMRIDASGKVEQKVWWTLPYGPHEDEKNLTLED 240
Cdd:TIGR03104 161 SLPALLAAGGVDTDIDPVALHHYLTFHAVVPAPHTILKGVRKLPPATWMTVEPDGSRTQRSYWSLDAGRPADDAARTEAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 241 WRDRVLDSTREAVAIRQRAAVDVGVLLSGGVDSSMLVGLLREVGVEDLSTFSIGFQDAGGERGDEFQYSDLIAKHYGTRH 320
Cdd:TIGR03104 241 WQDAILEALRLAVKRRLVADVPVGVLLSGGLDSSLIVGLLAEAGVDGLRTFSIGFEDVGGEKGDEFEYSDIIAERFHTRH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 321 HQLRIQEREIIEQLPAAFRAMSEPMVSHDCIAFYLLSREVSKHCKVVQSGQGADELFAGYHWYPQVD-GASDPVAAYRDA 399
Cdd:TIGR03104 321 HKIRIPNHRVLPALPEAVAAMSEPMVSHDCVAFYLLSEEVSKHVKVVQSGQGADEVFGGYHWYPPLAaGAGDPVAAYRRA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 400 FVDRSYAEYAETVQPKWRtANDAAGDFVRDHFAQPGASAAVDKALRLDSTVMLVDDPVKRVDNMTMAWGLEARTPFLDYR 479
Cdd:TIGR03104 401 FFDRDHAEYLEMVGPRFH-AEDVSGEFVADHFARPGADTAVDQALRLDTTVMLVDDPVKRVDNMTMAWGLEARVPFLDHE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 480 LVELSARIPGKFKLPDGGKQVLKEAARMVIPSEVIDRKKGYFPVPGLKHLQGDTLNWVRELLTD-SSQDRGLFNPAMVDK 558
Cdd:TIGR03104 480 LVELAARIPPELKLADGGKGVLKEAARGVIPSEVIDRPKGYFPVPALKYLRGPFLEWVRDALTSpAARERGLFQRAYVDR 559
|
570 580 590
....*....|....*....|....*....|
gi 489497627 559 LLTNPEGQLTPLRGSKLWQLAALNLWLSEQ 588
Cdd:TIGR03104 560 LLADPDGHLTPLRGSKLWQLALLELWLQRH 589
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-585 |
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: 689.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 1 MCGLAGELRFDHqPADLAAVERITHELAPRGPDAWGFHSQGPVALGHRRLKIMDLSDGSAQPMIDSNLGLSLAFNGAIYN 80
Cdd:COG0367 1 MCGIAGIIDFDG-GADREVLERMLDALAHRGPDGSGIWVDGGVALGHRRLSIIDLSEGGHQPMVSEDGRYVLVFNGEIYN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 81 FPELRAELESLGYQFHSGGDTEVLLKGYHAWGADMLPKLNGMFAFAIWERDSKQLFIARDRLGVKPLYLSKTDKRLRFAS 160
Cdd:COG0367 80 YRELRAELEALGHRFRTHSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDGGGLAFAS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 161 SLPALLKGGDISGMLDPVALNHYLNFHaVVPAPRTLLAGVEKLPPASWMRIDASGKVEQKVWWTLPYGPHEDEKnlTLED 240
Cdd:COG0367 160 ELKALLAHPGVDRELDPEALAEYLTLG-YVPAPRTIFKGIRKLPPGHYLTVDAGGELEIRRYWDLEFVPHERSD--SEEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 241 WRDRVLDSTREAVAIRQRAAVDVGVLLSGGVDSSMLVGLLREVGVEDLSTFSIGFQDAGgerGDEFQYSDLIAKHYGTRH 320
Cdd:COG0367 237 AVEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKGPLKTFSIGFEDSA---YDESPYARAVAEHLGTEH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 321 HQLRIQEREIIEQLPAAFRAMSEPMVSHDCIAFYLLSREVSKHCKVVQSGQGADELFAGYHWYPqvdgasDPVAAYRDAF 400
Cdd:COG0367 314 HEVTVTPEDLLDALPDLVWHLDEPFADPSAVPTYLLSRLAREHVKVVLSGEGADELFGGYPRYR------EAALLLSPDF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 401 VDRsyaeyaetvqpkwrtandAAGDFVRDHFAQPGASAAVDKALRLDSTVMLVDDPVKRVDNMTMAWGLEARTPFLDYRL 480
Cdd:COG0367 388 AEA------------------LGGELVPRLYAESGAEDPLRRMLYLDLKTYLPGDLLVKVDRMSMAHSLEVRVPFLDHRL 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 481 VELSARIPGKFKLPDG-GKQVLKEAARMVIPSEVIDRKKGYFPVPGLKHLQGDTLNWVRELLTDSS-QDRGLFNPAMVDK 558
Cdd:COG0367 450 VEFALSLPPELKLRGGrGKYLLRKALEGLLPDEVLDRPKQGFPVPLGPWLRGPLREWLEDLLSDESlAARGLFDPDAVRR 529
|
570 580
....*....|....*....|....*...
gi 489497627 559 LLTN-PEGQLtpLRGSKLWQLAALNLWL 585
Cdd:COG0367 530 LLEEhLAGRR--DHSRKLWSLLMLELWL 555
|
|
| eps_aminotran_1 |
TIGR03108 |
exosortase A system-associated amidotransferase 1; The predicted protein-sorting ... |
1-578 |
1.35e-124 |
|
exosortase A system-associated amidotransferase 1; The predicted protein-sorting transpeptidase that we call exosortase (see TIGR02602) has distinct subclasses that associated with different types of exopolysaccharide production loci. This model represents a distinct clade among a set of amidotransferases largely annotated (not necessarily accurately) as glutatime-hydrolyzing asparagine synthases. Members of this clade are essentially restricted to the characteristic exopolysaccharide (EPS) regions that contain the exosortase 1 genome (xrtA), in genomes that also have numbers of PEP-CTERM domain (TIGR02595) proteins.
Pssm-ID: 132152 [Multi-domain] Cd Length: 628 Bit Score: 380.62 E-value: 1.35e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 1 MCGLAGELRFDHQ-PADLAAVERITHELAPRGPDAWGFHSQGPVALGHRRLKIMDLSdGSAQPMIDSNLGLSLAFNGAIY 79
Cdd:TIGR03108 1 MCGITGIFDLTGQrPIDRDLLRRMNDAQAHRGPDGGGVHVEPGIGLGHRRLSIIDLS-GGQQPLFNEDGSVVVVFNGEIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 80 NFPELRAELESLGYQFHSGGDTEVLLKGYHAWGADMLPKLNGMFAFAIWERDSKQLFIARDRLGVKPLYLSKT-DKRLRF 158
Cdd:TIGR03108 80 NFQELVAELQALGHVFRTRSDTEVIVHAWEEWGEACVERFRGMFAFALWDRNQETLFLARDRLGIKPLYYALLaDGWFIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 159 ASSLPALLKGGDISGMLDPVALNHYLNFhAVVPAPRTLLAGVEKLPPASWMRID-ASGKVEQKVWWTLPYGPHedeKNLT 237
Cdd:TIGR03108 160 GSELKALTAHPSLPRELDPLAVEDYFAY-GYVPDPRTIFKGVKKLEPGHTLTLRrGAPPARPRCYWDVSFAPA---APLS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 238 LEDWRDRVLDSTREAVAIRQRAAVDVGVLLSGGVDSSMLVGLLREVGVEDLSTFSIGFQDAggeRGDEFQYSDLIAKHYG 317
Cdd:TIGR03108 236 EADALAELIERLREAVRSRMVADVPLGAFLSGGVDSSAVVALMAGLSDTPVNTCSIAFDDP---AFDESAYARQVAERYG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 318 TRHH--QLRIQEREIIEQLPAAFramSEPMVSHDCIAFYLLSREVSKHCKVVQSGQGADELFAGY--------------- 380
Cdd:TIGR03108 313 TNHRveTVDPDDFSLVDRLAGLY---DEPFADSSALPTYRVCELARKRVTVALSGDGGDELFAGYrryrwhmaeervrgi 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 381 --------------HWYPQVDGA--------------SDPVAAYRDAFVDRSYAEYAETVQPKWRT--ANDAAGDFVRDH 430
Cdd:TIGR03108 390 lplglrrplfgtlgRLYPKADWAprmlrakttfqalaRDPLEGYFHSVSVLDNALRRQLFSPDFRRelQGYRAIEVLRRH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 431 FAQPGASAAVDKALRLDSTVMLVDDPVKRVDNMTMAWGLEARTPFLDYRLVELSARIPGKFKLPDG-GKQVLKEAARMVI 509
Cdd:TIGR03108 470 AARAPTDDALSLAQYLDLKTYLPGDILTKVDRASMAHGLEVRVPLLDHRLVEWAAGLPPDLKLRGGeGKYLLKKAMRPYL 549
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489497627 510 PSEVIDRKKGYFPVPGLKHLQGDTLNWVRELLTDSSQDR-GLFNPAMVDKLLtnpEGQLTPLR--GSKLWQL 578
Cdd:TIGR03108 550 PDDVLYRPKMGFSVPLAAWFRGPLRERVRTLVLGETLAEtGLFDPAFIRKLV---DQHQSGRRdySAPLWSL 618
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
19-518 |
2.86e-123 |
|
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: 371.67 E-value: 2.86e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 19 AVERITHELAPRGPDAWGF-HSQGPVALGHRRLKIMDLSDGsAQPMIDSNLGLSLAFNGAIYNFPELRAELESLGYQFHS 97
Cdd:TIGR01536 17 AIKRMSDTIAHRGPDASGIeYKDGNAILGHRRLAIIDLSGG-AQPMSNEGKTYVIVFNGEIYNHEELREELEAKGYTFQT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 98 GGDTEVLLKGYHAWGADMLPKLNGMFAFAIWERDSKQLFIARDRLGVKPLYLSKTDKRLRFASSLPALLKGGDISGMLDP 177
Cdd:TIGR01536 96 DSDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYDGGQLYFASEIKALLAHPNIKPFPDG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 178 VALNHYLnFHAVVPAPRTLLAGVEKLPPASWMRIDASGKVEQKVWWtlpygPHEDEKNLTLEDWRDRVLDSTREAVAIRQ 257
Cdd:TIGR01536 176 AALAPGF-GFVRVPPPSTFFRGVFELEPGHDLPLDDDGLNIERYYW-----ERRDEHTDSEEDLVDELRSLLEDAVKRRL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 258 RAAVDVGVLLSGGVDSSMLVGLL-REVGVEDLSTFSIGFQDAGGErgDEFQYSDLIAKHYGTRHHQLRIQEREIIEQLPA 336
Cdd:TIGR01536 250 VADVPVGVLLSGGLDSSLVAAIArREAPRGPVHTFSIGFEGSPDF--DESKYARKVADHLGTEHHEVLFSVEEGLDALPE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 337 AFRAMSEPMVSHDCIAFYLLSREVSKHC-KVVQSGQGADELFAGYHWYpqvdgasdpvaayrdafvdrsyaeyaetvqpk 415
Cdd:TIGR01536 328 VIYHLEEPTTIRASIPLYLLSKLAREDGvKVVLSGEGADELFGGYLYF-------------------------------- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 416 wrtandaagdfvrdHFAqPGASAAVDKALRLDSTVMLVDDpVKRVDNMTMAWGLEARTPFLDYRLVELSARIPGKFKLPD 495
Cdd:TIGR01536 376 --------------HEA-PAAEALREELQYLDLELYMPGL-LRRKDRMSMAHSLEVRVPFLDHELVEYALSIPPEMKLRD 439
|
490 500
....*....|....*....|....
gi 489497627 496 G-GKQVLKEAARMVIPSEVIDRKK 518
Cdd:TIGR01536 440 GkEKYLLREAFEGYLPEEILWRPK 463
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-224 |
2.18e-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: 303.71 E-value: 2.18e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 2 CGLAGELRFDHQPADLAAVERITHELAPRGPDAWGFHSQGPVALGHRRLKIMDLSDGsAQPMIDSNLGLSLAFNGAIYNF 81
Cdd:cd00712 1 CGIAGIIGLDGASVDRATLERMLDALAHRGPDGSGIWIDEGVALGHRRLSIIDLSGG-AQPMVSEDGRLVLVFNGEIYNY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 82 PELRAELESLGYQFHSGGDTEVLLKGYHAWGADMLPKLNGMFAFAIWERDSKQLFIARDRLGVKPLYLSKTDKRLRFASS 161
Cdd:cd00712 80 RELRAELEALGHRFRTHSDTEVILHLYEEWGEDCLERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGRDGGGLAFASE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489497627 162 LPALLKGGDISGMLDPVALNHYLnFHAVVPAPRTLLAGVEKLPPASWMRIDAsGKVEQKVWWT 224
Cdd:cd00712 160 LKALLALPGVPRELDEAALAEYL-AFQYVPAPRTIFKGIRKLPPGHYLTVDP-GGVEIRRYWD 220
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-529 |
1.66e-83 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 271.40 E-value: 1.66e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 1 MCGLAGELRFDHQPAD-----LAAVERITHelapRGPDAWGFHSQGPVALGHRRLKIMDLSDGsAQPMIDSNLGLSLAFN 75
Cdd:PRK09431 1 MCGIFGILDIKTDADElrkkaLEMSRLMRH----RGPDWSGIYASDNAILGHERLSIVDVNGG-AQPLYNEDGTHVLAVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 76 GAIYNFPELRAELESlGYQFHSGGDTEVLLKGYHAWGADMLPKLNGMFAFAIWERDSKQLFIARDRLGVKPLYLSKTDK- 154
Cdd:PRK09431 76 GEIYNHQELRAELGD-KYAFQTGSDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 155 RLRFASSLPALlkggdisgmldpvalnhylnfhavVPAPRTllagVEKLPPASWMRiDASGKVEQkvWWTLPYGPHEDEK 234
Cdd:PRK09431 155 NLYFASEMKAL------------------------VPVCKT----IKEFPPGHYYW-SKDGEFVR--YYQRDWFDYDAVK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 235 N--LTLEDWRDRVldstREAVAIRQRAAVDVGVLLSGGVDSSM-------------LVGLLREVGVEDLSTFSIGFQDAg 299
Cdd:PRK09431 204 DnvTDKNELRDAL----EAAVKKRLMSDVPYGVLLSGGLDSSLisaiakkyaarriEDDERSEAWWPQLHSFAVGLEGS- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 300 gergDEFQYSDLIAKHYGTRHHQLRIQEREIIEQLP-----------AAFRAmSEPMvshdciafYLLSREV-SKHCKVV 367
Cdd:PRK09431 279 ----PDLKAAREVADHLGTVHHEIHFTVQEGLDALRdviyhletydvTTIRA-STPM--------YLMARKIkAMGIKMV 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 368 QSGQGADELFAGYHWYpqvdgasdpvaayrdafvdrsyaeyaetvqpkwrtandaagdfvrdHFAqPGASAAVDKALRLD 447
Cdd:PRK09431 346 LSGEGADELFGGYLYF----------------------------------------------HKA-PNAKEFHEETVRKL 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 448 STVMLVDdpVKRVDNMTMAWGLEARTPFLDYRLVELSARIPGKFKLPDGG---KQVLKEAARMVIPSEVIDRKK------ 518
Cdd:PRK09431 379 RALHMYD--CLRANKAMMAWGVEARVPFLDKEFLDVAMRINPEDKMCGNGkmeKHILREAFEGYLPESILWRQKeqfsdg 456
|
570
....*....|..
gi 489497627 519 -GYFPVPGLKHL 529
Cdd:PRK09431 457 vGYSWIDTLKEV 468
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
244-586 |
1.65e-80 |
|
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: 254.46 E-value: 1.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 244 RVLDSTREAVAIRQRAAVDVGVLLSGGVDSSMLVGLLREVGVEDLSTFSIGFQdagGERGDEFQYSDLIAKHYGTRHHQL 323
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSPSPLHTFSIGFE---GRGYDEAPYAREVAEHLGTDHHEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 324 RIQEREIIEQLPAAFRAMSEPMVSHDCIAFYLLSREV-SKHCKVVQSGQGADELFAGYHWYPQVDgasdpvaayrdafvd 402
Cdd:pfam00733 78 VVTPEDLLDALPDVIWHLDEPFADPSAIPLYLLSRLArRKGVKVVLSGEGADELFGGYPFYKGED--------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 403 rsyaeyaetvqpkwrtandaagdfvrdhfaqpgasaAVDKALRLDSTVMLVDDPVkRVDNMTMAWGLEARTPFLDYRLVE 482
Cdd:pfam00733 143 ------------------------------------PLRRMLYLDLKTLLPGDLL-RADRMSMAHGLEVRVPFLDHRLVE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 483 LSARIPGKFKLPDG-GKQVLKEAARMVIPSEVIDRKKGYFPVP-GLKHLQGDTLNWVRELLTDS-SQDRGLFNPAMVDKL 559
Cdd:pfam00733 186 YALRLPPELKLRGGiEKYILREALEGILPDEILERPKEGFSAPvGDWKLRGPLRELAEDLLSDSrLAKEGLLDREAVREL 265
|
330 340
....*....|....*....|....*..
gi 489497627 560 LTNPEGqltplrgsklwqlAALNLWLS 586
Cdd:pfam00733 266 LDEHLA-------------GMLELWLR 279
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
47-166 |
1.17e-58 |
|
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: 191.58 E-value: 1.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 47 HRRLKIMDlSDGSAQPMIDSNLG-LSLAFNGAIYNFPELRAELESLGYQFHSGGDTEVLLKGYHA-WGADMLPKLNGMFA 124
Cdd:pfam13537 1 HRRLSIID-LEGGAQPMVSSEDGrYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAeWGEDCVDRLNGMFA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 489497627 125 FAIWERDSKQLFIARDRLGVKPLYLSKTD-KRLRFASSLPALL 166
Cdd:pfam13537 80 FAIWDRRRQRLFLARDRFGIKPLYYGRDDgGRLLFASELKALL 122
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
259-524 |
2.05e-56 |
|
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: 189.41 E-value: 2.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 259 AAVDVGVLLSGGVDSSMLVGLL-REVGVEDLSTFSIGFqdaGGERGDEFQYSDLIAKHYGTRHHQLRIQEREIIEQLPAA 337
Cdd:cd01991 1 SDVPVGVLLSGGLDSSLIAALAaRLLPETPIDLFTVGF---EGSPTPDRAAARRVAEELGTEHHEVEVTIEELLDALPDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 338 FRAM--SEPMVSHDCIAFYLLSREVSKH-CKVVQSGQGADELFAGYHWypqvdgasdpvaaYRDAFVDRSYAEYAETVQp 414
Cdd:cd01991 78 ILIYptDTPMDLSIAIPLYFASRLAGKLgAKVVLSGEGADELFGGYSR-------------HRDAPLRGWEALEEELLR- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 415 KWRtandaagdfvrdhfaqpgasaavdkalRLDSTvmlvddPVKRVDNMTMAWGLEARTPFLDYRLVELSARIPGKFKL- 493
Cdd:cd01991 144 DLD---------------------------RLWTR------NLGRDDRVAMAHGLEARVPFLDEELVEFALSLPPSLKId 190
|
250 260 270
....*....|....*....|....*....|...
gi 489497627 494 --PDGGKQVLKEAARMVIPSEVIDRKKGYFPVP 524
Cdd:cd01991 191 prGGGEKYILREAARDLLPDEIAWRPKRAIQFG 223
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-527 |
8.93e-54 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 192.67 E-value: 8.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 1 MCGLAGELRF-DHQPADLAAVERITHELAPRGPDAWGFHSQGPVALGHRRLKIMDLSDGSaQPMIDSNLGLSLAFNGAIY 79
Cdd:PLN02549 1 MCGILAVLGCsDDSQAKRSRVLELSRRLRHRGPDWSGLYGNEDCYLAHERLAIMDPESGD-QPLYNEDKTIVVTANGEIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 80 NFPELRAELESlgYQFHSGGDTEVLLKGYHAWGADMLPKLNGMFAFAIWERDSKQLFIARDRLGVKPLYLS-KTDKRLRF 158
Cdd:PLN02549 80 NHKELREKLKL--HKFRTGSDCEVIAHLYEEHGEEFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYIGwGLDGSVWF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 159 ASSLPALLkgGDISgmldpvalnHYLNFhavvpaprtllagveklpPASWMRIDASGKVEQkvW----WTLPYGPHEDEK 234
Cdd:PLN02549 158 ASEMKALC--DDCE---------RFEEF------------------PPGHYYSSKAGGFRR--WynppWFSESIPSTPYD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 235 NLTLedwrdrvldstREAV--AIRQRAAVDV--GVLLSGGVDSSMLVGL----LREVGV-----EDLSTFSIGFQDAgge 301
Cdd:PLN02549 207 PLVL-----------REAFekAVIKRLMTDVpfGVLLSGGLDSSLVASIaarhLAETKAarqwgQQLHSFCVGLEGS--- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 302 rgdefqySDLIA-----KHYGTRHHQLR--IQE-----REIIEQL----PAAFRAmSEPMvshdciafYLLSREV-SKHC 364
Cdd:PLN02549 273 -------PDLKAarevaDYLGTVHHEFHftVQEgidaiEDVIYHLetydVTTIRA-STPM--------FLMSRKIkSLGV 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 365 KVVQSGQGADELFAGYHWYpqvdgasdpvaayrdafvdrsyaeyaetvqpkwrtandaagdfvrdHFAqPGASAAVDKAL 444
Cdd:PLN02549 337 KMVLSGEGSDEIFGGYLYF----------------------------------------------HKA-PNKEEFHKETC 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 445 RLDSTVMLVDdpVKRVDNMTMAWGLEARTPFLDYRLVELSARIPGKFKLPDGG-----KQVLKEA----ARMVIPSEVID 515
Cdd:PLN02549 370 RKIKALHQYD--CLRANKSTSAWGLEARVPFLDKEFIDVAMSIDPEWKMIRPGegrieKWVLRKAfddeEDPYLPKHILW 447
|
570
....*....|....*....
gi 489497627 516 RKK-------GYFPVPGLK 527
Cdd:PLN02549 448 RQKeqfsdgvGYSWIDGLK 466
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-521 |
6.50e-53 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 190.31 E-value: 6.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 1 MCGLAGELRFDHQ-----PADLAAVERITHelapRGPDAWGFHSQ--GP---VALGHRRLKIMDLSDGsAQPMIDSNLGL 70
Cdd:PTZ00077 1 MCGILAIFNSKGErhelrRKALELSKRLRH----RGPDWSGIIVLenSPgtyNILAHERLAIVDLSDG-KQPLLDDDETV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 71 SLAFNGAIYNFPELRAELESLGYQFHSGGDTEVLLKGYHAWGA-DMLPKLNGMFAFAIWERDSKQLFIARDRLGVKPLYL 149
Cdd:PTZ00077 76 ALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKEYGPkDFWNHLDGMFATVIYDMKTNTFFAARDHIGIIPLYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 150 S-KTDKRLRFASSLPALlkgGDISGMLDPVALNHYLNFHAvvpaprtllagvEKLPPASWMridasgkveQKVWWTLPYG 228
Cdd:PTZ00077 156 GyAKDGSIWFSSELKAL---HDQCVEVKQFPPGHYYDQTK------------EKGEFVRYY---------NPNWHDFDHP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 229 PHEDEKNltLEDWRDRVLDSTREavaiRQRAAVDVGVLLSGGVDSSMLVGL---LREVGVEDLS--------TFSIGFQD 297
Cdd:PTZ00077 212 IPTGEID--LEEIREALEAAVRK----RLMGDVPFGLFLSGGLDSSIVAAIvakLIKNGEIDLSkrgmpklhSFCIGLEG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 298 AggergDEFQYSDLIAKHYGTRHHQLRIQEREIIEQLP-----------AAFRAmSEPMvshdciafYLLSREVSKHC-K 365
Cdd:PTZ00077 286 S-----PDLKAARKVAEYLGTEHHEFTFTVEEGIDALPdviyhtetydvTTIRA-STPM--------YLLSRRIKALGiK 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 366 VVQSGQGADELFAGYHWYPQvdgasdpvAAYRDAFvdrsyaeYAETVqpkwRTANDAagdfvrdHFAQpgasaavdkalr 445
Cdd:PTZ00077 352 MVLSGEGSDELFGGYLYFHK--------APNREEF-------HRELV----RKLHDL-------HKYD------------ 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 446 ldstvmlvddpVKRVDNMTMAWGLEARTPFLDYRLVELSARIPGKFKLPDGG-----KQVLKEA----ARMVIPSEVIDR 516
Cdd:PTZ00077 394 -----------CLRANKATMAWGIEARVPFLDKDFLEYVMNIDPKYKMCNAFegqmeKYILRKAfeglEKPYLPDEILWR 462
|
....*
gi 489497627 517 KKGYF 521
Cdd:PTZ00077 463 QKEQF 467
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
32-160 |
4.22e-49 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.
Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 166.71 E-value: 4.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 32 PDAWGFHSQGPVALGHRRLKIMDLSDGSAQPMIDSNLGLSLAFNGAIYNFPELRAELESLGYQFHSGGDTEVLLKGYHAW 111
Cdd:pfam13522 1 PDFSGIWVEGGVALGHVRLAIVDLPDAGNQPMLSRDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYEEW 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 489497627 112 GADMLPKLNGMFAFAIWERDSKQLFIARDRLGVKPLYLSKTDKRLRFAS 160
Cdd:pfam13522 81 GEDCLERLRGMFAFAIWDRRRRTLFLARDRLGIKPLYYGILGGGFVFAS 129
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-169 |
4.06e-45 |
|
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: 159.15 E-value: 4.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 2 CGLAGELRFDHQPADLA-AVERITHELAPRGPDAWGFHSQGP---------------------------VALGHRRLKIM 53
Cdd:cd00352 1 CGIFGIVGADGAASLLLlLLLRGLAALEHRGPDGAGIAVYDGdglfvekragpvsdvaldlldeplksgVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 54 DL-SDGSAQPMIDSNLGLSLAFNGAIYNFPELRAELESLGYQFHSGGDTEVLLKGYHAWGA---------DMLPKLNGMF 123
Cdd:cd00352 81 GLpSEANAQPFRSEDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGRegglfeaveDALKRLDGPF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489497627 124 AFAIWERDSKQLFIARDRLGVKPLYLSKT-DKRLRFASSLPALLKGG 169
Cdd:cd00352 161 AFALWDGKPDRLFAARDRFGIRPLYYGITkDGGLVFASEPKALLALP 207
|
|
| lass_lactam_cya |
NF033535 |
lasso peptide isopeptide bond-forming cyclase; Members of this family are the isopeptide ... |
1-321 |
1.51e-38 |
|
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: 150.91 E-value: 1.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 1 MCGLAGELRFDHQPADLAAVERITHELAPRGPDAWGFHSQGPVALGHRRLKIMDLSDGSAQPMIDSNLGLSLAFNGAIYN 80
Cdd:NF033535 1 MSGIVGIYYLDGRPVDREDLQQMVDILAHRGPDGADIWCEGSVGLGHRMLWTTPESLLEKLPLVNQTGDLVITADARIDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 81 FPELRAELESLGYQFHSGGDTEVLLKGYHAWGADMLPKLNGMFAFAIWERDSKQLFIARDRLGVKPLYLSKTDKRLRFAS 160
Cdd:NF033535 81 RDELISALQLNNCPPEKITDSQLILAAYEKWGEQCPEHLLGDFAFAIWDKRKQQLFCARDHFGVKPFYYYQSDKRFAFAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 161 SLPALLKGGDISGMLDPVALNHYLnfhAVVPAPR--TLLAGVEKLPPASWMRIDASGkVEQKVWWTLpygphEDEKNLTL 238
Cdd:NF033535 161 EIKALLCLPEVPRRLNEVRIADYL---ALMLEDKviTFYQDIFRLPPAHSMTVSQSG-LQIRSYWSL-----DPSRELRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 239 ---EDWRDRVLDSTREAVAIRQRAAVDVGVLLSGGVDSS----MLVGLLREVGVEDLSTFSIGFqDAGGErGDEFQYSDL 311
Cdd:NF033535 232 dsdEEYAEAFREIFTEAVRCRLRSAFPVGSHLSGGLDSSsitcVARQLLAEEKKAPLHTFSNIF-DKVTE-CDERPFINA 309
|
330
....*....|
gi 489497627 312 IAKHYGTRHH 321
Cdd:NF033535 310 VLEQGGLIPH 319
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-160 |
1.05e-12 |
|
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: 70.44 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 1 MCGLAGelRFDHQPadlaaVERIT----HELAPRGPDAWG--------FHS-------------------QGPVALGHRR 49
Cdd:COG0034 7 ECGVFG--IYGHED-----VAQLTyyglYALQHRGQESAGiatsdggrFHLhkgmglvsdvfdeedlerlKGNIAIGHVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 50 LKIMDLSDGS-AQPM-IDSNLG-LSLAFNGAIYNFPELRAELESLGYQFHSGGDTEVLLK------GYHAWG---ADMLP 117
Cdd:COG0034 80 YSTTGSSSLEnAQPFyVNSPFGsIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHliarelTKEDLEeaiKEALR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489497627 118 KLNGMFAFAIweRDSKQLFIARDRLGVKPLYLSKTDKRLRFAS 160
Cdd:COG0034 160 RVKGAYSLVI--LTGDGLIAARDPNGIRPLVLGKLEDGYVVAS 200
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
56-167 |
2.71e-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: 63.23 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 56 SDGSAQPMIDSNLGLSLAFNGAIYNFPELRAELESLGYQFHSGGDTEV---LLKGYHAWGADM-------LPKLNGMFAF 125
Cdd:cd00714 80 TDVNAHPHRSCDGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEViahLIEYYYDGGLDLleavkkaLKRLEGAYAL 159
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 489497627 126 AIWERD-SKQLFIARdrlgvK--PLYLSKTDKRLRFASSLPALLK 167
Cdd:cd00714 160 AVISKDePDEIVAAR-----NgsPLVIGIGDGENFVASDAPALLE 199
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
40-151 |
1.72e-10 |
|
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: 61.71 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 40 QGPVALGHRRLKimdlSDGS-----AQPMI-DSNLG-LSLAFNGAIYNFPELRAELESLGYQFHSGGDTEVLL----KGY 108
Cdd:cd00715 63 PGNIAIGHVRYS----TAGSsslenAQPFVvNSPLGgIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILhliaRSL 138
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 489497627 109 HAWG-----ADMLPKLNGMFAFAIWERDskQLFIARDRLGVKPLYLSK 151
Cdd:cd00715 139 AKDDlfeaiIDALERVKGAYSLVIMTAD--GLIAVRDPHGIRPLVLGK 184
|
|
| Gn_AT_II_novel |
cd03766 |
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its ... |
1-183 |
1.57e-09 |
|
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: 57.30 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 1 MCGLAGEL--RFDHQPADLAaVERITHELAPRGPDawgfhSQGPVALGHRRLKIMDLS-------DGSA-QPMIDSNLGL 70
Cdd:cd03766 1 MCGILCSVspSGPHINSSLL-SEELLPNLRNRGPD-----YLSTRQLSVTNWTLLFTSsvlslrgDHVTrQPLVDQSTGN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 71 SLAFNGAIYNfpelraelesLGYQFHSGGDTEVLLKGYHAWGA------DMLPKLNGMFAFAIWERDSKQLFIARDRLGV 144
Cdd:cd03766 75 VLQWNGELYN----------IDGVEDEENDTEVIFELLANCSSesqdilDVLSSIEGPFAFIYYDASENKLYFGRDCLGR 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 489497627 145 KPLYLSKTDKRLRFASSLPAllKGGDISGMLDPVALNHY 183
Cdd:cd03766 145 RSLLYKLDPNGFELSISSVS--GSSSGSGFQEVLAGGIY 181
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
56-139 |
1.35e-08 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 57.75 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 56 SDGSAQPMIDSNLGLSLAFNGAIYNFPELRAELESLGYQFHSGGDTEV---LLKGYHAWGAD-------MLPKLNGMFAF 125
Cdd:PRK00331 81 TERNAHPHTDCSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEViahLIEEELKEGGDlleavrkALKRLEGAYAL 160
|
90
....*....|....*
gi 489497627 126 A-IWERDSKQLFIAR 139
Cdd:PRK00331 161 AvIDKDEPDTIVAAR 175
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
56-139 |
1.69e-08 |
|
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440218 [Multi-domain] Cd Length: 610 Bit Score: 57.33 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 56 SDGSAQPMIDSNLGLSLAFNGAIYNFPELRAELESLGYQFHSGGDTEV---LLKGYHAWGADM-------LPKLNGMFAF 125
Cdd:COG0449 81 SDENAHPHTSCSGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEViahLIEEYLKGGGDLleavrkaLKRLEGAYAL 160
|
90
....*....|....*
gi 489497627 126 A-IWERDSKQLFIAR 139
Cdd:COG0449 161 AvISADEPDRIVAAR 175
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
40-165 |
9.17e-08 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 54.65 E-value: 9.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 40 QGPVALGHRRLKIMDLSD-GSAQPMI-DSNLG-LSLAFNGAIYNFPELRAELESLGYQFHSGGDTEVLL--------KGY 108
Cdd:PRK05793 79 KGNSAIGHVRYSTTGASDlDNAQPLVaNYKLGsIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILnliarsakKGL 158
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 489497627 109 HAWGADMLPKLNGMFAFAIWERDskQLFIARDRLGVKPLYLSKTDKRLRFASSLPAL 165
Cdd:PRK05793 159 EKALVDAIQAIKGSYALVILTED--KLIGVRDPHGIRPLCLGKLGDDYILSSESCAL 213
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
38-171 |
3.20e-07 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 53.49 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 38 HSQGPVALGHRRLKIM-DLSDGSAQPMIDSNLGLSLAFNGAIYNFPELRAELESLGYQFHSGGDTEV---LLKGYHAWGA 113
Cdd:PTZ00295 92 HKNSTIGIAHTRWATHgGKTDENAHPHCDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVianLIGLELDQGE 171
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489497627 114 DM-------LPKLNGMFAFAIWERDSK-QLFIARDRlgvKPLYLSKTDKRLRFASSLPAL---------LKGGDI 171
Cdd:PTZ00295 172 DFqeavksaISRLQGTWGLCIIHKDNPdSLIVARNG---SPLLVGIGDDSIYVASEPSAFakytneyisLKDGEI 243
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
41-165 |
3.26e-06 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 49.68 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497627 41 GPVALGHRRLKIM-DLSDGSAQPMI-DSNLG-LSLAFNGAIYNFPELRAELESLGYQFHSGGDTEVLL--------KGYH 109
Cdd:PLN02440 65 GDIAIGHVRYSTAgASSLKNVQPFVaNYRFGsIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLhliaiskaRPFF 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 489497627 110 AWGADMLPKLNGmfAFAIWERDSKQLFIARDRLGVKPLYL-SKTDKRLRFASSLPAL 165
Cdd:PLN02440 145 SRIVDACEKLKG--AYSMVFLTEDKLVAVRDPHGFRPLVMgRRSNGAVVFASETCAL 199
|
|
| betaLS_CarA_N |
cd01909 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_betaLS-type. Carbapenam ... |
76-215 |
7.77e-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: 47.10 E-value: 7.77e-06
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gi 489497627 76 GAIYNFPELRAELESLGYQFHSGGDTEVLLKGYHAWGADMLPKLNGMFAFAIWERdSKQLFIARDRLGVKPLYLSKTDKR 155
Cdd:cd01909 58 GELYNRDELRSLLGAGEGRSAVLGDAELLLLLLTRLGLHAFRLAEGDFCFFIEDG-NGRLTLATDHAGSVPVYLVQAGEV 136
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gi 489497627 156 lRFASSLPALLKGGDISGMLDPVAlnhylNFHAVVPaprtlLAGVEKLPPASWMRIDASG 215
Cdd:cd01909 137 -WATTELKLLAAHEGPKAFPFKSA-----GADTVSG-----LTGVQRVPPGTVNVLTFDG 185
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