|
Name |
Accession |
Description |
Interval |
E-value |
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-651 |
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: 737.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 1 MCGIDGFLNsvaFDEETARGTLARMTASLAHRGPDGQGIWVDPeaGIALGHRRLAIVDLSVHGRQPMASACGRYVLVFNG 80
Cdd:COG0367 1 MCGIAGIID---FDGGADREVLERMLDALAHRGPDGSGIWVDG--GVALGHRRLSIIDLSEGGHQPMVSEDGRYVLVFNG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 81 EIYNHRELRAELERAGRApaWRGHSDSEVLIAAIVAWGvEATLRRATGMFAFALWNRASRVLTLARDRIGEKPLYYGRIG 160
Cdd:COG0367 76 EIYNYRELRAELEALGHR--FRTHSDTEVILHAYEEWG-EDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 161 DALVFASELKALRGYPGFDGTVDRDALCLYLRQSSVPAPYTIYRGIRKLPPGTYIQFEHARdTPRLRAYWTLEQaieagR 240
Cdd:COG0367 153 GGLAFASELKALLAHPGVDRELDPEALAEYLTLGYVPAPRTIFKGIRKLPPGHYLTVDAGG-ELEIRRYWDLEF-----V 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 241 AQPFDGTSDEAVGQLDAILRQAVARQMEADVPLGAFLSGGVDSSAIVALMQAQSATPVDTFTIGFHEAGYDEAGYAKAVA 320
Cdd:COG0367 227 PHERSDSEEEAVEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKGPLKTFSIGFEDSAYDESPYARAVA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 321 RHLGTRHTELYVTADHALGVVPKLPSIYDEPFSDASQIPTFLVSELTRRHVKVSLSGDGGDELFGGYTRYFltprlwrkl 400
Cdd:COG0367 307 EHLGTEHHEVTVTPEDLLDALPDLVWHLDEPFADPSAVPTYLLSRLAREHVKVVLSGEGADELFGGYPRYR--------- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 401 hrvpgavrariaAALHALRPDHADQLAAvaqgawgggvearestsrigdrlhklghvmtaesriglyrllmssvhhperi 480
Cdd:COG0367 378 ------------EAALLLSPDFAEALGG---------------------------------------------------- 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 481 alsgqeppTPLDTVSAWPAHLSFAEQAMAIDTLTYLPTDILAKVDRAAMAVSLETRMPFLDHHVVEFAWRVPASVRLPEG 560
Cdd:COG0367 394 --------ELVPRLYAESGAEDPLRRMLYLDLKTYLPGDLLVKVDRMSMAHSLEVRVPFLDHRLVEFALSLPPELKLRGG 465
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 561 QSKALLRRLLDRYVPSALIDRPKQGFCAPVDHWLRGALRDWAEALLRPSRLREEGFFDAAAVERLWRQHQTGRMNWQHQL 640
Cdd:COG0367 466 RGKYLLRKALEGLLPDEVLDRPKQGFPVPLGPWLRGPLREWLEDLLSDESLAARGLFDPDAVRRLLEEHLAGRRDHSRKL 545
|
650
....*....|.
gi 1409814730 641 WTVLMFQAWLE 651
Cdd:COG0367 546 WSLLMLELWLR 556
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-586 |
4.81e-148 |
|
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: 437.54 E-value: 4.81e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 4 IDGFLNSVAfDEETARGTLARMTASLAHRGPDGQGIwVDPEAGIALGHRRLAIVDLSVhGRQPMASACGRYVLVFNGEIY 83
Cdd:TIGR01536 1 IAGFFDLDD-KAVEEDEAIKRMSDTIAHRGPDASGI-EYKDGNAILGHRRLAIIDLSG-GAQPMSNEGKTYVIVFNGEIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 84 NHRELRAELERAGRApaWRGHSDSEVLIAAIVAWGvEATLRRATGMFAFALWNRASRVLTLARDRIGEKPLYYGRIGDAL 163
Cdd:TIGR01536 78 NHEELREELEAKGYT--FQTDSDTEVILHLYEEWG-EECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYDGGQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 164 VFASELKALRGYPGFDGTVDRDALCLYLRQSSVPAPYTIYRGIRKLPPGtyIQFEHARDTPRLRAYWTLEQaieagraQP 243
Cdd:TIGR01536 155 YFASEIKALLAHPNIKPFPDGAALAPGFGFVRVPPPSTFFRGVFELEPG--HDLPLDDDGLNIERYYWERR-------DE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 244 FDGTSDEAVGQLDAILRQAVARQMEADVPLGAFLSGGVDSSAIVALMQAQS-ATPVDTFTIGF-HEAGYDEAGYAKAVAR 321
Cdd:TIGR01536 226 HTDSEEDLVDELRSLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREApRGPVHTFSIGFeGSPDFDESKYARKVAD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 322 HLGTRHTELYVTADHALGVVPKLPSIYDEPFSDASQIPTFLVSELTRRH-VKVSLSGDGGDELFGGYTRYFLTPRLwrkl 400
Cdd:TIGR01536 306 HLGTEHHEVLFSVEEGLDALPEVIYHLEEPTTIRASIPLYLLSKLAREDgVKVVLSGEGADELFGGYLYFHEAPAA---- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 401 hrvpgavrariaaalhalrpdhadqlaavaqGAWGggvearestsrigdrlhklghvmtaesriglyrllmssvhhperi 480
Cdd:TIGR01536 382 -------------------------------EALR--------------------------------------------- 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 481 alsgqepptpldtvsawpahlsfaEQAMAIDTLTYLPTDILAKvDRAAMAVSLETRMPFLDHHVVEFAWRVPASVRLPEG 560
Cdd:TIGR01536 386 ------------------------EELQYLDLELYMPGLLRRK-DRMSMAHSLEVRVPFLDHELVEYALSIPPEMKLRDG 440
|
570 580
....*....|....*....|....*.
gi 1409814730 561 QSKALLRRLLDRYVPSALIDRPKQGF 586
Cdd:TIGR01536 441 KEKYLLREAFEGYLPEEILWRPKEGF 466
|
|
| trio_amidotrans |
TIGR03104 |
asparagine synthase family amidotransferase; Members of this protein family are closely ... |
1-653 |
7.32e-132 |
|
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: 400.23 E-value: 7.32e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 1 MCGIDGFLNsvaFDEETAR-GTLARMTASLAHRGPDGQGIWVdpEAGIALGHRRLAIVDLSVHGRQPMASACGRYVLVFN 79
Cdd:TIGR03104 1 MCGICGEIR---FDGQAPDvAAVVRMLAVLAPRGPDAGGVHA--QGPVALGHRRLKIIDLSEASQQPMVDAELGLALVFN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 80 GEIYNHRELRAELERAGRapAWRGHSDSEVLIAAIVAWGVEAtLRRATGMFAFALWNRASRVLTLARDRIGEKPLYYGRI 159
Cdd:TIGR03104 76 GCIYNYRELRAELEALGY--RFFSDGDTEVILKAYHAWGRDC-VSRFNGMFAFAIWERDSGRLLLARDRLGIKPLYYAED 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 160 GDALVFASELKALRGYPGFDGTVDRDALCLYLR-QSSVPAPYTIYRGIRKLPPGTYIQFEhARDTPRLRAYWTLEQAIEA 238
Cdd:TIGR03104 153 AGRLRFASSLPALLAAGGVDTDIDPVALHHYLTfHAVVPAPHTILKGVRKLPPATWMTVE-PDGSRTQRSYWSLDAGRPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 239 GRAqpfDGTSDEAVGQLDAILRQAVARQMEADVPLGAFLSGGVDSSAIVALMQAQSATPVDTFTIGFHEAGY---DEAGY 315
Cdd:TIGR03104 232 DDA---ARTEADWQDAILEALRLAVKRRLVADVPVGVLLSGGLDSSLIVGLLAEAGVDGLRTFSIGFEDVGGekgDEFEY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 316 AKAVARHLGTRHTELYVTADHALGVVPKLPSIYDEPFSDASQIPTFLVSELTRRHVKVSLSGDGGDELFGGYTRYfltPR 395
Cdd:TIGR03104 309 SDIIAERFHTRHHKIRIPNHRVLPALPEAVAAMSEPMVSHDCVAFYLLSEEVSKHVKVVQSGQGADEVFGGYHWY---PP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 396 LwrklhrVPGAVRARIAAALHALRPDHADQLAAVAQgAWGGGVEARESTSrigdrlhklghvmtaesriglyrllmssvh 475
Cdd:TIGR03104 386 L------AAGAGDPVAAYRRAFFDRDHAEYLEMVGP-RFHAEDVSGEFVA------------------------------ 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 476 hpERIALSGQEppTPLDtvsawpahlsfaeQAMAIDTLTYLPTDILAKVDRAAMAVSLETRMPFLDHHVVEFAWRVPASV 555
Cdd:TIGR03104 429 --DHFARPGAD--TAVD-------------QALRLDTTVMLVDDPVKRVDNMTMAWGLEARVPFLDHELVELAARIPPEL 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 556 RLPEGqSKALLRRLLDRYVPSALIDRPKQGFCAPVDHWLRGALRDWAEALLRPSRLREEGFFDAAAVERLW---RQHQTG 632
Cdd:TIGR03104 492 KLADG-GKGVLKEAARGVIPSEVIDRPKGYFPVPALKYLRGPFLEWVRDALTSPAARERGLFQRAYVDRLLadpDGHLTP 570
|
650 660
....*....|....*....|.
gi 1409814730 633 RMNwqHQLWTVLMFQAWLEAQ 653
Cdd:TIGR03104 571 LRG--SKLWQLALLELWLQRH 589
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-231 |
2.37e-103 |
|
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: 313.34 E-value: 2.37e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 2 CGIDGFLNSVafDEETARGTLARMTASLAHRGPDGQGIWVDPeaGIALGHRRLAIVDLSvHGRQPMASACGRYVLVFNGE 81
Cdd:cd00712 1 CGIAGIIGLD--GASVDRATLERMLDALAHRGPDGSGIWIDE--GVALGHRRLSIIDLS-GGAQPMVSEDGRLVLVFNGE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 82 IYNHRELRAELERAGRApaWRGHSDSEVLIAAIVAWGvEATLRRATGMFAFALWNRASRVLTLARDRIGEKPLYYGRIGD 161
Cdd:cd00712 76 IYNYRELRAELEALGHR--FRTHSDTEVILHLYEEWG-EDCLERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGRDGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 162 ALVFASELKALRGYPGFDGTVDRDALCLYLRQSSVPAPYTIYRGIRKLPPGTYIQFEhaRDTPRLRAYWT 231
Cdd:cd00712 153 GLAFASELKALLALPGVPRELDEAALAEYLAFQYVPAPRTIFKGIRKLPPGHYLTVD--PGGVEIRRYWD 220
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
254-651 |
2.09e-102 |
|
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: 313.01 E-value: 2.09e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 254 QLDAILRQAVARQMEADVPLGAFLSGGVDSSAIVALMQAQSATPVDTFTIGFHEAGYDEAGYAKAVARHLGTRHTELYVT 333
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSPSPLHTFSIGFEGRGYDEAPYAREVAEHLGTDHHELVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 334 ADHALGVVPKLPSIYDEPFSDASQIPTFLVSELTRR-HVKVSLSGDGGDELFGGYTRYfltpRLWRKLHRvpgavraria 412
Cdd:pfam00733 81 PEDLLDALPDVIWHLDEPFADPSAIPLYLLSRLARRkGVKVVLSGEGADELFGGYPFY----KGEDPLRR---------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 413 aalhalrpdhadqlaavaqgawgggvearestsrigdrlhklghvmtaesriglyrllmssvhhperialsgqepptpld 492
Cdd:pfam00733 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 493 tvsawpahlsfaeqAMAIDTLTYLPTDILAkVDRAAMAVSLETRMPFLDHHVVEFAWRVPASVRLPEGQSKALLRRLLDR 572
Cdd:pfam00733 147 --------------MLYLDLKTLLPGDLLR-ADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKLRGGIEKYILREALEG 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 573 YVPSALIDRPKQGFCAPVDHW-LRGALRDWAEALLRPSRLREEGFFDAAAVERLWRQHQTGrmnwqhqlwtvlMFQAWLE 651
Cdd:pfam00733 212 ILPDEILERPKEGFSAPVGDWkLRGPLRELAEDLLSDSRLAKEGLLDREAVRELLDEHLAG------------MLELWLR 279
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-604 |
3.67e-83 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 272.17 E-value: 3.67e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 1 MCGIDGFLNSvAFDEETARGTLARMTASLAHRGPDGQGIWVDpEAGIaLGHRRLAIVDLSvHGRQPMASACGRYVLVFNG 80
Cdd:PRK09431 1 MCGIFGILDI-KTDADELRKKALEMSRLMRHRGPDWSGIYAS-DNAI-LGHERLSIVDVN-GGAQPLYNEDGTHVLAVNG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 81 EIYNHRELRAELEragRAPAWRGHSDSEVLIAAIVAWGVEAtLRRATGMFAFALWNRASRVLTLARDRIGEKPLYYGRIG 160
Cdd:PRK09431 77 EIYNHQELRAELG---DKYAFQTGSDCEVILALYQEKGPDF-LDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 161 D-ALVFASELKALRGypgfdgtvdrdaLClylrqssvpapytiyRGIRKLPPGTYIqfeHARDtPRLRAYWTLEQaieag 239
Cdd:PRK09431 153 HgNLYFASEMKALVP------------VC---------------KTIKEFPPGHYY---WSKD-GEFVRYYQRDW----- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 240 raQPFDGTSDE--AVGQLDAILRQAVARQMEADVPLGAFLSGGVDSSAIVALMQAQSATPVD-------------TFTIG 304
Cdd:PRK09431 197 --FDYDAVKDNvtDKNELRDALEAAVKKRLMSDVPYGVLLSGGLDSSLISAIAKKYAARRIEdderseawwpqlhSFAVG 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 305 FHEAgyDEAGYAKAVARHLGTRHTELYVTADHALGVVPKLpsI-----YDEPFSDASqIPTFLVSELTR-RHVKVSLSGD 378
Cdd:PRK09431 275 LEGS--PDLKAAREVADHLGTVHHEIHFTVQEGLDALRDV--IyhletYDVTTIRAS-TPMYLMARKIKaMGIKMVLSGE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 379 GGDELFGGYTrYFltprlwrklHRVPGavrariAAALHalrpdhadqlaavaqgawgggvearESTSRIGDRLHklghvm 458
Cdd:PRK09431 350 GADELFGGYL-YF---------HKAPN------AKEFH-------------------------EETVRKLRALH------ 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 459 taesrigLYRLLmssvhhperialsgqepptpldtvsawpahlsfaeqamaidtltylptdilaKVDRAAMAVSLETRMP 538
Cdd:PRK09431 383 -------MYDCL----------------------------------------------------RANKAMMAWGVEARVP 403
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1409814730 539 FLDHHVVEFAWRVPASVRL--PEGQSKALLRRLLDRYVPSALIDRPKQGFCAPVDHWLRGALRDWAEA 604
Cdd:PRK09431 404 FLDKEFLDVAMRINPEDKMcgNGKMEKHILREAFEGYLPESILWRQKEQFSDGVGYSWIDTLKEVAAE 471
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-606 |
1.07e-62 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 218.43 E-value: 1.07e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 1 MCGIDGFLNSVAfDEETARGTLARMTASLAHRGPDGQGIWV---DPEAGIALGHRRLAIVDLSvHGRQPMASACGRYVLV 77
Cdd:PTZ00077 1 MCGILAIFNSKG-ERHELRRKALELSKRLRHRGPDWSGIIVlenSPGTYNILAHERLAIVDLS-DGKQPLLDDDETVALM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 78 FNGEIYNHRELRAELERAGRapAWRGHSDSEVLIAAIVAWGVEATLRRATGMFAFALWNRASRVLTLARDRIGEKPLYYG 157
Cdd:PTZ00077 79 QNGEIYNHWEIRPELEKEGY--KFSSNSDCEIIGHLYKEYGPKDFWNHLDGMFATVIYDMKTNTFFAARDHIGIIPLYIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 158 RIGD-ALVFASELKALrgypgfdgtvdrDALCLYLRQssvpapytiyrgirkLPPGTYIQFEHARDTPRlRAY----WTL 232
Cdd:PTZ00077 157 YAKDgSIWFSSELKAL------------HDQCVEVKQ---------------FPPGHYYDQTKEKGEFV-RYYnpnwHDF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 233 EQAIEAGRAQPfdgtsdeavGQLDAILRQAVARQMEADVPLGAFLSGGVDSS---AIVALMqAQSATP---------VDT 300
Cdd:PTZ00077 209 DHPIPTGEIDL---------EEIREALEAAVRKRLMGDVPFGLFLSGGLDSSivaAIVAKL-IKNGEIdlskrgmpkLHS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 301 FTIGFHEAgyDEAGYAKAVARHLGTRHTELYVTADHALGVVPKLpsIYDEPFSDASQI----PTFLVSELTR-RHVKVSL 375
Cdd:PTZ00077 279 FCIGLEGS--PDLKAARKVAEYLGTEHHEFTFTVEEGIDALPDV--IYHTETYDVTTIrastPMYLLSRRIKaLGIKMVL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 376 SGDGGDELFGGYTrYFltprlwrklHRVPGAVrariaaALHalrpdhadqlaavaqgawgggveaRESTSRIGDrLHKlg 455
Cdd:PTZ00077 355 SGEGSDELFGGYL-YF---------HKAPNRE------EFH------------------------RELVRKLHD-LHK-- 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 456 hvmtaesriglYRLLmssvhhperialsgqepptpldtvsawpahlsfaeqamaidtltylptdilaKVDRAAMAVSLET 535
Cdd:PTZ00077 392 -----------YDCL----------------------------------------------------RANKATMAWGIEA 408
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1409814730 536 RMPFLDHHVVEFAWRVPASVRLP---EGQ-SKALLRR----LLDRYVPSALIDRPKQGFCAPVDHWLRGALRDWAEALL 606
Cdd:PTZ00077 409 RVPFLDKDFLEYVMNIDPKYKMCnafEGQmEKYILRKafegLEKPYLPDEILWRQKEQFSDGVGYSWIDGLKEYAEKKI 487
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
51-172 |
4.01e-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: 188.88 E-value: 4.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 51 HRRLAIVDLSvHGRQPM-ASACGRYVLVFNGEIYNHRELRAELERAGRApaWRGHSDSEVLIAAIVAWGVEATLRRATGM 129
Cdd:pfam13537 1 HRRLSIIDLE-GGAQPMvSSEDGRYVIVFNGEIYNYRELRAELEAKGYR--FRTHSDTEVILHLYEAEWGEDCVDRLNGM 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1409814730 130 FAFALWNRASRVLTLARDRIGEKPLYYGRI-GDALVFASELKAL 172
Cdd:pfam13537 78 FAFAIWDRRRQRLFLARDRFGIKPLYYGRDdGGRLLFASELKAL 121
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-441 |
2.42e-55 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 198.06 E-value: 2.42e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 1 MCGIDGFLNSVAfDEETARGTLARMTASLAHRGPDGQGIWVDPEAGIAlgHRRLAIVDLSvHGRQPMASACGRYVLVFNG 80
Cdd:PLN02549 1 MCGILAVLGCSD-DSQAKRSRVLELSRRLRHRGPDWSGLYGNEDCYLA--HERLAIMDPE-SGDQPLYNEDKTIVVTANG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 81 EIYNHRELRAELEragrAPAWRGHSDSEVlIAAIVAWGVEATLRRATGMFAFALWNRASRVLTLARDRIGEKPLYYGRIG 160
Cdd:PLN02549 77 EIYNHKELREKLK----LHKFRTGSDCEV-IAHLYEEHGEEFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 161 DALV-FASELKALrgypgfdgtVDRdalClylrqssvpAPYTIYrgirklPPGTYiqfeHARDTPRLRAYWTLEQAIEAG 239
Cdd:PLN02549 152 DGSVwFASEMKAL---------CDD---C---------ERFEEF------PPGHY----YSSKAGGFRRWYNPPWFSESI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 240 RAQPFDGTsdeavgQLDAILRQAVARQMEADVPLGAFLSGGVDSS---AIVALMQA------QSATPVDTFTIGFHeaGY 310
Cdd:PLN02549 201 PSTPYDPL------VLREAFEKAVIKRLMTDVPFGVLLSGGLDSSlvaSIAARHLAetkaarQWGQQLHSFCVGLE--GS 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 311 DEAGYAKAVARHLGTRHTELYVTADHALGVVPKLpsIY-DEPFsDASQI----PTFLVS-ELTRRHVKVSLSGDGGDELF 384
Cdd:PLN02549 273 PDLKAAREVADYLGTVHHEFHFTVQEGIDAIEDV--IYhLETY-DVTTIrastPMFLMSrKIKSLGVKMVLSGEGSDEIF 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1409814730 385 GGYTrYFltprlwrklHRVPGAVR-----ARIAAALHALRPDHADQlaavAQGAWggGVEAR 441
Cdd:PLN02549 350 GGYL-YF---------HKAPNKEEfhketCRKIKALHQYDCLRANK----STSAW--GLEAR 395
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
34-168 |
1.63e-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: 176.73 E-value: 1.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 34 PDGQGIWVdpEAGIALGHRRLAIVDLSVHGRQPMASACGRYVLVFNGEIYNHRELRAELERAGRapAWRGHSDSEVLIAA 113
Cdd:pfam13522 1 PDFSGIWV--EGGVALGHVRLAIVDLPDAGNQPMLSRDGRLVLVHNGEIYNYGELREELADLGH--AFRSRSDTEVLLAL 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1409814730 114 IVAWGvEATLRRATGMFAFALWNRASRVLTLARDRIGEKPLYYGRIGDALVFASE 168
Cdd:pfam13522 77 YEEWG-EDCLERLRGMFAFAIWDRRRRTLFLARDRLGIKPLYYGILGGGFVFASE 130
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
269-590 |
4.72e-52 |
|
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or synthetase) B is always associated with an N-terminal amidotransferase domain. Family members that contain this domain catalyze the conversion of aspartate to asparagine. Asparagine synthase B catalyzes the synthesis of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase.
Pssm-ID: 467495 [Multi-domain] Cd Length: 224 Bit Score: 179.01 E-value: 4.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 269 ADVPLGAFLSGGVDSSAIVALM-QAQSATPVDTFTIGFHEAGYDEAGYAKAVARHLGTRHTELYVTADHALGVVPKLPSI 347
Cdd:cd01991 1 SDVPVGVLLSGGLDSSLIAALAaRLLPETPIDLFTVGFEGSPTPDRAAARRVAEELGTEHHEVEVTIEELLDALPDVILI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 348 Y--DEPFSDASQIPTFLVSELTRRHV-KVSLSGDGGDELFGGYTRYFLTPRLWRKLHrvpgavrariaaalhalrpdhad 424
Cdd:cd01991 81 YptDTPMDLSIAIPLYFASRLAGKLGaKVVLSGEGADELFGGYSRHRDAPLRGWEAL----------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 425 qlaavaqgawgggveARESTSRIgDRLHKLGhvmtaesriglyrllmssvhhperialsgqepptpldtvsawpahlsfa 504
Cdd:cd01991 138 ---------------EEELLRDL-DRLWTRN------------------------------------------------- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 505 eqamaidtltylptdiLAKVDRAAMAVSLETRMPFLDHHVVEFAWRVPAS--VRLPEGQSKALLRRLLDRYVPSALIDRP 582
Cdd:cd01991 153 ----------------LGRDDRVAMAHGLEARVPFLDEELVEFALSLPPSlkIDPRGGGEKYILREAARDLLPDEIAWRP 216
|
....*...
gi 1409814730 583 KQGFCAPV 590
Cdd:cd01991 217 KRAIQFGS 224
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-215 |
5.70e-51 |
|
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: 176.10 E-value: 5.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 2 CGIDGFLNSVAFDEETARgTLARMTASLAHRGPDGQGIWVD-------------------------PEAGIALGHRRLAI 56
Cdd:cd00352 1 CGIFGIVGADGAASLLLL-LLLRGLAALEHRGPDGAGIAVYdgdglfvekragpvsdvaldlldepLKSGVALGHVRLAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 57 VDL-SVHGRQPMASACGRYVLVFNGEIYNHRELRAELERAGRAPawRGHSDSEVLIAAIVAWG--------VEATLRRAT 127
Cdd:cd00352 80 NGLpSEANAQPFRSEDGRIALVHNGEIYNYRELREELEARGYRF--EGESDSEVILHLLERLGregglfeaVEDALKRLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 128 GMFAFALWNRASRVLTLARDRIGEKPLYYG-RIGDALVFASELKALRGYPgfdgtvdrdalclylrqssvpapytiYRGI 206
Cdd:cd00352 158 GPFAFALWDGKPDRLFAARDRFGIRPLYYGiTKDGGLVFASEPKALLALP--------------------------FKGV 211
|
....*....
gi 1409814730 207 RKLPPGTYI 215
Cdd:cd00352 212 RRLPPGELL 220
|
|
| Gn_AT_II_novel |
cd03766 |
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its ... |
1-167 |
2.10e-12 |
|
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its function has not yet been determined. The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.
Pssm-ID: 239735 [Multi-domain] Cd Length: 181 Bit Score: 66.16 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 1 MCGIdGFLNSVAFDEETARGTLARMTASLAHRGPD--GQGIWVDPEAGIALGHRRLAIVDLSVHgRQPMASACGRYVLVF 78
Cdd:cd03766 1 MCGI-LCSVSPSGPHINSSLLSEELLPNLRNRGPDylSTRQLSVTNWTLLFTSSVLSLRGDHVT-RQPLVDQSTGNVLQW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 79 NGEIYNHRELRAEleragrapawrgHSDSEVLIAAIVAW-----GVEATLRRATGMFAFALWNRASRVLTLARDRIGEKP 153
Cdd:cd03766 79 NGELYNIDGVEDE------------ENDTEVIFELLANCssesqDILDVLSSIEGPFAFIYYDASENKLYFGRDCLGRRS 146
|
170
....*....|....*.
gi 1409814730 154 LYYGRI--GDALVFAS 167
Cdd:cd03766 147 LLYKLDpnGFELSISS 162
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
65-168 |
3.66e-10 |
|
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; Glutamine phosphoribosylpyrophosphate amidotransferase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439804 [Multi-domain] Cd Length: 464 Bit Score: 62.73 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 65 QPM--ASACGRYVLVFNGEIYNHRELRAELERAGRAPawRGHSDSEVLIAAI--------VAWGVEATLRRATGMFAFAL 134
Cdd:COG0034 92 QPFyvNSPFGSIALAHNGNLTNAEELREELEEEGAIF--QTTSDTEVILHLIareltkedLEEAIKEALRRVKGAYSLVI 169
|
90 100 110
....*....|....*....|....*....|....
gi 1409814730 135 WNRasRVLTLARDRIGEKPLYYGRIGDALVFASE 168
Cdd:COG0034 170 LTG--DGLIAARDPNGIRPLVLGKLEDGYVVASE 201
|
|
| betaLS_CarA_N |
cd01909 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_betaLS-type. Carbapenam ... |
63-219 |
1.71e-07 |
|
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: 52.11 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 63 GRQPMASACG-RYVLVFNGEIYNHRELRaeleraGRAPAWRGHS----DSEVLIAAIVAWGVEAtLRRATGMFAFALWNR 137
Cdd:cd01909 40 GSVDVQVARSeTGTAYLIGELYNRDELR------SLLGAGEGRSavlgDAELLLLLLTRLGLHA-FRLAEGDFCFFIEDG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 138 ASRvLTLARDRIGEKPLYYgRIGDALVFASELKALRGYPGFDGtvdrdalclYLRQSSVPAPYTIYRGIRKLPPGTYIQF 217
Cdd:cd01909 113 NGR-LTLATDHAGSVPVYL-VQAGEVWATTELKLLAAHEGPKA---------FPFKSAGADTVSGLTGVQRVPPGTVNVL 181
|
..
gi 1409814730 218 EH 219
Cdd:cd01909 182 TF 183
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
65-168 |
2.24e-07 |
|
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: 52.46 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 65 QPMA--SACGRYVLVFNGEIYNHRELRAELERAGRapAWRGHSDSEVLIAAI--------VAWGVEATLRRATGMFAFAL 134
Cdd:cd00715 85 QPFVvnSPLGGIALAHNGNLVNAKELREELEEEGR--IFQTTSDSEVILHLIarslakddLFEAIIDALERVKGAYSLVI 162
|
90 100 110
....*....|....*....|....*....|....*
gi 1409814730 135 WNRAsrVLTLARDRIGEKPLYYGRIG-DALVFASE 168
Cdd:cd00715 163 MTAD--GLIAVRDPHGIRPLVLGKLEgDGYVVASE 195
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
43-175 |
1.21e-06 |
|
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: 49.75 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 43 PEAGIALGHRRLAivdlsVHGR------QPMASACGRYVLVFNGEIYNHRELRAELERagrapawRGHS-----DSEV-- 109
Cdd:cd00714 62 LSGHVGIGHTRWA-----THGEptdvnaHPHRSCDGEIAVVHNGIIENYAELKEELEA-------KGYKfesetDTEVia 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1409814730 110 -LIAAIVAWG------VEATLRRATGMFAFA-LWNRASRVLTLARDrigEKPLYYGrIGD-ALVFASELKALRGY 175
Cdd:cd00714 130 hLIEYYYDGGldlleaVKKALKRLEGAYALAvISKDEPDEIVAARN---GSPLVIG-IGDgENFVASDAPALLEH 200
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-173 |
3.25e-06 |
|
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: 48.80 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 2 CGIDGFLNSvafDEETARG-TLARMTASLAHRGPD---GQGIWVDPEAGI-----------ALGH-----RRLAIVDLS- 60
Cdd:cd01907 1 CGIFGIMSK---DGEPFVGaLLVEMLDAMQERGPGdgaGFALYGDPDAFVyssgkdmevfkGVGYpediaRRYDLEEYKg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 61 ----VHGRQPMASACGRY----------VLVFNGEIYNHRELRAELERAGRAPawRGHSDSEVlIAAIVAW--------- 117
Cdd:cd01907 78 yhwiAHTRQPTNSAVWWYgahpfsigdiAVVHNGEISNYGSNREYLERFGYKF--ETETDTEV-IAYYLDLllrkgglpl 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1409814730 118 ------------------GVEATLRRA--TGMFAFALWNRASRVltLARDRIGEKPLYYGRIGDALVFASELKALR 173
Cdd:cd01907 155 eyykhiirmpeeerelllALRLTYRLAdlDGPFTIIVGTPDGFI--VIRDRIKLRPAVVAETDDYVAIASEECAIR 228
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
42-134 |
4.01e-06 |
|
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440218 [Multi-domain] Cd Length: 610 Bit Score: 50.01 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 42 DPEAGIALGHRRLAivdlsVHGR------QPMASACGRYVLVFNGEIYNHRELRAELERagrapawRGHS-----DSEV- 109
Cdd:COG0449 62 PLSGTIGIGHTRWA-----THGApsdenaHPHTSCSGRIAVVHNGIIENYAELREELEA-------KGHTfksetDTEVi 129
|
90 100 110
....*....|....*....|....*....|...
gi 1409814730 110 --LIAAIVAWG------VEATLRRATGMFAFAL 134
Cdd:COG0449 130 ahLIEEYLKGGgdlleaVRKALKRLEGAYALAV 162
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
44-134 |
7.53e-05 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 45.80 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 44 EAGIALGHRRLAivdlsVHGR------QPMASACGRYVLVFNGEIYNHRELRAELERagrapawRGHS-----DSEV--- 109
Cdd:PRK00331 64 PGTTGIGHTRWA-----THGKpternaHPHTDCSGRIAVVHNGIIENYAELKEELLA-------KGHVfksetDTEViah 131
|
90 100 110
....*....|....*....|....*....|.
gi 1409814730 110 LIAAIVAWG------VEATLRRATGMFAFAL 134
Cdd:PRK00331 132 LIEEELKEGgdlleaVRKALKRLEGAYALAV 162
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
47-175 |
1.13e-04 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 45.40 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 47 IALGHRRLAIV----DLSVHGRQPMAsacGRYVLVFNGEIYNHRELRAELERAGraPAWRGHSDSEVlIAAIVAW----- 117
Cdd:PTZ00295 97 IGIAHTRWATHggktDENAHPHCDYK---KRIALVHNGTIENYVELKSELIAKG--IKFRSETDSEV-IANLIGLeldqg 170
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1409814730 118 -----GVEATLRRATGMFAFALWNRAS-RVLTLARDrigEKPLYYGRIGDALVFASELKALRGY 175
Cdd:PTZ00295 171 edfqeAVKSAISRLQGTWGLCIIHKDNpDSLIVARN---GSPLLVGIGDDSIYVASEPSAFAKY 231
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
28-172 |
1.25e-03 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 41.94 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 28 SLAHRGPDGQGIWV-------------------DPE------AGIALGHRRLAIVDLS-VHGRQPMAS--ACGRYVLVFN 79
Cdd:PRK05793 38 ALQHRGQESAGIAVsdgekikvhkgmglvsevfSKEklkglkGNSAIGHVRYSTTGASdLDNAQPLVAnyKLGSIAIAHN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409814730 80 GEIYNHRELRAELERAGRApaWRGHSDSEV---LIAAIVAWGVEATLRRAtgMFA----FALWNRASRVLTLARDRIGEK 152
Cdd:PRK05793 118 GNLVNADVIRELLEDGGRI--FQTSIDSEVilnLIARSAKKGLEKALVDA--IQAikgsYALVILTEDKLIGVRDPHGIR 193
|
170 180
....*....|....*....|
gi 1409814730 153 PLYYGRIGDALVFASELKAL 172
Cdd:PRK05793 194 PLCLGKLGDDYILSSESCAL 213
|
|
| |
