|
Name |
Accession |
Description |
Interval |
E-value |
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-607 |
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: 644.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 1 MCGIAGWVDFQKQlvQEKHIMNNMIDTLSKRGPDDSNVWGEPHVLFGHKRLSVVDI-EGGRQPMacTHQEETYTIIYNGE 79
Cdd:COG0367 1 MCGIAGIIDFDGG--ADREVLERMLDALAHRGPDGSGIWVDGGVALGHRRLSIIDLsEGGHQPM--VSEDGRYVLVFNGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 80 LYNTEELRKELQARGHRFERTSDTEVLLHSYIEWREECVDRLNGIFAFAIWDEKRERLFGARDRLGVKPFFYKEHGSSFL 159
Cdd:COG0367 77 IYNYRELRAELEALGHRFRTHSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDGGGLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 160 FGSELKAILAHPDVKARTDSGGLAEVFGLGPSrTPGCGVFKGIHEVRPAHAFTFSKDG-LSIWRYWNVKSEKHT--DSFD 236
Cdd:COG0367 157 FASELKALLAHPGVDRELDPEALAEYLTLGYV-PAPRTIFKGIRKLPPGHYLTVDAGGeLEIRRYWDLEFVPHErsDSEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 237 ETAAHIRYLFQDAVTRQLVSDVPVCTFLSGGLDssaitaiaaahfeKQGRDPLHTYSIDYEENskffkasafqPNDDGPW 316
Cdd:COG0367 236 EAVEELRELLEDAVRRRLRADVPVGAFLSGGLDssaia----alaaRLSKGPLKTFSIGFEDS----------AYDESPY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 317 IDKMTNAFGTQHHKCVITQDQLVEHLEESVLVRDLPGMADVDSSLLWFCREIKKDFVVSLSGECADEIFGGYPWFHTAAe 396
Cdd:COG0367 302 ARAVAEHLGTEHHEVTVTPEDLLDALPDLVWHLDEPFADPSAVPTYLLSRLAREHVKVVLSGEGADELFGGYPRYREAA- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 397 edgfpwmrsteeriTLLDEKWQKRLNlREYVNARYEETIAETPLldgetgtdkarRQLFYLNMLWFMTN-LLDRKDRMSM 475
Cdd:COG0367 381 --------------LLLSPDFAEALG-GELVPRLYAESGAEDPL-----------RRMLYLDLKTYLPGdLLVKVDRMSM 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 476 GASLEVRVPFADHRLVEYVWNIPWEMKMHGSREKGILRKALEGLLPEDILYRKKSPYPKTHHPKYTQGVTEWLKTILQQK 555
Cdd:COG0367 435 AHSLEVRVPFLDHRLVEFALSLPPELKLRGGRGKYLLRKALEGLLPDEVLDRPKQGFPVPLGPWLRGPLREWLEDLLSDE 514
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 2287790176 556 DSVLHTLLDRKKLEMLLETDGSsfqvpwfGQLMkGPQLIAHLAQIHTWFEAY 607
Cdd:COG0367 515 SLAARGLFDPDAVRRLLEEHLA-------GRRD-HSRKLWSLLMLELWLRRF 558
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-532 |
0e+00 |
|
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 562.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 4 IAGWVDFQKQLVQEKHIMNNMIDTLSKRGPDDSNV-WGEPHVLFGHKRLSVVDIEGGRQPMACThqEETYTIIYNGELYN 82
Cdd:TIGR01536 1 IAGFFDLDDKAVEEDEAIKRMSDTIAHRGPDASGIeYKDGNAILGHRRLAIIDLSGGAQPMSNE--GKTYVIVFNGEIYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 83 TEELRKELQARGHRFERTSDTEVLLHSYIEWREECVDRLNGIFAFAIWDEKRERLFGARDRLGVKPFFYKEHGSSFLFGS 162
Cdd:TIGR01536 79 HEELREELEAKGYTFQTDSDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYDGGQLYFAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 163 ELKAILAHPDVKARTDSGGLAEVFGLGPSRTPGCgVFKGIHEVRPAHAFTFSKDGLSIWRYWNVKSEKHTDSFDETAAHI 242
Cdd:TIGR01536 159 EIKALLAHPNIKPFPDGAALAPGFGFVRVPPPST-FFRGVFELEPGHDLPLDDDGLNIERYYWERRDEHTDSEEDLVDEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 243 RYLFQDAVTRQLVSDVPVCTFLSGGLDSSAITAIAAAHFEkqgRDPLHTYSIDYEENSKFfkasafqpnDDGPWIDKMTN 322
Cdd:TIGR01536 238 RSLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAP---RGPVHTFSIGFEGSPDF---------DESKYARKVAD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 323 AFGTQHHKCVITQDQLVEHLEESVLVRDLPG-MADVDSSLLWFCREIKKDFVVSLSGECADEIFGGYPWFHTAaeedgfP 401
Cdd:TIGR01536 306 HLGTEHHEVLFSVEEGLDALPEVIYHLEEPTtIRASIPLYLLSKLAREDGVKVVLSGEGADELFGGYLYFHEA------P 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 402 WMRsteeritlldekwqkrlnlreyvnaryeetiaetplldgetgtdKARRQLFYLNMLWFMTNLLDRKDRMSMGASLEV 481
Cdd:TIGR01536 380 AAE--------------------------------------------ALREELQYLDLELYMPGLLRRKDRMSMAHSLEV 415
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2287790176 482 RVPFADHRLVEYVWNIPWEMKMHGSREKGILRKALEGLLPEDILYRKKSPY 532
Cdd:TIGR01536 416 RVPFLDHELVEYALSIPPEMKLRDGKEKYLLREAFEGYLPEEILWRPKEGF 466
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-225 |
8.17e-106 |
|
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: 318.35 E-value: 8.17e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 2 CGIAGWVDFQKQLVQEKHImNNMIDTLSKRGPDDSNVWGEPHVLFGHKRLSVVDIEGGRQPMacTHQEETYTIIYNGELY 81
Cdd:cd00712 1 CGIAGIIGLDGASVDRATL-ERMLDALAHRGPDGSGIWIDEGVALGHRRLSIIDLSGGAQPM--VSEDGRLVLVFNGEIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 82 NTEELRKELQARGHRFERTSDTEVLLHSYIEWREECVDRLNGIFAFAIWDEKRERLFGARDRLGVKPFFYKEHGSSFLFG 161
Cdd:cd00712 78 NYRELRAELEALGHRFRTHSDTEVILHLYEEWGEDCLERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGRDGGGLAFA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2287790176 162 SELKAILAHPDVKARTDSGGLAEVFgLGPSRTPGCGVFKGIHEVRPAHAFTFSKDGLSIWRYWN 225
Cdd:cd00712 158 SELKALLALPGVPRELDEAALAEYL-AFQYVPAPRTIFKGIRKLPPGHYLTVDPGGVEIRRYWD 220
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-529 |
3.62e-92 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 294.89 E-value: 3.62e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 1 MCGIAGWVDFQKQLVQEKHIMNNMIDTLSKRGPDDSNVWGEPHVLFGHKRLSVVDIEGGRQPMacTHQEETYTIIYNGEL 80
Cdd:PRK09431 1 MCGIFGILDIKTDADELRKKALEMSRLMRHRGPDWSGIYASDNAILGHERLSIVDVNGGAQPL--YNEDGTHVLAVNGEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 81 YNTEELRKELqARGHRFERTSDTEVLLHSYIEWREECVDRLNGIFAFAIWDEKRERLFGARDRLGVKPFFY--KEHGsSF 158
Cdd:PRK09431 79 YNHQELRAEL-GDKYAFQTGSDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYgyDEHG-NL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 159 LFGSELKAIlahpdvkartdsgglaevfglgpsrTPGCgvfKGIHEVRPAHAFTfSKDGLSIwRYWNVKSEKHTDSFDET 238
Cdd:PRK09431 157 YFASEMKAL-------------------------VPVC---KTIKEFPPGHYYW-SKDGEFV-RYYQRDWFDYDAVKDNV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 239 AA--HIRYLFQDAVTRQLVSDVPVCTFLSGGLDSSAITAIAAAHFEKQGRD---------PLHTYSIDYEEnSKFFKASA 307
Cdd:PRK09431 207 TDknELRDALEAAVKKRLMSDVPYGVLLSGGLDSSLISAIAKKYAARRIEDderseawwpQLHSFAVGLEG-SPDLKAAR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 308 fqpnddgpwidKMTNAFGTQHHKCVITQDQLVEHLEESV---------LVRDLPGMadvdsSLLwfCREIKKDFV-VSLS 377
Cdd:PRK09431 286 -----------EVADHLGTVHHEIHFTVQEGLDALRDVIyhletydvtTIRASTPM-----YLM--ARKIKAMGIkMVLS 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 378 GECADEIFGGYPWFHTAAEEDGFpwmrsteeritlldekwqkrlnlreyvnarYEETiaetplldgetgtdkaRRQLFYL 457
Cdd:PRK09431 348 GEGADELFGGYLYFHKAPNAKEF------------------------------HEET----------------VRKLRAL 381
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2287790176 458 nmlwFMTNLLdRKDRMSMGASLEVRVPFADHRLVEYVWNIPWEMKM--HGSREKGILRKALEGLLPEDILYRKK 529
Cdd:PRK09431 382 ----HMYDCL-RANKAMMAWGVEARVPFLDKEFLDVAMRINPEDKMcgNGKMEKHILREAFEGYLPESILWRQK 450
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
241-573 |
7.50e-86 |
|
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: 269.10 E-value: 7.50e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 241 HIRYLFQDAVTRQLVSDVPVCTFLSGGLDSSAITAIAAahfeKQGRDPLHTYSIDYEEnskffkasafQPNDDGPWIDKM 320
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAA----RQSPSPLHTFSIGFEG----------RGYDEAPYAREV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 321 TNAFGTQHHKCVITQDQLVEHLEESVLVRDLPGMADVDSSLLWFCREIKKDFV-VSLSGECADEIFGGYPWFHtaaeedg 399
Cdd:pfam00733 67 AEHLGTDHHELVVTPEDLLDALPDVIWHLDEPFADPSAIPLYLLSRLARRKGVkVVLSGEGADELFGGYPFYK------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 400 fpwmrsteeritlldekwqkrlnlreyvnaryeetiaetplldgetgTDKARRQLFYLNMLWFMTNLLDRKDRMSMGASL 479
Cdd:pfam00733 140 -----------------------------------------------GEDPLRRMLYLDLKTLLPGDLLRADRMSMAHGL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 480 EVRVPFADHRLVEYVWNIPWEMKMHGSREKGILRKALEGLLPEDILYRKKSPYPK-THHPKYTQGVTEWLKTILQQKDSV 558
Cdd:pfam00733 173 EVRVPFLDHRLVEYALRLPPELKLRGGIEKYILREALEGILPDEILERPKEGFSApVGDWKLRGPLRELAEDLLSDSRLA 252
|
330
....*....|....*
gi 2287790176 559 LHTLLDRKKLEMLLE 573
Cdd:pfam00733 253 KEGLLDREAVRELLD 267
|
|
| lass_lactam_cya |
NF033535 |
lasso peptide isopeptide bond-forming cyclase; Members of this family are the isopeptide ... |
1-527 |
9.06e-59 |
|
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: 208.31 E-value: 9.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 1 MCGIAGWVDFQKQLVQEKHImNNMIDTLSKRGPDDSNVWGEPHVLFGHKRLSVVDIEG-GRQPMacTHQEETYTIIYNGE 79
Cdd:NF033535 1 MSGIVGIYYLDGRPVDREDL-QQMVDILAHRGPDGADIWCEGSVGLGHRMLWTTPESLlEKLPL--VNQTGDLVITADAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 80 LYNTEELRKELQARGHRFERTSDTEVLLHSYIEWREECVDRLNGIFAFAIWDEKRERLFGARDRLGVKPFFYKEHGSSFL 159
Cdd:NF033535 78 IDNRDELISALQLNNCPPEKITDSQLILAAYEKWGEQCPEHLLGDFAFAIWDKRKQQLFCARDHFGVKPFYYYQSDKRFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 160 FGSELKAILAHPDVKARTD----SGGLAEVFGlGPSRTPgcgvFKGIHEVRPAHAFTFSKDGLSIWRYW--NVKSEKHTD 233
Cdd:NF033535 158 FASEIKALLCLPEVPRRLNevriADYLALMLE-DKVITF----YQDIFRLPPAHSMTVSQSGLQIRSYWslDPSRELRLD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 234 SFDETAAHIRYLFQDAVTRQLVSDVPVCTFLSGGLDSSAITAIAAAHFEKQGRDPLHTYSIDYEENSKFfkasafqpnDD 313
Cdd:NF033535 233 SDEEYAEAFREIFTEAVRCRLRSAFPVGSHLSGGLDSSSITCVARQLLAEEKKAPLHTFSNIFDKVTEC---------DE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 314 GPWIDKMTNAFGTQHHkcVITQDQL--VEHLEESVLVRDLPGMADvDSSLLW-FCREIKKDFV-VSLSGECADE-IFGGY 388
Cdd:NF033535 304 RPFINAVLEQGGLIPH--YVHADQFgpLSDLEQIFEYEDEPFLGP-NHFLPWgLNRAAQKEGVrILLDGFDGDStVSHGH 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 389 PWFHTAAEED---------------------------GFPWMRSTEER---ITLLDEKWQ---------KRLNL------ 423
Cdd:NF033535 381 GYLTELANQGkwltfaqeiralsknygtspwgllrqyGLPYLEKLARQfkwLTFLKPANQihkhfgisrRQLFLqhgikp 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 424 -----------------------REYVNARYEETIaetPLLDGETGTDKAR-------RQLFYLNMLW-FMTNLLDRKDR 472
Cdd:NF033535 461 lvprallklwrklrgqaqpgnswRPIINPDFAERI---GLKERIQRLDPPPssspltvREEHWQSLTSgILPFVLEVLDK 537
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 2287790176 473 MSMGASLEVRVPFADHRLVEYVWNIPWEMKMHGSREKGILRKALEGLLPEDILYR 527
Cdd:NF033535 538 YAAAFSLEARHPFMDKRLVEFCLALPPEQKLRQGWSRMVMRRAMEGILPPQVQWR 592
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-607 |
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: 644.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 1 MCGIAGWVDFQKQlvQEKHIMNNMIDTLSKRGPDDSNVWGEPHVLFGHKRLSVVDI-EGGRQPMacTHQEETYTIIYNGE 79
Cdd:COG0367 1 MCGIAGIIDFDGG--ADREVLERMLDALAHRGPDGSGIWVDGGVALGHRRLSIIDLsEGGHQPM--VSEDGRYVLVFNGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 80 LYNTEELRKELQARGHRFERTSDTEVLLHSYIEWREECVDRLNGIFAFAIWDEKRERLFGARDRLGVKPFFYKEHGSSFL 159
Cdd:COG0367 77 IYNYRELRAELEALGHRFRTHSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDGGGLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 160 FGSELKAILAHPDVKARTDSGGLAEVFGLGPSrTPGCGVFKGIHEVRPAHAFTFSKDG-LSIWRYWNVKSEKHT--DSFD 236
Cdd:COG0367 157 FASELKALLAHPGVDRELDPEALAEYLTLGYV-PAPRTIFKGIRKLPPGHYLTVDAGGeLEIRRYWDLEFVPHErsDSEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 237 ETAAHIRYLFQDAVTRQLVSDVPVCTFLSGGLDssaitaiaaahfeKQGRDPLHTYSIDYEENskffkasafqPNDDGPW 316
Cdd:COG0367 236 EAVEELRELLEDAVRRRLRADVPVGAFLSGGLDssaia----alaaRLSKGPLKTFSIGFEDS----------AYDESPY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 317 IDKMTNAFGTQHHKCVITQDQLVEHLEESVLVRDLPGMADVDSSLLWFCREIKKDFVVSLSGECADEIFGGYPWFHTAAe 396
Cdd:COG0367 302 ARAVAEHLGTEHHEVTVTPEDLLDALPDLVWHLDEPFADPSAVPTYLLSRLAREHVKVVLSGEGADELFGGYPRYREAA- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 397 edgfpwmrsteeriTLLDEKWQKRLNlREYVNARYEETIAETPLldgetgtdkarRQLFYLNMLWFMTN-LLDRKDRMSM 475
Cdd:COG0367 381 --------------LLLSPDFAEALG-GELVPRLYAESGAEDPL-----------RRMLYLDLKTYLPGdLLVKVDRMSM 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 476 GASLEVRVPFADHRLVEYVWNIPWEMKMHGSREKGILRKALEGLLPEDILYRKKSPYPKTHHPKYTQGVTEWLKTILQQK 555
Cdd:COG0367 435 AHSLEVRVPFLDHRLVEFALSLPPELKLRGGRGKYLLRKALEGLLPDEVLDRPKQGFPVPLGPWLRGPLREWLEDLLSDE 514
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 2287790176 556 DSVLHTLLDRKKLEMLLETDGSsfqvpwfGQLMkGPQLIAHLAQIHTWFEAY 607
Cdd:COG0367 515 SLAARGLFDPDAVRRLLEEHLA-------GRRD-HSRKLWSLLMLELWLRRF 558
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-532 |
0e+00 |
|
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 562.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 4 IAGWVDFQKQLVQEKHIMNNMIDTLSKRGPDDSNV-WGEPHVLFGHKRLSVVDIEGGRQPMACThqEETYTIIYNGELYN 82
Cdd:TIGR01536 1 IAGFFDLDDKAVEEDEAIKRMSDTIAHRGPDASGIeYKDGNAILGHRRLAIIDLSGGAQPMSNE--GKTYVIVFNGEIYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 83 TEELRKELQARGHRFERTSDTEVLLHSYIEWREECVDRLNGIFAFAIWDEKRERLFGARDRLGVKPFFYKEHGSSFLFGS 162
Cdd:TIGR01536 79 HEELREELEAKGYTFQTDSDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYDGGQLYFAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 163 ELKAILAHPDVKARTDSGGLAEVFGLGPSRTPGCgVFKGIHEVRPAHAFTFSKDGLSIWRYWNVKSEKHTDSFDETAAHI 242
Cdd:TIGR01536 159 EIKALLAHPNIKPFPDGAALAPGFGFVRVPPPST-FFRGVFELEPGHDLPLDDDGLNIERYYWERRDEHTDSEEDLVDEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 243 RYLFQDAVTRQLVSDVPVCTFLSGGLDSSAITAIAAAHFEkqgRDPLHTYSIDYEENSKFfkasafqpnDDGPWIDKMTN 322
Cdd:TIGR01536 238 RSLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAP---RGPVHTFSIGFEGSPDF---------DESKYARKVAD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 323 AFGTQHHKCVITQDQLVEHLEESVLVRDLPG-MADVDSSLLWFCREIKKDFVVSLSGECADEIFGGYPWFHTAaeedgfP 401
Cdd:TIGR01536 306 HLGTEHHEVLFSVEEGLDALPEVIYHLEEPTtIRASIPLYLLSKLAREDGVKVVLSGEGADELFGGYLYFHEA------P 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 402 WMRsteeritlldekwqkrlnlreyvnaryeetiaetplldgetgtdKARRQLFYLNMLWFMTNLLDRKDRMSMGASLEV 481
Cdd:TIGR01536 380 AAE--------------------------------------------ALREELQYLDLELYMPGLLRRKDRMSMAHSLEV 415
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2287790176 482 RVPFADHRLVEYVWNIPWEMKMHGSREKGILRKALEGLLPEDILYRKKSPY 532
Cdd:TIGR01536 416 RVPFLDHELVEYALSIPPEMKLRDGKEKYLLREAFEGYLPEEILWRPKEGF 466
|
|
| eps_aminotran_1 |
TIGR03108 |
exosortase A system-associated amidotransferase 1; The predicted protein-sorting ... |
1-529 |
9.05e-115 |
|
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: 355.97 E-value: 9.05e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 1 MCGIAGWVDFQKQLVQEKHIMNNMIDTLSKRGPDDSNVWGEPHVLFGHKRLSVVDIEGGRQPMacTHQEETYTIIYNGEL 80
Cdd:TIGR03108 1 MCGITGIFDLTGQRPIDRDLLRRMNDAQAHRGPDGGGVHVEPGIGLGHRRLSIIDLSGGQQPL--FNEDGSVVVVFNGEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 81 YNTEELRKELQARGHRFERTSDTEVLLHSYIEWREECVDRLNGIFAFAIWDEKRERLFGARDRLGVKPFFYK--EHGsSF 158
Cdd:TIGR03108 79 YNFQELVAELQALGHVFRTRSDTEVIVHAWEEWGEACVERFRGMFAFALWDRNQETLFLARDRLGIKPLYYAllADG-WF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 159 LFGSELKAILAHPDVKARTDSGGLAEVFGLGPSRTPGcGVFKGIHEVRPAHAFTFsKDGLSIWR---YWNVKSEKHTD-S 234
Cdd:TIGR03108 158 IFGSELKALTAHPSLPRELDPLAVEDYFAYGYVPDPR-TIFKGVKKLEPGHTLTL-RRGAPPARprcYWDVSFAPAAPlS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 235 FDETAAHIRYLFQDAVTRQLVSDVPVCTFLSGGLDSSAITAIaaahFEKQGRDPLHTYSIDyeenskfFKASAFqpnDDG 314
Cdd:TIGR03108 236 EADALAELIERLREAVRSRMVADVPLGAFLSGGVDSSAVVAL----MAGLSDTPVNTCSIA-------FDDPAF---DES 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 315 PWIDKMTNAFGTQHHKCVITQDQLvehleesVLVRDLPGMAD---VDSSLL---WFCREIKKDFVVSLSGECADEIFGGY 388
Cdd:TIGR03108 302 AYARQVAERYGTNHRVETVDPDDF-------SLVDRLAGLYDepfADSSALptyRVCELARKRVTVALSGDGGDELFAGY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 389 P---WFHtaAEE-------------------------DGFPWM-----------RSTEE----RITLLDEKWQKRLnlre 425
Cdd:TIGR03108 375 RryrWHM--AEErvrgilplglrrplfgtlgrlypkaDWAPRMlrakttfqalaRDPLEgyfhSVSVLDNALRRQL---- 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 426 YVNARYEETI---AETPL--LDGETGTDKARRQLFYLNM-LWFMTNLLDRKDRMSMGASLEVRVPFADHRLVEYVWNIPW 499
Cdd:TIGR03108 449 FSPDFRRELQgyrAIEVLrrHAARAPTDDALSLAQYLDLkTYLPGDILTKVDRASMAHGLEVRVPLLDHRLVEWAAGLPP 528
|
570 580 590
....*....|....*....|....*....|
gi 2287790176 500 EMKMHGSREKGILRKALEGLLPEDILYRKK 529
Cdd:TIGR03108 529 DLKLRGGEGKYLLKKAMRPYLPDDVLYRPK 558
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-225 |
8.17e-106 |
|
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: 318.35 E-value: 8.17e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 2 CGIAGWVDFQKQLVQEKHImNNMIDTLSKRGPDDSNVWGEPHVLFGHKRLSVVDIEGGRQPMacTHQEETYTIIYNGELY 81
Cdd:cd00712 1 CGIAGIIGLDGASVDRATL-ERMLDALAHRGPDGSGIWIDEGVALGHRRLSIIDLSGGAQPM--VSEDGRLVLVFNGEIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 82 NTEELRKELQARGHRFERTSDTEVLLHSYIEWREECVDRLNGIFAFAIWDEKRERLFGARDRLGVKPFFYKEHGSSFLFG 161
Cdd:cd00712 78 NYRELRAELEALGHRFRTHSDTEVILHLYEEWGEDCLERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGRDGGGLAFA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2287790176 162 SELKAILAHPDVKARTDSGGLAEVFgLGPSRTPGCGVFKGIHEVRPAHAFTFSKDGLSIWRYWN 225
Cdd:cd00712 158 SELKALLALPGVPRELDEAALAEYL-AFQYVPAPRTIFKGIRKLPPGHYLTVDPGGVEIRRYWD 220
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-529 |
3.62e-92 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 294.89 E-value: 3.62e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 1 MCGIAGWVDFQKQLVQEKHIMNNMIDTLSKRGPDDSNVWGEPHVLFGHKRLSVVDIEGGRQPMacTHQEETYTIIYNGEL 80
Cdd:PRK09431 1 MCGIFGILDIKTDADELRKKALEMSRLMRHRGPDWSGIYASDNAILGHERLSIVDVNGGAQPL--YNEDGTHVLAVNGEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 81 YNTEELRKELqARGHRFERTSDTEVLLHSYIEWREECVDRLNGIFAFAIWDEKRERLFGARDRLGVKPFFY--KEHGsSF 158
Cdd:PRK09431 79 YNHQELRAEL-GDKYAFQTGSDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYgyDEHG-NL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 159 LFGSELKAIlahpdvkartdsgglaevfglgpsrTPGCgvfKGIHEVRPAHAFTfSKDGLSIwRYWNVKSEKHTDSFDET 238
Cdd:PRK09431 157 YFASEMKAL-------------------------VPVC---KTIKEFPPGHYYW-SKDGEFV-RYYQRDWFDYDAVKDNV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 239 AA--HIRYLFQDAVTRQLVSDVPVCTFLSGGLDSSAITAIAAAHFEKQGRD---------PLHTYSIDYEEnSKFFKASA 307
Cdd:PRK09431 207 TDknELRDALEAAVKKRLMSDVPYGVLLSGGLDSSLISAIAKKYAARRIEDderseawwpQLHSFAVGLEG-SPDLKAAR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 308 fqpnddgpwidKMTNAFGTQHHKCVITQDQLVEHLEESV---------LVRDLPGMadvdsSLLwfCREIKKDFV-VSLS 377
Cdd:PRK09431 286 -----------EVADHLGTVHHEIHFTVQEGLDALRDVIyhletydvtTIRASTPM-----YLM--ARKIKAMGIkMVLS 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 378 GECADEIFGGYPWFHTAAEEDGFpwmrsteeritlldekwqkrlnlreyvnarYEETiaetplldgetgtdkaRRQLFYL 457
Cdd:PRK09431 348 GEGADELFGGYLYFHKAPNAKEF------------------------------HEET----------------VRKLRAL 381
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2287790176 458 nmlwFMTNLLdRKDRMSMGASLEVRVPFADHRLVEYVWNIPWEMKM--HGSREKGILRKALEGLLPEDILYRKK 529
Cdd:PRK09431 382 ----HMYDCL-RANKAMMAWGVEARVPFLDKEFLDVAMRINPEDKMcgNGKMEKHILREAFEGYLPESILWRQK 450
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
241-573 |
7.50e-86 |
|
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: 269.10 E-value: 7.50e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 241 HIRYLFQDAVTRQLVSDVPVCTFLSGGLDSSAITAIAAahfeKQGRDPLHTYSIDYEEnskffkasafQPNDDGPWIDKM 320
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAA----RQSPSPLHTFSIGFEG----------RGYDEAPYAREV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 321 TNAFGTQHHKCVITQDQLVEHLEESVLVRDLPGMADVDSSLLWFCREIKKDFV-VSLSGECADEIFGGYPWFHtaaeedg 399
Cdd:pfam00733 67 AEHLGTDHHELVVTPEDLLDALPDVIWHLDEPFADPSAIPLYLLSRLARRKGVkVVLSGEGADELFGGYPFYK------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 400 fpwmrsteeritlldekwqkrlnlreyvnaryeetiaetplldgetgTDKARRQLFYLNMLWFMTNLLDRKDRMSMGASL 479
Cdd:pfam00733 140 -----------------------------------------------GEDPLRRMLYLDLKTLLPGDLLRADRMSMAHGL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 480 EVRVPFADHRLVEYVWNIPWEMKMHGSREKGILRKALEGLLPEDILYRKKSPYPK-THHPKYTQGVTEWLKTILQQKDSV 558
Cdd:pfam00733 173 EVRVPFLDHRLVEYALRLPPELKLRGGIEKYILREALEGILPDEILERPKEGFSApVGDWKLRGPLRELAEDLLSDSRLA 252
|
330
....*....|....*
gi 2287790176 559 LHTLLDRKKLEMLLE 573
Cdd:pfam00733 253 KEGLLDREAVRELLD 267
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
48-169 |
4.64e-64 |
|
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: 206.22 E-value: 4.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 48 HKRLSVVDIEGGRQPMaCTHQEETYTIIYNGELYNTEELRKELQARGHRFERTSDTEVLLHSY-IEWREECVDRLNGIFA 126
Cdd:pfam13537 1 HRRLSIIDLEGGAQPM-VSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYeAEWGEDCVDRLNGMFA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2287790176 127 FAIWDEKRERLFGARDRLGVKPFFY-KEHGSSFLFGSELKAILA 169
Cdd:pfam13537 80 FAIWDRRRQRLFLARDRFGIKPLYYgRDDGGRLLFASELKALLA 123
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-529 |
1.73e-61 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 214.19 E-value: 1.73e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 1 MCGIAGWVDfqkqLVQEKHIMNNMIDTLSK----RGPDDSNVW------GEPHVLfGHKRLSVVDIEGGRQPMacTHQEE 70
Cdd:PTZ00077 1 MCGILAIFN----SKGERHELRRKALELSKrlrhRGPDWSGIIvlenspGTYNIL-AHERLAIVDLSDGKQPL--LDDDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 71 TYTIIYNGELYNTEELRKELQARGHRFERTSDTEVLLHSYIEWRE-ECVDRLNGIFAFAIWDEKRERLFGARDRLGVKPF 149
Cdd:PTZ00077 74 TVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKEYGPkDFWNHLDGMFATVIYDMKTNTFFAARDHIGIIPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 150 F--YKEHGSSFlFGSELKAIlahpdvkarTDSgglaevfglgpsrtpgCGVFKgihEVRPAHAFTFSKDGLSIWRY---- 223
Cdd:PTZ00077 154 YigYAKDGSIW-FSSELKAL---------HDQ----------------CVEVK---QFPPGHYYDQTKEKGEFVRYynpn 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 224 -WNVKSEKHTDSFDETAahIRYLFQDAVTRQLVSDVPVCTFLSGGLDSSAITAIAAAHFE-------KQGRDPLHTYSID 295
Cdd:PTZ00077 205 wHDFDHPIPTGEIDLEE--IREALEAAVRKRLMGDVPFGLFLSGGLDSSIVAAIVAKLIKngeidlsKRGMPKLHSFCIG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 296 YEENSKFFKASafqpnddgpwidKMTNAFGTQHHKCVITQDQLVEHLEESVLVRDLPGMADVDSS--LLWFCREIKKDFV 373
Cdd:PTZ00077 283 LEGSPDLKAAR------------KVAEYLGTEHHEFTFTVEEGIDALPDVIYHTETYDVTTIRAStpMYLLSRRIKALGI 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 374 -VSLSGECADEIFGGYPWFHTAAEEDGFpwmrsteeritllDEKWQKRLNlreyvnaryeetiaetplldgetgtdkarr 452
Cdd:PTZ00077 351 kMVLSGEGSDELFGGYLYFHKAPNREEF-------------HRELVRKLH------------------------------ 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 453 QLFYLNMLwfmtnlldRKDRMSMGASLEVRVPFADHRLVEYVWNIPWEMKMHGSR----EKGILRKALEGL----LPEDI 524
Cdd:PTZ00077 388 DLHKYDCL--------RANKATMAWGIEARVPFLDKDFLEYVMNIDPKYKMCNAFegqmEKYILRKAFEGLekpyLPDEI 459
|
....*
gi 2287790176 525 LYRKK 529
Cdd:PTZ00077 460 LWRQK 464
|
|
| lass_lactam_cya |
NF033535 |
lasso peptide isopeptide bond-forming cyclase; Members of this family are the isopeptide ... |
1-527 |
9.06e-59 |
|
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: 208.31 E-value: 9.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 1 MCGIAGWVDFQKQLVQEKHImNNMIDTLSKRGPDDSNVWGEPHVLFGHKRLSVVDIEG-GRQPMacTHQEETYTIIYNGE 79
Cdd:NF033535 1 MSGIVGIYYLDGRPVDREDL-QQMVDILAHRGPDGADIWCEGSVGLGHRMLWTTPESLlEKLPL--VNQTGDLVITADAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 80 LYNTEELRKELQARGHRFERTSDTEVLLHSYIEWREECVDRLNGIFAFAIWDEKRERLFGARDRLGVKPFFYKEHGSSFL 159
Cdd:NF033535 78 IDNRDELISALQLNNCPPEKITDSQLILAAYEKWGEQCPEHLLGDFAFAIWDKRKQQLFCARDHFGVKPFYYYQSDKRFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 160 FGSELKAILAHPDVKARTD----SGGLAEVFGlGPSRTPgcgvFKGIHEVRPAHAFTFSKDGLSIWRYW--NVKSEKHTD 233
Cdd:NF033535 158 FASEIKALLCLPEVPRRLNevriADYLALMLE-DKVITF----YQDIFRLPPAHSMTVSQSGLQIRSYWslDPSRELRLD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 234 SFDETAAHIRYLFQDAVTRQLVSDVPVCTFLSGGLDSSAITAIAAAHFEKQGRDPLHTYSIDYEENSKFfkasafqpnDD 313
Cdd:NF033535 233 SDEEYAEAFREIFTEAVRCRLRSAFPVGSHLSGGLDSSSITCVARQLLAEEKKAPLHTFSNIFDKVTEC---------DE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 314 GPWIDKMTNAFGTQHHkcVITQDQL--VEHLEESVLVRDLPGMADvDSSLLW-FCREIKKDFV-VSLSGECADE-IFGGY 388
Cdd:NF033535 304 RPFINAVLEQGGLIPH--YVHADQFgpLSDLEQIFEYEDEPFLGP-NHFLPWgLNRAAQKEGVrILLDGFDGDStVSHGH 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 389 PWFHTAAEED---------------------------GFPWMRSTEER---ITLLDEKWQ---------KRLNL------ 423
Cdd:NF033535 381 GYLTELANQGkwltfaqeiralsknygtspwgllrqyGLPYLEKLARQfkwLTFLKPANQihkhfgisrRQLFLqhgikp 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 424 -----------------------REYVNARYEETIaetPLLDGETGTDKAR-------RQLFYLNMLW-FMTNLLDRKDR 472
Cdd:NF033535 461 lvprallklwrklrgqaqpgnswRPIINPDFAERI---GLKERIQRLDPPPssspltvREEHWQSLTSgILPFVLEVLDK 537
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 2287790176 473 MSMGASLEVRVPFADHRLVEYVWNIPWEMKMHGSREKGILRKALEGLLPEDILYR 527
Cdd:NF033535 538 YAAAFSLEARHPFMDKRLVEFCLALPPEQKLRQGWSRMVMRRAMEGILPPQVQWR 592
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-529 |
1.52e-58 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 206.15 E-value: 1.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 1 MCGIAGWVDFQKQLVQEKHIMNNMIDTLSKRGPDDSNVWGEPHVLFGHKRLSVVDIEGGRQPMacTHQEETYTIIYNGEL 80
Cdd:PLN02549 1 MCGILAVLGCSDDSQAKRSRVLELSRRLRHRGPDWSGLYGNEDCYLAHERLAIMDPESGDQPL--YNEDKTIVVTANGEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 81 YNTEELRKELQArgHRFERTSDTEVLLHSYIEWREECVDRLNGIFAFAIWDEKRERLFGARDRLGVKPFF--YKEHGSSF 158
Cdd:PLN02549 79 YNHKELREKLKL--HKFRTGSDCEVIAHLYEEHGEEFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYigWGLDGSVW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 159 lFGSELKAIlahpdvkartdsgglaevfglgpsrtpgCGVFKGIHEVRPAHAFTFSKDGLSiwRYWNVK--SEkHTDSFD 236
Cdd:PLN02549 157 -FASEMKAL----------------------------CDDCERFEEFPPGHYYSSKAGGFR--RWYNPPwfSE-SIPSTP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 237 ETAAHIRYLFQDAVTRQLVSDVPVCTFLSGGLDSSAITAIAAAHFE-----KQGRDPLHTYSIDyEENSKFFKASAfqpn 311
Cdd:PLN02549 205 YDPLVLREAFEKAVIKRLMTDVPFGVLLSGGLDSSLVASIAARHLAetkaaRQWGQQLHSFCVG-LEGSPDLKAAR---- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 312 ddgpwidKMTNAFGTQHHKCVIT-QDQL------VEHLE--ESVLVRdlpgmADVDSSLLwfCREIKKDFV-VSLSGECA 381
Cdd:PLN02549 280 -------EVADYLGTVHHEFHFTvQEGIdaiedvIYHLEtyDVTTIR-----ASTPMFLM--SRKIKSLGVkMVLSGEGS 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 382 DEIFGGYPWFHTAAEEDGFpwmrsteeritlldekwqkrlnlreyvnarYEETiaetplldgetgtdkaRRQLFYLnmlw 461
Cdd:PLN02549 346 DEIFGGYLYFHKAPNKEEF------------------------------HKET----------------CRKIKAL---- 375
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2287790176 462 FMTNLLdRKDRMSMGASLEVRVPFADHRLVEYVWNIPWEMKM----HGSREKGILRKALEG----LLPEDILYRKK 529
Cdd:PLN02549 376 HQYDCL-RANKSTSAWGLEARVPFLDKEFIDVAMSIDPEWKMirpgEGRIEKWVLRKAFDDeedpYLPKHILWRQK 450
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
256-533 |
4.44e-52 |
|
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or synthetase) B is always associated with an N-terminal amidotransferase domain. Family members that contain this domain catalyze the conversion of aspartate to asparagine. Asparagine synthase B catalyzes the synthesis of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase.
Pssm-ID: 467495 [Multi-domain] Cd Length: 224 Bit Score: 178.24 E-value: 4.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 256 SDVPVCTFLSGGLDSSAITAIAAAHFEKQgrdPLHTYSIDYEENskffkasafqPNDDGPWIDKMTNAFGTQHHKCVITQ 335
Cdd:cd01991 1 SDVPVGVLLSGGLDSSLIAALAARLLPET---PIDLFTVGFEGS----------PTPDRAAARRVAEELGTEHHEVEVTI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 336 DQLVEHLEESVLVRDLP-GMADVDSSLLWF-CREIKKD-FVVSLSGECADEIFGGYPWFHTAAeedgfpwmrsteeritl 412
Cdd:cd01991 68 EELLDALPDVILIYPTDtPMDLSIAIPLYFaSRLAGKLgAKVVLSGEGADELFGGYSRHRDAP----------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 413 ldekwqkrlnlreyvNARYEETIAETplldgetgtdkarrqLFYLNMLWfmTNLLDRKDRMSMGASLEVRVPFADHRLVE 492
Cdd:cd01991 131 ---------------LRGWEALEEEL---------------LRDLDRLW--TRNLGRDDRVAMAHGLEARVPFLDEELVE 178
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2287790176 493 YVWNIPWEMKM--HGSREKGILRKALEGLLPEDILYRKKSPYP 533
Cdd:cd01991 179 FALSLPPSLKIdpRGGGEKYILREAARDLLPDEIAWRPKRAIQ 221
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
33-163 |
2.18e-50 |
|
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: 170.56 E-value: 2.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 33 PDDSNVWGEPHVLFGHKRLSVVDI-EGGRQPMacTHQEETYTIIYNGELYNTEELRKELQARGHRFERTSDTEVLLHSYI 111
Cdd:pfam13522 1 PDFSGIWVEGGVALGHVRLAIVDLpDAGNQPM--LSRDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYE 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2287790176 112 EWREECVDRLNGIFAFAIWDEKRERLFGARDRLGVKPFFYKEHGSSFLFGSE 163
Cdd:pfam13522 79 EWGEDCLERLRGMFAFAIWDRRRRTLFLARDRLGIKPLYYGILGGGFVFASE 130
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-171 |
4.67e-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: 159.54 E-value: 4.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 2 CGIAGWVDFQKQLVQEKHIMNNMIDTLSKRGPDDSNVW---------------------------GEPHVLFGHKRLSVV 54
Cdd:cd00352 1 CGIFGIVGADGAASLLLLLLLRGLAALEHRGPDGAGIAvydgdglfvekragpvsdvaldlldepLKSGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 55 DI--EGGRQPMacTHQEETYTIIYNGELYNTEELRKELQARGHRFERTSDTEVLLHSYIEWR---------EECVDRLNG 123
Cdd:cd00352 81 GLpsEANAQPF--RSEDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGregglfeavEDALKRLDG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2287790176 124 IFAFAIWDEKRERLFGARDRLGVKPFFYKE-HGSSFLFGSELKAILAHP 171
Cdd:cd00352 159 PFAFALWDGKPDRLFAARDRFGIRPLYYGItKDGGLVFASEPKALLALP 207
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
61-223 |
9.28e-15 |
|
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: 76.98 E-value: 9.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 61 QPMACTHQEETYTIIYNGELYNTEELRKELQARGHRFERTSDTEVLLH------SYIEWRE---ECVDRLNGIFAFAIWD 131
Cdd:COG0034 92 QPFYVNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHliarelTKEDLEEaikEALRRVKGAYSLVILT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 132 EKreRLFGARDRLGVKPFFYKEHGSSFLFGSELKAIlahpDVkartdsgglaevfgLGpsrtpgcgvFKGIHEVRPAHAF 211
Cdd:COG0034 172 GD--GLIAARDPNGIRPLVLGKLEDGYVVASESCAL----DI--------------LG---------AEFVRDVEPGEIV 222
|
170
....*....|..
gi 2287790176 212 TFSKDGLSIWRY 223
Cdd:COG0034 223 VIDEDGLRSRQF 234
|
|
| Gn_AT_II_novel |
cd03766 |
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its ... |
1-145 |
8.67e-13 |
|
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: 66.93 E-value: 8.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 1 MCGIAGWVDFQKQLVQEKHIMNNMIDTLSKRGPDDSNV----WGEPHVLFGHKRLSVVDIEGGRQPMacTHQEETYTIIY 76
Cdd:cd03766 1 MCGILCSVSPSGPHINSSLLSEELLPNLRNRGPDYLSTrqlsVTNWTLLFTSSVLSLRGDHVTRQPL--VDQSTGNVLQW 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2287790176 77 NGELYNTEELRKElqarghrferTSDTEVLLHSYIEWREECVD------RLNGIFAFAIWDEKRERLFGARDRLG 145
Cdd:cd03766 79 NGELYNIDGVEDE----------ENDTEVIFELLANCSSESQDildvlsSIEGPFAFIYYDASENKLYFGRDCLG 143
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
73-148 |
3.88e-12 |
|
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: 66.72 E-value: 3.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 73 TIIYNGELYNTEELRKELQARGHRFERTSDTEVLLH------SYIEWREECVD---RLNGIFAFAIWDekRERLFGARDR 143
Cdd:cd00715 97 ALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHliarslAKDDLFEAIIDaleRVKGAYSLVIMT--ADGLIAVRDP 174
|
....*
gi 2287790176 144 LGVKP 148
Cdd:cd00715 175 HGIRP 179
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
74-170 |
6.74e-10 |
|
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: 59.38 E-value: 6.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 74 IIYNGELYNTEELRKELQARGHRFERTSDTEVLLH----------SYIEWREECVDRLNGIFAFAIWDEK-RERLFGARD 142
Cdd:cd00714 96 VVHNGIIENYAELKEELEAKGYKFESETDTEVIAHlieyyydgglDLLEAVKKALKRLEGAYALAVISKDePDEIVAARN 175
|
90 100 110
....*....|....*....|....*....|..
gi 2287790176 143 R----LGVKPFFYkehgssFLfGSELKAILAH 170
Cdd:cd00714 176 GsplvIGIGDGEN------FV-ASDAPALLEH 200
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
74-141 |
7.12e-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: 55.40 E-value: 7.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 74 IIYNG--ElyNTEELRKELQARGHRFERTSDTEVLLHsYIEWR-----------EECVDRLNGIFAFA-IWDEKRERLFG 139
Cdd:COG0449 97 VVHNGiiE--NYAELREELEAKGHTFKSETDTEVIAH-LIEEYlkgggdlleavRKALKRLEGAYALAvISADEPDRIVA 173
|
..
gi 2287790176 140 AR 141
Cdd:COG0449 174 AR 175
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
73-141 |
7.23e-08 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 55.43 E-value: 7.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 73 TIIYNGELYNTEELRKELQARGHRFERTSDTEVLLHsYIEWREE-----------CVDRLNGIFAFA-IWDEKRERLFGA 140
Cdd:PRK00331 96 AVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAH-LIEEELKeggdlleavrkALKRLEGAYALAvIDKDEPDTIVAA 174
|
.
gi 2287790176 141 R 141
Cdd:PRK00331 175 R 175
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
43-163 |
1.10e-07 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 54.65 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 43 HVLFGHKRLSVV---DIEGGrQPMACTHQEETYTIIYNGELYNTEELRKELQARGHRFERTSDTEVLLH--------SYI 111
Cdd:PRK05793 81 NSAIGHVRYSTTgasDLDNA-QPLVANYKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNliarsakkGLE 159
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2287790176 112 EWREECVDRLNGIFAFAIWDEKreRLFGARDRLGVKPFFYKEHGSSFLFGSE 163
Cdd:PRK05793 160 KALVDAIQAIKGSYALVILTED--KLIGVRDPHGIRPLCLGKLGDDYILSSE 209
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-178 |
2.61e-07 |
|
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: 52.27 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 2 CGIAGWVDFQKQLVQEKhIMNNMIDTLSKRGPDDSN---VWGEPHVL---FGH---------------KRLSVVDIEG-- 58
Cdd:cd01907 1 CGIFGIMSKDGEPFVGA-LLVEMLDAMQERGPGDGAgfaLYGDPDAFvysSGKdmevfkgvgypediaRRYDLEEYKGyh 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 59 ----GRQP-------MACtH--QEETYTIIYNGELYNTEELRKELQARGHRFERTSDTEVLLHsYIEW------------ 113
Cdd:cd01907 80 wiahTRQPtnsavwwYGA-HpfSIGDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAY-YLDLllrkgglpleyy 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 114 ------------------REECVDRLNGIFAFAIWDekRERLFGARDRLGVKPFFYKEHGSSFLFGSELKAILAHPDVKA 175
Cdd:cd01907 158 khiirmpeeerelllalrLTYRLADLDGPFTIIVGT--PDGFIVIRDRIKLRPAVVAETDDYVAIASEECAIREIPDRDN 235
|
...
gi 2287790176 176 RTD 178
Cdd:cd01907 236 AKV 238
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
74-163 |
7.52e-06 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 48.91 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 74 IIYNGELYNTEELRKELQARGHRFERTSDTEVLLHSYIEWREE-----CVD---RLNGIFA--FAIWDekreRLFGARDR 143
Cdd:PLN02440 99 VAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKARpffsrIVDaceKLKGAYSmvFLTED----KLVAVRDP 174
|
90 100
....*....|....*....|.
gi 2287790176 144 LGVKPF-FYKEHGSSFLFGSE 163
Cdd:PLN02440 175 HGFRPLvMGRRSNGAVVFASE 195
|
|
| betaLS_CarA_N |
cd01909 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_betaLS-type. Carbapenam ... |
70-217 |
3.29e-05 |
|
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: 45.18 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 70 ETYTIIYNGELYNTEELRKELQARGHRFERTSDTEVLLHSYIEWREECVDRLNGIFAFAIwDEKRERLFGARDRLGVKPF 149
Cdd:cd01909 50 ETGTAYLIGELYNRDELRSLLGAGEGRSAVLGDAELLLLLLTRLGLHAFRLAEGDFCFFI-EDGNGRLTLATDHAGSVPV 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 150 FYKEHGSSFLfGSELKAILAHPDVKARTDSgglaevfGLGPSRTPGcgvFKGIHEVRP--AHAFTFSKDG 217
Cdd:cd01909 129 YLVQAGEVWA-TTELKLLAAHEGPKAFPFK-------SAGADTVSG---LTGVQRVPPgtVNVLTFDGGS 187
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
74-161 |
7.07e-04 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 42.70 E-value: 7.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287790176 74 IIYNGELYNTEELRKELQARGHRFERTSDTEV---LLHSYIEWRE-------ECVDRLNGIFAFAIWD-EKRERLFGARd 142
Cdd:PTZ00295 127 LVHNGTIENYVELKSELIAKGIKFRSETDSEVianLIGLELDQGEdfqeavkSAISRLQGTWGLCIIHkDNPDSLIVAR- 205
|
90
....*....|....*....
gi 2287790176 143 rlgvkpffykeHGSSFLFG 161
Cdd:PTZ00295 206 -----------NGSPLLVG 213
|
|
| |
