|
Name |
Accession |
Description |
Interval |
E-value |
| TrpE |
COG0147 |
Anthranilate/para-aminobenzoate synthases component I [Amino acid transport and metabolism, ... |
197-625 |
3.39e-161 |
|
Anthranilate/para-aminobenzoate synthases component I [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthases component I is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439917 [Multi-domain] Cd Length: 416 Bit Score: 468.04 E-value: 3.39e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 197 YQCVDVDLDTESTFRALAGESAeAFWLDSATGEG----FSILGTD----------RGSLTRSHTFRLGEDDILDTLGAEL 262
Cdd:COG0147 6 YRELLALETPVSLFLKLADGPY-AFLLESAEGGEkwgrYSFIGADplatltvrggRVTIEGGGEVEPSEGDPLDALRALL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 263 AvRVDTSPLPDLP-FTGGWVGYLGYECATL--TLPRLTPsAPSAYPDAWWVRPQSFIVYDHSAQRahlmvlyrgapdeet 339
Cdd:COG0147 85 A-RFRLPPLPGLPpFTGGLVGYFGYDLVRYfeRLPDLAP-DDLGLPDAALGLYDRLLVFDHLKGT--------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 340 rclmgelvaatsarasegeigvgvekgSWRLSREDYLARIGRIKEALASGDSYEVCLTDTWSARTSSAGIDLYSRLRRFN 419
Cdd:COG0147 148 ---------------------------RSNFTREEYLAAVERAKEYIRAGDIFQVVLSQRFSAPFEGDPLALYRALRRIN 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 420 PAPYAAYFRIESVEVLSSSPERFLTVHGRDVETKPIKGTIPREEDPS-------ALRTDAKTRAENLMIVDLLRNDLGRV 492
Cdd:COG0147 201 PSPYMFYLRFGDFAIVGSSPERLVRVEDGRVETRPIAGTRPRGATPEedaalaeELLADEKERAEHLMLVDLARNDLGRV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 493 CEPGTVTVPKLMHVETYATVHQLVSTVRGVLRPGTTLIDLLRAAFPGGSMTGAPKERTCAMISELEPGARGVYSGVAGYL 572
Cdd:COG0147 281 CEPGSVKVPELMVVERYSHVMHLVSTVTGRLRPGLDALDALRATFPAGTLTGAPKIRAMEIIDELEPTRRGVYGGAVGYL 360
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2537977332 573 GFNGRADLSILIRTAVKQGDTVEVGAGGAVVWASHPAAEYEEKELKARAVTAA 625
Cdd:COG0147 361 SFDGNMDLAIAIRTAVVKDGRAYVQAGAGIVADSDPEAEYQETLNKARALLRA 413
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
3-621 |
7.09e-137 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 422.33 E-value: 7.09e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 3 LLIDNRDSYTYNLAHLIHAAAGEEPLVVRADDVEKYDLARRV-EGGEFSHIVISPGPGTPADDGDFRGSRLIIQAAGETP 81
Cdd:PLN02889 85 LLIDNYDSYTYNIYQELSIVNGVPPVVVRNDEWTWEEVYHYLyEEKAFDNIVISPGPGSPTCPADIGICLRLLLECRDIP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 82 VLGVCLGHQGLAHLAGAS-VQRGAPHHGATSTITHSGEGIFAGLPQG----FTAVRYHSLTV------------------ 138
Cdd:PLN02889 165 ILGVCLGHQALGYVHGARiVHAPEPVHGRLSEIEHNGCRLFDDIPSGrnsgFKVVRYHSLVIdaeslpkelvpiawtsss 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 139 -------SEAPGVRVHA----------------RAEDGT---------VQGLEVV------GRPHWGVQFHPESVLTDCG 180
Cdd:PLN02889 245 dtlsfleSQKSGLVPDAyesqigqsgssdpfssKLKNGTswpsshserMQNGKILmgimhsTRPHYGLQFHPESIATCYG 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 181 VELLRNFLSLSQ-----------------------------------LRVEYQCVDVDLDTESTFRA------------- 212
Cdd:PLN02889 325 RQIFKNFREITQdywlrlrstslrrrnsnltanmqvpdasqlfkvprRGQLGNGEDALGNRELSRRAqlrgsvdvfslln 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 213 --------------------LAGESAEA----------------FWLDSATGEG----FSILGTDRGSLTRSHTFRLG-- 250
Cdd:PLN02889 405 lsepssgvkflklkwrkfnkLAAQVGGArnifcelfgknkaentFWLDSSSTEKkrgrFSFMGGKGGSLWKQMTFRLShq 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 251 -------------------------EDDILDTLGAEL-AVRVDTSPLPDLPFT--GGWVGYLGY----ECATLTlprltP 298
Cdd:PLN02889 485 sdmdskggghlsiedsqgsiestflEKGFLDFLNKELlSIRYDEKDFEGLPFDfhGGYVGYIGYdlkvECGMAS-----N 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 299 SAPSAYPDAWWVRPQSFIVYDHSAQRAHLMVLYRGAP-------DEETR--CLMG------ELVAATSARASEGEIGVGV 363
Cdd:PLN02889 560 RHKSTTPDACFFFADNVVVIDHHYDDVYILSLHEGSTattqwldDTEQKllGLKAsatrklEVQTSPTATFSPSKAGFLA 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 364 EKgswrlSREDYLARIGRIKEALASGDSYEVCLTDTWSARTSSAG-IDLYSRLRRFNPAPYAAY--FRIESVEVLSSSPE 440
Cdd:PLN02889 640 DK-----SREQYIKDVQKCLKYIKDGESYELCLTTQMRKRIGEIDsLGLYLHLREKNPAPYAAWlnFSNENLCICSSSPE 714
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 441 RFLTVHGRDV-ETKPIKGTIPR----EEDPS---ALRTDAKTRAENLMIVDLLRNDLGRVCEPGTVTVPKLMHVETYATV 512
Cdd:PLN02889 715 RFLKLDRNGMlEAKPIKGTIARgstpEEDEQlklQLQYSEKDQAENLMIVDLLRNDLGRVCEPGSVHVPNLMDVESYTTV 794
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 513 HQLVSTVRGVLRPGTTLIDLLRAAFPGGSMTGAPKERTCAMISELEPGARGVYSGVAGYLGFNGRADLSILIRTAVKQGD 592
Cdd:PLN02889 795 HTMVSTIRGKKRSNMSPVDCVRAAFPGGSMTGAPKLRSMELLDSLESSSRGIYSGSIGFFSYNQTFDLNIVIRTVVIHEG 874
|
810 820
....*....|....*....|....*....
gi 2537977332 593 TVEVGAGGAVVWASHPAAEYEEKELKARA 621
Cdd:PLN02889 875 EASIGAGGAIVALSNPEDEYEEMILKTRA 903
|
|
| Chorismate_bind |
pfam00425 |
chorismate binding enzyme; This family includes the catalytic regions of the chorismate ... |
373-618 |
1.14e-113 |
|
chorismate binding enzyme; This family includes the catalytic regions of the chorismate binding enzymes anthranilate synthase, isochorismate synthase, aminodeoxychorismate synthase and para-aminobenzoate synthase.
Pssm-ID: 425674 [Multi-domain] Cd Length: 255 Bit Score: 340.30 E-value: 1.14e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 373 EDYLARIGRIKEALASGDSYEVCLTDTWSARTSSAG--IDLYSRLRRFNPAPYAAYFRIESVEVLSSSPERFLTVHGRDV 450
Cdd:pfam00425 1 EDYLAAVEKAKEAIRAGDLYKVVLSRRLTLPLAGDIdpLALYRRLRARNPAPYSFYFRTGDFTFLGASPERLLSVDGGRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 451 ETKPIKGTIPREEDP-------SALRTDAKTRAENLMIVDLLRNDLGRVCEPGTVTVPKLMHVETYATVHQLVSTVRGVL 523
Cdd:pfam00425 81 ITEPIAGTRPRGKDPaedealaAELLADPKERAEHLMVVDLIRNDLGRVCVPGSVKVPELPEVERYGTVQHLVSTISGRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 524 RPGTTLIDLLRAAFPGGSMTGAPKERTCAMISELEPGARGVYSGVAGYLGFNGRADLSILIRTAVKQGDTVEVGAGGAVV 603
Cdd:pfam00425 161 KPGLSLLDLLKALFPTGAVTGAPKKRAMEIIRELEPFPRGLYAGAVGYLDPDGDADFAVAIRTALVDNGRARLYAGAGIV 240
|
250
....*....|....*
gi 2537977332 604 WASHPAAEYEEKELK 618
Cdd:pfam00425 241 ADSDPEAEWEETEAK 255
|
|
| PabB-fungal |
TIGR01823 |
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ... |
2-626 |
9.83e-111 |
|
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a para-aminobenzoate synthesis enzyme, aminodeoxychorismate synthase, which acts on chorismate in a pathway that yields PABA, a precursor of folate.
Pssm-ID: 273821 [Multi-domain] Cd Length: 742 Bit Score: 349.20 E-value: 9.83e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 2 ILLIDNRDSYTYNLAHLIHAAAGEEPLVVRAD-DVEKYDLARRVEggEFSHIVISPGPGTPADDGDFRGSRLIIQAAG-- 78
Cdd:TIGR01823 8 VLFIDSYDSFTYNVVRLLEQQTDISVHVTTVHsDTFQDQLLELLP--LFDAIVVGPGPGNPNNAQDMGIISELWELANld 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 79 ETPVLGVCLGHQGLAHLAGASVQR-GAPHHGATSTITHSGEGIFAGLpQGFTAVRYHSLTVSEAPGVRVHAR--AEDGT- 154
Cdd:TIGR01823 86 EVPVLGICLGFQSLCLAQGADISRlPTPKHGQVYEMHTNDAAIFCGL-FSVKSTRYHSLYANPEGIDTLLPLclTEDEEg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 155 --VQGLEVVGRPHWGVQFHPESVLTDCG-VELLRNFLSLS-------------QLRVEYQCV------------------ 200
Cdd:TIGR01823 165 iiLMSAQTKKKPWFGVQYHPESCCSELGsGKLVSNFLKLAfinnvktgrwekkKLNGSFSDIssrldrtddrdpiykvke 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 201 ------------DVDLDTESTFRALAGESAEAFWLDSATGEG-FSILGTDRGS-----------LTRSHTFR-------- 248
Cdd:TIGR01823 245 kypsgttyvkqfEVSEDPKLTFEICNIIREPKFVMSSSVITGrYSIIALPNSAsqvfthygamlKTTVHYWQdteisytr 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 249 -----------LGEDDILDTLGAELAVRVDTSPLPDLPFTGGWVGYLGYEC------ATLTLPRLTPSAPSAYPDAWWVR 311
Cdd:TIGR01823 325 lkkclsgvdsdLDKSQFWITLGKFMENKKIDNPHREIPFIGGLVGILGYEIgsdlstQYIACGRCNDDENSLVPDAKLVF 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 312 PQSFIVYDHSAQRAHLMVLyrgAPDEET-RCLMGELVAATS-----ARASEGEIGVGVEKGSWRL--SREDYLARIGRIK 383
Cdd:TIGR01823 405 INRSIVIDHKQGKLYVQSL---DNTFPVaLEWSGELRDSFVrkkniKQSLSWPFYLPEEIDFVITfpDKEDYAKAFKACQ 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 384 EALASGDSYEVCLTDTWSARTS---SAGIDLYSRLRRFNPAPYAAYFRIESVEVLSSSPERFLTVhGRD--VETKPIKGT 458
Cdd:TIGR01823 482 DYLHAGDSYEMCLTTQTKVVPPaviSPDWEIYQRLRQRNPAPFSGFFRLKHIIFLSTSPEKFLEV-GMDthAKLRPIKGT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 459 IPREEDPSALRT-----DAKTRAENLMIVDLLRNDLGRVCEPGTVTVPKLMHVETYATVHQLVSTVRG-VLRPGTTL--- 529
Cdd:TIGR01823 561 VKKGPQMNLEKArrilkTPKEMGENLMILDLIRNDLYELVPKNDVHVEELMSVEEHATVYQLVSVVKAhGLTSASKKtry 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 530 --IDLLRAAFPGGSMTGAPKERTCAMISELEPGARGVYSGVAGYLGFNGRADLSILIRTAV--KQGDTVEVGAGGAVVWA 605
Cdd:TIGR01823 641 sgIDVLKHSLPPGSMTGAPKKRSVQLLQDVEGGARGIYSGVTGYWDVNGNGDFSVNIRCAFsyNGGTSWRIGAGGAVTVL 720
|
730 740
....*....|....*....|.
gi 2537977332 606 SHPAAEYEEKELKARAVTAAW 626
Cdd:TIGR01823 721 STPEGELEEMYNKLESNLQIF 741
|
|
| pabB |
TIGR00553 |
aminodeoxychorismate synthase, component I, bacterial clade; Members of this family, ... |
280-620 |
1.13e-108 |
|
aminodeoxychorismate synthase, component I, bacterial clade; Members of this family, aminodeoxychorismate synthase, component I (PabB), were designated para-aminobenzoate synthase component I until it was recognized that PabC, a lyase, completes the pathway of PABA synthesis. This family is closely related to anthranilate synthase component I (trpE), and both act on chorismate. The clade of PabB enzymes represented by this model includes sequences from Gram-positive and alpha and gamma Proteobacteria as well as Chlorobium, Nostoc, Fusobacterium and Arabidopsis. A closely related clade of fungal PabB enzymes is identified by TIGR01823, while another bacterial clade of potential PabB enzymes is more closely related to TrpE (TIGR01824). [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
Pssm-ID: 273133 Cd Length: 328 Bit Score: 330.11 E-value: 1.13e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 280 WVGYLGYECATltlprltPSAPSAYPDAWWVRPQsfivydhsaQRAHLMVLYRGAPDEETRclmgELVAATSARASEGEI 359
Cdd:TIGR00553 1 LVGYLSYEAGP-------DAAFEPYDAALLADHR---------RTPLLRFLVFERVEAQPR----AAVEAEDDAPADRQA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 360 GVGveKGSWRLSREDYLARIGRIKEALASGDSYEVCLTDTWSARTSSAGIDLYSRLRRFNPAPYAAYFRIESVEVLSSSP 439
Cdd:TIGR00553 61 PTS--DIQSEMTRAEYGEAIDQLQDYIRAGDCYQANLTQQFHATWDGDPLAAFRKLRRRQPAPFSAFLDLGDGAILSLSP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 440 ERFLTVHGRDVETKPIKGTIPREEDP-------SALRTDAKTRAENLMIVDLLRNDLGRVCEPGTVTVPKLMHVETYATV 512
Cdd:TIGR00553 139 ELFFSIDGSEIETRPIKGTLPRGADPqedraqaSALAESAKDRAENLMIVDLLRNDLGRIAEVGSVKVPELFVVETYPTV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 513 HQLVSTVRGVLRPGTTLIDLLRAAFPGGSMTGAPKERTCAMISELEPGARGVYSGVAGYLGFNGRADLSILIRTAVKQGD 592
Cdd:TIGR00553 219 HQLVSTITARLREDLTLSDLFRALFPGGSITGAPKVRAMEIIDELEPQPRGVYCGAIGYLSPEGDMDFNVAIRTLTLDGG 298
|
330 340
....*....|....*....|....*...
gi 2537977332 593 TVEVGAGGAVVWASHPAAEYEEKELKAR 620
Cdd:TIGR00553 299 RAVYGVGGGIVADSDPEAEYRECLLKAA 326
|
|
| PRK09070 |
PRK09070 |
aminodeoxychorismate synthase component I; |
199-625 |
4.47e-103 |
|
aminodeoxychorismate synthase component I;
Pssm-ID: 236371 [Multi-domain] Cd Length: 447 Bit Score: 320.11 E-value: 4.47e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 199 CVDVDLDTestFRALAGESAEAFWLDSATGE---GFSILGTDRGSLTRSH----TFRLGEDDILDTLGAE-LAVRVDTSP 270
Cdd:PRK09070 8 PADIDLLA---LHRLAPERYPALLESSASGTaqgRWDVLLLAQGKCLRLDpdgvTRQLLEGDFLDALDAAwQAERVPHDG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 271 LPDLPFTGGWVGYLGYECATLTLPRL-TPSAPSAYPDAWWVRPQSFIVYDHSAQRAHLMvlyrGAPDEETrcLMGELVAA 349
Cdd:PRK09070 85 ESSLPFRGGWAVLLDYELAGQVEPILkLPMRTDGLPLALALRAPAAVLRDRHSGRCVLV----AEPGREH--LLDQIEAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 350 TSARASEGEIGVGVEKGSwrLSRED---YLARIGRIKEALASGDSYEVCLTDTWSAR--TSSAGIDLYSRLRRFNPAPYA 424
Cdd:PRK09070 159 LAACAALPPLPVWLAPQA--VEEDPperFTDGVERVLDYIRAGDVFQVNLSRAWQAQfaNAVDPAALYARLRAANPAPFS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 425 AYFRIESVEVLSSSPERFLTVHGRDVETKPIKGTIPREEDPSA------LRTDAKTRAENLMIVDLLRNDLGRVCEPGTV 498
Cdd:PRK09070 237 GLFVAAGRAIVSSSPERLVSVQGGVVQTRPIAGTRPRFAGDDDaalireLVGHPKERAEHVMLIDLERNDLGRICAPGSV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 499 TVPKLMHVETYATVHQLVSTVRGVLRPGTTLIDLLRAAFPGGSMTGAPKERTCAMISELEPGARGVYSGVAGYLGFNGRA 578
Cdd:PRK09070 317 EVDELMTVESYAHVHHIVSNVRGRLRDGVTPGEVIRAVFPGGTITGCPKVRCMQIIAELEQTPRGAYTGSFGYLNRDGDM 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2537977332 579 DLSILIRTAVKQGDTVEVGAGGAVVWASHPAAEYEEKELKARAVTAA 625
Cdd:PRK09070 397 DLNILIRTAEVQGNQVRFRTGAGIVVDSDPERELDETRAKARGLLRA 443
|
|
| PabB-clade2 |
TIGR01824 |
aminodeoxychorismate synthase, component I, clade 2; This clade of sequences is more closely ... |
278-622 |
3.16e-101 |
|
aminodeoxychorismate synthase, component I, clade 2; This clade of sequences is more closely related to TrpE (anthranilate synthase, TIGR00564/TIGR01820/TIGR00565) than to the better characterized group of PabB enzymes (TIGR00553/TIGR01823). This clade includes one characterized enzyme from Lactococcus and the conserved function across the clade is supported by these pieces of evidence: 1) all genomes with a member in this clade also have a separate TrpE gene, 2) none of these genomes contain an aparrent PabB from any of the other PabB clades, 3) none of these sequences are found in a region of the genome in association with other Trp biosynthesis genes, 4) all of these genomes aparrently contain most if not all of the steps of the folate biosynthetic pathway (for which PABA is a precursor). Many of the sequences hit by this model are annotated as TrpE enzymes, however, we believe that all members of this clade are, in fact, PabB. The sequences from Bacillus halodurans and subtilus which score below the trusted cutoff for this model are also likely to be PabB enzymes, but are too closely related to TrpE to be separated at this time.
Pssm-ID: 130883 Cd Length: 355 Bit Score: 312.09 E-value: 3.16e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 278 GGWVGYLGYECATLTLPRL-TPSAPSAYPDAWWVRPQSFIVYDHSAQRAHLMVLYRGAPDEETRCLMGELVAATSARASE 356
Cdd:TIGR01824 1 GGRLGWLAYDVARRLEGIPdLGTSDGGWPVAADFRYEAAVARDHQRQIVALATVPAETEGEFATSSDQLPAVAAATSLPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 357 GEIGVGVEKGSWRLSREDYLARIGRIKEALASGDSYEVCLTDTWSARTSSAG--IDLYSRLRRFNPAPYAAYFRIESVEV 434
Cdd:TIGR01824 81 PDVGPLPVDLEASIDRAAYETGVRRIKDYIRAGDVFQANLSRRLTAPIAADVdpLQLFLALRAPNPAPYAIYLEEPGVDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 435 LSSSPERFLTVHGRDVETKPIKGTIPREEDP-------SALRTDAKTRAENLMIVDLLRNDLGRVCEPGTVTVPKLMHVE 507
Cdd:TIGR01824 161 ASASPELFLAREGRVVQTRPIAGTRPRGATLaedgalaAELLQHDKDRAEHVMIVDLERNDLGRVCATGTVRVPELCAVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 508 TYATVHQLVSTVRGVLRPGTTLIDLLRAAFPGGSMTGAPKERTCAMISELEPGARGVYSGVAGYLGFNGRADLSILIRTA 587
Cdd:TIGR01824 241 SYSHVHHLVSRVTGRLREGAGLADLIRALFPGGSITGAPKVRAMEIIDELEPQPRGPYTGSVGWIDADGNADLNILIRTL 320
|
330 340 350
....*....|....*....|....*....|....*
gi 2537977332 588 VKQGDTVEVGAGGAVVWASHPAAEYEEKELKARAV 622
Cdd:TIGR01824 321 EGGGAQLHFRTGAGIVADSDPAGEWDETEAKARAL 355
|
|
| PRK05940 |
PRK05940 |
anthranilate synthase component I; |
246-625 |
9.54e-92 |
|
anthranilate synthase component I;
Pssm-ID: 235651 [Multi-domain] Cd Length: 463 Bit Score: 291.25 E-value: 9.54e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 246 TFRLGEddILDTLGAELAVRVDTSPLPD-LPFTGGWVGYLGYECA--TLTLPRLTPSaPSAYPDAWWVRPQSFIVYDHSA 322
Cdd:PRK05940 67 TPKLGE--ILPFLRQLLARSLDPSALPEhLPFTGGWLGWLGYDLAweIERLPHLNPD-PLPFPVAYWYEPESFAILDHQE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 323 QRAHLMVlyrgAPDEETRCLMGELVAATSARASEGEIGVGVEKGSWRLSREDYLARIGRIKEALASGDSYEVCLTDTWSA 402
Cdd:PRK05940 144 QILWLAA----SDPSQLDRLEQQLEQPTPEPDLPLDLRTPPSSLIFYTTQQEYEAAVRQAKKYIQAGDIFQANLSLRFQT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 403 RTSSAGIDLYSRLRRFNPAPYAAYFRIESVEVLSSSPERFLTVHGRDVETKPIKGTIPREEDPSA-------LRTDAKTR 475
Cdd:PRK05940 220 TTSADSWQIYRRLQQINPSPFASYWRTPWGDVVSCSPERLVQLQGNQAQTRPIAGTRPRGKTPAEdqqlaeeLLSNIKER 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 476 AENLMIVDLLRNDLGRVCEPGTVTVPKLMHVETYATVHQLVSTVRGVLRPGTTLIDLLRAAFPGGSMTGAPKERTCAMIS 555
Cdd:PRK05940 300 AEHIMLVDLERNDLGRVCQWGSVEVDELLTIERYSHVIHLVSNVVGTLQPNRDAIDLIRALFPGGTITGCPKVRCMEIIE 379
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2537977332 556 ELEPGARGVYSGVAGYLGFNGRADLSILIRTAVK-----QGDTV--EVGAGgaVVWASHPAAEYEEKELKARAVTAA 625
Cdd:PRK05940 380 ELEPVRRNLFYGSCGYLDQRGNLDLNILIRTLLYtplsrGLSTIwgQVGAG--IVADSDPEKEWLESLQKAKAQLAA 454
|
|
| PRK07508 |
PRK07508 |
aminodeoxychorismate synthase component I; |
278-626 |
2.54e-88 |
|
aminodeoxychorismate synthase component I;
Pssm-ID: 236035 [Multi-domain] Cd Length: 378 Bit Score: 279.59 E-value: 2.54e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 278 GGWV-GYLGYECATLTLPRLTPSAPSAYPdawwvRPQ-SFIVYDHSAQRAHLmvlyrgapdeetrclmgelvaatSARAS 355
Cdd:PRK07508 45 GKWLaGYLSYEAGYLLEPKLAPLMPEGRE-----TPLlCFGVFDAPSPEAPA-----------------------PARPS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 356 EGEIGVGVEKGSWrlSREDYLARIGRIKEALASGDSYEVCLTDTWSARTSSAGIDLYSRLRRFNPAPYAAYFRIESVEVL 435
Cdd:PRK07508 97 ENAARLRDPVARW--DFADYAQRFERLHRHIRAGDCYQANLTFPLDARWGGDPLALFWALAARQPVGYGALVDLGGPVIL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 436 SSSPERFLTVHG-RDVETKPIKGTIPREEDP-------SALRTDAKTRAENLMIVDLLRNDLGRVCEPGTVTVPKLMHVE 507
Cdd:PRK07508 175 SRSPELFFRVDGeGWIETHPMKGTAPRGATPaedarlrAALLNDEKNQAENRMIVDLLRNDISRISEVGSLDVPELFDIE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 508 TYATVHQLVSTVRGVLRPGTTLIDLLRAAFPGGSMTGAPKERTCAMISELEPGARGVYSGVAGYLGFNGRADLSILIRT- 586
Cdd:PRK07508 255 TYPTVHQMVSRVRARLLPGLGLADIFAALFPCGSITGAPKIRAMEILRELEPGPRDLYCGAIGWIAPDGRMRFNVAIRTl 334
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2537977332 587 AVKQGDTVEVGAGGAVVWASHPAAEYEEKELKAR-AVTAAW 626
Cdd:PRK07508 335 SLFPGGRAVFNVGGGIVFDSTAEAEYEECLLKARfAVGDTP 375
|
|
| PRK13571 |
PRK13571 |
anthranilate synthase component I; Provisional |
208-625 |
7.81e-83 |
|
anthranilate synthase component I; Provisional
Pssm-ID: 184152 [Multi-domain] Cd Length: 506 Bit Score: 269.20 E-value: 7.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 208 STFRALAGESAEAFWLDSATGEG----FSILGTDRGSltrSHTFRLGE--------------DDILDTLGAELAvRVDTS 269
Cdd:PRK13571 38 GAYRKLAANRPGTFLLESAENGRswsrWSFIGVGSPA---ALTVRDGEavwlgtppagaptgGDPLAALRATLE-LLATP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 270 PLPDLP-FTGGWVGYLGYEcATLTLPRLTPSAPSAY--PDAWWVRPQSFIVYDHSAQRAHLM---VLYRGAPDEETRCL- 342
Cdd:PRK13571 114 RLPGLPpLTGGMVGFLGYD-AVRRLERLPELAVDDLglPEMLLLLATDLAAVDHHEGTITLIanaVNWNGTDERVDAAYd 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 343 --MGELVAATSARASEGEIGVGV---EKGSWRLSR--EDYLARIGRIKEALASGDSYEVCLTDTWSARTSSAGIDLYSRL 415
Cdd:PRK13571 193 daVARLDVMTAALAQPLPSTVATfsrPVPEFRAQRtvEEFGAAVEKLVEEIRAGEAFQVVPSQRFEMDTTADPLDVYRVL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 416 RRFNPAPYAAYFRIESV------EVLSSSPERFLTVHGRDVETKPIKGTIPREEDPSA-------LRTDAKTRAENLMIV 482
Cdd:PRK13571 273 RVTNPSPYMYLLRVPNSdggtdfSIVGSSPEALVTVTDGRATTHPIAGTRWRGATPEEdallekeLLADPKERAEHLMLV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 483 DLLRNDLGRVCEPGTVTVPKLMHVETYATVHQLVSTVRGVLRPGTTLIDLLRAAFPGGSMTGAPKERTCAMISELEPGAR 562
Cdd:PRK13571 353 DLGRNDLGRVCRPGTVRVVDFSHIERYSHVMHLVSTVTGELAEGRTALDAVTACFPAGTLSGAPKVRAMELIEELEPTRR 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2537977332 563 GVYSGVAGYLGFNGRADLSILIRTAVKQGDTVEVGAGGAVVWASHPAAEYEEKELKARAVTAA 625
Cdd:PRK13571 433 GLYGGVVGYLDFAGDADTAIAIRTALMRDGTAYVQAGGGVVADSDPDYEDNEARNKAAAVLRA 495
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
2-188 |
4.62e-81 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.
Pssm-ID: 153214 [Multi-domain] Cd Length: 184 Bit Score: 253.61 E-value: 4.62e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 2 ILLIDNRDSYTYNLAHLIhAAAGEEPLVVRADDVEKYDLARRveggEFSHIVISPGPGTPADDGDfrgSRLIIQA-AGET 80
Cdd:cd01743 1 ILLIDNYDSFTYNLVQYL-RELGAEVVVVRNDEITLEELELL----NPDAIVISPGPGHPEDAGI---SLEIIRAlAGKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 81 PVLGVCLGHQGLAHLAGASVQRGA-PHHGATSTITHSGEGIFAGLPQGFTAVRYHSLTVSEAP---GVRVHARAEDGTVQ 156
Cdd:cd01743 73 PILGVCLGHQAIAEAFGGKVVRAPePMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPlpdLLEVTASTEDGVIM 152
|
170 180 190
....*....|....*....|....*....|..
gi 2537977332 157 GLEVVGRPHWGVQFHPESVLTDCGVELLRNFL 188
Cdd:cd01743 153 ALRHRDLPIYGVQFHPESILTEYGLRLLENFL 184
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
2-190 |
8.67e-81 |
|
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440278 [Multi-domain] Cd Length: 189 Bit Score: 253.04 E-value: 8.67e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 2 ILLIDNRDSYTYNLAHLIhAAAGEEPLVVRADDVEkydlARRVEGGEFSHIVISPGPGTPADDGdfrGSRLIIQA-AGET 80
Cdd:COG0512 1 ILLIDNYDSFTYNLVQYL-GELGAEVVVVRNDEIT----LEEIEALAPDGIVLSPGPGTPEEAG---ISLEVIRAfAGKI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 81 PVLGVCLGHQGLAHLAGASVQR-GAPHHGATSTITHSGEGIFAGLPQGFTAVRYHSLTVSEA---PGVRVHARAEDGTVQ 156
Cdd:COG0512 73 PILGVCLGHQAIGEAFGGKVVRaPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDREtlpDELEVTAWTEDGEIM 152
|
170 180 190
....*....|....*....|....*....|....
gi 2537977332 157 GLEVVGRPHWGVQFHPESVLTDCGVELLRNFLSL 190
Cdd:COG0512 153 GIRHRELPIEGVQFHPESILTEHGHQLLANFLEL 186
|
|
| pabB |
PRK15465 |
aminodeoxychorismate synthase component 1; |
236-614 |
5.33e-74 |
|
aminodeoxychorismate synthase component 1;
Pssm-ID: 185362 [Multi-domain] Cd Length: 453 Bit Score: 244.44 E-value: 5.33e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 236 TDRGSLTR---SHTFRLGEDDILDTLGAEL-AVRVDTSPLPDLPFTGGWVGYLGYEcatltLPRLTPSAPS------AYP 305
Cdd:PRK15465 58 TTFGKETVvseSEKRTTTTDDPLQVLQQVLdRADIRPTHNEDLPFQGGALGLFGYD-----LGRRFESLPEiaeqdiVLP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 306 D-AWWVRPQSFIVyDHSAQRAHLM----VLYRGAPDEETRCLMGELVAATSARASEgeigvgvekgswrLSREDYLARIG 380
Cdd:PRK15465 133 DmAVGIYDWALIV-DHQRQTVSLLshndVNARRAWLESQQFSPQEDFTLTSDWQSN-------------MTREQYGEKFR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 381 RIKEALASGDSYEVCLTDTWSARTSSAGIDLYSRLRRFNPAPYAAYFRIESVEVLSSSPERFLTVHGRDVETKPIKGTIP 460
Cdd:PRK15465 199 QVQEYLHSGDCYQVNLAQRFHATYSGDEWQAFLQLNQANRAPFSAFLRLEQGAILSLSPERFILCDNSEIQTRPIKGTLP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 461 REEDPSA-------LRTDAKTRAENLMIVDLLRNDLGRVCEPGTVTVPKLMHVETYATVHQLVSTVRGVLRPGTTLIDLL 533
Cdd:PRK15465 279 RLPDPQEdskqaekLANSAKDRAENLMIVDLMRNDIGRVAVAGSVKVPELFVVEPFPAVHHLVSTITARLPEQLHASDLL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 534 RAAFPGGSMTGAPKERTCAMISELEPGARGVYSGVAGYLGFNGRADLSILIRTAVKQGDTVEVGAGGAVVWASHPAAEYE 613
Cdd:PRK15465 359 RAAFPGGSITGAPKVRAMEIIDELEPQRRNAWCGSIGYLSFCGNMDTSITIRTLTAINGQIYCSAGGGIVADSQEEAEYQ 438
|
.
gi 2537977332 614 E 614
Cdd:PRK15465 439 E 439
|
|
| PRK13574 |
PRK13574 |
anthranilate synthase component I; Provisional |
270-625 |
9.54e-72 |
|
anthranilate synthase component I; Provisional
Pssm-ID: 184155 [Multi-domain] Cd Length: 420 Bit Score: 237.41 E-value: 9.54e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 270 PLPDLP--FTGGWVGYLGYECATL--TLPRLTPsAPSAYPDAWWVRPQSFIVYDHSAQRAHLMvlyrgapdeetrclmGE 345
Cdd:PRK13574 70 KLVDIPglFKGGMIGYISYDAVRFweKIRDLKP-AAEDWPYAEFFIPDNIIIYDHNEGKVYVN---------------GD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 346 LVAATSArASEGEIGVGVEKGSwrLSREDYLARIGRIKEALASGDSYEVCLTDTWSARTSSAGIDLYSRLRRFNPAPYAA 425
Cdd:PRK13574 134 LSSVGGC-GDMGEFKISFYDES--LNKNNYEKIVSESLEYIRSGYIFQVVLSRFYRYLFSGDPLRIYYNLRRINPSPYMF 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 426 YFRIESVEVLSSSPERFLTVHGRDVETKPIKGTIPR----EED---PSALRTDAKTRAENLMIVDLLRNDLGRVCEPGTV 498
Cdd:PRK13574 211 YLKFDERYLIGSSPELLFRVQDNIVETYPIAGTRPRgsdqEEDlklELELMNSEKDKAEHLMLVDLARNDLGKVCVPGTV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 499 TVPKLMHVETYATVHQLVSTVRGVLRPGTTLIDLLRAAFPGGSMTGAPKERTCAMISELEPGARGVYSGVAGYLGFNGRA 578
Cdd:PRK13574 291 RVPELMYVEKYSHVQHIVSKVIGTLKKKYNALDVLKATFPAGTVSGAPKPMAMNIIETLEEYKRGPYAGAVGFISADGNA 370
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2537977332 579 DLSILIRTAVKQGDTVEVGAGGAVVWASHPAAEYEEKELKARAVTAA 625
Cdd:PRK13574 371 EFAIAIRTAFLNKDLLRIQAGAGIVYDSNPESEYFETEHKLRALKTA 417
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
1-192 |
1.62e-66 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 215.76 E-value: 1.62e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 1 MILLIDNRDSYTYNLAHLIhAAAGEEPLVVRADDVEKYDLARRVEGGefshIVISPGPGTPADDG---DfrgsrLIIQAA 77
Cdd:PRK05670 1 MILLIDNYDSFTYNLVQYL-GELGAEVVVYRNDEITLEEIEALNPDA----IVLSPGPGTPAEAGislE-----LIREFA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 78 GETPVLGVCLGHQGLAHLAGASVQR-GAPHHGATSTITHSGEGIFAGLPQGFTAVRYHSLTVSEA---PGVRVHARAEDG 153
Cdd:PRK05670 71 GKVPILGVCLGHQAIGEAFGGKVVRaKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVDREslpDCLEVTAWTDDG 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 2537977332 154 TVQGLEVVGRPHWGVQFHPESVLTDCGVELLRNFLSLSQ 192
Cdd:PRK05670 151 EIMGVRHKELPIYGVQFHPESILTEHGHKLLENFLELAR 189
|
|
| PRK13572 |
PRK13572 |
anthranilate synthase component I; Provisional |
276-625 |
3.19e-63 |
|
anthranilate synthase component I; Provisional
Pssm-ID: 237432 [Multi-domain] Cd Length: 435 Bit Score: 215.37 E-value: 3.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 276 FTGGWVGYLGYECATLTLPRL--TPSAPSAYPdawWVrpqsfIVYDHSAQRAHLMVLyRGAPDEETRclmGELVAATSAR 353
Cdd:PRK13572 86 FTGGFVGYIAYDAVHNYIGGKieEPSVFGYYD---HV-----FVYDHVTRKFYFHSL-NNNPEELFN---AEKIVEKAKR 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 354 ASEGEIGVGVEKGSWRLSREDYLARIGRIKEALASGDSYEVCLTDTWSARTSSAGIDLYSRLRRFNPAPYAAYFRIESVe 433
Cdd:PRK13572 154 FEIEEEDGGSEVLGCDADREEFVEMVEKAKEYIYSGDVFQVVLSREYRLKTDLSPFQLYRNLREINPSPYMFLLEFDKD- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 434 VLSSSPERFLTVHGRDVETKPIKGTIPR----EED---PSALRTDAKTRAENLMIVDLLRNDLGRVCEPGTVTVPKLMHV 506
Cdd:PRK13572 233 VVGASPETMASVENNILKINPIAGTAPRgkteEEDkklAEALLSDEKERAEHVMLVDLARNDVRKVSKSGSVRLERFFDV 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 507 ETYATVHQLVSTVRGVLRPGTTLIDLLRAAFPGGSMTGAPKERTCAMISELEPGARGVYSGVAGYLGFNGRADLSILIRT 586
Cdd:PRK13572 313 VKYSHVQHIESEVVGELKEDSTMFDAIEAAFPAGTLTGAPKFRAMEIIDELEKSRRKVYGGAVGYFSNSGNADLAIAIRM 392
|
330 340 350
....*....|....*....|....*....|....*....
gi 2537977332 587 AvKQGDTVEVGAGGAVVWASHPAAEYEEKELKARAVTAA 625
Cdd:PRK13572 393 A-EIDKVCRVRAGAGIVADSVPEKEFYETERKMAAVLKA 430
|
|
| PRK05877 |
PRK05877 |
aminodeoxychorismate synthase component I; Provisional |
268-619 |
1.61e-59 |
|
aminodeoxychorismate synthase component I; Provisional
Pssm-ID: 235634 [Multi-domain] Cd Length: 405 Bit Score: 204.55 E-value: 1.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 268 TSPLPDLPFTGGWVGYLGYecatltlPRLTPSA-PSAYPDAWWVRPQSFIVYDHSAQRAHLMVLyrGAPDEETrcLMGEL 346
Cdd:PRK05877 53 AGAAAPGAVGGGWFGYLSY-------PDAGADGrPPRIPEAAGGWTDHVLRRDRDGQWWYESLS--GAPDPDW--LASAL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 347 VAATSARASEGEIgvgvekgSWRLS-REDYLARIGRIKEALASGDSYEVCLTDTWSARTSSAGIDLY-SRLRRFNPApYA 424
Cdd:PRK05877 122 ATTRARPAPPCRI-------DWTPPdRAAHRDGVLACLEAIAAGEVYQACVCTQFTGTVTGSPLDFFaDGVARTAPA-RA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 425 AYFRIESVEVLSSSPERFLTVHGRDVETKPIKGTIPREEDPSALRTDAKTRAENLMIVDLLRNDLGRVCEPGTVTVPKLM 504
Cdd:PRK05877 194 AYLAGDWGAVASLSPELFLRRRGSVVTSSPIKGTLPLDADPSALRASAKDVAENIMIVDLVRNDLGRVARTGTVTVPELL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 505 HVETYATVHQLVSTVRGVLRPGTTLIDLLRAAFPGGSMTGAPKERTCAMISELEPGARGVYSGVAGYLGFNGRADLSILI 584
Cdd:PRK05877 274 VVRPAPGVWHLVSTVSAQVPDELPMSDLLDATFPPASVTGTPKLRARELISQWEPVRRGIYCGTVGLASPVAGCELNVAI 353
|
330 340 350
....*....|....*....|....*....|....*.
gi 2537977332 585 RTA-VKQGDTVEVGAGGAVVWASHPAAEYEEKELKA 619
Cdd:PRK05877 354 RTVeFDADGNAVLGVGGGITADSDPDAEWQECLHKA 389
|
|
| PLN02445 |
PLN02445 |
anthranilate synthase component I |
271-625 |
2.49e-58 |
|
anthranilate synthase component I
Pssm-ID: 215244 [Multi-domain] Cd Length: 523 Bit Score: 204.53 E-value: 2.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 271 LPDLpFTGGWVGYLGYECATLTLPRLTP--SAPS---AYPDAWWVRPQSFIVYDHSAQRAHLMVLYR----GAPDEETRC 341
Cdd:PLN02445 114 LPDV-FCGGWVGYFSYDTVRYVEKKKLPfsGAPEddrNLPDIHLGLYDDVIVFDHVEKKAYVIHWVRldrySSVEEAYED 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 342 LMGELVAATSA-------RASEGEI-------GVGVEKGSwrLSREDYLARIGRIKEALASGDSYEVCLTDTWSARTSSA 407
Cdd:PLN02445 193 GMKRLEALVSRlqdinppKLSPGSVklstnqfGPSLEKSN--MTSEEYKNAVLQAKEHILAGDIFQIVLSQRFERRTFAD 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 408 GIDLYSRLRRFNPAPYAAYFRIESVEVLSSSPERFLTVHGRDVETKPIKGTIPR----EED---PSALRTDAKTRAENLM 480
Cdd:PLN02445 271 PFEVYRALRIVNPSPYMIYLQARGCILVASSPEILTRVKKNKIVNRPLAGTRRRgktpEEDkalEKDLLADEKQCAEHIM 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 481 IVDLLRNDLGRVCEPGTVTVPKLMHVETYATVHQLVSTVRGVLRPGTTLIDLLRAAFPGGSMTGAPKERTCAMISELEPG 560
Cdd:PLN02445 351 LVDLGRNDVGKVSKAGSVKVEKLMNIERYSHVMHISSTVTGELLDHLTSWDALRAALPVGTVSGAPKVRAMELIDELEVT 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 561 ARGVYSGVAGYLGFNGRADLSILIRTAV----KQGDT--------------VEVGAGGAVVWASHPAAEYEEKELKARAV 622
Cdd:PLN02445 431 RRGPYSGGFGGVSFTGDMDIALALRTMVfptaARYDTmysykdtnsrrewvAHLQAGAGIVADSDPEDEYRECVNKAAGL 510
|
...
gi 2537977332 623 TAA 625
Cdd:PLN02445 511 ARA 513
|
|
| PRK13567 |
PRK13567 |
anthranilate synthase component I; Provisional |
266-622 |
3.48e-52 |
|
anthranilate synthase component I; Provisional
Pssm-ID: 184148 [Multi-domain] Cd Length: 468 Bit Score: 186.50 E-value: 3.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 266 VDTSPLPDLPFTGGWVGYLGYECATLTLPRLTPSAPSAYP--DAWWVRPQSFIVYDHsaQRAHLMV----LYRGAPDEET 339
Cdd:PRK13567 87 IQDEQLKSLPFISGYVGTCSFDLVRHEFPKLQSIQLEDHKqhDVRLYMVEQVYVFDH--YKDELYIiatnQFSNSTKSDL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 340 RCLMGELVAA----------TSARASEGEIGVGVekgswrlSREDYLARIGRIKEALASGDSYEVCLTDTWS------AR 403
Cdd:PRK13567 165 ENRVNKSIEDltkiqpfmptQDFDFKTKEIQSNI-------SEERFIEMIQYFKEKITEGDMFQVVPSRIYKyahhasQH 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 404 TSSAGIDLYSRLRRFNPAPYAAYFRIESVEVLSSSPERFLTVHGRDVETKPIKGTIPR-------EEDPSALRTDAKTRA 476
Cdd:PRK13567 238 LNQLSFQLYQNLKRQNPSPYMYYLNIDQPYIVGSSPESFVSVKDQIVTTNPIAGTIQRgettqidNENMKQLLNDPKECS 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 477 ENLMIVDLLRNDLGRVCEPGTVTVPKLMHVETYATVHQLVSTVRGVLRPGTTLIDLLRAAFPGGSMTGAPKERTCAMISE 556
Cdd:PRK13567 318 EHRMLVDLGRNDIHRVSKIGTSKITKLMVIEKYEHVMHIVSEVTGKINQNLSPMTVIANLLPTGTVSGAPKLRAIERIYE 397
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2537977332 557 LEPGARGVYSGVAGYLGFNGRADLSILIRTAVKQGDTVEVGAGGAVVWASHPAAEYEEKELKARAV 622
Cdd:PRK13567 398 QYPHKRGVYSGGVGYINCNHNLDFALAIRTMMIDEQYINVEAGCGVVYDSIPEKELNETKLKAKSL 463
|
|
| PRK06404 |
PRK06404 |
anthranilate synthase component I; Reviewed |
364-622 |
2.44e-49 |
|
anthranilate synthase component I; Reviewed
Pssm-ID: 102361 [Multi-domain] Cd Length: 351 Bit Score: 175.44 E-value: 2.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 364 EKGSwrLSREDYLARIGRIKEALASGDSYEVCLTdtwsaRTSSAGIDLYSRLRRF---NPAPYAAYFRIESVEVLSSSPE 440
Cdd:PRK06404 98 LKGN--YNDISLSLKIKELIELIRAGEVLQVVIS-----REFEANIDFKEKLSEFinnDRSRYVFYYRFGKYRVVGSSPE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 441 RFLTVHGRDVETKPIKGTIPREEDPSALRTDAKTRAENLMIVDLLRNDLGRVCEPGTVTVPKLMHVETYATVHQLVSTVR 520
Cdd:PRK06404 171 NVFTVNGNIINVDPIAGTYDDKILSNELLNSEKDKLEHRMLLDLARNDLSKFADIGTLNVDKVMKIEEFSSVKHLVSQVT 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 521 GVLrPGTTLIDLLRAAFPGGSMTGAPKERTCAMISELEPGARGVYSGVAGYLGfNGRADLSILIRTAVKQGDTVEVGAGG 600
Cdd:PRK06404 251 AKF-SNASYRDILASMFPAGTVSGSPKERAIEIINKYEETPRGPYGGAIGIIS-KGYTDMALVIRTAYSHGNGFRVRAGA 328
|
250 260
....*....|....*....|..
gi 2537977332 601 AVVWASHPAAEYEEKELKARAV 622
Cdd:PRK06404 329 GIVKDSDPEDEVNEIYSKARSV 350
|
|
| PRK13564 |
PRK13564 |
anthranilate synthase component 1; |
266-625 |
9.46e-48 |
|
anthranilate synthase component 1;
Pssm-ID: 237428 [Multi-domain] Cd Length: 520 Bit Score: 175.41 E-value: 9.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 266 VDTSPLPDLP-FTGGWVGY---LGYEcatlTLPRLTpsAPSAYPDAWWVRPQSFIVYDHSAQRAHLM-VLYRGAPDEETR 340
Cdd:PRK13564 134 VNTPKEEREAlFLGGLFAYdlvAGFE----PLPQLP--AGNNCPDYCFYLAETLLVIDHQKKSARLQaSLFTPDEEEKQR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 341 C------LMGELVAATSARASEGEIGVGVekgSWRLSREDYLARIGRIKEALASGDSYEV---------CLtDTWSArts 405
Cdd:PRK13564 208 LaarlaqLKQQLTQPAPPLPVTSVPDMEV---SVNISDEEFCAVVRKLKEHIRAGDIFQVvpsrrfslpCP-SPLAA--- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 406 sagidlYSRLRRFNPAPYAAYFRIESVEVLSSSPERFL--TVHGRDVETKPIKGTIPREEDPSA-------------LRT 470
Cdd:PRK13564 281 ------YRVLKKSNPSPYMFYMQDEDFTLFGASPESALkyDASSRQVEIYPIAGTRPRGRRADGsidrdldsrieleLRT 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 471 DAKTRAENLMIVDLLRNDLGRVCEPGTVTVPKLMHVETYATVHQLVSTVRGVLRPGttlIDLL---RAAFPGGSMTGAPK 547
Cdd:PRK13564 355 DHKELAEHLMLVDLARNDLARICQPGSRYVADLLKVDRYSHVMHLVSRVVGELRHD---LDALhayRACMNMGTLTGAPK 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 548 ERtcAM--ISELEPGARGVYSGVAGYLGFNGRADLSILIRTA-VKQG-DTVEVGAGgaVVWASHPAAEYEEKELKARAVT 623
Cdd:PRK13564 432 VR--AMqlIREVEGQRRGSYGGAVGYLTGHGDLDTCIVIRSAfVENGiATVQAGAG--VVLDSDPQSEADETRNKAQAVL 507
|
..
gi 2537977332 624 AA 625
Cdd:PRK13564 508 RA 509
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
1-221 |
1.03e-47 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 175.68 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 1 MILLIDNRDSYTYNLAHLIHAAAGEEPLVVRADDVEkydlARRVEGGEFSHIVISPGPGTPADDGDfrGSRLIIQAAGET 80
Cdd:PRK14607 1 MIILIDNYDSFTYNIYQYIGELGPEEIEVVRNDEIT----IEEIEALNPSHIVISPGPGRPEEAGI--SVEVIRHFSGKV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 81 PVLGVCLGHQGLAHLAGASVQRgAPH--HGATSTITHSGEGIFAGLPQGFTAVRYHSLTVSEA--PGV-RVHARAEDGTV 155
Cdd:PRK14607 75 PILGVCLGHQAIGYAFGGKIVH-AKRilHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEAslPEClEVTAKSDDGEI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2537977332 156 QGLEVVGRPHWGVQFHPESVLTDCGVELLRNFLSLSqlRVEYQCVDVdLDTESTFRALAGESAEAF 221
Cdd:PRK14607 154 MGIRHKEHPIFGVQFHPESILTEEGKRILKNFLNYQ--REEIDIKSY-LKKLVEGEDLSFEEAEDV 216
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
1-191 |
7.85e-46 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 160.67 E-value: 7.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 1 MILLIDNRDSYTYNLAHLIhAAAGEEPLVVRAD--DVEKYDLArrveggEFSHIVISPGPGTPADDGDFRGsrLIIQAAG 78
Cdd:CHL00101 1 MILIIDNYDSFTYNLVQSL-GELNSDVLVCRNDeiDLSKIKNL------NIRHIIISPGPGHPRDSGISLD--VISSYAP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 79 ETPVLGVCLGHQGLAHLAGASVQRgAPH--HGATSTITHSGEGIFAGLPQGFTAVRYHSLTVSEA---PGVRVHARAEDG 153
Cdd:CHL00101 72 YIPILGVCLGHQSIGYLFGGKIIK-APKpmHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIDPLnlpSPLEITAWTEDG 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 2537977332 154 TVQGLEVVGRPH-WGVQFHPESVLTDCGVELLRNFLSLS 191
Cdd:CHL00101 151 LIMACRHKKYKMlRGIQFHPESLLTTHGQQILRNFLSLS 189
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
2-220 |
8.21e-45 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 158.67 E-value: 8.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 2 ILLIDNRDSYTYNLAHLIhAAAGEEPLVVRADDVEKYDLARRVEGgeFSHIVISPGPGTPADDGdfrGSRLIIQ--AAGE 79
Cdd:PRK07765 3 ILVVDNYDSFVFNLVQYL-GQLGVEAEVWRNDDPRLADEAAVAAQ--FDGVLLSPGPGTPERAG---ASIDMVRacAAAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 80 TPVLGVCLGHQGLAHLAGASVQRgAPH--HGATSTITHSGEGIFAGLPQGFTAVRYHSLTVSEA---PGVRVHARAEDGT 154
Cdd:PRK07765 77 TPLLGVCLGHQAIGVAFGATVDR-APEllHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTILPEtlpAELEVTARTDSGV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2537977332 155 VQGLEVVGRPHWGVQFHPESVLTDCGVELLRNFLSlsqlrveyQCVDVDLDTEStfRALAGESAEA 220
Cdd:PRK07765 156 IMAVRHRELPIHGVQFHPESVLTEGGHRMLANWLT--------VCGWAPDEALV--RRLENEVAAA 211
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
3-188 |
2.87e-44 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 156.24 E-value: 2.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 3 LLIDNRDSYTYNLAHLIhAAAGEEPLVVRADDvekydLARRVEGGEFSHIVISPGPGTPADDGdfrGSRLIIQAAGE--T 80
Cdd:pfam00117 1 LLIDNGDSFTYNLARAL-RELGVEVTVVPNDT-----PAEEILEENPDGIILSGGPGSPGAAG---GAIEAIREARElkI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 81 PVLGVCLGHQGLAHLAGASVQRGA--PHHGATSTITHSGEGIFAGLPQGFTAVRYHSLTV---SEAPGVRV-HARAEDGT 154
Cdd:pfam00117 72 PILGICLGHQLLALAFGGKVVKAKkfGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVdpdTLPDGLEVtATSENDGT 151
|
170 180 190
....*....|....*....|....*....|....
gi 2537977332 155 VQGLEVVGRPHWGVQFHPESVLTDCGVELLRNFL 188
Cdd:pfam00117 152 IMGIRHKKLPIFGVQFHPESILTPHGPEILFNFF 185
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
1-190 |
5.12e-43 |
|
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.
Pssm-ID: 273144 [Multi-domain] Cd Length: 188 Bit Score: 153.02 E-value: 5.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 1 MILLIDNRDSYTYNLAHLIhAAAGEEPLVVRADDVEKYDLARRVEggefSHIVISPGPGTPADDGdfRGSRLIIQAAGET 80
Cdd:TIGR00566 1 MVLMIDNYDSFTYNLVQYF-CELGAEVVVKRNDSLTLQEIEALLP----LLIVISPGPCTPNEAG--ISLEAIRHFAGKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 81 PVLGVCLGHQGLAHLAGASVQRGAP-HHGATSTITHSGEGIFAGLPQGFTAVRYHSLTVsEAPGVRVHARAEDGTVQGLE 159
Cdd:TIGR00566 74 PILGVCLGHQAMGQAFGGDVVRANTvMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVV-EPETLPTCFPVTAWEEENIE 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 2537977332 160 VVGRPH-----WGVQFHPESVLTDCGVELLRNFLSL 190
Cdd:TIGR00566 153 IMAIRHrdlplEGVQFHPESILSEQGHQLLANFLHR 188
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
1-188 |
5.86e-42 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 150.34 E-value: 5.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 1 MILLIDNRDSYTYNLAHLIhAAAGEEPLVVRADDVEKYDLARRVEggEFshIVISPGPGTPADDGDfrgSRLIIQA-AGE 79
Cdd:PRK07649 1 MILMIDNYDSFTFNLVQFL-GELGQELVVKRNDEVTISDIENMKP--DF--LMISPGPCSPNEAGI---SMEVIRYfAGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 80 TPVLGVCLGHQGLAHLAGASVQRgAPH--HGATSTITHSGEGIFAGLPQGFTAVRYHSLTVSEA--PG-VRVHARAEDGT 154
Cdd:PRK07649 73 IPIFGVCLGHQSIAQVFGGEVVR-AERlmHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIVKKEtlPDcLEVTSWTEEGE 151
|
170 180 190
....*....|....*....|....*....|....
gi 2537977332 155 VQGLEVVGRPHWGVQFHPESVLTDCGVELLRNFL 188
Cdd:PRK07649 152 IMAIRHKTLPIEGVQFHPESIMTSHGKELLQNFI 185
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
312-625 |
7.22e-41 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 158.54 E-value: 7.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 312 PQSFIVYDHSAQRAHLMvLYRGAPDE-ETRCLMGELVAATSARASEGEIGVGVEKGswrlsreDYLARIGRIKEALASGD 390
Cdd:PRK13566 190 PDEILVVDHYAARAWVD-RYEFAVGGvSTEGLPRETAPSPYKPTTARPGFADHAPG-------EYAALVEKAKESFRRGD 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 391 SYEVCLTDTWSARTSSAGIDLYSRLRRFNPAPYAAYFRIESVEVL-SSSPERFLTVHGRDVETKPIKGTIPREEDPSA-- 467
Cdd:PRK13566 262 LFEVVPGQTFYEPCERSPSEIFRRLKEINPSPYGFFINLGDGEYLvGASPEMFVRVEGRRVETCPISGTIKRGADAIGda 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 468 -----LRTDAKTRAENLMIVDLLRNDLGRVCEPGTVTVPKLMHVETYATVHQLVSTVRGVLRPGTTLIDllraAFPGG-- 540
Cdd:PRK13566 342 eqirkLLNSKKDESELTMCTDVDRNDKSRVCEPGSVKVIGRRQIEMYSRLIHTVDHVEGRLRPGFDALD----AFLTHaw 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 541 --SMTGAPKERTCAMISELEPGARGVYSGVAGYLGFNGRADLSILIRTAVKQGDTVEVGAGGAVVWASHPAAEYEEKELK 618
Cdd:PRK13566 418 avTVTGAPKLWAMQFIEDHERSPRRWYGGAVGMVGFDGDMNTGLTLRTIRIKDGVAEVRVGATLLFDSDPEAEEAETELK 497
|
....*..
gi 2537977332 619 ARAVTAA 625
Cdd:PRK13566 498 ASALLQA 504
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
1-189 |
7.76e-40 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 144.29 E-value: 7.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 1 MILLIDNRDSYTYNLAHLIhAAAGEEPLVVRADDVEKYDLARRVEggefSHIVISPGPGTPADDGdfRGSRLIIQAAGET 80
Cdd:PRK08007 1 MILLIDNYDSFTWNLYQYF-CELGADVLVKRNDALTLADIDALKP----QKIVISPGPCTPDEAG--ISLDVIRHYAGRL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 81 PVLGVCLGHQGLAHLAGASVQRGAP-HHGATSTITHSGEGIFAGLPQGFTAVRYHSLTVSEAP---GVRVHARAEDGTVQ 156
Cdd:PRK08007 74 PILGVCLGHQAMAQAFGGKVVRAAKvMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSlpaCFEVTAWSETREIM 153
|
170 180 190
....*....|....*....|....*....|...
gi 2537977332 157 GLEVVGRPHWGVQFHPESVLTDCGVELLRNFLS 189
Cdd:PRK08007 154 GIRHRQWDLEGVQFHPESILSEQGHQLLANFLH 186
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
1-188 |
3.74e-39 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 142.31 E-value: 3.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 1 MILLIDNRDSYTYNLAHLIhAAAGEEPLVVRADDVEKYDLARRVEggefSHIVISPGPGTPADDGDFRGSrlIIQAAGET 80
Cdd:PRK06774 1 MLLLIDNYDSFTYNLYQYF-CELGTEVMVKRNDELQLTDIEQLAP----SHLVISPGPCTPNEAGISLAV--IRHFADKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 81 PVLGVCLGHQGLAHLAGASVQRGAP-HHGATSTITHSGEGIFAGLPQGFTAVRYHSLTVSEA--PG-VRVHARAE-DGTV 155
Cdd:PRK06774 74 PILGVCLGHQALGQAFGARVVRARQvMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLVIAADslPGcFELTAWSErGGEM 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 2537977332 156 QglEVVGRPHW-----GVQFHPESVLTDCGVELLRNFL 188
Cdd:PRK06774 154 D--EIMGIRHRtlpleGVQFHPESILSEQGHQLLDNFL 189
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
1-189 |
1.92e-38 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 140.40 E-value: 1.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 1 MILLIDNRDSYTYNLAHLIhAAAGEEPLVVRADDVekyDLARrVEGGEFSHIVISPGPGTPADDGdfRGSRLIIQAAGET 80
Cdd:PRK08857 1 MLLMIDNYDSFTYNLYQYF-CELGAQVKVVRNDEI---DIDG-IEALNPTHLVISPGPCTPNEAG--ISLQAIEHFAGKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 81 PVLGVCLGHQGLAHLAGASVQRGAP-HHGATSTITHSGEGIFAGLPQGFTAVRYHSL-----TVSEAPGVRVHARAEDGT 154
Cdd:PRK08857 74 PILGVCLGHQAIAQVFGGQVVRARQvMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLvvkndTLPECFELTAWTELEDGS 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2537977332 155 VQglEVVGRPHW-----GVQFHPESVLTDCGVELLRNFLS 189
Cdd:PRK08857 154 MD--EIMGFQHKtlpieAVQFHPESIKTEQGHQLLANFLA 191
|
|
| PRK07093 |
PRK07093 |
para-aminobenzoate synthase component I; Validated |
370-614 |
1.76e-36 |
|
para-aminobenzoate synthase component I; Validated
Pssm-ID: 235932 [Multi-domain] Cd Length: 323 Bit Score: 139.23 E-value: 1.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 370 LSREDYLARIGRIKEALASGDSYEVCLTDTWSARTSSAGIDLYSRLRrfnpAPYAAYFRIESVevlSSSPERFLTVHGRD 449
Cdd:PRK07093 71 ISFEEYQQGFELVQEEIQAGNSYLLNLTYPTPIETNLSLEEIFQASK----AKYKLLFKDQFV---CFSPEPFVRIEDNK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 450 VETKPIKGTIPREEdPSA---LRTDAKTRAENLMIVDLLRNDLGRVCEpgTVTVPKLMHVETYATVH----QLVSTVRGV 522
Cdd:PRK07093 144 ISTYPMKGTIDASL-PNAeekLLNDEKEFAEHATIVDLLRNDLSMVAK--NVRVTRFRYIDKIKTNKgeilQTSSEISGT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 523 LRP------GTTLIDLLraafPGGSMTGAPKERTCAMISELEPGARGVYSGVAGYlgFNGRA-DLSILIRTAVKQGDTVE 595
Cdd:PRK07093 221 LPEnwqeniGDILAKLL----PAGSITGAPKEKTVEIIEQAEGYERGFYTGVFGY--FDGESlDSAVMIRFIEQENDGLY 294
|
250
....*....|....*....
gi 2537977332 596 VGAGGAVVWASHPAAEYEE 614
Cdd:PRK07093 295 FKSGGGITIDSDLKDEYNE 313
|
|
| MenF |
COG1169 |
Isochorismate synthase EntC [Coenzyme transport and metabolism, Secondary metabolites ... |
370-627 |
4.58e-36 |
|
Isochorismate synthase EntC [Coenzyme transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; Isochorismate synthase EntC is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440783 [Multi-domain] Cd Length: 353 Bit Score: 138.75 E-value: 4.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 370 LSREDYLARIGRIKEALASGD--------SYEVCLTDTWSARtssagiDLYSRLRRFNPAPYAAYFRIESVEVL-SSSPE 440
Cdd:COG1169 86 PDPAEWREAVAQALEAIRAGEldkvvlarALDLTLDEPIDPR------ALLARLRRRNPDCYTFAVELGAGDGFvGASPE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 441 RFLTVHGRDVETKPIKGTIPREEDPS-------ALRTDAKTRAENLMIVDLLRNDLGRVCEpgTVTVPKLMHVETYATVH 513
Cdd:COG1169 160 RLVRRRGGQLTTEALAGTAPRGADPEedaalaaALLASEKDRREHALVVDSIREALAPLCS--SLDVPEEPELLRLRNVQ 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 514 QLVSTVRGVLRPGTTLIDLLRAAFPGGSMTGAPKERTCAMISELEPGARGVYSGVAGYLGFNGRADLSILIRTAVKQGDT 593
Cdd:COG1169 238 HLATPITGTLDPGVSALDLAAALHPTPAVGGTPREAALALIRELEPFDRGWYAGPVGWVDADGDGEFAVAIRSALIDGNR 317
|
250 260 270
....*....|....*....|....*....|....
gi 2537977332 594 VEVGAGGAVVWASHPAAEYEEKELKARAVTAAWQ 627
Cdd:COG1169 318 ARLFAGAGIVAGSDPEAEWAETEAKLRTMLRALG 351
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
2-190 |
1.31e-34 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 130.69 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 2 ILLIDNRDSYTYNLAHLIhAAAGEEPLVVRADDVEKYDLARRVEGGefshIVISPGPGTPADDGDfrgSRLIIQAAG-ET 80
Cdd:PLN02335 21 IIVIDNYDSFTYNLCQYM-GELGCHFEVYRNDELTVEELKRKNPRG----VLISPGPGTPQDSGI---SLQTVLELGpLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 81 PVLGVCLGHQGLAHLAGASVQRgAPH---HGATSTITHS---GEGIFAGLPQGFTAVRYHSLTVSEA--PG--VRVHARA 150
Cdd:PLN02335 93 PLFGVCMGLQCIGEAFGGKIVR-SPFgvmHGKSSPVHYDekgEEGLFSGLPNPFTAGRYHSLVIEKDtfPSdeLEVTAWT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2537977332 151 EDGTVQGLEVVGRPH-WGVQFHPESVLTDCGVELLRNFLSL 190
Cdd:PLN02335 172 EDGLIMAARHRKYKHiQGVQFHPESIITTEGKTIVRNFIKI 212
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
2-190 |
7.82e-32 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 131.19 E-value: 7.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 2 ILLIDNRDSYTYNLAHLIHAAaGEEPLVVRAD------DVEKYDLarrveggefshIVISPGPGTPADdgdFRGSRLIIQ 75
Cdd:PRK13566 529 VLLVDHEDSFVHTLANYFRQT-GAEVTTVRYGfaeemlDRVNPDL-----------VVLSPGPGRPSD---FDCKATIDA 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 76 A-AGETPVLGVCLGHQGLAHLAGASVQRGA-PHHGATSTITHSG-EGIFAGLPQGFTAVRYHSLTVSEA---PGVRVHAR 149
Cdd:PRK13566 594 AlARNLPIFGVCLGLQAIVEAFGGELGQLAyPMHGKPSRIRVRGpGRLFSGLPEEFTVGRYHSLFADPEtlpDELLVTAE 673
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2537977332 150 AEDGTVQGLEVVGRPHWGVQFHPESVLT---DCGVELLRNFLSL 190
Cdd:PRK13566 674 TEDGVIMAIEHKTLPVAAVQFHPESIMTlggDVGLRIIENVVRL 717
|
|
| PRK09522 |
PRK09522 |
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ... |
2-198 |
1.73e-31 |
|
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;
Pssm-ID: 181927 [Multi-domain] Cd Length: 531 Bit Score: 128.99 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 2 ILLIDNRDSYTYNLAHLIHAAAgeEPLVVRADDVEKYDLARRVEGGEFSHIVISPGPGTPADDGDFrgSRLIIQAAGETP 81
Cdd:PRK09522 4 ILLLDNIDSFTYNLADQLRSNG--HNVVIYRNHIPAQTLIERLATMSNPVLMLSPGPGVPSEAGCM--PELLTRLRGKLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 82 VLGVCLGHQGLAHLAGASV-QRGAPHHGATSTITHSGEGIFAGLPQGFTAVRYHSLTVSEAP-GVRVHARAEdGTVQGLE 159
Cdd:PRK09522 80 IIGICLGHQAIVEAYGGYVgQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSNIPaGLTINAHFN-GMVMAVR 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 2537977332 160 VVGRPHWGVQFHPESVLTDCGVELLRNFLSLSQLRVEYQ 198
Cdd:PRK09522 159 HDADRVCGFQFHPESILTTQGARLLEQTLAWAQQKLEPT 197
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
1-191 |
2.51e-27 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 109.06 E-value: 2.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 1 MILLIDNRDSYTYNLAHLIHAAAGEEPLVvradDVEKYDLarrVEGGEFSHIVISPGPGTP-ADDGDFRgsrLIIQAAGE 79
Cdd:PRK06895 3 KLLIINNHDSFTFNLVDLIRKLGVPMQVV----NVEDLDL---DEVENFSHILISPGPDVPrAYPQLFA---MLERYHQH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 80 TPVLGVCLGHQGLAHLAGASVQR-GAPHHG-ATSTITHSGEGIFAGLPQGFTAVRYHSLTVSE----APgVRVHARAEDG 153
Cdd:PRK06895 73 KSILGVCLGHQTLCEFFGGELYNlNNVRHGqQRPLKVRSNSPLFDGLPEEFNIGLYHSWAVSEenfpTP-LEITAVCDEN 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 2537977332 154 TVQGLEVVGRPHWGVQFHPESVLTDCGVELLRNFLSLS 191
Cdd:PRK06895 152 VVMAMQHKTLPIYGVQFHPESYISEFGEQILRNWLAIS 189
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
2-188 |
4.47e-24 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153213 [Multi-domain] Cd Length: 181 Bit Score: 99.53 E-value: 4.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 2 ILLIDNRDSYTynlaHLIHAAAGEepLVVRADDVEKYDLARRVEGGEFSHIVISPGPGTPADDGDFRGSRLIIQAagETP 81
Cdd:cd01742 1 ILILDFGSQYT----HLIARRVRE--LGVYSEILPNTTPLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFEL--GVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 82 VLGVCLGHQGLAHLAGASVQRG-APHHGATS-TITHSGEgIFAGLPQGFTAVRYHSLTVSEAP-GVRVHARAEDGTVQGL 158
Cdd:cd01742 73 VLGICYGMQLIAKALGGKVERGdKREYGKAEiEIDDSSP-LFEGLPDEQTVWMSHGDEVVKLPeGFKVIASSDNCPVAAI 151
|
170 180 190
....*....|....*....|....*....|
gi 2537977332 159 EVVGRPHWGVQFHPESVLTDCGVELLRNFL 188
Cdd:cd01742 152 ANEEKKIYGVQFHPEVTHTEKGKEILKNFL 181
|
|
| PRK05637 |
PRK05637 |
anthranilate synthase component II; Provisional |
2-180 |
6.01e-22 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 180178 [Multi-domain] Cd Length: 208 Bit Score: 94.14 E-value: 6.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 2 ILLIDNRDSYTYNLAHLIhAAAGEEPLVVRAD-DVEKydlarrVEGGEFSHIVISPGPGTPADDGDFRgsRLIIQAAGET 80
Cdd:PRK05637 4 VVLIDNHDSFVYNLVDAF-AVAGYKCTVFRNTvPVEE------ILAANPDLICLSPGPGHPRDAGNMM--ALIDRTLGQI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 81 PVLGVCLGHQGLAHLAGASVQRGAPHHGATSTITHSGEG----IFAGLPQGFT------------AVRYHSLTVSEAPG- 143
Cdd:PRK05637 75 PLLGICLGFQALLEHHGGKVEPCGPVHGTTDNMILTDAGvqspVFAGLATDVEpdhpeipgrkvpIARYHSLGCVVAPDg 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2537977332 144 -------------VRVHARAEDGTVQGLevvgrphwgvQFHPESVLTDCG 180
Cdd:PRK05637 155 meslgtcsseigpVIMAAETTDGKAIGL----------QFHPESVLSPTG 194
|
|
| PRK07054 |
PRK07054 |
isochorismate synthase; |
411-625 |
4.28e-21 |
|
isochorismate synthase;
Pssm-ID: 235920 [Multi-domain] Cd Length: 475 Bit Score: 96.76 E-value: 4.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 411 LYSRLRRFNPAPYAAYFRIESVEVLSSSPERFLTVHGRDVETKPIKGTIPREEDP-------SALRTDAKTRAENLMIVD 483
Cdd:PRK07054 235 LLRRLRLRDPHAHLFAFRRGNACFLGATPERLVRVAAGDLHTHALAGTIARGADPaedarlgAALMASAKDRLEHALVVD 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 484 LLRNDLGRVCEpgTVTVPKLMHVETYATVHQLVSTVRGVLRPGTTLIDLLRAAFPGGSMTGAPKERTCAMISELEPGARG 563
Cdd:PRK07054 315 AIRAALAPLSR--ALDIPDQPSLHRLPRLQHLSTPIRATLAPDATLLQVVAALHPTPAVGGHPRAAALDYIRAHEGFDRG 392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2537977332 564 VYSGVAGYLGFNGRADLSILIRTAVKQGDTVEVGAGGAVVWASHPAAEYEEKELKARAVTAA 625
Cdd:PRK07054 393 WYAAPIGWLDAHGNGDFAVALRSALITGGACRLFAGCGIVADSEPASEYRETCLKLSGMREA 454
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
2-173 |
1.90e-19 |
|
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440284 [Multi-domain] Cd Length: 225 Bit Score: 87.69 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 2 ILLIDNRDSYTyNLAHLIH---AAAGEEPLVVRADDVEKYDLARRVEggEFSHIVISPGPGTPADDGDF-RGSRLIIQAA 77
Cdd:COG0518 2 ILILDHDPFGG-QYPGLIArrlREAGIELDVLRVYAGEILPYDPDLE--DPDGLILSGGPMSVYDEDPWlEDEPALIREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 78 GE--TPVLGVCLGHQGLAHLAGASVQRGaPHHG---ATSTITHSGEgIFAGLPQGFTAVRYHSLTVSEAP-GVRVHARAE 151
Cdd:COG0518 79 FElgKPVLGICYGAQLLAHALGGKVEPG-PGREigwAPVELTEADP-LFAGLPDEFTVWMSHGDTVTELPeGAEVLASSD 156
|
170 180
....*....|....*....|..
gi 2537977332 152 DGTVQGLEvVGRPHWGVQFHPE 173
Cdd:COG0518 157 NCPNQAFR-YGRRVYGVQFHPE 177
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
2-189 |
4.60e-19 |
|
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 129966 [Multi-domain] Cd Length: 188 Bit Score: 85.44 E-value: 4.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 2 ILLIDNRDSYTynlaHLIHAA---AGEEPLVVRADDVEKYDLARRVEGgefshIVISPGPGTPADDGDFRGSRLIIQAag 78
Cdd:TIGR00888 1 ILVLDFGSQYT----QLIARRlreLGVYSELVPNTTPLEEIREKNPKG-----IILSGGPSSVYAENAPRADEKIFEL-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 79 ETPVLGVCLGHQGLAHLAGASVQRG-APHHGATST-ITHSGEgIFAGLPQGFTAVRYHSLTVSEAP-GVRVHARAEDGTV 155
Cdd:TIGR00888 70 GVPVLGICYGMQLMAKQLGGEVGRAeKREYGKAELeILDEDD-LFRGLPDESTVWMSHGDKVKELPeGFKVLATSDNCPV 148
|
170 180 190
....*....|....*....|....*....|....
gi 2537977332 156 QGLEVVGRPHWGVQFHPESVLTDCGVELLRNFLS 189
Cdd:TIGR00888 149 AAMAHEEKPIYGVQFHPEVTHTEYGNELLENFVY 182
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
17-188 |
1.50e-17 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153212 [Multi-domain] Cd Length: 188 Bit Score: 81.14 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 17 HLIHAAAGEEPLvvradDVEKYDLarrveggefshIVISPGPGTPADDGDF---RGSRLIIQA-AGETPVLGVCLGHQGL 92
Cdd:cd01741 31 DVVDVYAGELLP-----DLDDYDG-----------LVILGGPMSVDEDDYPwlkKLKELIRQAlAAGKPVLGICLGHQLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 93 AHLAGASVQRGapHHGA---TSTITHSGEG----IFAGLPQGFTAVRYHSLTVSEAP-GVRVHARAEDGTVQGLEvVGRP 164
Cdd:cd01741 95 ARALGGKVGRN--PKGWeigWFPVTLTEAGkadpLFAGLPDEFPVFHWHGDTVVELPpGAVLLASSEACPNQAFR-YGDR 171
|
170 180
....*....|....*....|....
gi 2537977332 165 HWGVQFHPESvltdcgvELLRNFL 188
Cdd:cd01741 172 ALGLQFHPEE-------RLLRNFL 188
|
|
| PRK06772 |
PRK06772 |
salicylate synthase; |
416-622 |
1.56e-17 |
|
salicylate synthase;
Pssm-ID: 102546 [Multi-domain] Cd Length: 434 Bit Score: 85.56 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 416 RRFNPAPYAAYFRIESVEVLSSSPERFLTVHGRDVETKPIKGTIPREEDP-------SALRTDAKTRAENLMIVDLLRND 488
Cdd:PRK06772 216 RQANTPVRSFMFRQEGREALGFSPELVMSVTGNKVVTEPLAGTRDRMGNPehnkakeAELLHDSKEVLEHILSVKEAIAE 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 489 LGRVCEPGTVTVPKLMHVETYATVHQLVSTVRGVLRPGTTLIDLLRAAFPGGSMTGAPKERTCAMISELEPGARGVYSGV 568
Cdd:PRK06772 296 LEAVCQPGSVVVEDLMSVRQRGSVQHLGSGVSGQLAENKDAWDAFTVLFPSITASGIPKNAALNAIMQIEKTPRELYSGA 375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2537977332 569 AGYLGfNGRADLSILIRTAVKQGDTVEVGAGGAVVWASHPAAEYEEKELKARAV 622
Cdd:PRK06772 376 ILLLD-DTRFDAALVLRSVFQDSQRCWIQAGAGIIAQSTPERELTETREKLASI 428
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
1-190 |
5.11e-17 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 79.51 E-value: 5.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 1 MILLIDNRDSYTynlaHLIHAA----AGEEPLVVRADDVEkyDLARRVEGgefshIVISPGPgtpadDGDFRG-SRLIIQ 75
Cdd:PRK00758 1 KIVVVDNGGQYN----HLIHRTlrylGVDAKIIPNTTPVE--EIKAFEDG-----LILSGGP-----DIERAGnCPEYLK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 76 AAGeTPVLGVCLGHQGLAHLAGASVQRG-APHHGATS-TITHSgEGIFAGLPQGFTAVRYHSLTVSEAP-GVRVHARAED 152
Cdd:PRK00758 65 ELD-VPILGICLGHQLIAKAFGGEVGRGeYGEYALVEvEILDE-DDILKGLPPEIRVWASHADEVKELPdGFEILARSDI 142
|
170 180 190
....*....|....*....|....*....|....*...
gi 2537977332 153 GTVQGLEVVGRPHWGVQFHPESVLTDCGVELLRNFLSL 190
Cdd:PRK00758 143 CEVEAMKHKEKPIYGVQFHPEVAHTEYGEEIFKNFLEI 180
|
|
| PRK07912 |
PRK07912 |
salicylate synthase; |
412-614 |
9.21e-17 |
|
salicylate synthase;
Pssm-ID: 169151 [Multi-domain] Cd Length: 449 Bit Score: 83.30 E-value: 9.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 412 YSRLRRFNPAPYAAYFRIESVEVLSSSPERFLTVHG-RDVETKPIKGTIP----REEDPSA---LRTDAKTRAENLMIVD 483
Cdd:PRK07912 223 YRLGRRHNTPVRSFLLRLGGIRALGYSPELVTAVRAdGVVITEPLAGTRAfgrgAAIDRLArddLESNSKEIVEHAISVR 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 484 LLRNDLGRVCEPGTVTVPKLMHVETYATVHQLVSTVRGVLRPGTTLIDLLRAAFPGGSMTGAPKERTCAMISELEPGARG 563
Cdd:PRK07912 303 SSLAEITEIAEPGSAAVIDFMTVRERGSVQHLGSTVRGRLDASSDRMDALEALFPAVTASGIPKAAGVDAIFRLDEAPRG 382
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2537977332 564 VYSGVAGYLGFNGRADLSILIRTAVKQGDTVEVGAGGAVVWASHPAAEYEE 614
Cdd:PRK07912 383 LYSGAVVMLSADGGLDAALTLRAAYQVGGRTWLRAGAGIIEESEPEREFEE 433
|
|
| PRK06923 |
PRK06923 |
isochorismate synthase DhbC; Validated |
373-625 |
1.49e-16 |
|
isochorismate synthase DhbC; Validated
Pssm-ID: 235886 [Multi-domain] Cd Length: 399 Bit Score: 82.09 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 373 EDYLARIGRIKEALASGDSYEVCLTDTWSArTSSAGIDLYSRLR---RFNPAPY--AAYFRIESVE----VLSSSPERFL 443
Cdd:PRK06923 122 EVYMNGVKQGIAKIQDGDLKKIVLSRSLDV-KSSEKIDKQKLLRelaEHNKHGYtfAVNLPKDENEnsktLIGASPELLV 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 444 TVHGRDVETKPIKGTIPREEDP-------SALRTDAKTRAENLMIVDLLRNDLGRVCEpgTVTVPK---LMHVETyatVH 513
Cdd:PRK06923 201 SRHGMQVISNPLAGSRPRSDDPvedkrraEELLSSPKDLHEHAVVVEAVAAALRPYCH--TLHVPEkpsVIHTEA---MW 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 514 QLVSTVRGVLR-PGTTLIDLLRAAFPGGSMTGAPKERTCAMISELEPGARGVYSGVAGYLGFNGRADLSILIRTAVKQGD 592
Cdd:PRK06923 276 HLSTEVKGELKdPNTSSLELAIALHPTPAVCGTPTEEAREAIQQIEPFDREFFTGMLGWSDLNGDGEWIVTIRCAEVEEN 355
|
250 260 270
....*....|....*....|....*....|...
gi 2537977332 593 TVEVGAGGAVVWASHPAAEYEEKELKARAVTAA 625
Cdd:PRK06923 356 TLRLYAGAGVVAESKPEDELAETSAKFQTMLKA 388
|
|
| guaA |
PRK00074 |
GMP synthase; Reviewed |
52-188 |
2.06e-16 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 82.40 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 52 IVISPGPGTPADDGDFRGSRLIIQAAgeTPVLGVCLGHQGLAHLAGASVQRGapHH---GATSTITHSGEGIFAGLPQGF 128
Cdd:PRK00074 50 IILSGGPASVYEEGAPRADPEIFELG--VPVLGICYGMQLMAHQLGGKVERA--GKreyGRAELEVDNDSPLFKGLPEEQ 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2537977332 129 TAVRYHSLTVSEAP-GVRVHARAEDGTVQGLEVVGRPHWGVQFHPESVLTDCGVELLRNFL 188
Cdd:PRK00074 126 DVWMSHGDKVTELPeGFKVIASTENCPIAAIANEERKFYGVQFHPEVTHTPQGKKLLENFV 186
|
|
| Anth_synt_I_N |
pfam04715 |
Anthranilate synthase component I, N terminal region; Anthranilate synthase (EC:4.1.3.27) ... |
203-327 |
2.42e-16 |
|
Anthranilate synthase component I, N terminal region; Anthranilate synthase (EC:4.1.3.27) catalyzes the first step in the biosynthesis of tryptophan. Component I catalyzes the formation of anthranilate using ammonia and chorismate. The catalytic site lies in the adjacent region, described in the chorismate binding enzyme family (pfam00425). This region is involved in feedback inhibition by tryptophan. This family also contains a region of Para-aminobenzoate synthase component I (EC 4.1.3.-).
Pssm-ID: 428082 [Multi-domain] Cd Length: 140 Bit Score: 76.19 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 203 DLDT-ESTFRALAGESAeAFWLDSA-TGEG-FSILGTD-------RGSLTRSHTF----RLGEDDILDTLGAELAV-RVD 267
Cdd:pfam04715 1 DLLTpLSVYLKLAGEPH-SFLLESAeGGEGrYSFIGINplltiksKNGEVSVSGPdgqeLEQEDGPLDALRALLARfRIE 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2537977332 268 TSPLPDLPFTGGWVGYLGYECATL--TLPRLTPsAPSAYPDAWWVRPQSFIVYDHSAQRAHL 327
Cdd:pfam04715 80 DSPPTLPPFSGGLVGYLGYDLVRYieKLPRTAP-DDLNLPDARLILYEDLIVFDHQENKLYL 140
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
52-174 |
6.96e-13 |
|
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.
Pssm-ID: 153215 [Multi-domain] Cd Length: 178 Bit Score: 67.14 E-value: 6.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 52 IVISPGPGTPADDGDFRgsRLIIQAAGET-PVLGVCLGHQGLAHLAGASV------QRGAPH------HGATSTITHSge 118
Cdd:cd01744 43 IFLSNGPGDPALLDEAI--KTVRKLLGKKiPIFGICLGHQLLALALGAKTykmkfgHRGSNHpvkdliTGRVYITSQN-- 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2537977332 119 gifaglpQGFtAVRYHSLtvseAPGVRV-HARAEDGTVQGLEVVGRPHWGVQFHPES 174
Cdd:cd01744 119 -------HGY-AVDPDSL----PGGLEVtHVNLNDGTVEGIRHKDLPVFSVQFHPEA 163
|
|
| PRK15016 |
PRK15016 |
isochorismate synthase EntC; Provisional |
404-618 |
9.04e-13 |
|
isochorismate synthase EntC; Provisional
Pssm-ID: 184977 [Multi-domain] Cd Length: 391 Bit Score: 70.29 E-value: 9.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 404 TSSAGID---LYSRLRRFNPAPYAAYFRIESVEVL-SSSPERFLTVHGRDVETKPIKGTIPREEDP-------SALRTDA 472
Cdd:PRK15016 157 TTDAAIDsgaLLERLIAQNPVSYNFHVPLADGGVLlGASPELLLRKDGERFSSLPLAGSARRQPDEvldreagNRLLASE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 473 KTRAENLMIVDLLRNDLG-RVCEPGTVTVPKLMhveTYATVHQLVSTVRGVLRPGTTLIDLLRAAFPGGSMTGAPKERTC 551
Cdd:PRK15016 237 KDRHEHELVTQAMKEVLReRSSELHVPSSPQLI---TTPTLWHLATPFEGKANAQENALTLACLLHPTPALSGFPHQAAK 313
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2537977332 552 AMISELEPGARGVYSGVAGYLGFNGRADLSILIRTAVKQGDTVEVGAGGAVVWASHPAAEYEEKELK 618
Cdd:PRK15016 314 QVIAELEPFDRELFGGIVGWCDSEGNGEWVVTIRCAKLRENQVRLFAGAGIVPASSPLGEWRETGVK 380
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
52-174 |
9.21e-12 |
|
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 66.97 E-value: 9.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 52 IVISPGPGTPADDGDfrgsrlIIQAAGE-----TPVLGVCLGHQGLAHLAGASVQR---GapHHGA----------TSTI 113
Cdd:COG0505 221 VFLSNGPGDPAALDY------AIETIREllgkgIPIFGICLGHQLLALALGAKTYKlkfG--HRGAnhpvkdletgRVEI 292
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2537977332 114 T---HsgegifaglpqGFtAVRYHSLtvsEAPGVRV-HARAEDGTVQGLEVVGRPHWGVQFHPES 174
Cdd:COG0505 293 TsqnH-----------GF-AVDEDSL---PATDLEVtHVNLNDGTVEGLRHKDLPAFSVQYHPEA 342
|
|
| PLN02347 |
PLN02347 |
GMP synthetase |
43-188 |
1.12e-11 |
|
GMP synthetase
Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 67.40 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 43 RVEGGEFSHIVISPGP------GTPA-DDGDFRgsrlIIQAAGeTPVLGVCLGHQGLAHLAGASVQRGAPH-HGATSTIT 114
Cdd:PLN02347 48 RIASLNPRVVILSGGPhsvhveGAPTvPEGFFD----YCRERG-VPVLGICYGMQLIVQKLGGEVKPGEKQeYGRMEIRV 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2537977332 115 HSGEGIFAGLPQGFTAVRYHSL---TVSEAPGVRVHARAEDGTVQGLEVVGRPHWGVQFHPESVLTDCGVELLRNFL 188
Cdd:PLN02347 123 VCGSQLFGDLPSGETQTVWMSHgdeAVKLPEGFEVVAKSVQGAVVAIENRERRIYGLQYHPEVTHSPKGMETLRHFL 199
|
|
| PLN02786 |
PLN02786 |
isochorismate synthase |
365-619 |
2.21e-11 |
|
isochorismate synthase
Pssm-ID: 178383 [Multi-domain] Cd Length: 533 Bit Score: 66.73 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 365 KGSWRLSREDYLARIGRikealASGDSYEVCLtdtwsARTSSAGID-------LYSRLRRFNPAPYAayFRI---ESVEV 434
Cdd:PLN02786 259 KGAWHLAVNKALQIIKR-----KSSPLKKVVL-----ARSSRIITDtdidpiaWLACLQVEGQNAYQ--FCLqppDAPAF 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 435 LSSSPERFLTVHGRDVETKPIKGTIPReedpsalrtdAKTRAENLMI-VDLL----------------RNDLGRVCEpgT 497
Cdd:PLN02786 327 IGNTPEQLFHRKGLGVCSEALAATRPR----------GGSSARDLQIeLDLLtspkddlefsivreniREKLEAICD--R 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 498 VTVPKLMHVETYATVHQLVSTVRGVLRPGTTLIDLLRAAFPGGSMTGAPKERTCAMISELEPGARGVYSGVAGYLGfNGR 577
Cdd:PLN02786 395 VVVEPHKAIRKLARVQHLYAQLAGRLRSEDDEFDILAALHPTPAVCGHPTEEARLLIAETESFDRGMYAGPVGWFG-GGE 473
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2537977332 578 ADLSILIRTA-VKQGDTVEVGAGGAVVWASHPAAEYEEKELKA 619
Cdd:PLN02786 474 SEFAVGIRSAlVEKGLGALIYAGTGIVEGSNPSSEWNELELKI 516
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
59-173 |
4.10e-11 |
|
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.
Pssm-ID: 429620 [Multi-domain] Cd Length: 219 Bit Score: 63.04 E-value: 4.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 59 GTPADDGDFRGSRLIIQAAGE--TPVLGVCLGHQ-------GLAHLAgASVQRGAPHH-----GATSTITHS----GEGI 120
Cdd:pfam07722 83 GGPYDPARDAYELALIRAALArgKPILGICRGFQllnvalgGTLYQD-IQEQPGFTDHrehcqVAPYAPSHAvnvePGSL 161
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2537977332 121 FAGL-PQGFTAVR-YHSLTVSE-APGVRVHARAEDGTVQGLEVVGRPHW--GVQFHPE 173
Cdd:pfam07722 162 LASLlGSEEFRVNsLHHQAIDRlAPGLRVEAVAPDGTIEAIESPNAKGFalGVQWHPE 219
|
|
| PRK09065 |
PRK09065 |
glutamine amidotransferase; Provisional |
15-173 |
5.86e-10 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181635 [Multi-domain] Cd Length: 237 Bit Score: 59.98 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 15 LAHLIHAAAGEEPLVVRADDVEKYDLARrvEGGEFSHIVISpgpGTPA---DDGDF--RGSRLIIQAAG-ETPVLGVCLG 88
Cdd:PRK09065 23 FPHWIRVALGLAEQPVVVVRVFAGEPLP--APDDFAGVIIT---GSWAmvtDRLDWseRTADWLRQAAAaGMPLLGICYG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 89 HQGLAHLAGASVQrgapHHGA-----TSTITHSGEG----IFAGLPQGFTAVRYHSLTVSEAP-GVRVHARAEDGTVQGL 158
Cdd:PRK09065 98 HQLLAHALGGEVG----YNPAgresgTVTVELHPAAaddpLFAGLPAQFPAHLTHLQSVLRLPpGAVVLARSAQDPHQAF 173
|
170
....*....|....*
gi 2537977332 159 EvVGRPHWGVQFHPE 173
Cdd:PRK09065 174 R-YGPHAWGVQFHPE 187
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
52-174 |
1.84e-09 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 59.70 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 52 IVISPGPGTPADDGDfrGSRLIIQAAGET-PVLGVCLGHQGLAHLAGASVQR---GapHHGA------TST----IT--- 114
Cdd:PRK12564 222 VFLSNGPGDPAALDY--AIEMIRELLEKKiPIFGICLGHQLLALALGAKTYKmkfG--HRGAnhpvkdLETgkveITsqn 297
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2537977332 115 HsgegifaglpqGFtAVRYHSLtvseAPGVRV-HARAEDGTVQGLEVVGRPHWGVQFHPES 174
Cdd:PRK12564 298 H-----------GF-AVDEDSL----PANLEVtHVNLNDGTVEGLRHKDLPAFSVQYHPEA 342
|
|
| PRK15012 |
PRK15012 |
menaquinone-specific isochorismate synthase; Provisional |
372-619 |
3.31e-09 |
|
menaquinone-specific isochorismate synthase; Provisional
Pssm-ID: 184974 [Multi-domain] Cd Length: 431 Bit Score: 59.47 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 372 REDYLARIGRIKEALASGDSYEVCL---TD-TWSARTSSAGIDLYSRLRRFNPAPYAAYFRIESVeVLSSSPERFLTVHG 447
Cdd:PRK15012 169 KTGWTQLIELATKTIAEGELDKVVLaraTDlHFASPVNAAAMMAASRRLNLNCYHFYMAFDAENA-FLGSSPERLWRRRD 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 448 RDVETKPIKGTIPREEDPSA-------LRTDAKTRAENLMIVDLLRNDLGRVCEPGTVTVPKLMHVETyatVHQLVSTVR 520
Cdd:PRK15012 248 KALRTEALAGTVANHPDDKQaqqlgewLMADDKNQRENMLVVEDICQRLQADTQTLDVLPPQVLRLRK---VQHLRRCIW 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 521 GVLRPGTTLIDLLRAAfPGGSMTGAPKERTCAMISELEPGARGVYSGVAGYLGFNgRADLSILIRTAVKQGDTVEVGAGG 600
Cdd:PRK15012 325 TSLNKADDVICLHQLQ-PTAAVAGLPRDLARQFIARHEPFTREWYAGSAGYLSLQ-QSEFCVSLRSAKVSGNVVRLYAGA 402
|
250
....*....|....*....
gi 2537977332 601 AVVWASHPAAEYEEKELKA 619
Cdd:PRK15012 403 GIVRGSDPEQEWQEIDNKA 421
|
|
| IMP_synth_hisH |
TIGR01855 |
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ... |
2-190 |
6.43e-09 |
|
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273836 [Multi-domain] Cd Length: 196 Bit Score: 56.18 E-value: 6.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 2 ILLID----NRDSYTYNLAHLihaaaGEEPLVVR-ADDVEKYDLarrveggefshiVISPGPGTPADDGDF---RGSRLI 73
Cdd:TIGR01855 1 IVIIDygvgNLGSVKRALKRV-----GAEPVVVKdSKEAELADK------------LILPGVGAFGAAMARlreNGLDLF 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 74 IQ--AAGETPVLGVCLGHQ-------------GLAHLAGASVQ---RGAPHHGATSTITHSGEGIFAGLPQGFTAVRYHS 135
Cdd:TIGR01855 64 VElvVRLGKPVLGICLGMQllferseegggvpGLGLIKGNVVKleaRKVPHMGWNEVHPVKESPLLNGIDEGAYFYFVHS 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2537977332 136 LTVSEAPGVrVHARAEDGTvQGLEVVGRPH-WGVQFHPESVlTDCGVELLRNFLSL 190
Cdd:TIGR01855 144 YYAVCEEEA-VLAYADYGE-KFPAAVQKGNiFGTQFHPEKS-GKTGLKLLENFLEL 196
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
52-173 |
1.44e-08 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 56.82 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 52 IVISPGPGTPADDGDFRgsRLIIQAAGETPVLGVCLGHQGLAHLAGASVQRGAP-HHGATSTI--THSGEGIFAGLPQGF 128
Cdd:PRK12838 212 IVLSNGPGDPKELQPYL--PEIKKLISSYPILGICLGHQLIALALGADTEKLPFgHRGANHPVidLTTGRVWMTSQNHGY 289
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2537977332 129 TAVRyhsLTVSEAPGVRVHARAEDGTVQGLEVVGRPHWGVQFHPE 173
Cdd:PRK12838 290 VVDE---DSLDGTPLSVRFFNVNDGSIEGLRHKKKPVLSVQFHPE 331
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
2-92 |
3.05e-08 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 52.22 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 2 ILLIDNRDSYTYNLAHLIHA--AAGEEPLVVRADDVEKYDLarrVEGGEFSHIVISPGPGTPADDGDFRGSRLIIQAAGE 79
Cdd:cd01653 1 VAVLLFPGFEELELASPLDAlrEAGAEVDVVSPDGGPVESD---VDLDDYDGLILPGGPGTPDDLARDEALLALLREAAA 77
|
90
....*....|....*
gi 2537977332 80 --TPVLGVCLGHQGL 92
Cdd:cd01653 78 agKPILGICLGAQLL 92
|
|
| PRK07567 |
PRK07567 |
glutamine amidotransferase; Provisional |
20-173 |
7.01e-08 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181035 [Multi-domain] Cd Length: 242 Bit Score: 53.79 E-value: 7.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 20 HAAAGEEPLVVRADDVEKYDLAR-RVEGGE--------FSHIVISPGPGTPADDGDFRG----------SRLIIQAAGET 80
Cdd:PRK07567 14 EAADAEYAAFLRYTGLDPAELRRiRLDREPlpdldlddYSGVIVGGSPFNVSDPAESKSpwqrrveaelSGLLDEVVARD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 81 -PVLGVCLGHQGLAHLAGASVQRGAPHHGATSTITHSGEG----IFAGLPQGFTAVRYHSLTVSEAP-GVRVHARAEDGT 154
Cdd:PRK07567 94 fPFLGACYGVGTLGHHQGGVVDRTYGEPVGAVTVSLTDAGradpLLAGLPDTFTAFVGHKEAVSALPpGAVLLATSPTCP 173
|
170
....*....|....*....
gi 2537977332 155 VQGLEvVGRPHWGVQFHPE 173
Cdd:PRK07567 174 VQMFR-VGENVYATQFHPE 191
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
2-92 |
7.85e-08 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 50.28 E-value: 7.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 2 ILLIDNRDSYTYNLAHLIHA--AAGEEPLVVRADDVEKYDLarrVEGGEFSHIVISPGPGTPADDGDFRGSRLIIQAAGE 79
Cdd:cd03128 1 VAVLLFGGSEELELASPLDAlrEAGAEVDVVSPDGGPVESD---VDLDDYDGLILPGGPGTPDDLAWDEALLALLREAAA 77
|
90
....*....|....*
gi 2537977332 80 --TPVLGVCLGHQGL 92
Cdd:cd03128 78 agKPVLGICLGAQLL 92
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
8-173 |
1.39e-07 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153216 [Multi-domain] Cd Length: 189 Bit Score: 52.19 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 8 RDSYTYNLAHLIHAAAGEePLVVR--ADDVEKYDLARRVEG--------------GEFSHIVIspGPGTPADDgdfRGSR 71
Cdd:cd01745 17 RDYLNQYYVDAVRKAGGL-PVLLPpvDDEEDLEQYLELLDGllltgggdvdpplyGEEPHPEL--GPIDPERD---AFEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 72 LIIQAAGE--TPVLGVCLGHQGLAhlagasVqrgapHHGATstithsgegifagLPQGFTAVRYHSLTVSE-APGVRVHA 148
Cdd:cd01745 91 ALLRAALErgKPILGICRGMQLLN------V-----ALGGT-------------LYQDIRVNSLHHQAIKRlADGLRVEA 146
|
170 180
....*....|....*....|....*.
gi 2537977332 149 RAEDGTVQGLEVVGRPHW-GVQFHPE 173
Cdd:cd01745 147 RAPDGVIEAIESPDRPFVlGVQWHPE 172
|
|
| PuuD |
COG2071 |
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
81-173 |
2.96e-07 |
|
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains GATase1-like domain [Amino acid transport and metabolism];
Pssm-ID: 441674 [Multi-domain] Cd Length: 231 Bit Score: 51.71 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 81 PVLGVCLGHQGLAHLAGASV--------------QRGAPHHGATSTITHSGEGIFAG-LPQGFTAVR-YHSLTVSE-APG 143
Cdd:COG2071 98 PVLGICRGMQLLNVALGGTLyqdlpdqvpgaldhRQPAPRYAPRHTVEIEPGSRLARiLGEEEIRVNsLHHQAVKRlGPG 177
|
90 100 110
....*....|....*....|....*....|.
gi 2537977332 144 VRVHARAEDGTVQGLEVVGRPH-WGVQFHPE 173
Cdd:COG2071 178 LRVSARAPDGVIEAIESPGAPFvLGVQWHPE 208
|
|
| hisH |
PRK13141 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
1-192 |
1.74e-06 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 48.97 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 1 MILLID----NRDSYTYNLAHLihaaaGEEPLVVR-ADDVEKYDlarrveggefshIVISPGPGTpADDG--DFRGSRLI 73
Cdd:PRK13141 1 MIAIIDygmgNLRSVEKALERL-----GAEAVITSdPEEILAAD------------GVILPGVGA-FPDAmaNLRERGLD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 74 I----QAAGETPVLGVCLG-------------HQGLAHLAGaSVQR---GA----PHHGATSTITHSGEGIFAGLPQGfT 129
Cdd:PRK13141 63 EvikeAVASGKPLLGICLGmqllfesseefgeTEGLGLLPG-RVRRfppEEglkvPHMGWNQLELKKESPLLKGIPDG-A 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2537977332 130 AVRY-HSLTVSEAP----------GVRVHAraedgtvqgleVVGRPH-WGVQFHPE-SvlTDCGVELLRNFLSLSQ 192
Cdd:PRK13141 141 YVYFvHSYYADPCDeeyvaattdyGVEFPA-----------AVGKDNvFGAQFHPEkS--GDVGLKILKNFVEMVE 203
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
52-174 |
3.74e-06 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 49.41 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 52 IVISPGPGTPA--DDGDFRGSRLIIQaagETPVLGVCLGHQGLAHLAGASVQRGAPHHGAtstITHSgegifAGLPQ--- 126
Cdd:CHL00197 237 ILLSNGPGDPSaiHYGIKTVKKLLKY---NIPIFGICMGHQILSLALEAKTFKLKFGHRG---LNHP-----SGLNQqve 305
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2537977332 127 ------GFtAVRYHSLtvSEAPGVRVHARAEDGTVQGLEVVGRPHWGVQFHPES 174
Cdd:CHL00197 306 itsqnhGF-AVNLESL--AKNKFYITHFNLNDGTVAGISHSPKPYFSVQYHPEA 356
|
|
| hisH |
PRK13146 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
20-188 |
6.51e-06 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237290 [Multi-domain] Cd Length: 209 Bit Score: 47.47 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 20 HAAAGEEPLVVRaddveKYDLARRVEGgefshiVISPGPGTPAD-----DGDFRGSRLIIQA-AGETPVLGVCLGHQ--- 90
Cdd:PRK13146 23 RAGAGADVVVTA-----DPDAVAAADR------VVLPGVGAFADcmrglRAVGLGEAVIEAVlAAGRPFLGICVGMQllf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 91 ----------GLAHLAGaSVQRGA--------PHHG---ATSTITHSgegIFAGLPQGFTAVRYHSLTV-SEAPGVRVhA 148
Cdd:PRK13146 92 erglehgdtpGLGLIPG-EVVRFQpdgpalkvPHMGwntVDQTRDHP---LFAGIPDGARFYFVHSYYAqPANPADVV-A 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2537977332 149 RAEDGtVQGLEVVGR-PHWGVQFHPE-SvlTDCGVELLRNFL 188
Cdd:PRK13146 167 WTDYG-GPFTAAVARdNLFATQFHPEkS--QDAGLALLRNFL 205
|
|
| hisH |
PRK13181 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
1-190 |
2.68e-05 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 45.63 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 1 MILLIDnrdsytY---NLAHLIHA--AAGEEplVVRADDVEKYDLARRVeggefshivISPGPGTpADDG--DFRGSRLI 73
Cdd:PRK13181 1 MIAIID------YgagNLRSVANAlkRLGVE--AVVSSDPEEIAGADKV---------ILPGVGA-FGQAmrSLRESGLD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 74 ----IQAAGETPVLGVCLG------------HQGLAHLAG-----ASVQRGAPHHGaTSTITHSGE-GIFAGLPQG--FT 129
Cdd:PRK13181 63 ealkEHVEKKQPVLGICLGmqllfesseegnVKGLGLIPGdvkrfRSEPLKVPQMG-WNSVKPLKEsPLFKGIEEGsyFY 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2537977332 130 AVryHSLTVSEAPGVRVHARAEDGT-----VQGLEVVgrphwGVQFHPE-SvlTDCGVELLRNFLSL 190
Cdd:PRK13181 142 FV--HSYYVPCEDPEDVLATTEYGVpfcsaVAKDNIY-----AVQFHPEkS--GKAGLKLLKNFAEL 199
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
23-188 |
1.19e-04 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153219 [Multi-domain] Cd Length: 198 Bit Score: 43.64 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 23 AGEEPLVVR-ADDVEKYDLarrveggefshiVISPGPGTpADDGDF----RG-SRLIIQAAGE-TPVLGVCLGHQ----- 90
Cdd:cd01748 21 LGAEVIITSdPEEILSADK------------LILPGVGA-FGDAMAnlreRGlIEALKEAIASgKPFLGICLGMQllfes 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 91 --------GLAHLAG------ASVQRGAPHHGATSTITHSGEGIFAGLPQGFTAvrY--HSLTVSEAPGVRVHARAEDGt 154
Cdd:cd01748 88 seegggtkGLGLIPGkvvrfpASEGLKVPHMGWNQLEITKESPLFKGIPDGSYF--YfvHSYYAPPDDPDYILATTDYG- 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 2537977332 155 VQGLEVVGRPH-WGVQFHPE-SvlTDCGVELLRNFL 188
Cdd:cd01748 165 GKFPAAVEKDNiFGTQFHPEkS--GKAGLKLLKNFL 198
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
52-174 |
3.55e-04 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 43.43 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 52 IVISPGPGTPAddGDFRGSRLIIQAAGETPVLGVCLGHQGLAH-LAGASVQRGAPHHGATSTITHSGEGifaglpQGFTA 130
Cdd:PLN02771 285 VLFSNGPGDPS--AVPYAVETVKELLGKVPVFGICMGHQLLGQaLGGKTFKMKFGHHGGNHPVRNNRTG------RVEIS 356
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2537977332 131 VRYHSLTVSEAP---GVRV-HARAEDGTVQGLEVVGRPHWGVQFHPES 174
Cdd:PLN02771 357 AQNHNYAVDPASlpeGVEVtHVNLNDGSCAGLAFPALNVMSLQYHPEA 404
|
|
| HisH |
COG0118 |
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
1-173 |
4.65e-04 |
|
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 439888 [Multi-domain] Cd Length: 196 Bit Score: 41.56 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 1 MILLIDnrdsytY---NLAHLIHA--AAGEEPLVVR-ADDVEKYDlarrveggefsHIVIsPGPGTpADDG-----DFRG 69
Cdd:COG0118 2 MIAIID------YgmgNLRSVAKAleRLGAEVVVTSdPDEIRAAD-----------RLVL-PGVGA-FGDAmenlrERGL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 70 SRLIIQA-AGETPVLGVCLGHQ-------------GLAHLAGaSVQRGA------PHHGATSTITHSGEGIFAGLPQG-- 127
Cdd:COG0118 63 DEAIREAvAGGKPVLGICLGMQllferseengdteGLGLIPG-EVVRFPasdlkvPHMGWNTVEIAKDHPLFAGIPDGey 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2537977332 128 --FT-----AVRYHSLTVSEAP-GVRVHAraedgtvqgleVVGRPH-WGVQFHPE 173
Cdd:COG0118 142 fyFVhsyyvPPDDPEDVVATTDyGVPFTA-----------AVERGNvFGTQFHPE 185
|
|
| hisH |
PRK13152 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
81-190 |
4.22e-03 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 171876 [Multi-domain] Cd Length: 201 Bit Score: 39.05 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537977332 81 PVLGVCLG-------------HQGLAHLAGASVQ------RGAPHHGATSTITHSGEGIFAGLPQGFTAVRYHSLTVsEA 141
Cdd:PRK13152 75 PILGICLGmqlflergyeggvCEGLGFIEGEVVKfeedlnLKIPHMGWNELEILKQSPLYQGIPEKSDFYFVHSFYV-KC 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2537977332 142 PGVRVHARAEDGtVQGLEVVGRPH-WGVQFHPESVlTDCGVELLRNFLSL 190
Cdd:PRK13152 154 KDEFVSAKAQYG-HKFVASLQKDNiFATQFHPEKS-QNLGLKLLENFARL 201
|
|
| |
