|
Name |
Accession |
Description |
Interval |
E-value |
| TrpE |
COG0147 |
Anthranilate/para-aminobenzoate synthases component I [Amino acid transport and metabolism, ... |
202-611 |
1.49e-129 |
|
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: 393.70 E-value: 1.49e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 202 LCCSPVEIFHALGGRgalLEFEGTAIIALPSGRVAHHIEELEVSGISMAPETWAPL--GWYGYIGYEANDATFGTAVHAP 279
Cdd:COG0147 46 IGADPLATLTVRGGR---VTIEGGGEVEPSEGDPLDALRALLARFRLPPLPGLPPFtgGLVGYFGYDLVRYFERLPDLAP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 280 KPAEVPTTAMMFCTEVIAIrgDRAQITapssrwgrlrdavlaaskstptvpsfdptvigrlHVRDSRERYMATIERIQEA 359
Cdd:COG0147 123 DDLGLPDAALGLYDRLLVF--DHLKGT----------------------------------RSNFTREEYLAAVERAKEY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 360 IRAGETYEVCLTTELFAEVHGeiHPAAMYQALSTAVPAPMRSLVVTDDVAVISASPERFIAMNERMVASSPIKGTRKRSA 439
Cdd:COG0147 167 IRAGDIFQVVLSQRFSAPFEG--DPLALYRALRRINPSPYMFYLRFGDFAIVGSSPERLVRVEDGRVETRPIAGTRPRGA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 440 DHEEDRALADDLRTNPKDRAENLMIVDLVRNDLARVCESGSVRVPELCAVHSFTTVHQLISTVEGQLRPTSTPIDVLRAT 519
Cdd:COG0147 245 TPEEDAALAEELLADEKERAEHLMLVDLARNDLGRVCEPGSVKVPELMVVERYSHVMHLVSTVTGRLRPGLDALDALRAT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 520 FPGGSMTGAPKHRTMHLITELEGKQRGVYSGCIGYIGDDLRTDLAMVIRSVVLTPTTLSYGVGGAIIALSDPAEEWAEIT 599
Cdd:COG0147 325 FPAGTLTGAPKIRAMEIIDELEPTRRGVYGGAVGYLSFDGNMDLAIAIRTAVVKDGRAYVQAGAGIVADSDPEAEYQETL 404
|
410
....*....|..
gi 1437403794 600 TKSRVLLDLLGQ 611
Cdd:COG0147 405 NKARALLRALEL 416
|
|
| Chorismate_bind |
pfam00425 |
chorismate binding enzyme; This family includes the catalytic regions of the chorismate ... |
347-601 |
1.84e-111 |
|
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: 340.68 E-value: 1.84e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 347 ERYMATIERIQEAIRAGETYEVCLTTELFAEVHGEIHPAAMYQALSTAVPAPMRSLVVTDDVAVISASPERFIAMNERMV 426
Cdd:pfam00425 1 EDYLAAVEKAKEAIRAGDLYKVVLSRRLTLPLAGDIDPLALYRRLRARNPAPYSFYFRTGDFTFLGASPERLLSVDGGRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 427 ASSPIKGTRKRSADHEEDRALADDLRTNPKDRAENLMIVDLVRNDLARVCESGSVRVPELCAVHSFTTVHQLISTVEGQL 506
Cdd:pfam00425 81 ITEPIAGTRPRGKDPAEDEALAAELLADPKERAEHLMVVDLIRNDLGRVCVPGSVKVPELPEVERYGTVQHLVSTISGRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 507 RPTSTPIDVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSGCIGYIGDDLRTDLAMVIRSVVLTPTTLSYGVGGAII 586
Cdd:pfam00425 161 KPGLSLLDLLKALFPTGAVTGAPKKRAMEIIRELEPFPRGLYAGAVGYLDPDGDADFAVAIRTALVDNGRARLYAGAGIV 240
|
250
....*....|....*
gi 1437403794 587 ALSDPAEEWAEITTK 601
Cdd:pfam00425 241 ADSDPEAEWEETEAK 255
|
|
| pabB |
TIGR00553 |
aminodeoxychorismate synthase, component I, bacterial clade; Members of this family, ... |
259-605 |
7.25e-101 |
|
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: 315.86 E-value: 7.25e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 259 WYGYIGYEA-NDATFGTAVHAPKpaevpttammfcteVIAIRGDRAQITAPSSRWGRLRDAVLAasksTPTVPSFDPTVI 337
Cdd:TIGR00553 1 LVGYLSYEAgPDAAFEPYDAALL--------------ADHRRTPLLRFLVFERVEAQPRAAVEA----EDDAPADRQAPT 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 338 GRLHVRDSRERYMATIERIQEAIRAGETYEVCLTTELFAEVHGEihPAAMYQALSTAVPAPMRSLVVTDDVAVISASPER 417
Cdd:TIGR00553 63 SDIQSEMTRAEYGEAIDQLQDYIRAGDCYQANLTQQFHATWDGD--PLAAFRKLRRRQPAPFSAFLDLGDGAILSLSPEL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 418 FIAMNERMVASSPIKGTRKRSADHEEDRALADDLRTNPKDRAENLMIVDLVRNDLARVCESGSVRVPELCAVHSFTTVHQ 497
Cdd:TIGR00553 141 FFSIDGSEIETRPIKGTLPRGADPQEDRAQASALAESAKDRAENLMIVDLLRNDLGRIAEVGSVKVPELFVVETYPTVHQ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 498 LISTVEGQLRPTSTPIDVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSGCIGYIGDDLRTDLAMVIRSVVLTPTTL 577
Cdd:TIGR00553 221 LVSTITARLREDLTLSDLFRALFPGGSITGAPKVRAMEIIDELEPQPRGVYCGAIGYLSPEGDMDFNVAIRTLTLDGGRA 300
|
330 340
....*....|....*....|....*...
gi 1437403794 578 SYGVGGAIIALSDPAEEWAEITTKSRVL 605
Cdd:TIGR00553 301 VYGVGGGIVADSDPEAEYRECLLKAAPL 328
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
7-603 |
1.06e-97 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 325.26 E-value: 1.06e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 7 LVVDNFDSFTYNIVDYLHRCGARPHVVTNNA--SPEDI-----DLNRYHGIVISPGPGHPSVAEDVGIS-AWVLQTAQCP 78
Cdd:PLN02889 85 LLIDNYDSYTYNIYQELSIVNGVPPVVVRNDewTWEEVyhylyEEKAFDNIVISPGPGSPTCPADIGIClRLLLECRDIP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 79 VLGVCLGMQLMVTSEGGRVDRAPEAVHGRVDTLNiVAADELFAGLPR----TFSIVRYHSLA-------------AIT-- 139
Cdd:PLN02889 165 ILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIE-HNGCRLFDDIPSgrnsGFKVVRYHSLVidaeslpkelvpiAWTss 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 140 --------------VPPSMEV---------------------TSSNPEG-----IVMSIRHRSRPWWGVQFHPESIAGDF 179
Cdd:PLN02889 244 sdtlsflesqksglVPDAYESqigqsgssdpfssklkngtswPSSHSERmqngkILMGIMHSTRPHYGLQFHPESIATCY 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 180 GMEIIDRF-----------------------------------------------------------------------V 188
Cdd:PLN02889 324 GRQIFKNFreitqdywlrlrstslrrrnsnltanmqvpdasqlfkvprrgqlgngedalgnrelsrraqlrgsvdvfslL 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 189 DLCTPQYRTDEVEL-------------------C---------------CSPVEI----FHALGGRGALLEFEGTAIIAL 230
Cdd:PLN02889 404 NLSEPSSGVKFLKLkwrkfnklaaqvggarnifCelfgknkaentfwldSSSTEKkrgrFSFMGGKGGSLWKQMTFRLSH 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 231 PSGRVAHH-----IEEL-------------------EVSGISMAPETWAPL------GWYGYIGYEANdATFGTAVHAPK 280
Cdd:PLN02889 484 QSDMDSKGgghlsIEDSqgsiestflekgfldflnkELLSIRYDEKDFEGLpfdfhgGYVGYIGYDLK-VECGMASNRHK 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 281 pAEVPTTAMMFCTEVIAI--RGDRAQI------TAPSSRWgrLRDA--------VLAASK---STPTVPSFDPTVIGRLh 341
Cdd:PLN02889 563 -STTPDACFFFADNVVVIdhHYDDVYIlslhegSTATTQW--LDDTeqkllglkASATRKlevQTSPTATFSPSKAGFL- 638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 342 VRDSRERYMATIERIQEAIRAGETYEVCLTTELFAEVhGEIHPAAMYQALSTAVPAPMRSLV--VTDDVAVISASPERFI 419
Cdd:PLN02889 639 ADKSREQYIKDVQKCLKYIKDGESYELCLTTQMRKRI-GEIDSLGLYLHLREKNPAPYAAWLnfSNENLCICSSSPERFL 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 420 AMNER-MVASSPIKGTRKRSADHEEDRALADDLRTNPKDRAENLMIVDLVRNDLARVCESGSVRVPELCAVHSFTTVHQL 498
Cdd:PLN02889 718 KLDRNgMLEAKPIKGTIARGSTPEEDEQLKLQLQYSEKDQAENLMIVDLLRNDLGRVCEPGSVHVPNLMDVESYTTVHTM 797
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 499 ISTVEGQLRPTSTPIDVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSGCIGYIGDDLRTDLAMVIRSVVLTPTTLS 578
Cdd:PLN02889 798 VSTIRGKKRSNMSPVDCVRAAFPGGSMTGAPKLRSMELLDSLESSSRGIYSGSIGFFSYNQTFDLNIVIRTVVIHEGEAS 877
|
810 820
....*....|....*....|....*
gi 1437403794 579 YGVGGAIIALSDPAEEWAEITTKSR 603
Cdd:PLN02889 878 IGAGGAIVALSNPEDEYEEMILKTR 902
|
|
| PabB-fungal |
TIGR01823 |
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ... |
2-606 |
5.73e-97 |
|
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: 319.16 E-value: 5.73e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 2 QRAHILVVDNFDSFTYNIVDYLHR-CGARPHVVT---NNASPEDI-DLNRYHGIVISPGPGHPSVAEDVGI--SAWVLQT 74
Cdd:TIGR01823 4 QRLHVLFIDSYDSFTYNVVRLLEQqTDISVHVTTvhsDTFQDQLLeLLPLFDAIVVGPGPGNPNNAQDMGIisELWELAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 75 A-QCPVLGVCLGMQLMVTSEGGRVDRAPEAVHGRVDTLNIVAADeLFAGLpRTFSIVRYHSLAAITVPPS---MEVTSSN 150
Cdd:TIGR01823 84 LdEVPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAA-IFCGL-FSVKSTRYHSLYANPEGIDtllPLCLTED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 151 PEG-IVMSIRHRSRPWWGVQFHPESIAGDFG-MEIIDRFVDLC------------------------------------- 191
Cdd:TIGR01823 162 EEGiILMSAQTKKKPWFGVQYHPESCCSELGsGKLVSNFLKLAfinnvktgrwekkklngsfsdissrldrtddrdpiyk 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 192 ----TP---QYRTDEV-----ELCCspvEIFHALGGRGALLEFEGT----AIIALPSG-------------RVAHHIEEL 242
Cdd:TIGR01823 242 vkekYPsgtTYVKQFEvsedpKLTF---EICNIIREPKFVMSSSVItgrySIIALPNSasqvfthygamlkTTVHYWQDT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 243 EVSGISMA------------------------------PETWAPL--GWYGYIGYEANDATFGTAVHAPKPAE-----VP 285
Cdd:TIGR01823 319 EISYTRLKkclsgvdsdldksqfwitlgkfmenkkidnPHREIPFigGLVGILGYEIGSDLSTQYIACGRCNDdenslVP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 286 TTAMMFCTEVIAIRGDRAQITA---------PSSRWGRLRDAVLAAS--KSTPTVPSFDPTVIGRLHVRDSRERYMATIE 354
Cdd:TIGR01823 399 DAKLVFINRSIVIDHKQGKLYVqsldntfpvALEWSGELRDSFVRKKniKQSLSWPFYLPEEIDFVITFPDKEDYAKAFK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 355 RIQEAIRAGETYEVCLTTELFAEVHGEIHPA-AMYQALSTAVPAPMRSLVVTDDVAVISASPERFIAMNERMVAS-SPIK 432
Cdd:TIGR01823 479 ACQDYLHAGDSYEMCLTTQTKVVPPAVISPDwEIYQRLRQRNPAPFSGFFRLKHIIFLSTSPEKFLEVGMDTHAKlRPIK 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 433 GTRKRsadhEEDRALADDLRT--NPKDRAENLMIVDLVRNDLARVCESGSVRVPELCAVHSFTTVHQLISTVEGQ-LRPT 509
Cdd:TIGR01823 559 GTVKK----GPQMNLEKARRIlkTPKEMGENLMILDLIRNDLYELVPKNDVHVEELMSVEEHATVYQLVSVVKAHgLTSA 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 510 STP-----IDVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSGCIGYIGDDLRTDLAMVIRSVVLTPTTLSY--GVG 582
Cdd:TIGR01823 635 SKKtrysgIDVLKHSLPPGSMTGAPKKRSVQLLQDVEGGARGIYSGVTGYWDVNGNGDFSVNIRCAFSYNGGTSWriGAG 714
|
730 740
....*....|....*....|....
gi 1437403794 583 GAIIALSDPAEEWAEITTKSRVLL 606
Cdd:TIGR01823 715 GAVTVLSTPEGELEEMYNKLESNL 738
|
|
| PabB-clade2 |
TIGR01824 |
aminodeoxychorismate synthase, component I, clade 2; This clade of sequences is more closely ... |
312-605 |
6.41e-91 |
|
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: 290.91 E-value: 6.41e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 312 WGRLRDAVLAASKSTPTVPSFDPTVIGRLHVRDSRERYMATIERIQEAIRAGETYEVCLTTELFAEVHGEIHPAAMYQAL 391
Cdd:TIGR01824 62 FATSSDQLPAVAAATSLPSPDVGPLPVDLEASIDRAAYETGVRRIKDYIRAGDVFQANLSRRLTAPIAADVDPLQLFLAL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 392 STAVPAPMRSLVVTDDVAVISASPERFIAMNERMVASSPIKGTRKRSADHEEDRALADDLRTNPKDRAENLMIVDLVRND 471
Cdd:TIGR01824 142 RAPNPAPYAIYLEEPGVDVASASPELFLAREGRVVQTRPIAGTRPRGATLAEDGALAAELLQHDKDRAEHVMIVDLERND 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 472 LARVCESGSVRVPELCAVHSFTTVHQLISTVEGQLRPTSTPIDVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSGC 551
Cdd:TIGR01824 222 LGRVCATGTVRVPELCAVESYSHVHHLVSRVTGRLREGAGLADLIRALFPGGSITGAPKVRAMEIIDELEPQPRGPYTGS 301
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1437403794 552 IGYIGDDLRTDLAMVIRSVVLTPTTLSYGVGGAIIALSDPAEEWAEITTKSRVL 605
Cdd:TIGR01824 302 VGWIDADGNADLNILIRTLEGGGAQLHFRTGAGIVADSDPAGEWDETEAKARAL 355
|
|
| PRK09070 |
PRK09070 |
aminodeoxychorismate synthase component I; |
258-611 |
1.62e-79 |
|
aminodeoxychorismate synthase component I;
Pssm-ID: 236371 [Multi-domain] Cd Length: 447 Bit Score: 263.87 E-value: 1.62e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 258 GWYGYIGYEANdATFGTAVHAP-KPAEVPTTAMMFC-TEVIAIRG-DRAQITAPSSRWGRLrDAVLAASKSTPTVPSFdP 334
Cdd:PRK09070 93 GWAVLLDYELA-GQVEPILKLPmRTDGLPLALALRApAAVLRDRHsGRCVLVAEPGREHLL-DQIEADLAACAALPPL-P 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 335 TVIGRLHV-RDSRERYMATIERIQEAIRAGETYEVCLTTELFAEVHGEIHPAAMYQALSTAVPAPMRSLVVTDDVAVISA 413
Cdd:PRK09070 170 VWLAPQAVeEDPPERFTDGVERVLDYIRAGDVFQVNLSRAWQAQFANAVDPAALYARLRAANPAPFSGLFVAAGRAIVSS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 414 SPERFIAMNERMVASSPIKGTRKRSADhEEDRALADDLRTNPKDRAENLMIVDLVRNDLARVCESGSVRVPELCAVHSFT 493
Cdd:PRK09070 250 SPERLVSVQGGVVQTRPIAGTRPRFAG-DDDAALIRELVGHPKERAEHVMLIDLERNDLGRICAPGSVEVDELMTVESYA 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 494 TVHQLISTVEGQLRPTSTPIDVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSGCIGYIGDDLRTDLAMVIRSVVLT 573
Cdd:PRK09070 329 HVHHIVSNVRGRLRDGVTPGEVIRAVFPGGTITGCPKVRCMQIIAELEQTPRGAYTGSFGYLNRDGDMDLNILIRTAEVQ 408
|
330 340 350
....*....|....*....|....*....|....*...
gi 1437403794 574 PTTLSYGVGGAIIALSDPAEEWAEITTKSRVLLDLLGQ 611
Cdd:PRK09070 409 GNQVRFRTGAGIVVDSDPERELDETRAKARGLLRALEQ 446
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
6-188 |
5.88e-77 |
|
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: 247.45 E-value: 5.88e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 6 ILVVDNFDSFTYNIVDYLHRCGARPHVVTNNASPED-IDLNRYHGIVISPGPGHPsvaEDVGISAWVLQT--AQCPVLGV 82
Cdd:cd01743 1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEeLELLNPDAIVISPGPGHP---EDAGISLEIIRAlaGKVPILGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 83 CLGMQLMVTSEGGRVDRAPEAVHGRVDTLNIVAADeLFAGLPRTFSIVRYHSLAAI--TVPPSMEVTSSNPEGIVMSIRH 160
Cdd:cd01743 78 CLGHQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSG-LFKGLPQPFTVGRYHSLVVDpdPLPDLLEVTASTEDGVIMALRH 156
|
170 180
....*....|....*....|....*...
gi 1437403794 161 RSRPWWGVQFHPESIAGDFGMEIIDRFV 188
Cdd:cd01743 157 RDLPIYGVQFHPESILTEYGLRLLENFL 184
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
6-192 |
8.47e-76 |
|
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: 244.56 E-value: 8.47e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 6 ILVVDNFDSFTYNIVDYLHRCGARPHVVTNNA-SPEDIDLNRYHGIVISPGPGHPSVAedvGISAWVLQT--AQCPVLGV 82
Cdd:COG0512 1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEiTLEEIEALAPDGIVLSPGPGTPEEA---GISLEVIRAfaGKIPILGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 83 CLGMQLMVTSEGGRVDRAPEAVHGRVDTLNIvAADELFAGLPRTFSIVRYHSLAA--ITVPPSMEVTSSNPEGIVMSIRH 160
Cdd:COG0512 78 CLGHQAIGEAFGGKVVRAPEPMHGKTSPITH-DGSGLFAGLPNPFTATRYHSLVVdrETLPDELEVTAWTEDGEIMGIRH 156
|
170 180 190
....*....|....*....|....*....|..
gi 1437403794 161 RSRPWWGVQFHPESIAGDFGMEIIDRFVDLCT 192
Cdd:COG0512 157 RELPIEGVQFHPESILTEHGHQLLANFLELAG 188
|
|
| PRK07508 |
PRK07508 |
aminodeoxychorismate synthase component I; |
327-603 |
1.05e-74 |
|
aminodeoxychorismate synthase component I;
Pssm-ID: 236035 [Multi-domain] Cd Length: 378 Bit Score: 248.39 E-value: 1.05e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 327 PTVPSFDPTVIGRLHVRDSRERYMATIERIQEAIRAGETYEVCLTTELFAEVHGEihPAAMYQALSTAVPAPMRSLVVTD 406
Cdd:PRK07508 92 PARPSENAARLRDPVARWDFADYAQRFERLHRHIRAGDCYQANLTFPLDARWGGD--PLALFWALAARQPVGYGALVDLG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 407 DVAVISASPERFIAMN-ERMVASSPIKGTRKRSADHEEDRALADDLRTNPKDRAENLMIVDLVRNDLARVCESGSVRVPE 485
Cdd:PRK07508 170 GPVILSRSPELFFRVDgEGWIETHPMKGTAPRGATPAEDARLRAALLNDEKNQAENRMIVDLLRNDISRISEVGSLDVPE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 486 LCAVHSFTTVHQLISTVEGQLRPTSTPIDVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSGCIGYIGDDLRTDLAM 565
Cdd:PRK07508 250 LFDIETYPTVHQMVSRVRARLLPGLGLADIFAALFPCGSITGAPKIRAMEILRELEPGPRDLYCGAIGWIAPDGRMRFNV 329
|
250 260 270
....*....|....*....|....*....|....*....
gi 1437403794 566 VIRSVVLTPT-TLSYGVGGAIIALSDPAEEWAEITTKSR 603
Cdd:PRK07508 330 AIRTLSLFPGgRAVFNVGGGIVFDSTAEAEYEECLLKAR 368
|
|
| PRK05877 |
PRK05877 |
aminodeoxychorismate synthase component I; Provisional |
209-618 |
4.38e-69 |
|
aminodeoxychorismate synthase component I; Provisional
Pssm-ID: 235634 [Multi-domain] Cd Length: 405 Bit Score: 234.21 E-value: 4.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 209 IFHALGGRGALLE-----------FEGTAIIAlPSGRVAHhIEELEVSGISMAPETWAPL-----GWYGYIGYEANDATf 272
Cdd:PRK05877 1 VLRALGAATARLGlpppaaltgdwFGSRAVIA-PSVSIRP-VAPDDVFAVPPGTAGAAAPgavggGWFGYLSYPDAGAD- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 273 gtavhaPKPAEVPTTAMMFCTEVIAIRGD-----RAQITAPSSRWgrLRDAVLAASKSTPTVPSFDPTVIGRLHVRDSre 347
Cdd:PRK05877 78 ------GRPPRIPEAAGGWTDHVLRRDRDgqwwyESLSGAPDPDW--LASALATTRARPAPPCRIDWTPPDRAAHRDG-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 348 rymatIERIQEAIRAGETYEVCLTTELFAEVHGEihPAAMYQALSTAVpAPMRS-LVVTDDVAVISASPERFIAMNERMV 426
Cdd:PRK05877 148 -----VLACLEAIAAGEVYQACVCTQFTGTVTGS--PLDFFADGVART-APARAaYLAGDWGAVASLSPELFLRRRGSVV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 427 ASSPIKGTRKRSADHEEdraladdLRTNPKDRAENLMIVDLVRNDLARVCESGSVRVPELCAVHSFTTVHQLISTVEGQL 506
Cdd:PRK05877 220 TSSPIKGTLPLDADPSA-------LRASAKDVAENIMIVDLVRNDLGRVARTGTVTVPELLVVRPAPGVWHLVSTVSAQV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 507 RPTSTPIDVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSGCIGYIGDDLRTDLAMVIRSVVLTPT-TLSYGVGGAI 585
Cdd:PRK05877 293 PDELPMSDLLDATFPPASVTGTPKLRARELISQWEPVRRGIYCGTVGLASPVAGCELNVAIRTVEFDADgNAVLGVGGGI 372
|
410 420 430
....*....|....*....|....*....|...
gi 1437403794 586 IALSDPAEEWAEITTKSRVLLDLLGQDFPQSLI 618
Cdd:PRK05877 373 TADSDPDAEWQECLHKAAPIVGLPAAATSAPAR 405
|
|
| PRK05940 |
PRK05940 |
anthranilate synthase component I; |
258-617 |
1.13e-66 |
|
anthranilate synthase component I;
Pssm-ID: 235651 [Multi-domain] Cd Length: 463 Bit Score: 229.62 E-value: 1.13e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 258 GWYGYIGYEandatFGTAVHA---PKPAEVP-TTAMMFCTEVIAIRGDRAQI----TAPSSRWGRLRDAvLAASKSTPTV 329
Cdd:PRK05940 99 GWLGWLGYD-----LAWEIERlphLNPDPLPfPVAYWYEPESFAILDHQEQIlwlaASDPSQLDRLEQQ-LEQPTPEPDL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 330 PSFDPTVIGRLHVRDSRERYMATIERIQEAIRAGETYEVCLTTELfaEVHGEIHPAAMYQALSTAVPAPMRSLVVTDDVA 409
Cdd:PRK05940 173 PLDLRTPPSSLIFYTTQQEYEAAVRQAKKYIQAGDIFQANLSLRF--QTTTSADSWQIYRRLQQINPSPFASYWRTPWGD 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 410 VISASPERFIAMNERMVASSPIKGTRKRSADHEEDRALADDLRTNPKDRAENLMIVDLVRNDLARVCESGSVRVPELCAV 489
Cdd:PRK05940 251 VVSCSPERLVQLQGNQAQTRPIAGTRPRGKTPAEDQQLAEELLSNIKERAEHIMLVDLERNDLGRVCQWGSVEVDELLTI 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 490 HSFTTVHQLISTVEGQLRPTSTPIDVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSGCIGYIgdDLR--TDLAMVI 567
Cdd:PRK05940 331 ERYSHVIHLVSNVVGTLQPNRDAIDLIRALFPGGTITGCPKVRCMEIIEELEPVRRNLFYGSCGYL--DQRgnLDLNILI 408
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1437403794 568 RSVVLTPTTLS----YG-VGGAIIALSDPAEEWAEITTKSRVLLDLLGQDFPQSL 617
Cdd:PRK05940 409 RTLLYTPLSRGlstiWGqVGAGIVADSDPEKEWLESLQKAKAQLAALNLVRSQNS 463
|
|
| PRK13571 |
PRK13571 |
anthranilate synthase component I; Provisional |
256-606 |
9.21e-65 |
|
anthranilate synthase component I; Provisional
Pssm-ID: 184152 [Multi-domain] Cd Length: 506 Bit Score: 225.67 E-value: 9.21e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 256 PL--GWYGYIGYEANDATFGTAVHAPKPAEVPTTAMMFCTEVIAIRGDRAQIT--APSSRWGRLRDAVLAA--------- 322
Cdd:PRK13571 120 PLtgGMVGFLGYDAVRRLERLPELAVDDLGLPEMLLLLATDLAAVDHHEGTITliANAVNWNGTDERVDAAyddavarld 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 323 ------SKSTPTVPSFDPTVIGRLHVRDSRERYMATIERIQEAIRAGETYEVCLTTELfaEVHGEIHPAAMYQALSTAVP 396
Cdd:PRK13571 200 vmtaalAQPLPSTVATFSRPVPEFRAQRTVEEFGAAVEKLVEEIRAGEAFQVVPSQRF--EMDTTADPLDVYRVLRVTNP 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 397 APMRSLVVTDDVA------VISASPERFIAMNERMVASSPIKGTRKRSADHEEDRALADDLRTNPKDRAENLMIVDLVRN 470
Cdd:PRK13571 278 SPYMYLLRVPNSDggtdfsIVGSSPEALVTVTDGRATTHPIAGTRWRGATPEEDALLEKELLADPKERAEHLMLVDLGRN 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 471 DLARVCESGSVRVPELCAVHSFTTVHQLISTVEGQLRPTSTPIDVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSG 550
Cdd:PRK13571 358 DLGRVCRPGTVRVVDFSHIERYSHVMHLVSTVTGELAEGRTALDAVTACFPAGTLSGAPKVRAMELIEELEPTRRGLYGG 437
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1437403794 551 CIGYI---GDdlrTDLAMVIRSVVLTPTTLSYGVGGAIIALSDPAEEWAEITTKSRVLL 606
Cdd:PRK13571 438 VVGYLdfaGD---ADTAIAIRTALMRDGTAYVQAGGGVVADSDPDYEDNEARNKAAAVL 493
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
5-192 |
6.82e-61 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 204.21 E-value: 6.82e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 5 HILVVDNFDSFTYNIVDYLHRCGARPHVVTNNA-SPEDIDLNRYHGIVISPGPGHPsvaEDVGISAWVLQTA--QCPVLG 81
Cdd:PRK05670 1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEiTLEEIEALNPDAIVLSPGPGTP---AEAGISLELIREFagKVPILG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 82 VCLGMQLMVTSEGGRVDRAPEAVHGRVDTLnIVAADELFAGLPRTFSIVRYHSLAA--ITVPPSMEVTSSNPEGIVMSIR 159
Cdd:PRK05670 78 VCLGHQAIGEAFGGKVVRAKEIMHGKTSPI-EHDGSGIFAGLPNPFTVTRYHSLVVdrESLPDCLEVTAWTDDGEIMGVR 156
|
170 180 190
....*....|....*....|....*....|...
gi 1437403794 160 HRSRPWWGVQFHPESIAGDFGMEIIDRFVDLCT 192
Cdd:PRK05670 157 HKELPIYGVQFHPESILTEHGHKLLENFLELAR 189
|
|
| pabB |
PRK15465 |
aminodeoxychorismate synthase component 1; |
345-608 |
2.10e-57 |
|
aminodeoxychorismate synthase component 1;
Pssm-ID: 185362 [Multi-domain] Cd Length: 453 Bit Score: 203.61 E-value: 2.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 345 SRERYMATIERIQEAIRAGETYEVCLTTELFAEVHGEIHPAamYQALSTAVPAPMRSLVVTDDVAVISASPERFIAMNER 424
Cdd:PRK15465 189 TREQYGEKFRQVQEYLHSGDCYQVNLAQRFHATYSGDEWQA--FLQLNQANRAPFSAFLRLEQGAILSLSPERFILCDNS 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 425 MVASSPIKGTRKRSADHEEDRALADDLRTNPKDRAENLMIVDLVRNDLARVCESGSVRVPELCAVHSFTTVHQLISTVEG 504
Cdd:PRK15465 267 EIQTRPIKGTLPRLPDPQEDSKQAEKLANSAKDRAENLMIVDLMRNDIGRVAVAGSVKVPELFVVEPFPAVHHLVSTITA 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 505 QLRPTSTPIDVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSGCIGYIGDDLRTDLAMVIRSVVLTPTTLSYGVGGA 584
Cdd:PRK15465 347 RLPEQLHASDLLRAAFPGGSITGAPKVRAMEIIDELEPQRRNAWCGSIGYLSFCGNMDTSITIRTLTAINGQIYCSAGGG 426
|
250 260
....*....|....*....|....*
gi 1437403794 585 IIALSDPAEEWAEITTK-SRVLLDL 608
Cdd:PRK15465 427 IVADSQEEAEYQETFDKvNRILRQL 451
|
|
| Anth_synII_Halo |
NF041322 |
anthranilate synthase component II; |
8-191 |
7.35e-55 |
|
anthranilate synthase component II;
Pssm-ID: 469219 [Multi-domain] Cd Length: 190 Bit Score: 187.55 E-value: 7.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 8 VVDNFDSFTYNIVDYL--HRCGARPHVVTNNASPEDIDLNRYHGIVISPGPGHPSVAEDVGISAWVLQ--TAQCPVLGVC 83
Cdd:NF041322 1 FVDNFDSFTYNLVEYVseQREHAETTVLKNTASLAEVRAVDPDAIVISPGPGHPKNDRDVGVTADVLRelSPEVPTLGVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 84 LGMQLMVTSEGGRVDRAPEAVHGRVDTlniVAADE--LFAGLPRTFSIVRYHSLAAITVPPSMEVTSSNP---EGIVMSI 158
Cdd:NF041322 81 LGLEAAVYAYGGTVGRAPEPVHGKAFP---VDHDGegVFAGLEQGFQAGRYHSLVATEVPDCFEVTATTDhdgEELVMGI 157
|
170 180 190
....*....|....*....|....*....|...
gi 1437403794 159 RHRSRPWWGVQFHPESIAGDFGMEIIDRFVDLC 191
Cdd:NF041322 158 RHREHPIECVQFHPESVLTGVGHDVIENFLAAA 190
|
|
| PRK13572 |
PRK13572 |
anthranilate synthase component I; Provisional |
345-610 |
1.06e-53 |
|
anthranilate synthase component I; Provisional
Pssm-ID: 237432 [Multi-domain] Cd Length: 435 Bit Score: 192.64 E-value: 1.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 345 SRERYMATIERIQEAIRAGETYEVCLTTELfaEVHGEIHPAAMYQALSTAVPAPMRSLVVTDDvAVISASPERFIAMNER 424
Cdd:PRK13572 171 DREEFVEMVEKAKEYIYSGDVFQVVLSREY--RLKTDLSPFQLYRNLREINPSPYMFLLEFDK-DVVGASPETMASVENN 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 425 MVASSPIKGTRKRSADHEEDRALADDLRTNPKDRAENLMIVDLVRNDLARVCESGSVRVPELCAVHSFTTVHQLISTVEG 504
Cdd:PRK13572 248 ILKINPIAGTAPRGKTEEEDKKLAEALLSDEKERAEHVMLVDLARNDVRKVSKSGSVRLERFFDVVKYSHVQHIESEVVG 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 505 QLRPTSTPIDVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSGCIGYIGDDLRTDLAMVIRSVVLTpTTLSYGVGGA 584
Cdd:PRK13572 328 ELKEDSTMFDAIEAAFPAGTLTGAPKFRAMEIIDELEKSRRKVYGGAVGYFSNSGNADLAIAIRMAEID-KVCRVRAGAG 406
|
250 260
....*....|....*....|....*.
gi 1437403794 585 IIALSDPAEEWAEITTKSRVLLDLLG 610
Cdd:PRK13572 407 IVADSVPEKEFYETERKMAAVLKALG 432
|
|
| PRK13574 |
PRK13574 |
anthranilate synthase component I; Provisional |
345-610 |
2.35e-50 |
|
anthranilate synthase component I; Provisional
Pssm-ID: 184155 [Multi-domain] Cd Length: 420 Bit Score: 183.09 E-value: 2.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 345 SRERYMATIERIQEAIRAGETYEVCLTTELFAEVHGEihPAAMYQALSTAVPAPMRSLVVTDDVAVISASPERFIAMNER 424
Cdd:PRK13574 156 NKNNYEKIVSESLEYIRSGYIFQVVLSRFYRYLFSGD--PLRIYYNLRRINPSPYMFYLKFDERYLIGSSPELLFRVQDN 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 425 MVASSPIKGTRKRSADHEEDRALADDLRTNPKDRAENLMIVDLVRNDLARVCESGSVRVPELCAVHSFTTVHQLISTVEG 504
Cdd:PRK13574 234 IVETYPIAGTRPRGSDQEEDLKLELELMNSEKDKAEHLMLVDLARNDLGKVCVPGTVRVPELMYVEKYSHVQHIVSKVIG 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 505 QLRPTSTPIDVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSGCIGYIGDDLRTDLAMVIRSVVLTPTTLSYGVGGA 584
Cdd:PRK13574 314 TLKKKYNALDVLKATFPAGTVSGAPKPMAMNIIETLEEYKRGPYAGAVGFISADGNAEFAIAIRTAFLNKDLLRIQAGAG 393
|
250 260
....*....|....*....|....*.
gi 1437403794 585 IIALSDPAEEWAEITTKSRVLLDLLG 610
Cdd:PRK13574 394 IVYDSNPESEYFETEHKLRALKTAIG 419
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
7-188 |
4.83e-50 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 174.35 E-value: 4.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 7 LVVDNFDSFTYNIVDYLHRCGARPHVVTNNASPEDIDLNRYHGIVISPGPGHPSVAED-VGISAWVLqTAQCPVLGVCLG 85
Cdd:pfam00117 1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAAGGaIEAIREAR-ELKIPILGICLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 86 MQLMVTSEGGRVDRAPEAVHGRVDTLNIVAADELFAGLPRTFSIVRYHSLAAI--TVPPSMEVTSSNPEGI-VMSIRHRS 162
Cdd:pfam00117 80 HQLLALAFGGKVVKAKKFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDpdTLPDGLEVTATSENDGtIMGIRHKK 159
|
170 180
....*....|....*....|....*.
gi 1437403794 163 RPWWGVQFHPESIAGDFGMEIIDRFV 188
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFF 185
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
4-191 |
8.88e-46 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 163.30 E-value: 8.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 4 AHILVVDNFDSFTYNIVDYLHRCGARPHVVTNN----ASPEDIDLNrYHGIVISPGPGHPsvaEDVGISAWVLQ---TAQ 76
Cdd:PRK07765 1 MRILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDdprlADEAAVAAQ-FDGVLLSPGPGTP---ERAGASIDMVRacaAAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 77 CPVLGVCLGMQLMVTSEGGRVDRAPEAVHGRVDTLNIVAADeLFAGLPRTFSIVRYHSLAAI--TVPPSMEVTSSNPEGI 154
Cdd:PRK07765 77 TPLLGVCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVG-VLAGLPDPFTATRYHSLTILpeTLPAELEVTARTDSGV 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 1437403794 155 VMSIRHRSRPWWGVQFHPESIAGDFGMEIIDRFVDLC 191
Cdd:PRK07765 156 IMAVRHRELPIHGVQFHPESVLTEGGHRMLANWLTVC 192
|
|
| PLN02445 |
PLN02445 |
anthranilate synthase component I |
345-614 |
2.97e-45 |
|
anthranilate synthase component I
Pssm-ID: 215244 [Multi-domain] Cd Length: 523 Bit Score: 171.02 E-value: 2.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 345 SRERYMATIERIQEAIRAGETYEVCLTTELfaEVHGEIHPAAMYQALSTAVPAP-MRSLVVTDDVAVISaSPERFIAMNE 423
Cdd:PLN02445 234 TSEEYKNAVLQAKEHILAGDIFQIVLSQRF--ERRTFADPFEVYRALRIVNPSPyMIYLQARGCILVAS-SPEILTRVKK 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 424 RMVASSPIKGTRKRSADHEEDRALADDLRTNPKDRAENLMIVDLVRNDLARVCESGSVRVPELCAVHSFTTVHQLISTVE 503
Cdd:PLN02445 311 NKIVNRPLAGTRRRGKTPEEDKALEKDLLADEKQCAEHIMLVDLGRNDVGKVSKAGSVKVEKLMNIERYSHVMHISSTVT 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 504 GQLRPTSTPIDVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSGCIGYIGDDLRTDLAMVIRSVVLtPTTLSYGV-- 581
Cdd:PLN02445 391 GELLDHLTSWDALRAALPVGTVSGAPKVRAMELIDELEVTRRGPYSGGFGGVSFTGDMDIALALRTMVF-PTAARYDTmy 469
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1437403794 582 -----------------GGAIIALSDPAEEWAEITTKSRVL---LDLLGQDFP 614
Cdd:PLN02445 470 sykdtnsrrewvahlqaGAGIVADSDPEDEYRECVNKAAGLaraIDLAESAFV 522
|
|
| MenF |
COG1169 |
Isochorismate synthase EntC [Coenzyme transport and metabolism, Secondary metabolites ... |
293-612 |
2.82e-44 |
|
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: 163.78 E-value: 2.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 293 TEVIAIRGDRAQITAPSS-RWGRLRDAV---LAASKSTPTVP------SFDPT--------VIGRLHVR------DSRER 348
Cdd:COG1169 11 GEGLAGLGEAARFEAPGPdRFAALAAAWqalLADAALAGTGPrafggfAFDPDspapaarlVLPRLLLRrsrrgvPDPAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 349 YMATIERIQEAIRAGETYEVCLTTELFAEVHGEIHPAAMYQALSTAVPAPMR-SLVVTDDVAVISASPERFIAMNERMVA 427
Cdd:COG1169 91 WREAVAQALEAIRAGELDKVVLARALDLTLDEPIDPRALLARLRRRNPDCYTfAVELGAGDGFVGASPERLVRRRGGQLT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 428 SSPIKGTRKRSADHEEDRALADDLRTNPKDRAENLMIVDLVRNDLARVCESgsVRVPELCAVHSFTTVHQLISTVEGQLR 507
Cdd:COG1169 171 TEALAGTAPRGADPEEDAALAAALLASEKDRREHALVVDSIREALAPLCSS--LDVPEEPELLRLRNVQHLATPITGTLD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 508 PTSTPIDVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSGCIGYIGDDLRTDLAMVIRSVVLTPTTLSYGVGGAIIA 587
Cdd:COG1169 249 PGVSALDLAAALHPTPAVGGTPREAALALIRELEPFDRGWYAGPVGWVDADGDGEFAVAIRSALIDGNRARLFAGAGIVA 328
|
330 340
....*....|....*....|....*
gi 1437403794 588 LSDPAEEWAEITTKSRVLLDLLGQD 612
Cdd:COG1169 329 GSDPEAEWAETEAKLRTMLRALGLE 353
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
5-193 |
1.26e-42 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 166.25 E-value: 1.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 5 HILVVDNFDSFTYNIVDYLHRCGARPHVVTNNASPEDIDLNRYHGIVISPGPGHPSvaeDVGISAwVLQTA---QCPVLG 81
Cdd:PRK13566 528 RVLLVDHEDSFVHTLANYFRQTGAEVTTVRYGFAEEMLDRVNPDLVVLSPGPGRPS---DFDCKA-TIDAAlarNLPIFG 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 82 VCLGMQLMVTSEGGRVDRAPEAVHGRVDTLNIVAADELFAGLPRTFSIVRYHSLAA--ITVPPSMEVTSSNPEGIVMSIR 159
Cdd:PRK13566 604 VCLGLQAIVEAFGGELGQLAYPMHGKPSRIRVRGPGRLFSGLPEEFTVGRYHSLFAdpETLPDELLVTAETEDGVIMAIE 683
|
170 180 190
....*....|....*....|....*....|....*..
gi 1437403794 160 HRSRPWWGVQFHPESI---AGDFGMEIIDRFVDLCTP 193
Cdd:PRK13566 684 HKTLPVAAVQFHPESImtlGGDVGLRIIENVVRLLAG 720
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
5-190 |
6.17e-41 |
|
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: 148.78 E-value: 6.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 5 HILVVDNFDSFTYNIVDYLHRCGARPHVVTNNA-SPEDIDLNRYHGIVISPGPGHPSVAedvGISAWVLQTA--QCPVLG 81
Cdd:TIGR00566 1 MVLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSlTLQEIEALLPLLIVISPGPCTPNEA---GISLEAIRHFagKLPILG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 82 VCLGMQLMVTSEGGRVDRAPEAVHGRVDTLNIVAAdELFAGLPRTFSIVRYHSLA--AITVPPSMEVTSSNPEGI-VMSI 158
Cdd:TIGR00566 78 VCLGHQAMGQAFGGDVVRANTVMHGKTSEIEHNGA-GIFRGLFNPLTATRYHSLVvePETLPTCFPVTAWEEENIeIMAI 156
|
170 180 190
....*....|....*....|....*....|..
gi 1437403794 159 RHRSRPWWGVQFHPESIAGDFGMEIIDRFVDL 190
Cdd:TIGR00566 157 RHRDLPLEGVQFHPESILSEQGHQLLANFLHR 188
|
|
| PRK13564 |
PRK13564 |
anthranilate synthase component 1; |
314-569 |
7.17e-41 |
|
anthranilate synthase component 1;
Pssm-ID: 237428 [Multi-domain] Cd Length: 520 Bit Score: 158.07 E-value: 7.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 314 RLRDAVLAASKSTPTVPSfDPTVIGRLHVRDSRERYMATIERIQEAIRAGETYEV----CLTTELFAevhgeihPAAMYQ 389
Cdd:PRK13564 211 RLAQLKQQLTQPAPPLPV-TSVPDMEVSVNISDEEFCAVVRKLKEHIRAGDIFQVvpsrRFSLPCPS-------PLAAYR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 390 ALSTAVPAP----MRSlvvtDDVAVISASPE---RFIAMNeRMVASSPIKGTRKR------SADHEEDRALADDLRTNPK 456
Cdd:PRK13564 283 VLKKSNPSPymfyMQD----EDFTLFGASPEsalKYDASS-RQVEIYPIAGTRPRgrradgSIDRDLDSRIELELRTDHK 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 457 DRAENLMIVDLVRNDLARVCESGSVRVPELCAVHSFTTVHQLISTVEGQLRPTstpIDVL---RATFPGGSMTGAPKHRT 533
Cdd:PRK13564 358 ELAEHLMLVDLARNDLARICQPGSRYVADLLKVDRYSHVMHLVSRVVGELRHD---LDALhayRACMNMGTLTGAPKVRA 434
|
250 260 270
....*....|....*....|....*....|....*.
gi 1437403794 534 MHLITELEGKQRGVYSGCIGYIGDDLRTDLAMVIRS 569
Cdd:PRK13564 435 MQLIREVEGQRRGSYGGAVGYLTGHGDLDTCIVIRS 470
|
|
| PRK13567 |
PRK13567 |
anthranilate synthase component I; Provisional |
345-608 |
9.78e-41 |
|
anthranilate synthase component I; Provisional
Pssm-ID: 184148 [Multi-domain] Cd Length: 468 Bit Score: 156.46 E-value: 9.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 345 SRERYMATIERIQEAIRAGETYEVcLTTELFAEVH---GEIHPAA--MYQALSTAVPAPMRSLVVTDDVAVISASPERFI 419
Cdd:PRK13567 199 SEERFIEMIQYFKEKITEGDMFQV-VPSRIYKYAHhasQHLNQLSfqLYQNLKRQNPSPYMYYLNIDQPYIVGSSPESFV 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 420 AMNERMVASSPIKGTRKRSADHEEDRALADDLRTNPKDRAENLMIVDLVRNDLARVCESGSVRVPELCAVHSFTTVHQLI 499
Cdd:PRK13567 278 SVKDQIVTTNPIAGTIQRGETTQIDNENMKQLLNDPKECSEHRMLVDLGRNDIHRVSKIGTSKITKLMVIEKYEHVMHIV 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 500 STVEGQLRPTSTPIDVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSGCIGYIGDDLRTDLAMVIRSVVLTPTTLSY 579
Cdd:PRK13567 358 SEVTGKINQNLSPMTVIANLLPTGTVSGAPKLRAIERIYEQYPHKRGVYSGGVGYINCNHNLDFALAIRTMMIDEQYINV 437
|
250 260
....*....|....*....|....*....
gi 1437403794 580 GVGGAIIALSDPAEEWAEITTKSRVLLDL 608
Cdd:PRK13567 438 EAGCGVVYDSIPEKELNETKLKAKSLLEV 466
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
6-190 |
1.01e-40 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 147.96 E-value: 1.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 6 ILVVDNFDSFTYNIVDYLHRCGARPHVVTNNA-SPEDIDLNRYHGIVISPGPGHPsvaEDVGISAWVLQT--AQCPVLGV 82
Cdd:CHL00101 2 ILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEiDLSKIKNLNIRHIIISPGPGHP---RDSGISLDVISSyaPYIPILGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 83 CLGMQLMVTSEGGRVDRAPEAVHGRVDTLnIVAADELFAGLPRTFSIVRYHSLAA--ITVPPSMEVTSSNPEGIVMSIRH 160
Cdd:CHL00101 79 CLGHQSIGYLFGGKIIKAPKPMHGKTSKI-YHNHDDLFQGLPNPFTATRYHSLIIdpLNLPSPLEITAWTEDGLIMACRH 157
|
170 180 190
....*....|....*....|....*....|.
gi 1437403794 161 RSRPW-WGVQFHPESIAGDFGMEIIDRFVDL 190
Cdd:CHL00101 158 KKYKMlRGIQFHPESLLTTHGQQILRNFLSL 188
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
6-187 |
2.53e-40 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 156.42 E-value: 2.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 6 ILVVDNFDSFTYNIVDYLHRCGA-RPHVVTNNA-SPEDID-LNRYHgIVISPGPGHPsvaEDVGISAWVLQTAQ--CPVL 80
Cdd:PRK14607 2 IILIDNYDSFTYNIYQYIGELGPeEIEVVRNDEiTIEEIEaLNPSH-IVISPGPGRP---EEAGISVEVIRHFSgkVPIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 81 GVCLGMQLMVTSEGGRVDRAPEAVHGRVDTLNIVAADeLFAGLPRTFSIVRYHSLA--AITVPPSMEVTSSNPEGIVMSI 158
Cdd:PRK14607 78 GVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKG-LFRGIPNPTVATRYHSLVveEASLPECLEVTAKSDDGEIMGI 156
|
170 180
....*....|....*....|....*....
gi 1437403794 159 RHRSRPWWGVQFHPESIAGDFGMEIIDRF 187
Cdd:PRK14607 157 RHKEHPIFGVQFHPESILTEEGKRILKNF 185
|
|
| isochor_syn |
TIGR00543 |
isochorismate synthases; This enzyme interconverts chorismate and isochorismate. In E. coli, ... |
317-609 |
5.13e-40 |
|
isochorismate synthases; This enzyme interconverts chorismate and isochorismate. In E. coli, different loci encode isochorismate synthases for the pathways of menaquinone biosynthesis and enterobactin biosynthesis (via salicilate) and fail to complement each other. Among isochorismate synthases, the N-terminal domain is poorly conserved. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273127 Cd Length: 351 Bit Score: 151.37 E-value: 5.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 317 DAVLAASKSTPTVPSfDPTVIGRLHVRDsRERYMATIERIQEAIRAGETYEVCLTTELFAEVHGEIHPAAMYQALSTAVP 396
Cdd:TIGR00543 62 FAVSSGIRPLRALPE-QMTTLTTGEDPD-KAAWRTAVEEALENIRQGPLDKVVLARALTLKFADDIDPIAVLANLRQQYP 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 397 APMRSLVVT-DDVAVISASPERFIAMNERMVASSPIKGTRKRSADHEEDRALADDLRTNPKDRAENLMIVDLVRNDLARV 475
Cdd:TIGR00543 140 NAYIFLLEPpQGGVFLGATPERLLSREKGELLTEALAGTAPRSADPEEDRKLGELLLKDDKNLREHRLVVEYIRRRLQPI 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 476 CESgsVRVPELCAVHSFTTVHQLISTVEGQLRPTSTPIDVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSGCIGYI 555
Cdd:TIGR00543 220 CTS--LDVSETPELLKLANVQHLYTPISARLKDGDSLLDLLKQLHPTPAVGGLPREEALDFIREHEPFDRGLYAAPLGWL 297
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1437403794 556 GDDLRTDLAMVIRSVVLTPTTLSYGVGGAIIALSDPAEEWAEITTKSRVLLDLL 609
Cdd:TIGR00543 298 DGEGNGEFAVGIRSALVEDGQVRLYAGAGIVADSDPESEWEETELKLQTMLRAL 351
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
6-190 |
5.88e-40 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 146.87 E-value: 5.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 6 ILVVDNFDSFTYNIVDYLHRCGARPHVVTNNA-SPEDIDLNRYHGIVISPGPGHPsvaEDVGISawvLQTAQ-----CPV 79
Cdd:PLN02335 21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRNDElTVEELKRKNPRGVLISPGPGTP---QDSGIS---LQTVLelgplVPL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 80 LGVCLGMQLMVTSEGGRVDRAPEAV-HGRVDTL--NIVAADELFAGLPRTFSIVRYHSL--AAITVPP-SMEVTSSNPEG 153
Cdd:PLN02335 95 FGVCMGLQCIGEAFGGKIVRSPFGVmHGKSSPVhyDEKGEEGLFSGLPNPFTAGRYHSLviEKDTFPSdELEVTAWTEDG 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1437403794 154 IVMSIRHRSRPW-WGVQFHPESIAGDFGMEIIDRFVDL 190
Cdd:PLN02335 175 LIMAARHRKYKHiQGVQFHPESIITTEGKTIVRNFIKI 212
|
|
| PRK06404 |
PRK06404 |
anthranilate synthase component I; Reviewed |
353-606 |
1.55e-38 |
|
anthranilate synthase component I; Reviewed
Pssm-ID: 102361 [Multi-domain] Cd Length: 351 Bit Score: 146.94 E-value: 1.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 353 IERIQEAIRAGETYEVCLTTELFAEVHgeihpaaMYQALSTAVPAPmRSLVV----TDDVAVISASPERFIAMNERMVAS 428
Cdd:PRK06404 111 IKELIELIRAGEVLQVVISREFEANID-------FKEKLSEFINND-RSRYVfyyrFGKYRVVGSSPENVFTVNGNIINV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 429 SPIKGTRkrsadheEDRALADDLRTNPKDRAENLMIVDLVRNDLARVCESGSVRVPELCAVHSFTTVHQLISTVEGQLRP 508
Cdd:PRK06404 183 DPIAGTY-------DDKILSNELLNSEKDKLEHRMLLDLARNDLSKFADIGTLNVDKVMKIEEFSSVKHLVSQVTAKFSN 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 509 TSTpIDVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSGCIGYIGDDLrTDLAMVIRSVVLTPTTLSYGVGGAIIAL 588
Cdd:PRK06404 256 ASY-RDILASMFPAGTVSGSPKERAIEIINKYEETPRGPYGGAIGIISKGY-TDMALVIRTAYSHGNGFRVRAGAGIVKD 333
|
250
....*....|....*...
gi 1437403794 589 SDPAEEWAEITTKSRVLL 606
Cdd:PRK06404 334 SDPEDEVNEIYSKARSVM 351
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
6-189 |
1.86e-38 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 141.87 E-value: 1.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 6 ILVVDNFDSFTYNIVDYLHRCGARPHVVTNNA-SPEDIDLNRYHGIVISPGPGHPSVAedvGISAWVLQ--TAQCPVLGV 82
Cdd:PRK07649 2 ILMIDNYDSFTFNLVQFLGELGQELVVKRNDEvTISDIENMKPDFLMISPGPCSPNEA---GISMEVIRyfAGKIPIFGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 83 CLGMQLMVTSEGGRVDRAPEAVHGRVDTlniVAADE--LFAGLPRTFSIVRYHSL--AAITVPPSMEVTSSNPEGIVMSI 158
Cdd:PRK07649 79 CLGHQSIAQVFGGEVVRAERLMHGKTSL---MHHDGktIFSDIPNPFTATRYHSLivKKETLPDCLEVTSWTEEGEIMAI 155
|
170 180 190
....*....|....*....|....*....|.
gi 1437403794 159 RHRSRPWWGVQFHPESIAGDFGMEIIDRFVD 189
Cdd:PRK07649 156 RHKTLPIEGVQFHPESIMTSHGKELLQNFIR 186
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
6-188 |
6.63e-35 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 131.52 E-value: 6.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 6 ILVVDNFDSFTYNIVDYLHRCGARPHVVTNNA-SPEDIDLNRYHGIVISPGPGHPSVAedvGISAWVLQ--TAQCPVLGV 82
Cdd:PRK06774 2 LLLIDNYDSFTYNLYQYFCELGTEVMVKRNDElQLTDIEQLAPSHLVISPGPCTPNEA---GISLAVIRhfADKLPILGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 83 CLGMQLMVTSEGGRVDRAPEAVHGRVDTLNiVAADELFAGLPRTFSIVRYHSL--AAITVPPSMEVTS-SNPEGIV---M 156
Cdd:PRK06774 79 CLGHQALGQAFGARVVRARQVMHGKTSAIC-HSGQGVFRGLNQPLTVTRYHSLviAADSLPGCFELTAwSERGGEMdeiM 157
|
170 180 190
....*....|....*....|....*....|..
gi 1437403794 157 SIRHRSRPWWGVQFHPESIAGDFGMEIIDRFV 188
Cdd:PRK06774 158 GIRHRTLPLEGVQFHPESILSEQGHQLLDNFL 189
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
6-184 |
1.29e-33 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 127.93 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 6 ILVVDNFDSFTYNIVDYLHRCGARPHVVtnnaSPEDIDLN---RYHGIVISPGPGHPSVAEDvgISAWVLQTAQC-PVLG 81
Cdd:PRK06895 4 LLIINNHDSFTFNLVDLIRKLGVPMQVV----NVEDLDLDeveNFSHILISPGPDVPRAYPQ--LFAMLERYHQHkSILG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 82 VCLGMQLMVTSEGGRVDRAPEAVHGRVDTLNIVAADELFAGLPRTFSIVRYHSLA--AITVPPSMEVTSSNPEGIVMSIR 159
Cdd:PRK06895 78 VCLGHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSPLFDGLPEEFNIGLYHSWAvsEENFPTPLEITAVCDENVVMAMQ 157
|
170 180
....*....|....*....|....*
gi 1437403794 160 HRSRPWWGVQFHPESIAGDFGMEII 184
Cdd:PRK06895 158 HKTLPIYGVQFHPESYISEFGEQIL 182
|
|
| PRK07093 |
PRK07093 |
para-aminobenzoate synthase component I; Validated |
345-601 |
8.00e-33 |
|
para-aminobenzoate synthase component I; Validated
Pssm-ID: 235932 [Multi-domain] Cd Length: 323 Bit Score: 129.60 E-value: 8.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 345 SRERYMATIERIQEAIRAGETYEVCLT--TelfaEVHGEIHPAAMYQALStavpAPMRsLVVTDDVAVIsaSPERFIAMN 422
Cdd:PRK07093 72 SFEEYQQGFELVQEEIQAGNSYLLNLTypT----PIETNLSLEEIFQASK----AKYK-LLFKDQFVCF--SPEPFVRIE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 423 ERMVASSPIKGTRKRSADHEEDRALADdlrtnPKDRAENLMIVDLVRNDLARVCEsgSVRvpelcaVHSFTTVhQLISTV 502
Cdd:PRK07093 141 DNKISTYPMKGTIDASLPNAEEKLLND-----EKEFAEHATIVDLLRNDLSMVAK--NVR------VTRFRYI-DKIKTN 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 503 EGQLRPTSTPI-------------DVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSGCIGYI-GDDLRTdlAMVIR 568
Cdd:PRK07093 207 KGEILQTSSEIsgtlpenwqenigDILAKLLPAGSITGAPKEKTVEIIEQAEGYERGFYTGVFGYFdGESLDS--AVMIR 284
|
250 260 270
....*....|....*....|....*....|...
gi 1437403794 569 SVVLTPTTLSYGVGGAIIALSDPAEEWAEITTK 601
Cdd:PRK07093 285 FIEQENDGLYFKSGGGITIDSDLKDEYNELIQK 317
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
6-188 |
1.34e-32 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 124.64 E-value: 1.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 6 ILVVDNFDSFTYNIVDYLHRCGARPHVVTNNA-SPEDIDLNRYHGIVISPGPGHPSvaeDVGISAWVLQ--TAQCPVLGV 82
Cdd:PRK08007 2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDAlTLADIDALKPQKIVISPGPCTPD---EAGISLDVIRhyAGRLPILGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 83 CLGMQLMVTSEGGRVDRAPEAVHGRVDTLNiVAADELFAGLPRTFSIVRYHSLAA--ITVPPSMEVTSSNPEGIVMSIRH 160
Cdd:PRK08007 79 CLGHQAMAQAFGGKVVRAAKVMHGKTSPIT-HNGEGVFRGLANPLTVTRYHSLVVepDSLPACFEVTAWSETREIMGIRH 157
|
170 180
....*....|....*....|....*...
gi 1437403794 161 RSRPWWGVQFHPESIAGDFGMEIIDRFV 188
Cdd:PRK08007 158 RQWDLEGVQFHPESILSEQGHQLLANFL 185
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
6-188 |
8.09e-31 |
|
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: 119.56 E-value: 8.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 6 ILVVDNFDSFTYNIVDYLHRCGARPHVVTNNASPEDIDLNRYHGIVISPGPghPSV-AEDV-GISAWVLqTAQCPVLGVC 83
Cdd:cd01742 1 ILILDFGSQYTHLIARRVRELGVYSEILPNTTPLEEIKLKNPKGIILSGGP--SSVyEEDApRVDPEIF-ELGVPVLGIC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 84 LGMQLMVTSEGGRVDRAPEAVHGRVdTLNIVAADELFAGLPRTFSIVRYHSLAAITVPPSMEVTSSNPEGIVMSIRHRSR 163
Cdd:cd01742 78 YGMQLIAKALGGKVERGDKREYGKA-EIEIDDSSPLFEGLPDEQTVWMSHGDEVVKLPEGFKVIASSDNCPVAAIANEEK 156
|
170 180
....*....|....*....|....*
gi 1437403794 164 PWWGVQFHPESIAGDFGMEIIDRFV 188
Cdd:cd01742 157 KIYGVQFHPEVTHTEKGKEILKNFL 181
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
6-188 |
1.90e-30 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 118.83 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 6 ILVVDNFDSFTYNIVDYLHRCGARPHVVTNnaspEDID------LNRYHgIVISPGPGHPSvaeDVGISAWVLQ--TAQC 77
Cdd:PRK08857 2 LLMIDNYDSFTYNLYQYFCELGAQVKVVRN----DEIDidgieaLNPTH-LVISPGPCTPN---EAGISLQAIEhfAGKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 78 PVLGVCLGMQLMVTSEGGRVDRAPEAVHGRVDTLNIVAAdELFAGLPRTFSIVRYHSLA--AITVPPSMEVTS--SNPEG 153
Cdd:PRK08857 74 PILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRHTGR-SVFKGLNNPLTVTRYHSLVvkNDTLPECFELTAwtELEDG 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 1437403794 154 I---VMSIRHRSRPWWGVQFHPESIAGDFGMEIIDRFV 188
Cdd:PRK08857 153 SmdeIMGFQHKTLPIEAVQFHPESIKTEQGHQLLANFL 190
|
|
| PRK09522 |
PRK09522 |
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ... |
4-196 |
4.41e-30 |
|
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;
Pssm-ID: 181927 [Multi-domain] Cd Length: 531 Bit Score: 125.91 E-value: 4.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 4 AHILVVDNFDSFTYNIVDYLhRCGARPHVVTNNASPEDIDLNRYHG-----IVISPGPGHPSvaeDVGISAWVLQT--AQ 76
Cdd:PRK09522 2 ADILLLDNIDSFTYNLADQL-RSNGHNVVIYRNHIPAQTLIERLATmsnpvLMLSPGPGVPS---EAGCMPELLTRlrGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 77 CPVLGVCLGMQLMVTSEGGRVDRAPEAVHGRVDTLNiVAADELFAGLPRTFSIVRYHSLAAITVPPSMEVTSSNpEGIVM 156
Cdd:PRK09522 78 LPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIE-HDGQAMFAGLTNPLPVARYHSLVGSNIPAGLTINAHF-NGMVM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1437403794 157 SIRHRSRPWWGVQFHPESIAGDFGMEIIDRFVDLCTPQYR 196
Cdd:PRK09522 156 AVRHDADRVCGFQFHPESILTTQGARLLEQTLAWAQQKLE 195
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
6-191 |
4.64e-29 |
|
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: 114.72 E-value: 4.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 6 ILVVDNFDSFTYNIVDYLHRCGARPHVVTNNASPEDIDLNRYHGIVISPGPGhpSVAED--VGISAWVLQtAQCPVLGVC 83
Cdd:TIGR00888 1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGPS--SVYAEnaPRADEKIFE-LGVPVLGIC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 84 LGMQLMVTSEGGRVDRAPEAVHGRVdTLNIVAADELFAGLPRTFSIVRYHSLAAITVPPSMEVTSSNPEGIVMSIRHRSR 163
Cdd:TIGR00888 78 YGMQLMAKQLGGEVGRAEKREYGKA-ELEILDEDDLFRGLPDESTVWMSHGDKVKELPEGFKVLATSDNCPVAAMAHEEK 156
|
170 180
....*....|....*....|....*....
gi 1437403794 164 PWWGVQFHPESIAGDFGMEIIDRFV-DLC 191
Cdd:TIGR00888 157 PIYGVQFHPEVTHTEYGNELLENFVyDVC 185
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
349-639 |
3.52e-28 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 121.18 E-value: 3.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 349 YMATIERIQEAIRAGETYEVcLTTELFAEvHGEIHPAAMYQALSTAVPAPMRSLV-VTDDVAVISASPERFIAMNERMVA 427
Cdd:PRK13566 246 YAALVEKAKESFRRGDLFEV-VPGQTFYE-PCERSPSEIFRRLKEINPSPYGFFInLGDGEYLVGASPEMFVRVEGRRVE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 428 SSPIKGTRKRSADHEEDRALADDLRTNPKDRAENLMIVDLVRNDLARVCESGSVRV-----PELCAvHSFTTV-Hqlist 501
Cdd:PRK13566 324 TCPISGTIKRGADAIGDAEQIRKLLNSKKDESELTMCTDVDRNDKSRVCEPGSVKVigrrqIEMYS-RLIHTVdH----- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 502 VEGQLRPTSTPIDVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSGCIGYIG--DDLRTDLamVIRSVVLTPTTLSY 579
Cdd:PRK13566 398 VEGRLRPGFDALDAFLTHAWAVTVTGAPKLWAMQFIEDHERSPRRWYGGAVGMVGfdGDMNTGL--TLRTIRIKDGVAEV 475
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1437403794 580 GVGGAIIALSDPAEEWAEITTKSRVLLDLLGQDFPQSLII---DSFLVNDGKTSGLNLHLDRF 639
Cdd:PRK13566 476 RVGATLLFDSDPEAEEAETELKASALLQALRGAKPKNLSAeepDAAAVGEGKRVLLVDHEDSF 538
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
5-173 |
1.07e-27 |
|
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: 111.96 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 5 HILVVD---NFDSFTYNIVDYLHRCGARPHVV---TNNASPEDIDLNRYHGIVISPGPGhpSVAEDvgiSAWVLQTAQC- 77
Cdd:COG0518 1 KILILDhdpFGGQYPGLIARRLREAGIELDVLrvyAGEILPYDPDLEDPDGLILSGGPM--SVYDE---DPWLEDEPALi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 78 --------PVLGVCLGMQLMVTSEGGRVDRAPEAVHGRVdTLNIVAADELFAGLPRTFSIVRYHSLAAITVPPSMEVTSS 149
Cdd:COG0518 76 reafelgkPVLGICYGAQLLAHALGGKVEPGPGREIGWA-PVELTEADPLFAGLPDEFTVWMSHGDTVTELPEGAEVLAS 154
|
170 180
....*....|....*....|....
gi 1437403794 150 NPEGIVMSIRHrSRPWWGVQFHPE 173
Cdd:COG0518 155 SDNCPNQAFRY-GRRVYGVQFHPE 177
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
5-191 |
1.32e-27 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 110.33 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 5 HILVVDNFDSFTYNIVDYLHRCGARPHVVTNNASPEDIDlNRYHGIVISPGPGhpsvAEDVGISAWVLQTAQCPVLGVCL 84
Cdd:PRK00758 1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTTPVEEIK-AFEDGLILSGGPD----IERAGNCPEYLKELDVPILGICL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 85 GMQLMVTSEGGRVDRAPEAVHGRVDtLNIVAADELFAGLPRTFSIVRYHSLAAITVPPSMEVTSSNPEGIVMSIRHRSRP 164
Cdd:PRK00758 76 GHQLIAKAFGGEVGRGEYGEYALVE-VEILDEDDILKGLPPEIRVWASHADEVKELPDGFEILARSDICEVEAMKHKEKP 154
|
170 180
....*....|....*....|....*..
gi 1437403794 165 WWGVQFHPESIAGDFGMEIIDRFVDLC 191
Cdd:PRK00758 155 IYGVQFHPEVAHTEYGEEIFKNFLEIC 181
|
|
| PRK05637 |
PRK05637 |
anthranilate synthase component II; Provisional |
4-189 |
1.86e-26 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 180178 [Multi-domain] Cd Length: 208 Bit Score: 107.62 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 4 AHILVVDNFDSFTYNIVDYLHRCGARPHVVTNNASPEDIDLNRYHGIVISPGPGHPSvaeDVG-ISAWVLQT-AQCPVLG 81
Cdd:PRK05637 2 THVVLIDNHDSFVYNLVDAFAVAGYKCTVFRNTVPVEEILAANPDLICLSPGPGHPR---DAGnMMALIDRTlGQIPLLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 82 VCLGMQLMVTSEGGRVdRAPEAVHGRVD--TLNIVAADE-LFAGLP------------RTFSIVRYHSLAAITVPPSMEV 146
Cdd:PRK05637 79 ICLGFQALLEHHGGKV-EPCGPVHGTTDnmILTDAGVQSpVFAGLAtdvepdhpeipgRKVPIARYHSLGCVVAPDGMES 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1437403794 147 TSSNPEGI---VMSIRHRSRPWWGVQFHPESIAGDFGMEIIDRFVD 189
Cdd:PRK05637 158 LGTCSSEIgpvIMAAETTDGKAIGLQFHPESVLSPTGPIILSRCVE 203
|
|
| guaA |
PRK00074 |
GMP synthase; Reviewed |
32-191 |
3.88e-23 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 103.97 E-value: 3.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 32 VVTNNASPEDIDLNRYHGIVISPGP------GHPSVAEDV---GIsawvlqtaqcPVLGVCLGMQLMVTSEGGRVDRAPE 102
Cdd:PRK00074 32 IVPYDISAEEIRAFNPKGIILSGGPasvyeeGAPRADPEIfelGV----------PVLGICYGMQLMAHQLGGKVERAGK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 103 AVHGRVDtLNIVAADELFAGLPRTFSIVRYHSLAAITVPPSMEVTSSNPEGIVMSIRHRSRPWWGVQFHPESIAGDFGME 182
Cdd:PRK00074 102 REYGRAE-LEVDNDSPLFKGLPEEQDVWMSHGDKVTELPEGFKVIASTENCPIAAIANEERKFYGVQFHPEVTHTPQGKK 180
|
170
....*....|
gi 1437403794 183 IIDRFV-DLC 191
Cdd:PRK00074 181 LLENFVfDIC 190
|
|
| PRK06772 |
PRK06772 |
salicylate synthase; |
260-601 |
2.05e-22 |
|
salicylate synthase;
Pssm-ID: 102546 [Multi-domain] Cd Length: 434 Bit Score: 100.97 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 260 YGYIGYEANDATFGTAVHAPK----PAEVPTTAMMFCTEVIAIRGDraqiTAPSSRwgRLRDAVLAASKSTPTVP-SFDP 334
Cdd:PRK06772 95 YGQVGFNFAAHARGIAFNAGEwpllTLTVPREELIFEKGNVTVYAD----SADGCR--RLCEWVKEAGTTTQNAPlAVDT 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 335 TVIGrlhvrdsrERYMATIERIQEAIRAGETYEVCLTTELFAEVHGEIHPAAMYQALSTAvpaPMRSLVVTDD-VAVISA 413
Cdd:PRK06772 169 ALNG--------EAYKQQVARAVAEIRRGEYVKVIVSRAIPLPSRIDMPATLLYGRQANT---PVRSFMFRQEgREALGF 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 414 SPERFIAMNERMVASSPIKGTRKRSADHEEDRALADDLRTNPKDRAENLMIVDLVRNDLARVCESGSVRVPELCAVHSFT 493
Cdd:PRK06772 238 SPELVMSVTGNKVVTEPLAGTRDRMGNPEHNKAKEAELLHDSKEVLEHILSVKEAIAELEAVCQPGSVVVEDLMSVRQRG 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 494 TVHQLISTVEGQLRPTSTPIDVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSGCIgYIGDDLRTDLAMVIRSVVLT 573
Cdd:PRK06772 318 SVQHLGSGVSGQLAENKDAWDAFTVLFPSITASGIPKNAALNAIMQIEKTPRELYSGAI-LLLDDTRFDAALVLRSVFQD 396
|
330 340
....*....|....*....|....*...
gi 1437403794 574 PTTLSYGVGGAIIALSDPAEEWAEITTK 601
Cdd:PRK06772 397 SQRCWIQAGAGIIAQSTPERELTETREK 424
|
|
| PRK06923 |
PRK06923 |
isochorismate synthase DhbC; Validated |
299-613 |
3.39e-22 |
|
isochorismate synthase DhbC; Validated
Pssm-ID: 235886 [Multi-domain] Cd Length: 399 Bit Score: 99.81 E-value: 3.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 299 RGDRAQITAP-SSRW-GRLRDAVLAASKSTPTVpSFDPTVIgrlhvrDSRERYMATIERIQEAIRAGETYEVCLTTELFA 376
Cdd:PRK06923 79 RRKEVQLIVPeYSRIsERLQLDTTNHLEINRNL-TFEMTPV------PDPEVYMNGVKQGIAKIQDGDLKKIVLSRSLDV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 377 EVHGEIHPAAMYQALSTA----------VPAPMRSLVVTddvaVISASPERFIAMNERMVASSPIKGTRKRSADHEEDRA 446
Cdd:PRK06923 152 KSSEKIDKQKLLRELAEHnkhgytfavnLPKDENENSKT----LIGASPELLVSRHGMQVISNPLAGSRPRSDDPVEDKR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 447 LADDLRTNPKDRAENLMIVDLVRNDLARVCEsgSVRVPELCAV-HSFTTVHqLISTVEGQLR-PTSTPIDVLRATFPGGS 524
Cdd:PRK06923 228 RAEELLSSPKDLHEHAVVVEAVAAALRPYCH--TLHVPEKPSViHTEAMWH-LSTEVKGELKdPNTSSLELAIALHPTPA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 525 MTGAPKHRTMHLITELEGKQRGVYSGCIGYIGDDLRTDLAMVIRSVVLTPTTLSYGVGGAIIALSDPAEEWAEITTKSRV 604
Cdd:PRK06923 305 VCGTPTEEAREAIQQIEPFDREFFTGMLGWSDLNGDGEWIVTIRCAEVEENTLRLYAGAGVVAESKPEDELAETSAKFQT 384
|
....*....
gi 1437403794 605 LLDLLGQDF 613
Cdd:PRK06923 385 MLKAMGLND 393
|
|
| PRK07054 |
PRK07054 |
isochorismate synthase; |
292-611 |
9.47e-22 |
|
isochorismate synthase;
Pssm-ID: 235920 [Multi-domain] Cd Length: 475 Bit Score: 99.45 E-value: 9.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 292 CTEVIAIRGDRAQIT-APSSRWGRLRDAVLAASKSTPTvpsfdptvIGRLHVRDSRErYMATIERIQEAIRAGETYEVCL 370
Cdd:PRK07054 148 CQHLVAAHDDPAALAgACCARIERLARPAPAADDDAPR--------LLRASALQARE-WQHEVRRAVDAIRGGAFGKVVL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 371 TTELFAEVHGEIHPAAMYQALSTAVPAPMRSLVVTDDVAVISASPERFIAMNERMVASSPIKGTRKRSADHEEDRALADD 450
Cdd:PRK07054 219 ARDVLQQYARPVAIGPLLRRLRLRDPHAHLFAFRRGNACFLGATPERLVRVAAGDLHTHALAGTIARGADPAEDARLGAA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 451 LRTNPKDRAENLMIVDLVRNDLARVCESgsVRVPELCAVHSFTTVHQLISTVEGQLRPTSTPIDVLRATFPGGSMTGAPK 530
Cdd:PRK07054 299 LMASAKDRLEHALVVDAIRAALAPLSRA--LDIPDQPSLHRLPRLQHLSTPIRATLAPDATLLQVVAALHPTPAVGGHPR 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 531 HRTMHLITELEGKQRGVYSGCIGYIGDDLRTDLAMVIRSVVLTPTTLSYGVGGAIIALSDPAEEWAEITTKSRVLLDLLG 610
Cdd:PRK07054 377 AAALDYIRAHEGFDRGWYAAPIGWLDAHGNGDFAVALRSALITGGACRLFAGCGIVADSEPASEYRETCLKLSGMREALR 456
|
.
gi 1437403794 611 Q 611
Cdd:PRK07054 457 A 457
|
|
| PRK07912 |
PRK07912 |
salicylate synthase; |
260-601 |
2.13e-21 |
|
salicylate synthase;
Pssm-ID: 169151 [Multi-domain] Cd Length: 449 Bit Score: 97.94 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 260 YGYIGYEANDATFGTAVHAPKPAEVpttAMMFC--TEVIAIRGDRAQITAPSSRWGRLRDAVLAASKSTPTVPSFDptvi 337
Cdd:PRK07912 106 FGWVAFEFGVYRYGLQQRLAPGTPL---ARVFSprTRIVVTEKGIRLFGAGIRHREAIDRLLATGVREVPQSRSVD---- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 338 grlhVRDSRERYMATIERIQEAIRAGETYEVCLTTELfaEVHGEIHPAAMYQaLSTAVPAPMRS-LVVTDDVAVISASPE 416
Cdd:PRK07912 179 ----VSDDPSGYRDRVAVAVAEIAAGRYHKVILSRCV--EVPFAVDFPATYR-LGRRHNTPVRSfLLRLGGIRALGYSPE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 417 RFIAMNE-RMVASSPIKGTRKRSADHEEDRALADDLRTNPKDRAENLMIVDLVRNDLARVCESGSVRVPELCAVHSFTTV 495
Cdd:PRK07912 252 LVTAVRAdGVVITEPLAGTRAFGRGAAIDRLARDDLESNSKEIVEHAISVRSSLAEITEIAEPGSAAVIDFMTVRERGSV 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 496 HQLISTVEGQLRPTSTPIDVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSGCIGYIGDDLRTDLAMVIRSVVLTPT 575
Cdd:PRK07912 332 QHLGSTVRGRLDASSDRMDALEALFPAVTASGIPKAAGVDAIFRLDEAPRGLYSGAVVMLSADGGLDAALTLRAAYQVGG 411
|
330 340
....*....|....*....|....*.
gi 1437403794 576 TLSYGVGGAIIALSDPAEEWAEITTK 601
Cdd:PRK07912 412 RTWLRAGAGIIEESEPEREFEETCEK 437
|
|
| PLN02347 |
PLN02347 |
GMP synthetase |
37-191 |
8.17e-19 |
|
GMP synthetase
Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 90.90 E-value: 8.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 37 ASPEDIDLNRYHGIVISPGP------GHPSVAEdvGISAWVlQTAQCPVLGVCLGMQLMVTSEGGRVDRAPEAVHGRVDt 110
Cdd:PLN02347 44 ASLDRIASLNPRVVILSGGPhsvhveGAPTVPE--GFFDYC-RERGVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRME- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 111 LNIVAADELFAGLP--RTFSIVRYHSLAAITVPPSMEVTSSNPEGIVMSIRHRSRPWWGVQFHPESIAGDFGMEIIDRFV 188
Cdd:PLN02347 120 IRVVCGSQLFGDLPsgETQTVWMSHGDEAVKLPEGFEVVAKSVQGAVVAIENRERRIYGLQYHPEVTHSPKGMETLRHFL 199
|
....
gi 1437403794 189 -DLC 191
Cdd:PLN02347 200 fDVC 203
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
17-188 |
2.95e-18 |
|
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: 83.31 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 17 YNIVDYLHRCGARPHVVTNNASPEDIDLNRYHGIVISPGPGHPSVAEDVgISA--WVLQTAQcPVLGVCLGMQLMVTSEG 94
Cdd:cd01744 10 HNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEA-IKTvrKLLGKKI-PIFGICLGHQLLALALG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 95 GRVDRAPEAVHGR----VDTLN----IVAADELFAglprtfsivryhsLAAITVPPSMEVTSSNPE-GIVMSIRHRSRPW 165
Cdd:cd01744 88 AKTYKMKFGHRGSnhpvKDLITgrvyITSQNHGYA-------------VDPDSLPGGLEVTHVNLNdGTVEGIRHKDLPV 154
|
170 180
....*....|....*....|....
gi 1437403794 166 WGVQFHPESIAGDFGMEII-DRFV 188
Cdd:cd01744 155 FSVQFHPEASPGPHDTEYLfDEFL 178
|
|
| PLN02786 |
PLN02786 |
isochorismate synthase |
409-601 |
7.08e-17 |
|
isochorismate synthase
Pssm-ID: 178383 [Multi-domain] Cd Length: 533 Bit Score: 84.84 E-value: 7.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 409 AVISASPERFIAMNERMVASSPIKGTRKRSADHEEDRALADDLRTNPKDRAENLMIVDLVRNDLARVCEsgSVRVPELCA 488
Cdd:PLN02786 325 AFIGNTPEQLFHRKGLGVCSEALAATRPRGGSSARDLQIELDLLTSPKDDLEFSIVRENIREKLEAICD--RVVVEPHKA 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 489 VHSFTTVHQLISTVEGQLRPTSTPIDVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSGCIGYIGDDlRTDLAMVIR 568
Cdd:PLN02786 403 IRKLARVQHLYAQLAGRLRSEDDEFDILAALHPTPAVCGHPTEEARLLIAETESFDRGMYAGPVGWFGGG-ESEFAVGIR 481
|
170 180 190
....*....|....*....|....*....|....*.
gi 1437403794 569 SVVLTP--TTLSY-GVGgaIIALSDPAEEWAEITTK 601
Cdd:PLN02786 482 SALVEKglGALIYaGTG--IVEGSNPSSEWNELELK 515
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
618-812 |
8.34e-17 |
|
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to catalyze the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity.
Pssm-ID: 395844 [Multi-domain] Cd Length: 221 Bit Score: 80.09 E-value: 8.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 618 IIDSFLVNDGKTSGLNLHLDRFRTAC--LEHGYAH---------HEQLDAF--FAEALRsIPVTGQWFPRLEATPT-ELR 683
Cdd:pfam01063 2 VFETLRVYNGKIFFLDEHLARLRRSAklLGIPLPFdeedlrkiiEELLKANglGVGRLR-LTVSRGPGGFGLPTSDpTLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 684 IALRPAP------QLRGTTTLTSVAAVRPTPKYKGLD-LDYLAELRGSTTT--DDALLVTPAGVIAETTTAAIIAWDGTK 754
Cdd:pfam01063 81 IFVSALPpppeskKKGVISSLVRRNPPSPLPGAKTLNyLENVLARREAKAQgaDDALLLDEDGNVTEGSTSNVFLVKGGT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437403794 755 WMSMAPAR--LESVTESLLLQSARAQGEMVVTAALTVPEAQKLN-LWAVNSLHGVTPVTHI 812
Cdd:pfam01063 161 LYTPPLESgiLPGITRQALLDLAKALGLEVEERPITLADLQEADeAFLTNSLRGVTPVSSI 221
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
3-173 |
1.01e-16 |
|
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: 79.21 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 3 RAHILVVDNFDSfTYNIVDYLHRCGARPH--VVTNNASPEDI-DLNRYHGIVISPGPGhpSVAED-----VGISAWVLQ- 73
Cdd:cd01741 1 RILILQHDTPEG-PGLFEDLLREAGAETIeiDVVDVYAGELLpDLDDYDGLVILGGPM--SVDEDdypwlKKLKELIRQa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 74 -TAQCPVLGVCLGMQLMVTSEGGRVDRAPEAVHGRVDTLNIVAA---DELFAGLPRTFSIVRYHSLAAITVPPSMEVTSS 149
Cdd:cd01741 78 lAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAgkaDPLFAGLPDEFPVFHWHGDTVVELPPGAVLLAS 157
|
170 180
....*....|....*....|....
gi 1437403794 150 NPEGIVMSIRHRSRPwWGVQFHPE 173
Cdd:cd01741 158 SEACPNQAFRYGDRA-LGLQFHPE 180
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
3-190 |
1.31e-14 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 76.27 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 3 RAHILVVDnfdsF--TYNIVDYLHRCGARPHVVTNNASPEDI-DLNrYHGIVISPGPGHPSVAEDVGISAWVLQTAQCPV 79
Cdd:PRK12564 177 KYKVVAID----FgvKRNILRELAERGCRVTVVPATTTAEEIlALN-PDGVFLSNGPGDPAALDYAIEMIRELLEKKIPI 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 80 LGVCLGMQLMVTSEGGRV---------------DRAPEAV------HGrvdtlnivaadelFAglprtfsivryhsLAAI 138
Cdd:PRK12564 252 FGICLGHQLLALALGAKTykmkfghrganhpvkDLETGKVeitsqnHG-------------FA-------------VDED 305
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437403794 139 TVPPSMEVTSSNP-----EGivmsIRHRSRPWWGVQFHPESIAG----DFgmeIIDRFVDL 190
Cdd:PRK12564 306 SLPANLEVTHVNLndgtvEG----LRHKDLPAFSVQYHPEASPGphdsAY---LFDEFVEL 359
|
|
| PRK09266 |
PRK09266 |
hypothetical protein; Provisional |
621-828 |
1.70e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 236438 Cd Length: 266 Bit Score: 74.63 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 621 SFLVNDGKTSGLNLHLDRFRTACLE-HGYA-HHEQLDAFFAEALRS--------IPVTGQWF----PRLEATPTELrIAL 686
Cdd:PRK09266 30 SMQVRDGRVRGLDLHLQRLRRASRElFGAAlDDDRVRAQLRAALAAgpadasvrVTVFAPDFdfrnPLADVAPDVL-VAT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 687 RPAPQL-RGTTTLTSVAAVRPTPKYK------GLDLDYLAELRGsttTDDALLVTPAGVIAETTTAAIIAWDGTK--WMS 757
Cdd:PRK09266 109 SPPADGpAGPLRLQSVPYERELPHIKhvgtfgQLHLRRLAQRAG---FDDALFVDPDGRVSEGATWNLGFWDGGAvvWPQ 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437403794 758 mAPArLESVTESLLLQSARAQGEMVVTAALTVPEAQKLN-LWAVNSLHGVTPVTHIDGVALPNNPQRSGLLR 828
Cdd:PRK09266 186 -APA-LPGVTMALLQRGLERLGIPQRTRPVTLADLGRFAgAFACNAWRGQRAVSAIDDVALPDSHALLELLR 255
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
19-188 |
3.89e-14 |
|
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: 71.76 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 19 IVDY-----------LHRCGARPhVVTNNasPEDIDlnRYHGIVIsPGPGHPSVAEDV----GISAWVLQTAQC--PVLG 81
Cdd:cd01748 3 IIDYgmgnlrsvanaLERLGAEV-IITSD--PEEIL--SADKLIL-PGVGAFGDAMANlrerGLIEALKEAIASgkPFLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 82 VCLGMQLMVTS--EG----------GRVDRAPEAVHGRV-----DTLNIVAADELFAGLP--RTFSIVryHSLAAITVPP 142
Cdd:cd01748 77 ICLGMQLLFESseEGggtkglglipGKVVRFPASEGLKVphmgwNQLEITKESPLFKGIPdgSYFYFV--HSYYAPPDDP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1437403794 143 SMEVTSSNPEG-IVMSIRHRSRpwWGVQFHPE-SiaGDFGMEIIDRFV 188
Cdd:cd01748 155 DYILATTDYGGkFPAAVEKDNI--FGTQFHPEkS--GKAGLKLLKNFL 198
|
|
| PRK15016 |
PRK15016 |
isochorismate synthase EntC; Provisional |
330-610 |
2.12e-13 |
|
isochorismate synthase EntC; Provisional
Pssm-ID: 184977 [Multi-domain] Cd Length: 391 Bit Score: 72.98 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 330 PSFDPTVIGRLHVRDsRERYMATIERIQEAIRAGETYEVCLTTELFAEVHGEIHPAAMYQALSTAVPAPMRSLV-VTDDV 408
Cdd:PRK15016 111 RSQSLNVVERQAIPE-QTTFEAMVARAAALTATPQVDKVVLSRLIDITTDAAIDSGALLERLIAQNPVSYNFHVpLADGG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 409 AVISASPERFIAMNERMVASSPIKGTRKRSADHEEDRALADDLRTNPKDRAENLMIVDLVRNDLARvcESGSVRVPELCA 488
Cdd:PRK15016 190 VLLGASPELLLRKDGERFSSLPLAGSARRQPDEVLDREAGNRLLASEKDRHEHELVTQAMKEVLRE--RSSELHVPSSPQ 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 489 VHSFTTVHQLISTVEGQLRPTSTPIDVLRATFPGGSMTGAPKHRTMHLITELEGKQRGVYSGCIGYIGDDLRTDLAMVIR 568
Cdd:PRK15016 268 LITTPTLWHLATPFEGKANAQENALTLACLLHPTPALSGFPHQAAKQVIAELEPFDRELFGGIVGWCDSEGNGEWVVTIR 347
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1437403794 569 SVVLTPTTLSYGVGGAIIALSDPAEEWAEITTKSRVLLDLLG 610
Cdd:PRK15016 348 CAKLRENQVRLFAGAGIVPASSPLGEWRETGVKLSTMLNVFG 389
|
|
| IMP_synth_hisH |
TIGR01855 |
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ... |
19-190 |
4.61e-13 |
|
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: 68.51 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 19 IVDY-----------LHRCGARPHVVTNNAspediDLNRYHGIVIsPGPGH-PSVAEDV---GISAWVLQTAQC--PVLG 81
Cdd:TIGR01855 3 IIDYgvgnlgsvkraLKRVGAEPVVVKDSK-----EAELADKLIL-PGVGAfGAAMARLrenGLDLFVELVVRLgkPVLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 82 VCLGMQLM-------VTSEG-----GRVDRAPEAV--HGRVDTLNIVAADELFAGLPRTFSIVRYHSLAAitvPPSME-- 145
Cdd:TIGR01855 77 ICLGMQLLferseegGGVPGlglikGNVVKLEARKvpHMGWNEVHPVKESPLLNGIDEGAYFYFVHSYYA---VCEEEav 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1437403794 146 VTSSNPEGIVMSIRHRSRpWWGVQFHPESiAGDFGMEIIDRFVDL 190
Cdd:TIGR01855 154 LAYADYGEKFPAAVQKGN-IFGTQFHPEK-SGKTGLKLLENFLEL 196
|
|
| PRK09065 |
PRK09065 |
glutamine amidotransferase; Provisional |
45-173 |
7.18e-13 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181635 [Multi-domain] Cd Length: 237 Bit Score: 69.22 E-value: 7.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 45 NRYHGIVISpgpGHPSVAED-----VGISAWVLQTAQC--PVLGVCLGMQLMVTSEGGRVDRAPEavhGR------VDTL 111
Cdd:PRK09065 53 DDFAGVIIT---GSWAMVTDrldwsERTADWLRQAAAAgmPLLGICYGHQLLAHALGGEVGYNPA---GResgtvtVELH 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437403794 112 NIVAADELFAGLPRTFSIVRYHSLAAITVPPSMEVTSSNPEGIVMSIRHRSRPwWGVQFHPE 173
Cdd:PRK09065 127 PAAADDPLFAGLPAQFPAHLTHLQSVLRLPPGAVVLARSAQDPHQAFRYGPHA-WGVQFHPE 187
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
3-190 |
7.27e-13 |
|
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: 70.82 E-value: 7.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 3 RAHILVVDnfdsF--TYNIVDYLHRCGARPHVVTNNASPEDI-DLNrYHGIVISPGPGHPSVAEDVgISA-WVLQTAQCP 78
Cdd:COG0505 176 GFHVVALD----FgvKRNILRELAERGCRVTVVPATTSAEEIlALN-PDGVFLSNGPGDPAALDYA-IETiRELLGKGIP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 79 VLGVCLGMQLMVTSEGGRV---------------DRApeavHGRVDtlnIVAADELFAglprtfsiVRYHSLAAITVpps 143
Cdd:COG0505 250 IFGICLGHQLLALALGAKTyklkfghrganhpvkDLE----TGRVE---ITSQNHGFA--------VDEDSLPATDL--- 311
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1437403794 144 mEVTSSNP-----EGivmsIRHRSRPWWGVQFHPESIAG--DfGMEIIDRFVDL 190
Cdd:COG0505 312 -EVTHVNLndgtvEG----LRHKDLPAFSVQYHPEASPGphD-SAYLFDRFIEL 359
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
6-116 |
1.29e-12 |
|
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: 64.93 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 6 ILVVDNFDSFT---YNIVDYLHRCGARPHVVTNNASPE--DIDLNRYHGIVISPGPGHPSVAE-DVGISAWVLQTAQ--C 77
Cdd:cd01653 1 VAVLLFPGFEElelASPLDALREAGAEVDVVSPDGGPVesDVDLDDYDGLILPGGPGTPDDLArDEALLALLREAAAagK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1437403794 78 PVLGVCLGMQLMV-TSEGGrvdraPEAVHGRVDTLNIVAA 116
Cdd:cd01653 81 PILGICLGAQLLVlGVQFH-----PEAIDGAEAGARLLVN 115
|
|
| hisH |
PRK13143 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
19-191 |
3.21e-12 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 66.43 E-value: 3.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 19 IVDY-----------LHRCGARPhVVTNNasPEDIDlnRYHGIVIsPGPG-HPSVAEDVG-ISAWVLQTAQC--PVLGVC 83
Cdd:PRK13143 5 IIDYgvgnlrsvskaLERAGAEV-VITSD--PEEIL--DADGIVL-PGVGaFGAAMENLSpLRDVILEAARSgkPFLGIC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 84 LGMQLMVTS--EG----------GRVDRAPEAV---HGRVDTLNIVAADELFAGLPRTFsiVRY-HSLAAITVPPSMEVT 147
Cdd:PRK13143 79 LGMQLLFESseEGggvrglglfpGRVVRFPAGVkvpHMGWNTVKVVKDCPLFEGIDGEY--VYFvHSYYAYPDDEDYVVA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1437403794 148 SS----------NPEGIVmsirhrsrpwwGVQFHPESiAGDFGMEIIDRFVDLC 191
Cdd:PRK13143 157 TTdygiefpaavCNDNVF-----------GTQFHPEK-SGETGLKILENFVELI 198
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
6-89 |
1.93e-11 |
|
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: 61.06 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 6 ILVVDNFDSFT---YNIVDYLHRCGARPHVVTNNASPE--DIDLNRYHGIVISPGPGHPSVAE-DVGISAWVLQTAQ--C 77
Cdd:cd03128 1 VAVLLFGGSEElelASPLDALREAGAEVDVVSPDGGPVesDVDLDDYDGLILPGGPGTPDDLAwDEALLALLREAAAagK 80
|
90
....*....|..
gi 1437403794 78 PVLGVCLGMQLM 89
Cdd:cd03128 81 PVLGICLGAQLL 92
|
|
| HisH |
COG0118 |
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
19-184 |
2.67e-11 |
|
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: 63.52 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 19 IVDY-----------LHRCGARPHVVtnnASPEDIDlnRYHGIVIsPGPGHPSVA----EDVGISAWVLQTAQC--PVLG 81
Cdd:COG0118 5 IIDYgmgnlrsvakaLERLGAEVVVT---SDPDEIR--AADRLVL-PGVGAFGDAmenlRERGLDEAIREAVAGgkPVLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 82 VCLGMQLMVTS-------EG-----GRVDRAPEAVHgRV-----DTLNIVAADELFAGLPRT--FsivrY--HSLAAITV 140
Cdd:COG0118 79 ICLGMQLLFERseengdtEGlglipGEVVRFPASDL-KVphmgwNTVEIAKDHPLFAGIPDGeyF----YfvHSYYVPPD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1437403794 141 PPSMEVTSSNPEGIVMSIRHRsRPWWGVQFHPE-SiaGDFGMEII 184
Cdd:COG0118 154 DPEDVVATTDYGVPFTAAVER-GNVFGTQFHPEkS--GAAGLRLL 195
|
|
| PRK07567 |
PRK07567 |
glutamine amidotransferase; Provisional |
21-173 |
2.77e-11 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181035 [Multi-domain] Cd Length: 242 Bit Score: 64.58 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 21 DYLHRCGARPHVVT----NNASPEDIDLNRYHGIVISPGPGHPSVAEDVGiSAW-------------VLQTAQCPVLGVC 83
Cdd:PRK07567 22 AFLRYTGLDPAELRrirlDREPLPDLDLDDYSGVIVGGSPFNVSDPAESK-SPWqrrveaelsglldEVVARDFPFLGAC 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 84 LGMQLMVTSEGGRVDRA-PEAVHGRVDTL-NIVAADELFAGLPRTFSIVRYHSLAAITVPPSMEVTSSNPEGIVMSIRHR 161
Cdd:PRK07567 101 YGVGTLGHHQGGVVDRTyGEPVGAVTVSLtDAGRADPLLAGLPDTFTAFVGHKEAVSALPPGAVLLATSPTCPVQMFRVG 180
|
170
....*....|..
gi 1437403794 162 SRPwWGVQFHPE 173
Cdd:PRK07567 181 ENV-YATQFHPE 191
|
|
| hisH |
PRK13141 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
19-191 |
3.70e-11 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 63.23 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 19 IVDY----LH-------RCGARPhVVTNNasPEDIDlnRYHGIVIsPGPG--HPSVAE------DVGISAWVlqTAQCPV 79
Cdd:PRK13141 4 IIDYgmgnLRsvekaleRLGAEA-VITSD--PEEIL--AADGVIL-PGVGafPDAMANlrerglDEVIKEAV--ASGKPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 80 LGVCLGMQLMVTS-------EG-----GRVDRAPEAVHGRV-----DTLNIVAADELFAGLPRTFSIvrY--HSLAAITV 140
Cdd:PRK13141 76 LGICLGMQLLFESseefgetEGlgllpGRVRRFPPEEGLKVphmgwNQLELKKESPLLKGIPDGAYV--YfvHSYYADPC 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1437403794 141 PPSMEVTSSNPEGIVMSIRHRSRpWWGVQFHPE-SiaGDFGMEIIDRFVDLC 191
Cdd:PRK13141 154 DEEYVAATTDYGVEFPAAVGKDN-VFGAQFHPEkS--GDVGLKILKNFVEMV 202
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
27-173 |
5.89e-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: 5.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 27 GARPHVVTNNASPEDID--LNRYHGIVISPGP---------------GHPSVAEDVGISAWVLQTAQ--CPVLGVCLGMQ 87
Cdd:pfam07722 37 GGLPVLLPILGDPEDAAaiLDRLDGLLLTGGPnvdphfygeepsesgGPYDPARDAYELALIRAALArgKPILGICRGFQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 88 LMVTSEGG----RVDRAPEAVHGRVD----------TLNIVAADELFAGLPRTFSIVR-YHSLAAITVPPSMEVTSSNPE 152
Cdd:pfam07722 117 LLNVALGGtlyqDIQEQPGFTDHREHcqvapyapshAVNVEPGSLLASLLGSEEFRVNsLHHQAIDRLAPGLRVEAVAPD 196
|
170 180
....*....|....*....|...
gi 1437403794 153 GIVMSIRHRSRPWW--GVQFHPE 173
Cdd:pfam07722 197 GTIEAIESPNAKGFalGVQWHPE 219
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
5-190 |
2.03e-10 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 63.37 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 5 HILVVDnfdsFTY--NIVDYLHRCGARPHVVTNNASPEDIDLNRYHGIVISPGPGHPSvaEDVGISAWVLQTAQ-CPVLG 81
Cdd:PRK12838 169 HVALID----FGYkkSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPGDPK--ELQPYLPEIKKLISsYPILG 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 82 VCLGMQLMVTSEGGRVDRAP-----------EAVHGRV--DTLNI---VAADElfagLPRTFSIVRYHSLAAITVppsme 145
Cdd:PRK12838 243 ICLGHQLIALALGADTEKLPfghrganhpviDLTTGRVwmTSQNHgyvVDEDS----LDGTPLSVRFFNVNDGSI----- 313
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1437403794 146 vtssnpEGivmsIRHRSRPWWGVQFHPESIAG--DFGmEIIDRFVDL 190
Cdd:PRK12838 314 ------EG----LRHKKKPVLSVQFHPEAHPGphDAE-YIFDEFLEM 349
|
|
| PuuD |
COG2071 |
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
18-191 |
2.37e-10 |
|
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: 61.34 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 18 NIVDYLHRCGARPHVVTNNASPEDID--LNRYHGIVIS---------------PGPGHPSVAEDvgisAWVLQTAQC--- 77
Cdd:COG2071 19 DYVRAVRAAGGLPVLLPPVGDEEDLDelLDRLDGLVLTggadvdpalygeephPELGPIDPERD----AFELALIRAale 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 78 ---PVLGVCLGMQLMVTSEGGRV-----DRAPEAV-HGRVDTLN------IVAADELFAGL--PRTFSIVRYHSLAAITV 140
Cdd:COG2071 95 rgkPVLGICRGMQLLNVALGGTLyqdlpDQVPGALdHRQPAPRYaprhtvEIEPGSRLARIlgEEEIRVNSLHHQAVKRL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1437403794 141 PPSMEVTSSNPEGIVMSIRHRSRPW-WGVQFHPESIAGD--FGMEIIDRFVDLC 191
Cdd:COG2071 175 GPGLRVSARAPDGVIEAIESPGAPFvLGVQWHPEWLAASdpLSRRLFEAFVEAA 228
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
6-177 |
7.92e-10 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 61.74 E-value: 7.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 6 ILVVDNfdSFTYNIVDYLHRCGARPHVVTNNASPEDIDLNRYHGIVISPGPGHPSVAEDVGISAWVLQTAQCPVLGVCLG 85
Cdd:CHL00197 195 IIVIDF--GVKYNILRRLKSFGCSITVVPATSPYQDILSYQPDGILLSNGPGDPSAIHYGIKTVKKLLKYNIPIFGICMG 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 86 MQLMVTSEGGRV------DRA---PEAVHGRVDtlnIVAADELFAglprtfsiVRYHSLAAITVppsmEVTSSN-PEGIV 155
Cdd:CHL00197 273 HQILSLALEAKTfklkfgHRGlnhPSGLNQQVE---ITSQNHGFA--------VNLESLAKNKF----YITHFNlNDGTV 337
|
170 180
....*....|....*....|..
gi 1437403794 156 MSIRHRSRPWWGVQFHPESIAG 177
Cdd:CHL00197 338 AGISHSPKPYFSVQYHPEASPG 359
|
|
| PRK15012 |
PRK15012 |
menaquinone-specific isochorismate synthase; Provisional |
318-612 |
1.47e-09 |
|
menaquinone-specific isochorismate synthase; Provisional
Pssm-ID: 184974 [Multi-domain] Cd Length: 431 Bit Score: 61.01 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 318 AVLAASKSTPTVPSFDPTVIGRLHVRDsRERYMATIERIQEAIRAGETYEVCLTTELFAEVHGEIHPAAMyqalstaVPA 397
Cdd:PRK15012 142 EFLATLVSIKPLPGLHLTTTREQHWPD-KTGWTQLIELATKTIAEGELDKVVLARATDLHFASPVNAAAM-------MAA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 398 PMRS--------LVVTDDVAVISASPERFIAMNERMVASSPIKGTRKRSADHEEDRALADDLRTNPKDRAENLMIVDLVR 469
Cdd:PRK15012 214 SRRLnlncyhfyMAFDAENAFLGSSPERLWRRRDKALRTEALAGTVANHPDDKQAQQLGEWLMADDKNQRENMLVVEDIC 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 470 NDLARVCESGSVRVPELCAVHSFTTVHQLISTVEGQlrptstPIDV--LRATFPGGSMTGAPKHRTMHLITELEGKQRGV 547
Cdd:PRK15012 294 QRLQADTQTLDVLPPQVLRLRKVQHLRRCIWTSLNK------ADDVicLHQLQPTAAVAGLPRDLARQFIARHEPFTREW 367
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437403794 548 YSGCIGYIGDDlRTDLAMVIRSVVLTPTTLSYGVGGAIIALSDPAEEWAEITTKSRVLLDLLGQD 612
Cdd:PRK15012 368 YAGSAGYLSLQ-QSEFCVSLRSAKVSGNVVRLYAGAGIVRGSDPEQEWQEIDNKAAGLRTLLQME 431
|
|
| hisH |
PRK13146 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
19-189 |
2.47e-08 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237290 [Multi-domain] Cd Length: 209 Bit Score: 55.17 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 19 IVDY-----------LHRCGARPHV-VTNNasPEDI---DlnryhGIVIsPGPG-HPSVA---EDVGISAWVLQTAQC-- 77
Cdd:PRK13146 6 IIDYgsgnlrsaakaLERAGAGADVvVTAD--PDAVaaaD-----RVVL-PGVGaFADCMrglRAVGLGEAVIEAVLAag 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 78 -PVLGVCLGMQLM-------VTSEG-----GRVDR-APEAVHGRV-----DTLNIVAADELFAGLPRT--FSIVryHSLA 136
Cdd:PRK13146 78 rPFLGICVGMQLLferglehGDTPGlglipGEVVRfQPDGPALKVphmgwNTVDQTRDHPLFAGIPDGarFYFV--HSYY 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1437403794 137 AITVPPSMEVTSSNPEGIVMSIRHRSrPWWGVQFHPESiAGDFGMEIIDRFVD 189
Cdd:PRK13146 156 AQPANPADVVAWTDYGGPFTAAVARD-NLFATQFHPEK-SQDAGLALLRNFLA 206
|
|
| hisH |
PRK13181 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
19-190 |
2.61e-08 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 54.87 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 19 IVDY-----------LHRCGArPHVVTNNasPEDIDLnryHGIVISPGPGHPSVA----EDVGISAWVLQTAQ--CPVLG 81
Cdd:PRK13181 4 IIDYgagnlrsvanaLKRLGV-EAVVSSD--PEEIAG---ADKVILPGVGAFGQAmrslRESGLDEALKEHVEkkQPVLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 82 VCLGMQLMVTS--EG---------GRVDRAPeAVHGRV-----DTLNIVAADELFAGLP--RTFSIVryHSLAAITVPPS 143
Cdd:PRK13181 78 ICLGMQLLFESseEGnvkglglipGDVKRFR-SEPLKVpqmgwNSVKPLKESPLFKGIEegSYFYFV--HSYYVPCEDPE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1437403794 144 MEVTSSNPEGIVMSIRHRSRpWWGVQFHPESiAGDFGMEIIDRFVDL 190
Cdd:PRK13181 155 DVLATTEYGVPFCSAVAKDN-IYAVQFHPEK-SGKAGLKLLKNFAEL 199
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
13-173 |
2.83e-08 |
|
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: 54.50 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 13 DSFTYNIVDYLHRCGARPHVVTNNASPEDID--LNRYHGIVIS---------------PGPGHPSVAEDVGISAWV--LQ 73
Cdd:cd01745 18 DYLNQYYVDAVRKAGGLPVLLPPVDDEEDLEqyLELLDGLLLTgggdvdpplygeephPELGPIDPERDAFELALLraAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 74 TAQCPVLGVCLGMQLMVTSEGGrvdrapeavhgrvdTLNivaadelfaglpRTFSIVRYHSLAAITVPPSMEVTSSNPEG 153
Cdd:cd01745 98 ERGKPILGICRGMQLLNVALGG--------------TLY------------QDIRVNSLHHQAIKRLADGLRVEARAPDG 151
|
170 180
....*....|....*....|.
gi 1437403794 154 IVMSIRHRSRPWW-GVQFHPE 173
Cdd:cd01745 152 VIEAIESPDRPFVlGVQWHPE 172
|
|
| hisH |
PRK13170 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
71-190 |
9.91e-08 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183877 [Multi-domain] Cd Length: 196 Bit Score: 52.94 E-value: 9.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 71 VLQTAQCPVLGVCLGMQLMVT-SEggrvdrapEavHGRVDTLNIVAAD-------------------------ELFAGLP 124
Cdd:PRK13170 65 LIKACTQPVLGICLGMQLLGErSE--------E--SGGVDCLGIIDGPvkkmtdfglplphmgwnqvtpqaghPLFQGIE 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437403794 125 RT--FSIVryHSLAaitVPPSmEVTSSNPE-GIVMSIRHRSRPWWGVQFHPESiAGDFGMEIIDRFVDL 190
Cdd:PRK13170 135 DGsyFYFV--HSYA---MPVN-EYTIAQCNyGEPFSAAIQKDNFFGVQFHPER-SGAAGAQLLKNFLEM 196
|
|
| ADCL_like |
cd01559 |
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ... |
620-818 |
6.98e-07 |
|
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent enzymes that converts 4-amino-4-deoxychorismate (ADC) to p-aminobenzoate and pyruvate. Based on the information available from the crystal structure, most members of this subgroup are likely to function as dimers. The enzyme from E.Coli, the structure of which is available, is a homodimer that is folded into a small and a larger domain. The coenzyme pyridoxal 5; -phosphate resides at the interface of the two domains that is linked by a flexible loop. Members of this subgroup are found in Eukaryotes and bacteria.
Pssm-ID: 238800 [Multi-domain] Cd Length: 249 Bit Score: 51.54 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 620 DSFLVNDGKTSGLNLHLDRFRTACLEHGY------AHHEQLDAFFAE------ALRSIPVTGQ----WFPRLEATPTEL- 682
Cdd:cd01559 12 ETMRALDGRLFLLDAHLARLERSARRLGIpepdlpRLRAALESLLAAndidegRIRLILSRGPggrgYAPSVCPGPALYv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 683 -RIALRPAPQLRGTTTLTSVAAVRPTPKYKGL-DLDYL--------AELRGStttDDALLVTPAGVIAETTTAAIIAWDG 752
Cdd:cd01559 92 sVIPLPPAWRQDGVRLITCPVRLGEQPLLAGLkHLNYLenvlakreARDRGA---DEALFLDTDGRVIEGTASNLFFVKD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437403794 753 TKWMSMAPAR--LESVTESLLLQSARAQGEMVVTAALTVPEA-QKLNLWAVNSLHGVTPVTHIDGVALP 818
Cdd:cd01559 169 GELVTPSLDRggLAGITRQRVIELAAAKGYAVDERPLRLEDLlAADEAFLTNSLLGVAPVTAIDDHDGP 237
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
728-819 |
7.89e-07 |
|
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439885 [Multi-domain] Cd Length: 285 Bit Score: 51.73 E-value: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 728 DDALLVTPAGVIAETTTAAIIAWDGTKWMSMAPAR--LESVTESLLLQSARAQGEMVVTAALTVPEAQKLN-LWAVNSLH 804
Cdd:COG0115 167 DEALLLDTDGYVAEGSGSNVFIVKDGVLVTPPLSGgiLPGITRDSVIELARELGIPVEERPISLEELYTADeVFLTGTAA 246
|
90
....*....|....*
gi 1437403794 805 GVTPVTHIDGVALPN 819
Cdd:COG0115 247 EVTPVTEIDGRPIGD 261
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
687-831 |
2.47e-06 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 49.96 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 687 RPAP-QLRGTTTL---TSVAAVRptpkykgldldyLAELRGStttDDALLVTPAGVIAETTTAAIIAWDGTKWMSMAPAR 762
Cdd:PRK07849 149 ERAPwLLAGAKTLsyaVNMAALR------------YAARRGA---DDVIFTSTDGYVLEGPTSTVVIATDDRLLTPPPWY 213
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437403794 763 --LESVTESLLLQSARAQGEMVVTAALTVPE---AQklNLWAVNSLHGVTPVTHIDGVALP---NNPQRSGLLRGWL 831
Cdd:PRK07849 214 giLPGTTQAALFEVAREKGWDCEYRALRPADlfaAD--GVWLVSSVRLAARVHTLDGRPLPrdpLADELTELVDAAI 288
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
624-814 |
6.47e-05 |
|
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, one of five classes of PLPDE, consists of branched-chain amino acid aminotransferases (BCAT), D-amino acid transferases (DAAT), and 4-amino-4-deoxychorismate lyases (ADCL). BCAT catalyzes the reversible transamination reaction between the L-branched-chain amino and alpha-keto acids. DAAT catalyzes the synthesis of D-glutamic acid and D-alanine, and ADCL converts 4-amino-4-deoxychorismate to p-aminobenzoate and pyruvate. Except for a few enzymes, i. e., Escherichia coli and Salmonella BCATs, which are homohexamers arranged as a double trimer, the class IV PLPDEs are homodimers. Homodimer formation is required for catalytic activity.
Pssm-ID: 238254 [Multi-domain] Cd Length: 256 Bit Score: 45.28 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 624 VNDGKTSGLNLHLDRFRTAC----LEHGY-------AHHEQLDAFFAEAL-------RSIPVTGqwFPRLEATPTELRIA 685
Cdd:cd00449 16 AGKGRLFRLDEHLDRLNRSAkrlgLPIPYdreelreALKELVAANNGASLyirplltRGVGGLG--VAPPPSPEPTFVVF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 686 LRPAP-----QLRGTTTLTS----VAAVRPTPKYKGLDL------DYLAELRGsttTDDALLVTPAGVIAETTTAAI-IA 749
Cdd:cd00449 94 ASPVGayakgGEKGVRLITSpdrrRAAPGGTGDAKTGGNlnsvlaKQEAAEAG---ADEALLLDDNGYVTEGSASNVfIV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437403794 750 WDGTkwMSMAPAR---LESVTESLLLQSARAQGEMVVTAALTVPEAQKLN-LWAVNSLHGVTPVTHIDG 814
Cdd:cd00449 171 KDGE--LVTPPLDggiLPGITRDSVIELAKELGIKVEERPISLDELYAADeVFLTGTAAEVTPVTEIDG 237
|
|
| hisH |
PRK13152 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
78-190 |
1.17e-04 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 171876 [Multi-domain] Cd Length: 201 Bit Score: 44.06 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437403794 78 PVLGVCLGMQLMVT--SEGG-------------RVDRAPE--AVHGRVDTLNIVAADELFAGLPRTFSIVRYHSLaaitv 140
Cdd:PRK13152 75 PILGICLGMQLFLErgYEGGvceglgfiegevvKFEEDLNlkIPHMGWNELEILKQSPLYQGIPEKSDFYFVHSF----- 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1437403794 141 ppSME-----VTSSNPEGIVMSIRHRSRPWWGVQFHPESiAGDFGMEIIDRFVDL 190
Cdd:PRK13152 150 --YVKckdefVSAKAQYGHKFVASLQKDNIFATQFHPEK-SQNLGLKLLENFARL 201
|
|
| GATase1_CTP_Synthase |
cd01746 |
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ... |
43-90 |
6.23e-03 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153217 [Multi-domain] Cd Length: 235 Bit Score: 39.07 E-value: 6.23e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1437403794 43 DLNRYHGIVISPGPGhpsvaeDVGISAWVLQTAQC-----PVLGVCLGMQLMV 90
Cdd:cd01746 52 ALKGADGILVPGGFG------IRGVEGKILAIKYArenniPFLGICLGMQLAV 98
|
|
| |
