|
Name |
Accession |
Description |
Interval |
E-value |
| guaA |
PRK00074 |
GMP synthase; Reviewed |
5-517 |
0e+00 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 1108.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 5 IHDQRILILDFGSQYTQLVARRIREIGVYCELWSWDVEESDIRDFNPDGIILSGGPESVTEENSPRAPQYVFDSGVPVFG 84
Cdd:PRK00074 1 IHHDKILILDFGSQYTQLIARRVRELGVYSEIVPYDISAEEIRAFNPKGIILSGGPASVYEEGAPRADPEIFELGVPVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 85 VCYGMQTMAEQLGGKVATSTEREFGYAAVQVTGESALFKDLEATQDVWMSHGDKVVEIPSDFVKIAETETCPYAAMANEE 164
Cdd:PRK00074 81 ICYGMQLMAHQLGGKVERAGKREYGRAELEVDNDSPLFKGLPEEQDVWMSHGDKVTELPEGFKVIASTENCPIAAIANEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 165 KKYYGVQFHPEVTHTKNGMKMLENFVLNVCGCEGLWTSASIIEDAVARIKEQVGDDEVILGLSGGVDSSVVAMLAHRAIG 244
Cdd:PRK00074 161 RKFYGVQFHPEVTHTPQGKKLLENFVFDICGCKGDWTMENFIEEAIEEIREQVGDKKVILGLSGGVDSSVAAVLLHKAIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 245 DKLTCVFVDNGLLRLNEADQVMEMFGNKFGLNIVHVNAEQRFLDALEGESDPETKRKIIGHVFVDIFDEESKKLKNAKWL 324
Cdd:PRK00074 241 DQLTCVFVDHGLLRKNEAEQVMEMFREHFGLNLIHVDASDRFLSALAGVTDPEEKRKIIGREFIEVFEEEAKKLGGVKFL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 325 AQGTIYPDVIESAASKtgKAHVIKSHHNVGGLPDDMEMGLVEPLRELFKDEVRKIGLELGLPYNMLYRHPFPGPGLGVRV 404
Cdd:PRK00074 321 AQGTLYPDVIESGGTK--KAATIKSHHNVGGLPEDMKLKLVEPLRELFKDEVRKLGLELGLPEEIVYRHPFPGPGLAIRI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 405 LGEIKKEYCDLLRRADAIFIEELHNADLYNKVSQAFTVFLPVRSVGVMGDGRKYDWVVSLRAVETIDFMTAHWAHLPYDF 484
Cdd:PRK00074 399 LGEVTKEKLDILREADAIFIEELRKAGLYDKIWQAFAVLLPVKSVGVMGDGRTYDYVVALRAVTSIDGMTADWARLPYDF 478
|
490 500 510
....*....|....*....|....*....|...
gi 75354446 485 LGKVSNRIINEVNGISRVVYDISGKPPATIEWE 517
Cdd:PRK00074 479 LEKISNRIINEVKGVNRVVYDITSKPPATIEWE 511
|
|
| GuaA2 |
COG0519 |
GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, ... |
5-517 |
0e+00 |
|
GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, PP-ATPase domain/subunit is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440285 [Multi-domain] Cd Length: 512 Bit Score: 948.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 5 IHDQRILILDFGSQYTQLVARRIREIGVYCELWSWDVEESDIRDFNPDGIILSGGPESVTEENSPRAPQYVFDSGVPVFG 84
Cdd:COG0519 1 MDKEIIIVLDFGGQYQQLIARRRREEGVYSEIIPPDTAAEEIKAKGPPGIILSGGPSSVYEEGAPPDDPELFELGGPILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 85 VCYGMQTMAEQLGGKVATSTEREFGYAAVQVTGESALFKDLEATQDVWMSHGDKVVEIPSDFVKIAETETCPYAAMANEE 164
Cdd:COG0519 81 ICYGGQLMLHLLGGGVVRAERREYGGALLLVDDESDLFAGGPEELQVWMSHGDRVTELPPGFEVIASTENCPVAAIANEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 165 KKYYGVQFHPEVTHTKNGMKMLENFVLNVCGCEGLWTSASIIEDAVARIKEQVGDDEVILGLSGGVDSSVVAMLAHRAIG 244
Cdd:COG0519 161 RKLYGVQFHPEVVHTEQGKEILKNFLFDICGCKGDWTMENFIEEAIEEIREQVGDGKVICALSGGVDSSVAAALLHKAIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 245 DKLTCVFVDNGLLRLNEADQVMEMFGNKFGLNIVHVNAEQRFLDALEGESDPETKRKIIGHVFVDIFDEESKKLKNAKWL 324
Cdd:COG0519 241 DQLTCVFVDHGLLRKGEAEQVEETFKEHFGLNLIYVDASERFLSALKGVTDPEEKRKIIGEEFIEVFEEEAKKLGGAKFL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 325 AQGTIYPDVIESAASKtGKAHVIKSHHNVGGLPDDMEMGLVEPLRELFKDEVRKIGLELGLPYNMLYRHPFPGPGLGVRV 404
Cdd:COG0519 321 AQGTLYPDVIESGSVK-GPAATIKSHHNVGGLPEDMKFKLVEPLRELFKDEVRALGRELGLPEEIVYRHPFPGPGLAIRI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 405 LGEIKKEYCDLLRRADAIFIEELHNADLYNKVSQAFTVFLPVRSVGVMGDGRKYDWVVSLRAVETIDFMTAHWAHLPYDF 484
Cdd:COG0519 400 LGEVTKEKLEILREADAIFIEELRKAGLYDKVWQAFAVLLPVKSVGVMGDERTYEYVVALRAVTSVDGMTADWARLPYEV 479
|
490 500 510
....*....|....*....|....*....|...
gi 75354446 485 LGKVSNRIINEVNGISRVVYDISGKPPATIEWE 517
Cdd:COG0519 480 LERISNRIINEVKGVNRVVYDITSKPPATIEWE 512
|
|
| PLN02347 |
PLN02347 |
GMP synthetase |
10-517 |
0e+00 |
|
GMP synthetase
Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 687.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 10 ILILDFGSQYTQLVARRIREIGVYCELWSWDVEESDIRDFNPDGIILSGGPESVTEENSPRAP----QYVFDSGVPVFGV 85
Cdd:PLN02347 13 VLILDYGSQYTHLITRRVRELGVYSLLLSGTASLDRIASLNPRVVILSGGPHSVHVEGAPTVPegffDYCRERGVPVLGI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 86 CYGMQTMAEQLGGKVATSTEREFGYAAVQVTGESALFKDL--EATQDVWMSHGDKVVEIPSDFVKIAETETCPYAAMANE 163
Cdd:PLN02347 93 CYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCGSQLFGDLpsGETQTVWMSHGDEAVKLPEGFEVVAKSVQGAVVAIENR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 164 EKKYYGVQFHPEVTHTKNGMKMLENFVLNVCGCEGLWTSASIIEDAVARIKEQVG-DDEVILGLSGGVDSSVVAMLAHRA 242
Cdd:PLN02347 173 ERRIYGLQYHPEVTHSPKGMETLRHFLFDVCGVTADWKMQDVLEEQIELIKATVGpDEHVICALSGGVDSTVAATLVHKA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 243 IGDKLTCVFVDNGLLRLNEADQVMEMFGNKFGLNIVHVNAEQRFLDALEGESDPETKRKIIGHVFVDIFDEESKKL---- 318
Cdd:PLN02347 253 IGDRLHCVFVDNGLLRYKEQERVMETFKRDLHLPVTCVDASERFLSKLKGVTDPEKKRKIIGAEFIEVFDEFAHKLeqkl 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 319 -KNAKWLAQGTIYPDVIESA---ASKTGKAHVIKSHHNVGGLPDDMEMGLVEPLRELFKDEVRKIGLELGLPYNMLYRHP 394
Cdd:PLN02347 333 gKKPAFLVQGTLYPDVIESCpppGSGRTHSHTIKSHHNVGGLPKDMKLKLIEPLKLLFKDEVRKLGRLLGVPEAFLKRHP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 395 FPGPGLGVRVLGEIKKE-YCDLLRRADAIFIEELHNADLYNKVSQAFTVFLPVRSVGVMGDGRKYDWVVSLRAVETIDFM 473
Cdd:PLN02347 413 FPGPGLAVRVLGDVTEGnALDILRQVDEIFINSIKDAGLYDEIWQAFAVFLPVKSVGVQGDQRTHSHVVALRAVTSEDGM 492
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 75354446 474 TAHWAHLPYDFLGKVSNRIINEVNGISRVVYDISGKPPATIEWE 517
Cdd:PLN02347 493 TADWYHFEHKFLDDVSRKICNEVRGVNRVVYDITSKPPSTIEWE 536
|
|
| guaA_Cterm |
TIGR00884 |
GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; This protein of purine ... |
205-517 |
0e+00 |
|
GMP synthase (glutamine-hydrolyzing), C-terminal domain or B 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 C-terminal region would be the larger subunit [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273321 [Multi-domain] Cd Length: 311 Bit Score: 579.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 205 IIEDAVARIKEQVGDDEVILGLSGGVDSSVVAMLAHRAIGDKLTCVFVDNGLLRLNEADQVMEMFGNKFGLNIVHVNAEQ 284
Cdd:TIGR00884 2 FIEEAVEEIREQVGDAKVIIALSGGVDSSVAAVLAHRAIGDRLTCVFVDHGLLRKGEAEQVVKTFGDRLGLNLVYVDAKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 285 RFLDALEGESDPETKRKIIGHVFVDIFDEESKKLKNAKWLAQGTIYPDVIESAAsktGKAHVIKSHHNVGGLPDDMEMGL 364
Cdd:TIGR00884 82 RFLSALKGVTDPEEKRKIIGRVFIEVFEREAKKIGDAEYLAQGTIYPDVIESAA---GTAHVIKSHHNVGGLPEDMKLKL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 365 VEPLRELFKDEVRKIGLELGLPYNMLYRHPFPGPGLGVRVLGEIKKEYCDLLRRADAIFIEELHNADLYNKVSQAFTVFL 444
Cdd:TIGR00884 159 VEPLRELFKDEVRKLGKELGLPEEIVWRHPFPGPGLAVRVLGEVTKEKLEILRRADAIVIEELKKAGLYDKVWQAFAVLL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75354446 445 PVRSVGVMGDGRKYDWVVSLRAVETIDFMTAHWAHLPYDFLGKVSNRIINEVNGISRVVYDISGKPPATIEWE 517
Cdd:TIGR00884 239 PVKSVGVMGDGRTYGYVIALRAVESIDGMTADWARLPYDFLERISNRITNEVPGVNRVVYDITSKPPATIEWE 311
|
|
| GMP_synthase_C |
cd01997 |
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ... |
213-517 |
0e+00 |
|
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP synthetase (glutamine-hydrolyzing, EC 6.3.5.2) contains two subdomains: the ATP pyrophosphatase domain at the N-terminal and the dimerization domain at the C-terminal end. The ATP-PPase domain is a twisted, five-stranded parallel beta-sheet sandwiched between helical layers. It has a signature nucleotide-binding motif, or PP-loop, at the end of the first-beta strand. GMP synthetase is a homodimer, but in some archaea, it is a heterodimer made up of ATP pyrophosphatase (ATP-PPase) and a GATase subunit. In eukaryotes and bacteria, the two catalytic units are encoded by a single gene producing a two-domain-type GMP with a GATase domain in the N-terminus and an ATP-PPase domain in the C-terminus.
Pssm-ID: 467501 [Multi-domain] Cd Length: 311 Bit Score: 522.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 213 IKEQVGDDEVILGLSGGVDSSVVAMLAHRAIGD-KLTCVFVDNGLLRLNEADQVMEMFGNKFGLNIVHVNAEQRFLDALE 291
Cdd:cd01997 1 IKRTVGDKKVLCLVSGGVDSTVCAALLHKALGDeRVIAVHIDNGLMRKNESEQVEEALKKLGVINLAKVDASKRFLKKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 292 GESDPETKRKIIGHVFVDIFDEESKKLK---NAKWLAQGTIYPDVIESAASKT-GKAHVIKSHHNVGGLPDD-MEMGLVE 366
Cdd:cd01997 81 GVTDPEEKRKIIGDTFIEVFDEVAKELNldpDDVYLAQGTLYPDLIESASSLAsSKADTIKTHHNVGGLPRElLKGKLVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 367 PLRELFKDEVRKIGLELGLPYNMLYRHPFPGPGLGVRVLGEIKKEYCDLLRRADAIFIEELHNADLYNKVSQAFTVFLPV 446
Cdd:cd01997 161 PLRDLFKDEVRELGRELGLPEELVWRHPFPGPGLAIRVLGEVTPEKLEILREADAIVEEELREAGLYDKISQAFAVLLPI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75354446 447 RSVGVMGDGRKYDWVVSLRAVETIDFMTAHWAHLPYDFLGKVSNRIINEVNGISRVVYDISGKPPATIEWE 517
Cdd:cd01997 241 KSVGVQGDGRTYGYVVALRAVETEDFMTAEWARPPYEVLDKISNRITNEVPGVNRVVYDITSKPPATIEWE 311
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
10-197 |
2.38e-110 |
|
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: 325.42 E-value: 2.38e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 10 ILILDFGSQYTQLVARRIREIGVYCELWSWDVEESDIRDFNPDGIILSGGPESVTEENSPRAPQYVFDSGVPVFGVCYGM 89
Cdd:TIGR00888 1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGPSSVYAENAPRADEKIFELGVPVLGICYGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 90 QTMAEQLGGKVATSTEREFGYAAVQVTGESALFKDLEATQDVWMSHGDKVVEIPSDFVKIAETETCPYAAMANEEKKYYG 169
Cdd:TIGR00888 81 QLMAKQLGGEVGRAEKREYGKAELEILDEDDLFRGLPDESTVWMSHGDKVKELPEGFKVLATSDNCPVAAMAHEEKPIYG 160
|
170 180
....*....|....*....|....*...
gi 75354446 170 VQFHPEVTHTKNGMKMLENFVLNVCGCE 197
Cdd:TIGR00888 161 VQFHPEVTHTEYGNELLENFVYDVCGCE 188
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
10-190 |
6.74e-105 |
|
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: 311.39 E-value: 6.74e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 10 ILILDFGSQYTQLVARRIREIGVYCELWSWDVEESDIRDFNPDGIILSGGPESVTEENSPRAPQYVFDSGVPVFGVCYGM 89
Cdd:cd01742 1 ILILDFGSQYTHLIARRVRELGVYSEILPNTTPLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGICYGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 90 QTMAEQLGGKVATSTEREFGYAAVQVTGESALFKDLEATQDVWMSHGDKVVEIPSDFVKIAETETCPYAAMANEEKKYYG 169
Cdd:cd01742 81 QLIAKALGGKVERGDKREYGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVVKLPEGFKVIASSDNCPVAAIANEEKKIYG 160
|
170 180
....*....|....*....|.
gi 75354446 170 VQFHPEVTHTKNGMKMLENFV 190
Cdd:cd01742 161 VQFHPEVTHTEKGKEILKNFL 181
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
9-179 |
1.54e-73 |
|
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: 232.53 E-value: 1.54e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 9 RILILD---FGSQYTQLVARRIREIGVycELWSWDVEESDIRDF-----NPDGIILSGGPESVTEE-----NSPRAPQYV 75
Cdd:COG0518 1 KILILDhdpFGGQYPGLIARRLREAGI--ELDVLRVYAGEILPYdpdleDPDGLILSGGPMSVYDEdpwleDEPALIREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 76 FDSGVPVFGVCYGMQTMAEQLGGKVATSTEREFGYAAVQVTGESALFKDLEATQDVWMSHGDKVVEIPSDFVKIAETETC 155
Cdd:COG0518 79 FELGKPVLGICYGAQLLAHALGGKVEPGPGREIGWAPVELTEADPLFAGLPDEFTVWMSHGDTVTELPEGAEVLASSDNC 158
|
170 180
....*....|....*....|....
gi 75354446 156 PYAAMANeEKKYYGVQFHPEVTHT 179
Cdd:COG0518 159 PNQAFRY-GRRVYGVQFHPEVTHT 181
|
|
| GMP_synt_C |
pfam00958 |
GMP synthase C terminal domain; GMP synthetase is a glutamine amidotransferase from the de ... |
425-516 |
2.57e-62 |
|
GMP synthase C terminal domain; GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. This family is the C-terminal domain specific to the GMP synthases EC:6.3.5.2. In prokaryotes this domain mediates dimerization. Eukaryotic GMP synthases are monomers. This domain in eukaryotes includes several large insertions that may form globular domains.
Pssm-ID: 425963 [Multi-domain] Cd Length: 92 Bit Score: 198.40 E-value: 2.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 425 EELHNADLYNKVSQAFTVFLPVRSVGVMGDGRKYDWVVSLRAVETIDFMTAHWAHLPYDFLGKVSNRIINEVNGISRVVY 504
Cdd:pfam00958 1 EEIKKAGLYRKIWQAFAVLLPVKSVGVMGDERTYEYVVALRAVTSTDGMTADWARLPYEVLEKISNRIVNEVPGVNRVVY 80
|
90
....*....|..
gi 75354446 505 DISGKPPATIEW 516
Cdd:pfam00958 81 DITSKPPATIEW 92
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
11-193 |
3.59e-52 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 175.50 E-value: 3.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 11 LILDFGSQYTQLVARRIREIGVYCELWSWDVEESDIRDFNPDGIILSGGPESVTE-ENSPRAPQYVFDSGVPVFGVCYGM 89
Cdd:pfam00117 1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAaGGAIEAIREARELKIPILGICLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 90 QTMAEQLGGKVATSTEREFGYAAVQVTG-ESALFKDLEATQDVWMSHGDKVVE--IPSDFVKIAETET-CPYAAMANEEK 165
Cdd:pfam00117 81 QLLALAFGGKVVKAKKFGHHGKNSPVGDdGCGLFYGLPNVFIVRRYHSYAVDPdtLPDGLEVTATSENdGTIMGIRHKKL 160
|
170 180
....*....|....*....|....*...
gi 75354446 166 KYYGVQFHPEVTHTKNGMKMLENFVLNV 193
Cdd:pfam00117 161 PIFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
9-195 |
3.83e-52 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 175.04 E-value: 3.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 9 RILILDFGSQYTQLVARRIREIGVYCELWSWDVEESDIRDfNPDGIILSGGPESvteENSPRAPQYVFDSGVPVFGVCYG 88
Cdd:PRK00758 1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTTPVEEIKA-FEDGLILSGGPDI---ERAGNCPEYLKELDVPILGICLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 89 MQTMAEQLGGKVATSTEREFGYAAVQVTGESALFKDLEATQDVWMSHGDKVVEIPSDFVKIAETETCPYAAMANEEKKYY 168
Cdd:PRK00758 77 HQLIAKAFGGEVGRGEYGEYALVEVEILDEDDILKGLPPEIRVWASHADEVKELPDGFEILARSDICEVEAMKHKEKPIY 156
|
170 180
....*....|....*....|....*..
gi 75354446 169 GVQFHPEVTHTKNGMKMLENFvLNVCG 195
Cdd:PRK00758 157 GVQFHPEVAHTEYGEEIFKNF-LEICG 182
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
9-190 |
3.15e-29 |
|
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: 113.88 E-value: 3.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 9 RILILDFGSQYTQ-LVARRIREIGVYCELWS-WDVEES----DIRDFnpDGIILSGGPESVTEENSP------RAPQYVF 76
Cdd:cd01741 1 RILILQHDTPEGPgLFEDLLREAGAETIEIDvVDVYAGellpDLDDY--DGLVILGGPMSVDEDDYPwlkklkELIRQAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 77 DSGVPVFGVCYGMQTMAEQLGGKVATSTE-REFGYAAVQVTGE---SALFKDLEATQDVWMSHGDKVVEIPSDFVKIAET 152
Cdd:cd01741 79 AAGKPVLGICLGHQLLARALGGKVGRNPKgWEIGWFPVTLTEAgkaDPLFAGLPDEFPVFHWHGDTVVELPPGAVLLASS 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 75354446 153 ETCPYAAMANEEkKYYGVQFHPEvthtkngMKMLENFV 190
Cdd:cd01741 159 EACPNQAFRYGD-RALGLQFHPE-------ERLLRNFL 188
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
10-195 |
2.52e-20 |
|
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: 88.56 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 10 ILILD-FGS------QYtqlvarrIREIGVYCELWSWD-VEESDIRDFNPDGIILSGGPEsvTEENSPRAPQYV--FDSG 79
Cdd:COG0512 1 ILLIDnYDSftynlvQY-------LGELGAEVVVVRNDeITLEEIEALAPDGIVLSPGPG--TPEEAGISLEVIraFAGK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 80 VPVFGVCYGMQTMAEQLGGKVA---------TSTerefgyaaVQVTGeSALFKDLEATQDVWMSH---GDKvVEIPSDFV 147
Cdd:COG0512 72 IPILGVCLGHQAIGEAFGGKVVrapepmhgkTSP--------ITHDG-SGLFAGLPNPFTATRYHslvVDR-ETLPDELE 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 75354446 148 KIAETETCPYAAMANEEKKYYGVQFHPEVTHTKNGMKMLENFvLNVCG 195
Cdd:COG0512 142 VTAWTEDGEIMGIRHRELPIEGVQFHPESILTEHGHQLLANF-LELAG 188
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
10-190 |
1.46e-19 |
|
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: 86.43 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 10 ILILD-FGSqYTQLVARRIREIGVYCELWSWDVE-ESDIRDFNPDGIILSGGPESVTEE-NSPRAPQYvFDSGVPVFGVC 86
Cdd:cd01743 1 ILLIDnYDS-FTYNLVQYLRELGAEVVVVRNDEItLEELELLNPDAIVISPGPGHPEDAgISLEIIRA-LAGKVPILGVC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 87 YGMQTMAEQLGGKVATSTEREFGYAAVQVTGESALFKDLEATQDVwM---S-HGDKvVEIPSDFVKIAETETcpYAAMA- 161
Cdd:cd01743 79 LGHQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTV-GryhSlVVDP-DPLPDLLEVTASTED--GVIMAl 154
|
170 180 190
....*....|....*....|....*....|
gi 75354446 162 -NEEKKYYGVQFHPEVTHTKNGMKMLENFV 190
Cdd:cd01743 155 rHRDLPIYGVQFHPESILTEYGLRLLENFL 184
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
45-190 |
2.06e-18 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 83.26 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 45 DIRDFNPDGIILSGGPESVTE-ENSPRAPQYvFDSGVPVFGVCYGMQTMAEQLGGKVATSTEREFGYAAVQVTGESALFK 123
Cdd:PRK05670 38 EIEALNPDAIVLSPGPGTPAEaGISLELIRE-FAGKVPILGVCLGHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFA 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 124 DLEATQDVWMSH---GDKVvEIPSDFVKIAETETCPYAAMANEEKKYYGVQFHPEVTHTKNGMKMLENFV 190
Cdd:PRK05670 117 GLPNPFTVTRYHslvVDRE-SLPDCLEVTAWTDDGEIMGVRHKELPIYGVQFHPESILTEHGHKLLENFL 185
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
9-190 |
5.76e-16 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 81.12 E-value: 5.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 9 RILILDFGSQYTQLVARRIREIGVYCELWSWDVEESDIRDFNPDGIILSGGPESVTEENSPRAPQYVFDSGVPVFGVCYG 88
Cdd:PRK13566 528 RVLLVDHEDSFVHTLANYFRQTGAEVTTVRYGFAEEMLDRVNPDLVVLSPGPGRPSDFDCKATIDAALARNLPIFGVCLG 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 89 MQTMAEQLGGKVATSTEREFGYAA-VQVTGESALFKDLEATQDVWMSHG--DKVVEIPSDFVKIAETETCpyAAMANEEK 165
Cdd:PRK13566 608 LQAIVEAFGGELGQLAYPMHGKPSrIRVRGPGRLFSGLPEEFTVGRYHSlfADPETLPDELLVTAETEDG--VIMAIEHK 685
|
170 180 190
....*....|....*....|....*....|
gi 75354446 166 K--YYGVQFHPEVTHT---KNGMKMLENFV 190
Cdd:PRK13566 686 TlpVAAVQFHPESIMTlggDVGLRIIENVV 715
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
3-190 |
1.09e-15 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 76.37 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 3 TNIHDQRILILDFGSQYTQLVARRIREIGVYCELWSWD---VEEsdIRDFNPDGIILSGGPEsvTEENSPRAPQYVFDSG 79
Cdd:PLN02335 14 SSKQNGPIIVIDNYDSFTYNLCQYMGELGCHFEVYRNDeltVEE--LKRKNPRGVLISPGPG--TPQDSGISLQTVLELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 80 --VPVFGVCYGMQTMAEQLGGKVATSTereFGY-----AAVQVT--GESALFKDLEATQDVWMSHgDKVVE---IPSDFV 147
Cdd:PLN02335 90 plVPLFGVCMGLQCIGEAFGGKIVRSP---FGVmhgksSPVHYDekGEEGLFSGLPNPFTAGRYH-SLVIEkdtFPSDEL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 75354446 148 KI-AETETCpyAAMANEEKKY---YGVQFHPEVTHTKNGMKMLENFV 190
Cdd:PLN02335 166 EVtAWTEDG--LIMAARHRKYkhiQGVQFHPESIITTEGKTIVRNFI 210
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
8-212 |
1.70e-15 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 75.47 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 8 QRILILD-FGSQYTQLVaRRIREIGVYCELWSWD----VEESDI-RDFnpDGIILSGGPesvteeNSP-RAPQYV----- 75
Cdd:PRK07765 1 MRILVVDnYDSFVFNLV-QYLGQLGVEAEVWRNDdprlADEAAVaAQF--DGVLLSPGP------GTPeRAGASIdmvra 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 76 -FDSGVPVFGVCYGMQTMAEQLGGKVATSTEREFG-YAAVQVTGEsALFKDL----EATQdvwmSHGDKVVE--IPSDFV 147
Cdd:PRK07765 72 cAAAGTPLLGVCLGHQAIGVAFGATVDRAPELLHGkTSSVHHTGV-GVLAGLpdpfTATR----YHSLTILPetLPAELE 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75354446 148 KIAETETCPYAAMANEEKKYYGVQFHPEVTHTKNGMKMLENFvLNVCGCEGLWTSASIIEDAVAR 212
Cdd:PRK07765 147 VTARTDSGVIMAVRHRELPIHGVQFHPESVLTEGGHRMLANW-LTVCGWAPDEALVRRLENEVAA 210
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
21-190 |
2.37e-15 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 74.46 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 21 QLVARRIREIGVycelwswdveeSDIRDFNPDGIILSGGPESVTEENSPRAPQYVFDSGVPVFGVCYGMQTMAEQLGGKV 100
Cdd:PRK07649 25 ELVVKRNDEVTI-----------SDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCLGHQSIAQVFGGEV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 101 ATSTEREFGYAAVQVTGESALFKDLEA--TQDVWMSHGDKVVEIPSDFVKIAETETCPYAAMANEEKKYYGVQFHPEVTH 178
Cdd:PRK07649 94 VRAERLMHGKTSLMHHDGKTIFSDIPNpfTATRYHSLIVKKETLPDCLEVTSWTEEGEIMAIRHKTLPIEGVQFHPESIM 173
|
170
....*....|..
gi 75354446 179 TKNGMKMLENFV 190
Cdd:PRK07649 174 TSHGKELLQNFI 185
|
|
| PRK09065 |
PRK09065 |
glutamine amidotransferase; Provisional |
52-178 |
1.22e-14 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181635 [Multi-domain] Cd Length: 237 Bit Score: 73.46 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 52 DGIILSGGPESVTE--ENSPRAPQYVFDS---GVPVFGVCYGMQTMAEQLGGKVATSTE-REFGYAAVQVT---GESALF 122
Cdd:PRK09065 56 AGVIITGSWAMVTDrlDWSERTADWLRQAaaaGMPLLGICYGHQLLAHALGGEVGYNPAgRESGTVTVELHpaaADDPLF 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 75354446 123 KDLEATQDVWMSHGDKVVEIPSDFVKIAETETCPYAAMANEEKKyYGVQFHPEVTH 178
Cdd:PRK09065 136 AGLPAQFPAHLTHLQSVLRLPPGAVVLARSAQDPHQAFRYGPHA-WGVQFHPEFTA 190
|
|
| PRK07567 |
PRK07567 |
glutamine amidotransferase; Provisional |
18-175 |
1.35e-13 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181035 [Multi-domain] Cd Length: 242 Bit Score: 70.36 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 18 QYTQLVARRIREIGVycelwswDVEESDIRDFNP-DGIILSGGPESVT---EENSP---RAPQ-------YVFDSGVPVF 83
Cdd:PRK07567 25 RYTGLDPAELRRIRL-------DREPLPDLDLDDySGVIVGGSPFNVSdpaESKSPwqrRVEAelsglldEVVARDFPFL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 84 GVCYGMQTMAEQLGGKVATSTEREFGYAAVQVTGESA---LFKDLEATQDVWMSHGDKVVEIPSDFVKIAETETCPYAAM 160
Cdd:PRK07567 98 GACYGVGTLGHHQGGVVDRTYGEPVGAVTVSLTDAGRadpLLAGLPDTFTAFVGHKEAVSALPPGAVLLATSPTCPVQMF 177
|
170
....*....|....*.
gi 75354446 161 -ANEekKYYGVQFHPE 175
Cdd:PRK07567 178 rVGE--NVYATQFHPE 191
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
10-190 |
3.10e-13 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 68.22 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 10 ILILDFGSQYTQLVARRIREIGV-YCELWSWDVEESDIRDFNPDGIILSGGPESvtEENSPRAPQYV--FDSGVPVFGVC 86
Cdd:CHL00101 2 ILIIDNYDSFTYNLVQSLGELNSdVLVCRNDEIDLSKIKNLNIRHIIISPGPGH--PRDSGISLDVIssYAPYIPILGVC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 87 YGMQTMAEQLGGKVATSTEREFGYAAVQVTGESALFKDLEATQDVWMSHGDKV--VEIPSDFVKIAETETCpyAAMANEE 164
Cdd:CHL00101 80 LGHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIIdpLNLPSPLEITAWTEDG--LIMACRH 157
|
170 180
....*....|....*....|....*....
gi 75354446 165 KKY---YGVQFHPEVTHTKNGMKMLENFV 190
Cdd:CHL00101 158 KKYkmlRGIQFHPESLLTTHGQQILRNFL 186
|
|
| hisH |
PRK13181 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
79-189 |
1.58e-12 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 66.43 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 79 GVPVFGVCYGMQTMAEQ--------LG---GKVatsteREF----------GYAAVQVTGESALFKDLEATQDVWMSHGD 137
Cdd:PRK13181 72 KQPVLGICLGMQLLFESseegnvkgLGlipGDV-----KRFrseplkvpqmGWNSVKPLKESPLFKGIEEGSYFYFVHSY 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 75354446 138 KVVEIPSDFVkIAETE-TCPYAAmANEEKKYYGVQFHPEVTHtKNGMKMLENF 189
Cdd:PRK13181 147 YVPCEDPEDV-LATTEyGVPFCS-AVAKDNIYAVQFHPEKSG-KAGLKLLKNF 196
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
10-175 |
2.05e-12 |
|
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: 65.60 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 10 ILILDFGSQYTQLvaRRIREIGVYCELWSWDVEESDIRDFNPDGIILSGGPesvteeNSPRAPQY-------VFDSGVPV 82
Cdd:cd01744 1 VVVIDFGVKHNIL--RELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGP------GDPALLDEaiktvrkLLGKKIPI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 83 FGVCYGMQTMAEQLGGKvatsTER-EFGYAAVQ--VtgesalfKDLeATQDVWMS---HGDKVVE--IPSDfVKI----A 150
Cdd:cd01744 73 FGICLGHQLLALALGAK----TYKmKFGHRGSNhpV-------KDL-ITGRVYITsqnHGYAVDPdsLPGG-LEVthvnL 139
|
170 180
....*....|....*....|....*
gi 75354446 151 ETETCpyAAMANEEKKYYGVQFHPE 175
Cdd:cd01744 140 NDGTV--EGIRHKDLPVFSVQFHPE 162
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
9-190 |
1.37e-11 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 63.60 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 9 RILILDFGSQYTQLVARRIREIGVycELWSWDVEESDIRDF-NPDGIILSGGPesvteeNSPRA-PQYV-----FDSGVP 81
Cdd:PRK06895 3 KLLIINNHDSFTFNLVDLIRKLGV--PMQVVNVEDLDLDEVeNFSHILISPGP------DVPRAyPQLFamlerYHQHKS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 82 VFGVCYGMQTMAEQLGGKVATSTEREFGYAA-VQVTGESALFKDLEATQDVWMSHGDKVVEI--PSDFVKIAETETCPYA 158
Cdd:PRK06895 75 ILGVCLGHQTLCEFFGGELYNLNNVRHGQQRpLKVRSNSPLFDGLPEEFNIGLYHSWAVSEEnfPTPLEITAVCDENVVM 154
|
170 180 190
....*....|....*....|....*....|..
gi 75354446 159 AMANEEKKYYGVQFHPEVTHTKNGMKMLENFV 190
Cdd:PRK06895 155 AMQHKTLPIYGVQFHPESYISEFGEQILRNWL 186
|
|
| PRK07053 |
PRK07053 |
glutamine amidotransferase; Provisional |
51-177 |
1.61e-11 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 235919 [Multi-domain] Cd Length: 234 Bit Score: 64.20 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 51 PDGIILSGGPESVTEENsprapQYVF------------DSGVPVFGVCYGMQTMAEQLGGKVATSTEREFGYAAVQVTGE 118
Cdd:PRK07053 48 PDLLVVLGGPIGVYDDE-----LYPFlapeiallrqrlAAGLPTLGICLGAQLIARALGARVYPGGQKEIGWAPLTLTDA 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75354446 119 ---SALfKDLEATQDVWMSHGDKVvEIPSDFVKIAETETCPYAAMAnEEKKYYGVQFHPEVT 177
Cdd:PRK07053 123 graSPL-RHLGAGTPVLHWHGDTF-DLPEGATLLASTPACRHQAFA-WGNHVLALQFHPEAR 181
|
|
| PRK06490 |
PRK06490 |
glutamine amidotransferase; Provisional |
52-178 |
2.60e-10 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 180590 [Multi-domain] Cd Length: 239 Bit Score: 60.74 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 52 DGIILSGGPESVteeNSPRApqYV----------FDSGVPVFGVCYGMQTMAEQLGGKVATSTE--REFGYAAVQVTGES 119
Cdd:PRK06490 54 AGAVIFGGPMSA---NDPDD--FIrreidwisvpLKENKPFLGICLGAQMLARHLGARVAPHPDgrVEIGYYPLRPTEAG 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 75354446 120 ALFKDLEATQDVWMSHGdkvVEIPSDFVKIAETETCPYAAMANEEKKyYGVQFHPEVTH 178
Cdd:PRK06490 129 RALMHWPEMVYHWHREG---FDLPAGAELLATGDDFPNQAFRYGDNA-WGLQFHPEVTR 183
|
|
| IMP_synth_hisH |
TIGR01855 |
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ... |
10-190 |
4.03e-10 |
|
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: 59.26 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 10 ILILDFGSQYTQLVARRIREIGVYCELwswdVEESDIRDfNPDGIILSG------GPESVTEENSPRAPQYVFDSGVPVF 83
Cdd:TIGR01855 1 IVIIDYGVGNLGSVKRALKRVGAEPVV----VKDSKEAE-LADKLILPGvgafgaAMARLRENGLDLFVELVVRLGKPVL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 84 GVCYGMQTMAEQ------------LGGKVATSTER---EFGYAAVQVTGESALFKDLEATQDVWMSHGDKVVeiPSDFVK 148
Cdd:TIGR01855 76 GICLGMQLLFERseegggvpglglIKGNVVKLEARkvpHMGWNEVHPVKESPLLNGIDEGAYFYFVHSYYAV--CEEEAV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 75354446 149 IAeteTCPYAAM---ANEEKKYYGVQFHPEVTHtKNGMKMLENFV 190
Cdd:TIGR01855 154 LA---YADYGEKfpaAVQKGNIFGTQFHPEKSG-KTGLKLLENFL 194
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
44-190 |
4.47e-10 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 59.16 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 44 SDIRDFNPDGIILSGGPESVTEENSPRAPQYVFDSGVPVFGVCYGMQTMAEQLGGKVATSTEREFGYAAVQVTGESALFK 123
Cdd:PRK08007 37 ADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFR 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 124 DLEATQDVWMSHgDKVVE---IPSDFVKIAETETCPYAAMANEEKKYYGVQFHPEVTHTKNGMKMLENFV 190
Cdd:PRK08007 117 GLANPLTVTRYH-SLVVEpdsLPACFEVTAWSETREIMGIRHRQWDLEGVQFHPESILSEQGHQLLANFL 185
|
|
| LarE-like |
cd01990 |
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ... |
222-386 |
5.16e-10 |
|
Lactate racemization operon protein LarE and similar proteins; This subfamily includes Lactiplantibacillus plantarum LarE, a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family. LarE is part of the lar operon, encoding five Lar proteins (LarA-E) that collaboratively synthesize and incorporate a niacin-derived Ni-containing cofactor into LarA, an Ni-dependent lactate racemase. It catalyzes successive thiolation reactions by donating the sulfur atom of their exclusive cysteine residues to the substrate. The LarE-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. Proteins from this subfamily probably binds ATP. This domain is about 200 amino acids long with a strongly conserved motif SGGxDS at the N-terminus.
Pssm-ID: 467494 [Multi-domain] Cd Length: 222 Bit Score: 59.58 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 222 VILGLSGGVDSSVVAMLAHRAIGDKLTCVFVDNGLL---RLNEADQVMEmfgnkfglnivHVNAEQRFLDALEGEsDPET 298
Cdd:cd01990 2 VVVAFSGGVDSSLLAKLAKEVLGDNVVAVTADSPLVpreELEEAKRIAE-----------EIGIRHEIIKTDELD-DEEY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 299 KRKIIGHVFV--DIFDEESKKLKNAKW---LAQGTIYPDVIEsaaSKTGKAHVIKSHHNVgglpddmemglVEPLRELFK 373
Cdd:cd01990 70 VANDPDRCYHckKALYSTLKEIAKERGydvVLDGTNADDLKD---YRPGLLAAAELGIRS-----------PLPELGLTK 135
|
170
....*....|...
gi 75354446 374 DEVRKIGLELGLP 386
Cdd:cd01990 136 SEIRELARELGLP 148
|
|
| hisH |
PRK13141 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
77-190 |
8.93e-10 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 58.60 E-value: 8.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 77 DSGVPVFGVCYGMQTMAEQ---------LG---GKVatsteREF-----------GYAAVQVTGESALFKDLEATQDVWM 133
Cdd:PRK13141 70 ASGKPLLGICLGMQLLFESseefgetegLGllpGRV-----RRFppeeglkvphmGWNQLELKKESPLLKGIPDGAYVYF 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 134 SHGDKVVEIPSDFVkIAETE---TCPyAAMANeeKKYYGVQFHPEVTHTkNGMKMLENFV 190
Cdd:PRK13141 145 VHSYYADPCDEEYV-AATTDygvEFP-AAVGK--DNVFGAQFHPEKSGD-VGLKILKNFV 199
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
10-190 |
1.27e-09 |
|
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: 57.89 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 10 ILILDFGSQYTQLVARRIREIGVYCElwsWDVEESDIRDFnpDGIILSG----GPESVTEENSPRAP---QYVfDSGVPV 82
Cdd:cd01748 1 IAIIDYGMGNLRSVANALERLGAEVI---ITSDPEEILSA--DKLILPGvgafGDAMANLRERGLIEalkEAI-ASGKPF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 83 FGVCYGMQTMAEQ---------LG---GKVatsteREF-----------GYAAVQVTGESALFKDLEATQDVWMSHGDKV 139
Cdd:cd01748 75 LGICLGMQLLFESseegggtkgLGlipGKV-----VRFpaseglkvphmGWNQLEITKESPLFKGIPDGSYFYFVHSYYA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 75354446 140 VEIPSDFVkIAETE-----TCpyaamANEEKKYYGVQFHPEVTHtKNGMKMLENFV 190
Cdd:cd01748 150 PPDDPDYI-LATTDyggkfPA-----AVEKDNIFGTQFHPEKSG-KAGLKLLKNFL 198
|
|
| PRK08250 |
PRK08250 |
glutamine amidotransferase; Provisional |
45-177 |
1.50e-09 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181323 [Multi-domain] Cd Length: 235 Bit Score: 58.44 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 45 DIRDFnpDGIILSGGPES--VTEENSP----RAPQYVFDSGVP----VFGVCYGMQTMAEQLGGKVATSTEREFGYAAVQ 114
Cdd:PRK08250 42 NADGF--DLLIVMGGPQSprTTREECPyfdsKAEQRLINQAIKagkaVIGVCLGAQLIGEALGAKYEHSPEKEIGYFPIT 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75354446 115 VTGESA---LFKDLEATQDVWMSHGDkVVEIPSDFVKIAETETCPYAAMANEEkKYYGVQFHPEVT 177
Cdd:PRK08250 120 LTEAGLkdpLLSHFGSTLTVGHWHND-MPGLTDQAKVLATSEGCPRQIVQYSN-LVYGFQCHMEFT 183
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
9-175 |
3.03e-09 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 59.04 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 9 RILILDFGSQYTQLvaRRIREIGVYCELWSWDVEESDIRDFNPDGIILSGGPesvteeNSPRAPQYV-------FDSGVP 81
Cdd:CHL00197 194 KIIVIDFGVKYNIL--RRLKSFGCSITVVPATSPYQDILSYQPDGILLSNGP------GDPSAIHYGiktvkklLKYNIP 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 82 VFGVCYGMQTMAEQLGGKvatSTEREFGYAAVQvtGESALFKDLEATQDvwmSHGdKVVEIPSdFVKIAETET------C 155
Cdd:CHL00197 266 IFGICMGHQILSLALEAK---TFKLKFGHRGLN--HPSGLNQQVEITSQ---NHG-FAVNLES-LAKNKFYIThfnlndG 335
|
170 180
....*....|....*....|
gi 75354446 156 PYAAMANEEKKYYGVQFHPE 175
Cdd:CHL00197 336 TVAGISHSPKPYFSVQYHPE 355
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
45-189 |
8.74e-09 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 57.80 E-value: 8.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 45 DIRDFNPDGIILSGGPESVTEE-NSPRAPQYvFDSGVPVFGVCYGMQTMAEQLGGKVATSTEREFGYAAVQVTGESALFK 123
Cdd:PRK14607 39 EIEALNPSHIVISPGPGRPEEAgISVEVIRH-FSGKVPILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFR 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 124 DL----EATQdvWMSHGDKVVEIPSDFVKIAETETCPYAAMANEEKKYYGVQFHPEVTHTKNGMKMLENF 189
Cdd:PRK14607 118 GIpnptVATR--YHSLVVEEASLPECLEVTAKSDDGEIMGIRHKEHPIFGVQFHPESILTEEGKRILKNF 185
|
|
| COG1606 |
COG1606 |
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only]; |
206-387 |
1.06e-08 |
|
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
Pssm-ID: 441214 [Multi-domain] Cd Length: 265 Bit Score: 56.27 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 206 IEDAVARIKEQVGDDE-VILGLSGGVDSSVVAMLAHRAIGDKLTCVFVDNGLLR---LNEADQVMEMFGnkfglnIVHVN 281
Cdd:COG1606 1 LEEKLERLKAILKELGsVLVAFSGGVDSTLLAKVAHDVLGDRVLAVTADSPSLPereLEEAKELAKEIG------IRHEV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 282 AEQRFLDalegesDPETK----------RKIIGHVFVDIFDEEskklkNAKWLAQGTIYPDVIE----SAASKtgkahvi 347
Cdd:COG1606 75 IETDELE------DPEFVanppdrcyhcKKELFSKLKELAKEL-----GYAVVADGTNADDLGDyrpgLRAAK------- 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 75354446 348 kshhnvgglpddmEMGLVEPLRE--LFKDEVRKIGLELGLPY 387
Cdd:COG1606 137 -------------ELGVRSPLAEagLTKAEIRELARELGLPT 165
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
10-90 |
1.59e-08 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 52.60 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 10 ILILDFGSQYT---QLVARRIREIGVYCELWSWD--VEESDIRDFNPDGIILSGGPESVTEENSPRAP----QYVFDSGV 80
Cdd:cd01653 1 VAVLLFPGFEElelASPLDALREAGAEVDVVSPDggPVESDVDLDDYDGLILPGGPGTPDDLARDEALlallREAAAAGK 80
|
90
....*....|
gi 75354446 81 PVFGVCYGMQ 90
Cdd:cd01653 81 PILGICLGAQ 90
|
|
| hisH |
PRK13170 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
81-190 |
1.88e-08 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183877 [Multi-domain] Cd Length: 196 Bit Score: 54.48 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 81 PVFGVCYGMQTMAE--------QLGGKVATSTER---------EFGYAAVQVTGESALFKDLEATQDVWMSHGDKVveiP 143
Cdd:PRK13170 72 PVLGICLGMQLLGErseesggvDCLGIIDGPVKKmtdfglplpHMGWNQVTPQAGHPLFQGIEDGSYFYFVHSYAM---P 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 75354446 144 SDFVKIAeteTCPY-----AAMANeeKKYYGVQFHPEVThTKNGMKMLENFV 190
Cdd:PRK13170 149 VNEYTIA---QCNYgepfsAAIQK--DNFFGVQFHPERS-GAAGAQLLKNFL 194
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
45-190 |
2.29e-08 |
|
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: 54.02 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 45 DIRDFNPDGIILSGGPESVTEENSPRAPQYVFDSGVPVFGVCYGMQTMAEQLGGKVATSTEREFG-YAAVQVTGES---A 120
Cdd:TIGR00566 38 EIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCLGHQAMGQAFGGDVVRANTVMHGkTSEIEHNGAGifrG 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75354446 121 LFKDLEATQdvwmsHGDKVVE---IPSDFVKIAETETcPYAAMA--NEEKKYYGVQFHPEVTHTKNGMKMLENFV 190
Cdd:TIGR00566 118 LFNPLTATR-----YHSLVVEpetLPTCFPVTAWEEE-NIEIMAirHRDLPLEGVQFHPESILSEQGHQLLANFL 186
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
10-190 |
3.03e-08 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 53.73 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 10 ILILDFGSQYTQLVARRIREIGVYCELWSWD-VEESDIRDFNPDGIILSGGPESVTEENSPRAPQYVFDSGVPVFGVCYG 88
Cdd:PRK08857 2 LLMIDNYDSFTYNLYQYFCELGAQVKVVRNDeIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 89 MQTMAEQLGGKVATSTEREFG-YAAVQVTGESaLFKDLEATQDVWMSHgDKVVE---IPSDFVKIAETETCPYAA---MA 161
Cdd:PRK08857 82 HQAIAQVFGGQVVRARQVMHGkTSPIRHTGRS-VFKGLNNPLTVTRYH-SLVVKndtLPECFELTAWTELEDGSMdeiMG 159
|
170 180 190
....*....|....*....|....*....|.
gi 75354446 162 NEEKKY--YGVQFHPEVTHTKNGMKMLENFV 190
Cdd:PRK08857 160 FQHKTLpiEAVQFHPESIKTEQGHQLLANFL 190
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
10-90 |
3.84e-08 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 51.05 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 10 ILILDFGSQYT---QLVARRIREIGVYCELWSWD--VEESDIRDFNPDGIILSGGPESVTEENSPRAP----QYVFDSGV 80
Cdd:cd03128 1 VAVLLFGGSEElelASPLDALREAGAEVDVVSPDggPVESDVDLDDYDGLILPGGPGTPDDLAWDEALlallREAAAAGK 80
|
90
....*....|
gi 75354446 81 PVFGVCYGMQ 90
Cdd:cd03128 81 PVLGICLGAQ 90
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
9-175 |
2.42e-07 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 52.77 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 9 RILILDFGSQYTQLvaRRIREIGVYCELWSWDVEESDIRDFNPDGIILSGGP---ESVTEENSprAPQYVFDSGVPVFGV 85
Cdd:PRK12564 179 KVVAIDFGVKRNIL--RELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPgdpAALDYAIE--MIRELLEKKIPIFGI 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 86 CYGMQTMAEQLGGKVA---------------TSTER-EF-----GYAavqVTGESaLFKDLEATQdvwMSHGDKVVEips 144
Cdd:PRK12564 255 CLGHQLLALALGAKTYkmkfghrganhpvkdLETGKvEItsqnhGFA---VDEDS-LPANLEVTH---VNLNDGTVE--- 324
|
170 180 190
....*....|....*....|....*....|.
gi 75354446 145 dfvkiaetetcpyaAMANEEKKYYGVQFHPE 175
Cdd:PRK12564 325 --------------GLRHKDLPAFSVQYHPE 341
|
|
| AANH-like |
cd01986 |
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ... |
222-268 |
2.77e-07 |
|
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide alpha hydrolase (AANH)-like proteins includes N-type ATP PPases and ATP sulfurylases. The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.
Pssm-ID: 467490 [Multi-domain] Cd Length: 74 Bit Score: 47.83 E-value: 2.77e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 75354446 222 VILGLSGGVDSSVVAMLAHRAIGDK-LTCVFVDNGLLRLNEADQVMEM 268
Cdd:cd01986 1 VVVGYSGGKDSSVALHLASRLGRKAeVAVVHIDHGIGFKEEAESVASI 48
|
|
| PRK05637 |
PRK05637 |
anthranilate synthase component II; Provisional |
31-190 |
3.50e-07 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 180178 [Multi-domain] Cd Length: 208 Bit Score: 51.00 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 31 GVYCELWSWDVEESDIRDFNPDGIILSGGPesvteeNSPRapqyvfDSG------------VPVFGVCYGMQTMAEQLGG 98
Cdd:PRK05637 25 GYKCTVFRNTVPVEEILAANPDLICLSPGP------GHPR------DAGnmmalidrtlgqIPLLGICLGFQALLEHHGG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 99 KV-------ATSTEREFGYAAVQvtgeSALFKDL--EATQDVWMSHGDKV----------VEIPSDFVKIAeteTCPYA- 158
Cdd:PRK05637 93 KVepcgpvhGTTDNMILTDAGVQ----SPVFAGLatDVEPDHPEIPGRKVpiaryhslgcVVAPDGMESLG---TCSSEi 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 75354446 159 ---AMANE--EKKYYGVQFHPEVTHTKNGMKMLENFV 190
Cdd:PRK05637 166 gpvIMAAEttDGKAIGLQFHPESVLSPTGPIILSRCV 202
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
7-175 |
4.26e-07 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 51.82 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 7 DQRILILDFGsqYTQLVARRIREIGVYCELWSWDVEESDIRDFNPDGIILSGGPESVtEENSPRAPQyVFD--SGVPVFG 84
Cdd:PRK12838 167 GKHVALIDFG--YKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPGDP-KELQPYLPE-IKKliSSYPILG 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 85 VCYGMQTMAEQLGGkvatSTER-EFGYaavqvTGESALFKDLEaTQDVWMS---HGDKVVE--IPSDFVKIAET----ET 154
Cdd:PRK12838 243 ICLGHQLIALALGA----DTEKlPFGH-----RGANHPVIDLT-TGRVWMTsqnHGYVVDEdsLDGTPLSVRFFnvndGS 312
|
170 180
....*....|....*....|.
gi 75354446 155 CpyAAMANEEKKYYGVQFHPE 175
Cdd:PRK12838 313 I--EGLRHKKKPVLSVQFHPE 331
|
|
| PRK05665 |
PRK05665 |
amidotransferase; Provisional |
76-178 |
5.82e-07 |
|
amidotransferase; Provisional
Pssm-ID: 168162 [Multi-domain] Cd Length: 240 Bit Score: 50.58 E-value: 5.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 76 FDSGVPVFGVCYGMQTMAEQLGGKvatsTERefgyaAVQVTGESALFKDLEATQDvWM-----------SHGDKVVEIPS 144
Cdd:PRK05665 88 YERGDKLLGVCFGHQLLALLLGGK----AER-----ASQGWGVGIHRYQLAAHAP-WMspavteltlliSHQDQVTALPE 157
|
90 100 110
....*....|....*....|....*....|....
gi 75354446 145 DFVKIAETETCPYAAMANEEkKYYGVQFHPEVTH 178
Cdd:PRK05665 158 GATVIASSDFCPFAAYHIGD-QVLCFQGHPEFVH 190
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
9-175 |
6.10e-07 |
|
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: 51.56 E-value: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 9 RILILDFGSQYTQLvaRRIREIGVYCELWSWDVEESDIRDFNPDGIILSGGPesvteeNSPRAPQY-------VFDSGVP 81
Cdd:COG0505 178 HVVALDFGVKRNIL--RELAERGCRVTVVPATTSAEEILALNPDGVFLSNGP------GDPAALDYaietireLLGKGIP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 82 VFGVCYGMQTMAEQLGGKvatsTER-EFGY-AAVQ-VtgesalfKDLEaTQDVWMS---HGDKVVE--IPSDFVKIaeTE 153
Cdd:COG0505 250 IFGICLGHQLLALALGAK----TYKlKFGHrGANHpV-------KDLE-TGRVEITsqnHGFAVDEdsLPATDLEV--TH 315
|
170 180
....*....|....*....|....*.
gi 75354446 154 TCPY----AAMANEEKKYYGVQFHPE 175
Cdd:COG0505 316 VNLNdgtvEGLRHKDLPAFSVQYHPE 341
|
|
| NAD_synthase |
cd00553 |
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ... |
205-251 |
1.97e-06 |
|
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de novo nicotinamide adenine dinucleotide (NAD(+)) biosynthesis, an amide transfer from either ammonia or glutamine to nicotinic acid adenine dinucleotide (NaAD). The conversion of NaAD to NAD(+) occurs via a NAD-adenylate intermediate and requires ATP and Mg(2+). The intermediate is subsequently cleaved into NAD(+) and AMP. In many prokaryotes, such as Escherichia coli, NAD synthase consists of a single domain and is strictly ammonia dependent. In contrast, eukaryotes and other prokaryotes have an additional N-terminal amidohydrolase domain that prefer glutamine. Interestingly, NAD(+) synthases in these prokaryotes, can also utilize ammonia as an amide source.
Pssm-ID: 467484 [Multi-domain] Cd Length: 248 Bit Score: 49.09 E-value: 1.97e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 75354446 205 IIEDAVARIKEQV---GDDEVILGLSGGVDSSVVAMLAHRAIG-DKLTCVF 251
Cdd:cd00553 6 IIEALVCFLRDYLrksGAKGFVLGLSGGIDSAVVAALAVRALGaENVLALI 56
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
210-251 |
2.16e-06 |
|
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 439941 [Multi-domain] Cd Length: 542 Bit Score: 50.23 E-value: 2.16e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 75354446 210 VARIKEQV---GDDEVILGLSGGVDSSVVAMLAHRAIG-DKLTCVF 251
Cdd:COG0171 274 VLGLRDYVrknGFKGVVLGLSGGIDSALVAALAVDALGpENVLGVT 319
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
9-99 |
3.05e-06 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 49.59 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 9 RILILDFGSQYTQLvaRRIREIGvyCELW----SWDVEESdiRDFNPDGIILSGGPesvteeNSPRAPQYVFDS------ 78
Cdd:PLN02771 242 HVIAYDFGIKHNIL--RRLASYG--CKITvvpsTWPASEA--LKMKPDGVLFSNGP------GDPSAVPYAVETvkellg 309
|
90 100
....*....|....*....|.
gi 75354446 79 GVPVFGVCYGMQTMAEQLGGK 99
Cdd:PLN02771 310 KVPVFGICMGHQLLGQALGGK 330
|
|
| HisH |
COG0118 |
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
77-187 |
4.08e-06 |
|
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: 47.34 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 77 DSGVPVFGVCYGMQTMAEQ---------LG---GKVatsteREF----------GYAAVQVTGESALFKDLEATQDVWMS 134
Cdd:COG0118 71 AGGKPVLGICLGMQLLFERseengdtegLGlipGEV-----VRFpasdlkvphmGWNTVEIAKDHPLFAGIPDGEYFYFV 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 75354446 135 HGDKVVEIPSDFVkIAETE-TCPYAAMAnEEKKYYGVQFHPEVTHtKNGMKMLE 187
Cdd:COG0118 146 HSYYVPPDDPEDV-VATTDyGVPFTAAV-ERGNVFGTQFHPEKSG-AAGLRLLK 196
|
|
| PRK09522 |
PRK09522 |
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ... |
10-187 |
4.66e-06 |
|
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;
Pssm-ID: 181927 [Multi-domain] Cd Length: 531 Bit Score: 49.25 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 10 ILILDFGSQYTQLVARRIREIGVYCELWSWDVEESDIRD----FNPDGIILSGGPESVTEENSPRAPQYVFDSGVPVFGV 85
Cdd:PRK09522 4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIErlatMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 86 CYGMQTMAEQLGGKVATSTEREFGYA-AVQVTGEsALFKDLEATQDVWMSHGDKVVEIPSDFVKIAETETCpYAAMANEE 164
Cdd:PRK09522 84 CLGHQAIVEAYGGYVGQAGEILHGKAsSIEHDGQ-AMFAGLTNPLPVARYHSLVGSNIPAGLTINAHFNGM-VMAVRHDA 161
|
170 180
....*....|....*....|...
gi 75354446 165 KKYYGVQFHPEVTHTKNGMKMLE 187
Cdd:PRK09522 162 DRVCGFQFHPESILTTQGARLLE 184
|
|
| PuuD |
COG2071 |
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
52-190 |
5.25e-06 |
|
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: 47.86 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 52 DGIILSGGP--------ESVTEENSPRAP----------QYVFDSGVPVFGVCYGMQTMA------------EQLGGKVA 101
Cdd:COG2071 51 DGLVLTGGAdvdpalygEEPHPELGPIDPerdafelaliRAALERGKPVLGICRGMQLLNvalggtlyqdlpDQVPGALD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 102 --TSTEREFGYAAVQVTGESALFKDLEATQ-DVWMSHGDKVVEIPSDFVKIAetetcpYA------AMANEEKKY-YGVQ 171
Cdd:COG2071 131 hrQPAPRYAPRHTVEIEPGSRLARILGEEEiRVNSLHHQAVKRLGPGLRVSA------RApdgvieAIESPGAPFvLGVQ 204
|
170 180
....*....|....*....|.
gi 75354446 172 FHPE--VTHTKNGMKMLENFV 190
Cdd:COG2071 205 WHPEwlAASDPLSRRLFEAFV 225
|
|
| PRK13980 |
PRK13980 |
NAD synthetase; Provisional |
210-244 |
5.55e-06 |
|
NAD synthetase; Provisional
Pssm-ID: 184435 [Multi-domain] Cd Length: 265 Bit Score: 47.90 E-value: 5.55e-06
10 20 30
....*....|....*....|....*....|....*...
gi 75354446 210 VARIKEQV---GDDEVILGLSGGVDSSVVAMLAHRAIG 244
Cdd:PRK13980 18 VDFIREEVekaGAKGVVLGLSGGIDSAVVAYLAVKALG 55
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
40-190 |
5.57e-06 |
|
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: 47.19 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 40 DVEESDIRD--FNPDGIILSGGP--------ESVTEENSPRAPQ-YVFD---------SGVPVFGVCYGMQTMAEQLGGK 99
Cdd:cd01745 41 VDDEEDLEQylELLDGLLLTGGGdvdpplygEEPHPELGPIDPErDAFElallraaleRGKPILGICRGMQLLNVALGGT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 100 vatsterefgyaavqvtgesaLFKDLEATqdvwmS-HGDKVVEIPSDFVKIA-------EtetcpyaAMANEEKKYY-GV 170
Cdd:cd01745 121 ---------------------LYQDIRVN-----SlHHQAIKRLADGLRVEArapdgviE-------AIESPDRPFVlGV 167
|
170 180
....*....|....*....|..
gi 75354446 171 QFHPEVTHTKN--GMKMLENFV 190
Cdd:cd01745 168 QWHPEWLADTDpdSLKLFEAFV 189
|
|
| NAD_synthase |
pfam02540 |
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ... |
205-245 |
1.38e-05 |
|
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is induced by stress factors such as heat shock and glucose limitation.
Pssm-ID: 396888 [Multi-domain] Cd Length: 241 Bit Score: 46.61 E-value: 1.38e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 75354446 205 IIEDAVARIKEQV---GDDEVILGLSGGVDSSVVAMLAHRAIGD 245
Cdd:pfam02540 1 EINALVDFLRDYVqkaGFKGVVLGLSGGIDSSLVAYLAVKALGK 44
|
|
| nadE |
PRK00876 |
NAD(+) synthase; |
210-251 |
1.56e-05 |
|
NAD(+) synthase;
Pssm-ID: 179150 [Multi-domain] Cd Length: 326 Bit Score: 46.87 E-value: 1.56e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 75354446 210 VARIKEQVGDD----EVILGLSGGVDSSVVAMLAHRAIG-DKLTCVF 251
Cdd:PRK00876 20 RAAIREQVRGTlrrrGVVLGLSGGIDSSVTAALCVRALGkERVYGLL 66
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
52-175 |
1.65e-05 |
|
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: 46.10 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 52 DGIILSGGP--------ESVTEENSPRAPQ----------YVFDSGVPVFGVCYGMQTMAEQLGGKVAT----------- 102
Cdd:pfam07722 60 DGLLLTGGPnvdphfygEEPSESGGPYDPArdayelalirAALARGKPILGICRGFQLLNVALGGTLYQdiqeqpgftdh 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 103 -STEREFGYA---AVQVTGESALFKDLEATQDVWMS-HGDKVVEIPSDFVKIAeteTCPYAAM-----ANEEKKYYGVQF 172
Cdd:pfam07722 140 rEHCQVAPYApshAVNVEPGSLLASLLGSEEFRVNSlHHQAIDRLAPGLRVEA---VAPDGTIeaiesPNAKGFALGVQW 216
|
...
gi 75354446 173 HPE 175
Cdd:pfam07722 217 HPE 219
|
|
| hisH |
PRK13143 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
77-190 |
2.11e-05 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 45.63 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 77 DSGVPVFGVCYGMQTMAEQ---------LG---GKVATSTERE----FGYAAVQVTGESALFKDLEAtQDVWMSHGDKVV 140
Cdd:PRK13143 69 RSGKPFLGICLGMQLLFESseegggvrgLGlfpGRVVRFPAGVkvphMGWNTVKVVKDCPLFEGIDG-EYVYFVHSYYAY 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 75354446 141 EIPSDFVkIAETE-TCPYAAMANEEKkYYGVQFHPEVThTKNGMKMLENFV 190
Cdd:PRK13143 148 PDDEDYV-VATTDyGIEFPAAVCNDN-VFGTQFHPEKS-GETGLKILENFV 195
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
206-291 |
4.39e-05 |
|
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis
Pssm-ID: 440136 [Multi-domain] Cd Length: 558 Bit Score: 45.98 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 206 IEDAVARikEQVGDDEVilG--LSGGVDSSVVAMLAHRAIGDKL---TCVFVDNGllrLNE---ADQVMEMFGNKfgLNI 277
Cdd:COG0367 245 LEDAVRR--RLRADVPV--GafLSGGLDSSAIAALAARLSKGPLktfSIGFEDSA---YDEspyARAVAEHLGTE--HHE 315
|
90
....*....|....
gi 75354446 278 VHVNAEQrFLDALE 291
Cdd:COG0367 316 VTVTPED-LLDALP 328
|
|
| tRNA_Me_trans |
pfam03054 |
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ... |
222-386 |
6.29e-05 |
|
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.
Pssm-ID: 460787 [Multi-domain] Cd Length: 202 Bit Score: 44.17 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 222 VILGLSGGVDSSVVAMLAHRAiGDKLTCVFvdnglLRLNEADQVMEMFG---------------NKFGLNIVHVNAEQRF 286
Cdd:pfam03054 3 VVVAMSGGVDSSVAAYLLKEQ-GHNVIGVF-----MKNWDEEQSLDEEGkccseedladaqrvcEQLGIPLYVVNFEKEY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 287 ldalegesdpetKRKIIGHvFV-----------DI-------FDEESKKLKN---AKWLAQGTiYPDVIESAASKTGKAH 345
Cdd:pfam03054 77 ------------WEDVFEP-FLdeykngrtpnpDVlcnkeikFGALLDYALEnlgADYVATGH-YARVSLNKDGGSELLR 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 75354446 346 VIKSHHN----VGGLPDDMEMGLVEPLRELFKDEVRKIGLELGLP 386
Cdd:pfam03054 143 ALDKNKDqsyfLSTLSQEQLEKLLFPLGELTKEEVRKIAKEAGLA 187
|
|
| PRK08557 |
PRK08557 |
hypothetical protein; Provisional |
201-299 |
9.84e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 181465 [Multi-domain] Cd Length: 417 Bit Score: 44.74 E-value: 9.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 201 TSASIIEDAVARIKEQvgDDEVILGLSGGVDSSVVAMLAHRAIGDkLTCVFVDNGlLRLNEADQVMEMFGNKFGLNIVHV 280
Cdd:PRK08557 165 NSLSILKDYIEKYKNK--GYAINASFSGGKDSSVSTLLAKEVIPD-LEVIFIDTG-LEYPETINYVKDFAKKYDLNLDTL 240
|
90
....*....|....*....
gi 75354446 281 NAEQrFLDALEGESDPeTK 299
Cdd:PRK08557 241 DGDN-FWENLEKEGIP-TK 257
|
|
| hisH |
PRK13152 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
81-190 |
1.27e-04 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 171876 [Multi-domain] Cd Length: 201 Bit Score: 43.29 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 81 PVFGVCYGMQTMAEQ---------LG---GKVATSTER------EFGYAAVQVTGESALFKDLEATQDVWMSHgdkvvei 142
Cdd:PRK13152 75 PILGICLGMQLFLERgyeggvcegLGfieGEVVKFEEDlnlkipHMGWNELEILKQSPLYQGIPEKSDFYFVH------- 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 75354446 143 pSDFVKIAE---TETCPYA---AMANEEKKYYGVQFHPEVTHTKnGMKMLENFV 190
Cdd:PRK13152 148 -SFYVKCKDefvSAKAQYGhkfVASLQKDNIFATQFHPEKSQNL-GLKLLENFA 199
|
|
| MnmA |
COG0482 |
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ... |
222-242 |
2.87e-04 |
|
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]; tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440250 [Multi-domain] Cd Length: 353 Bit Score: 43.12 E-value: 2.87e-04
|
| nadE |
TIGR00552 |
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ... |
222-397 |
3.00e-04 |
|
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the biosynthesis of the essensial cofactor NAD. The member of this family from Bacillus subtilis is a strictly NH(3)-dependent NAD(+) synthetase of 272 amino acids. Proteins consisting only of the domain modeled here may be named as NH3-dependent NAD+ synthetase. Amidotransferase activity may reside in a separate protein, or not be present. Some other members of the family, such as from Mycobacterium tuberculosis, are considerably longer, contain an apparent amidotransferase domain, and show glutamine-dependent as well as NH(3)-dependent activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]
Pssm-ID: 273132 [Multi-domain] Cd Length: 250 Bit Score: 42.38 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 222 VILGLSGGVDSSVVAMLAHRAIGDkltcvfvDNGLLRLneadqvmeMFGNkfglnivhVNAEQRFLDALE-GESDPETKR 300
Cdd:TIGR00552 25 VVLGLSGGIDSAVVAALCVEALGE-------QNHALLL--------PHSV--------QTPEQDVQDALAlAEPLGINYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 301 KIIGHVFVDIFDEESKKL-KNAKWLAQGTIYPdvieSAASKTGKAHVIKSHHNVGGLPDDMEMGL------------VEP 367
Cdd:TIGR00552 82 NIDIAPIAASFQAQTETGdELSDFLAKGNLKA----RLRMAALYAIANKHNLLVLGTGNKSELMLgyftkygdggcdIAP 157
|
170 180 190
....*....|....*....|....*....|....
gi 75354446 368 LRELFKDEVRKIGLELGLPYNMLYRHP----FPG 397
Cdd:TIGR00552 158 IGDLFKTQVYELAKRLNVPERIIEKPPtadlFDG 191
|
|
| PRK13981 |
PRK13981 |
NAD synthetase; Provisional |
222-251 |
3.88e-04 |
|
NAD synthetase; Provisional
Pssm-ID: 237577 [Multi-domain] Cd Length: 540 Bit Score: 43.22 E-value: 3.88e-04
10 20 30
....*....|....*....|....*....|.
gi 75354446 222 VILGLSGGVDSSVVAMLAHRAIG-DKLTCVF 251
Cdd:PRK13981 283 VVLGLSGGIDSALVAAIAVDALGaERVRAVM 313
|
|
| mnmA |
PRK00143 |
tRNA-specific 2-thiouridylase MnmA; Reviewed |
222-242 |
4.19e-04 |
|
tRNA-specific 2-thiouridylase MnmA; Reviewed
Pssm-ID: 234664 [Multi-domain] Cd Length: 346 Bit Score: 42.75 E-value: 4.19e-04
|
| PAPS_reductase-like_YbdN |
cd23947 |
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ... |
209-280 |
4.30e-04 |
|
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to Escherichia coli YbdN; This subgroup contains Escherichia coli YbdN and other phosphoadenosine phosphosulfate (PAPS) reductase (or PAPS sulfotransferase EC 1.8.4.8)-like proteins. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N-type ATP PPases and ATP sulfurylases. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP).
Pssm-ID: 467512 [Multi-domain] Cd Length: 206 Bit Score: 41.61 E-value: 4.30e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75354446 209 AVARIKE-QVGDDEVILGLSGGVDSSVVAMLAHRAI---GDKLTCVFVDNGlLRLNEADQVMEMFGNKFGLNIVHV 280
Cdd:cd23947 1 ALERIRKvFEEFDPVIVSFSGGKDSLVLLHLALEALrrlRKDVYVVFIDTG-IEFPETIDFVEKLAETLGLDVEAA 75
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
219-291 |
9.69e-04 |
|
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or synthetase) B is always associated with an N-terminal amidotransferase domain. Family members that contain this domain catalyze the conversion of aspartate to asparagine. Asparagine synthase B catalyzes the synthesis of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase.
Pssm-ID: 467495 [Multi-domain] Cd Length: 224 Bit Score: 40.72 E-value: 9.69e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75354446 219 DDEVILGLSGGVDSSVVAMLAHRAIGD-KLTCVFVDNGLLRLNE---ADQVMEMFGNKFglNIVHVNAEQrFLDALE 291
Cdd:cd01991 2 DVPVGVLLSGGLDSSLIAALAARLLPEtPIDLFTVGFEGSPTPDraaARRVAEELGTEH--HEVEVTIEE-LLDALP 75
|
|
| AANH_superfamily |
cd01984 |
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ... |
222-253 |
1.90e-03 |
|
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase (AANH) superfamily includes N-type ATP PPases, ATP sulfurylases, universal stress response proteins (USPs), and electron transfer flavoproteins (ETFs). The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.
Pssm-ID: 467489 [Multi-domain] Cd Length: 56 Bit Score: 36.68 E-value: 1.90e-03
10 20 30
....*....|....*....|....*....|....*
gi 75354446 222 VILGLSGGVDSSVVAMLAHRAIG---DKLTCVFVD 253
Cdd:cd01984 1 ILVPLSGGEDSSIALKHAKKFKTskaEEVVVVHVG 35
|
|
| PRK13794 |
PRK13794 |
hypothetical protein; Provisional |
202-284 |
2.30e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237509 [Multi-domain] Cd Length: 479 Bit Score: 40.42 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75354446 202 SASIIEDAVARIKEQVgddevILGLSGGVDSSVVAMLAHRAIGDKLTCVFVDNGlLRLNEADQVMEMFGNKFGLNIVHVN 281
Cdd:PRK13794 235 SIGFIRNTAEKINKPV-----TVAYSGGKDSLATLLLALKALGINFPVLFNDTG-LEFPETLENVEDVEKHYGLEIIRTK 308
|
...
gi 75354446 282 AEQ 284
Cdd:PRK13794 309 SEE 311
|
|
| MnmA_TRMU-like |
cd01998 |
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
222-251 |
5.57e-03 |
|
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.
Pssm-ID: 467502 [Multi-domain] Cd Length: 349 Bit Score: 39.03 E-value: 5.57e-03
10 20 30
....*....|....*....|....*....|
gi 75354446 222 VILGLSGGVDSSVVAMLAHRAiGDKLTCVF 251
Cdd:cd01998 2 VAVAMSGGVDSSVAAALLKEQ-GYDVIGVF 30
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