|
Name |
Accession |
Description |
Interval |
E-value |
| guaA |
PRK00074 |
GMP synthase; Reviewed |
4-513 |
0e+00 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 1079.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 4 KQHDTIIVLDFGSQYNQLIARRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPNSVYGEGALHCDEKIFELGLPIFG 83
Cdd:PRK00074 1 IHHDKILILDFGSQYTQLIARRVRELGVYSEIVPYDISAEEIRAFNPKGIILSGGPASVYEEGAPRADPEIFELGVPVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 84 ICYGMQLMTQHFGGKVERANHREYGKAVLKVENESKLYANLPEEQVVWMSHGDLVTGLPEGFVVDATSESCPIAGMSNEA 163
Cdd:PRK00074 81 ICYGMQLMAHQLGGKVERAGKREYGRAELEVDNDSPLFKGLPEEQDVWMSHGDKVTELPEGFKVIASTENCPIAAIANEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 164 KNLYGVQFHPEVRHSEHGNDLIKNFVFGVCGCSEGWNMENFIEVELEKIRETVGDKKVLCALSGGVDSSVVAVLIHKAIG 243
Cdd:PRK00074 161 RKFYGVQFHPEVTHTPQGKKLLENFVFDICGCKGDWTMENFIEEAIEEIREQVGDKKVILGLSGGVDSSVAAVLLHKAIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 244 DQLTCIFVDHGLLRKGEAEGVMKTFSEGFHMNVIKVDARDRFMDKLKGVEDPEQKRKIIGNEFIYVFDDEASKLQGMDFL 323
Cdd:PRK00074 241 DQLTCVFVDHGLLRKNEAEQVMEMFREHFGLNLIHVDASDRFLSALAGVTDPEEKRKIIGREFIEVFEEEAKKLGGVKFL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 324 AQGTLYTDIVESGTAT-AQTIKSHHNVGGLPEDMQFKLIEPLNTLFKDEVRVLGSELGIPDEIVWRQPFPGPGLGIRVLG 402
Cdd:PRK00074 321 AQGTLYPDVIESGGTKkAATIKSHHNVGGLPEDMKLKLVEPLRELFKDEVRKLGLELGLPEEIVYRHPFPGPGLAIRILG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 403 EITEEKLEIVRESDAILREEIIKAGLDREIWQYFTALPGMRSVGVMGDERTYDYTVGIRAVTSIDGMTADWARIPWDVLE 482
Cdd:PRK00074 401 EVTKEKLDILREADAIFIEELRKAGLYDKIWQAFAVLLPVKSVGVMGDGRTYDYVVALRAVTSIDGMTADWARLPYDFLE 480
|
490 500 510
....*....|....*....|....*....|.
gi 1812584946 483 KISVRIVNEVKHVNRIVYDVTSKPPATIEWE 513
Cdd:PRK00074 481 KISNRIINEVKGVNRVVYDITSKPPATIEWE 511
|
|
| GuaA2 |
COG0519 |
GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, ... |
4-513 |
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: 967.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 4 KQHDTIIVLDFGSQYNQLIARRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPNSVYGEGALHCDEKIFELGLPIFG 83
Cdd:COG0519 1 MDKEIIIVLDFGGQYQQLIARRRREEGVYSEIIPPDTAAEEIKAKGPPGIILSGGPSSVYEEGAPPDDPELFELGGPILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 84 ICYGMQLMTQHFGGKVERANHREYGKAVLKVENESKLYANLPEEQVVWMSHGDLVTGLPEGFVVDATSESCPIAGMSNEA 163
Cdd:COG0519 81 ICYGGQLMLHLLGGGVVRAERREYGGALLLVDDESDLFAGGPEELQVWMSHGDRVTELPPGFEVIASTENCPVAAIANEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 164 KNLYGVQFHPEVRHSEHGNDLIKNFVFGVCGCSEGWNMENFIEVELEKIRETVGDKKVLCALSGGVDSSVVAVLIHKAIG 243
Cdd:COG0519 161 RKLYGVQFHPEVVHTEQGKEILKNFLFDICGCKGDWTMENFIEEAIEEIREQVGDGKVICALSGGVDSSVAAALLHKAIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 244 DQLTCIFVDHGLLRKGEAEGVMKTFSEGFHMNVIKVDARDRFMDKLKGVEDPEQKRKIIGNEFIYVFDDEASKLQGMDFL 323
Cdd:COG0519 241 DQLTCVFVDHGLLRKGEAEQVEETFKEHFGLNLIYVDASERFLSALKGVTDPEEKRKIIGEEFIEVFEEEAKKLGGAKFL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 324 AQGTLYTDIVESGTAT--AQTIKSHHNVGGLPEDMQFKLIEPLNTLFKDEVRVLGSELGIPDEIVWRQPFPGPGLGIRVL 401
Cdd:COG0519 321 AQGTLYPDVIESGSVKgpAATIKSHHNVGGLPEDMKFKLVEPLRELFKDEVRALGRELGLPEEIVYRHPFPGPGLAIRIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 402 GEITEEKLEIVRESDAILREEIIKAGLDREIWQYFTALPGMRSVGVMGDERTYDYTVGIRAVTSIDGMTADWARIPWDVL 481
Cdd:COG0519 401 GEVTKEKLEILREADAIFIEELRKAGLYDKVWQAFAVLLPVKSVGVMGDERTYEYVVALRAVTSVDGMTADWARLPYEVL 480
|
490 500 510
....*....|....*....|....*....|..
gi 1812584946 482 EKISVRIVNEVKHVNRIVYDVTSKPPATIEWE 513
Cdd:COG0519 481 ERISNRIINEVKGVNRVVYDITSKPPATIEWE 512
|
|
| PLN02347 |
PLN02347 |
GMP synthetase |
3-513 |
0e+00 |
|
GMP synthetase
Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 721.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 3 KKQHDTIIVLDFGSQYNQLIARRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPNSVYGEGALHCDEKIFEL----G 78
Cdd:PLN02347 7 KSYLDVVLILDYGSQYTHLITRRVRELGVYSLLLSGTASLDRIASLNPRVVILSGGPHSVHVEGAPTVPEGFFDYcrerG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 79 LPIFGICYGMQLMTQHFGGKVERANHREYGKAVLKVENESKLYANLPEE--QVVWMSHGDLVTGLPEGFVVDATSESCPI 156
Cdd:PLN02347 87 VPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCGSQLFGDLPSGetQTVWMSHGDEAVKLPEGFEVVAKSVQGAV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 157 AGMSNEAKNLYGVQFHPEVRHSEHGNDLIKNFVFGVCGCSEGWNMENFIEVELEKIRETVG-DKKVLCALSGGVDSSVVA 235
Cdd:PLN02347 167 VAIENRERRIYGLQYHPEVTHSPKGMETLRHFLFDVCGVTADWKMQDVLEEQIELIKATVGpDEHVICALSGGVDSTVAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 236 VLIHKAIGDQLTCIFVDHGLLRKGEAEGVMKTFSEGFHMNVIKVDARDRFMDKLKGVEDPEQKRKIIGNEFIYVFDDEAS 315
Cdd:PLN02347 247 TLVHKAIGDRLHCVFVDNGLLRYKEQERVMETFKRDLHLPVTCVDASERFLSKLKGVTDPEKKRKIIGAEFIEVFDEFAH 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 316 KLQGM-----DFLAQGTLYTDIVES------GTATAQTIKSHHNVGGLPEDMQFKLIEPLNTLFKDEVRVLGSELGIPDE 384
Cdd:PLN02347 327 KLEQKlgkkpAFLVQGTLYPDVIEScpppgsGRTHSHTIKSHHNVGGLPKDMKLKLIEPLKLLFKDEVRKLGRLLGVPEA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 385 IVWRQPFPGPGLGIRVLGEITEE-KLEIVRESDAILREEIIKAGLDREIWQYFTALPGMRSVGVMGDERTYDYTVGIRAV 463
Cdd:PLN02347 407 FLKRHPFPGPGLAVRVLGDVTEGnALDILRQVDEIFINSIKDAGLYDEIWQAFAVFLPVKSVGVQGDQRTHSHVVALRAV 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1812584946 464 TSIDGMTADWARIPWDVLEKISVRIVNEVKHVNRIVYDVTSKPPATIEWE 513
Cdd:PLN02347 487 TSEDGMTADWYHFEHKFLDDVSRKICNEVRGVNRVVYDITSKPPSTIEWE 536
|
|
| guaA_Cterm |
TIGR00884 |
GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; This protein of purine ... |
203-513 |
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: 570.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 203 NFIEVELEKIRETVGDKKVLCALSGGVDSSVVAVLIHKAIGDQLTCIFVDHGLLRKGEAEGVMKTFSEGFHMNVIKVDAR 282
Cdd:TIGR00884 1 NFIEEAVEEIREQVGDAKVIIALSGGVDSSVAAVLAHRAIGDRLTCVFVDHGLLRKGEAEQVVKTFGDRLGLNLVYVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 283 DRFMDKLKGVEDPEQKRKIIGNEFIYVFDDEASKLQGMDFLAQGTLYTDIVESGTATAQTIKSHHNVGGLPEDMQFKLIE 362
Cdd:TIGR00884 81 ERFLSALKGVTDPEEKRKIIGRVFIEVFEREAKKIGDAEYLAQGTIYPDVIESAAGTAHVIKSHHNVGGLPEDMKLKLVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 363 PLNTLFKDEVRVLGSELGIPDEIVWRQPFPGPGLGIRVLGEITEEKLEIVRESDAILREEIIKAGLDREIWQYFTALPGM 442
Cdd:TIGR00884 161 PLRELFKDEVRKLGKELGLPEEIVWRHPFPGPGLAVRVLGEVTKEKLEILRRADAIVIEELKKAGLYDKVWQAFAVLLPV 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1812584946 443 RSVGVMGDERTYDYTVGIRAVTSIDGMTADWARIPWDVLEKISVRIVNEVKHVNRIVYDVTSKPPATIEWE 513
Cdd:TIGR00884 241 KSVGVMGDGRTYGYVIALRAVESIDGMTADWARLPYDFLERISNRITNEVPGVNRVVYDITSKPPATIEWE 311
|
|
| GMP_synthase_C |
cd01997 |
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ... |
212-513 |
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: 512.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 212 IRETVGDKKVLCALSGGVDSSVVAVLIHKAIGD-QLTCIFVDHGLLRKGEAEGVMKTFSEGFHMNVIKVDARDRFMDKLK 290
Cdd:cd01997 1 IKRTVGDKKVLCLVSGGVDSTVCAALLHKALGDeRVIAVHIDNGLMRKNESEQVEEALKKLGVINLAKVDASKRFLKKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 291 GVEDPEQKRKIIGNEFIYVFDDEASKL---QGMDFLAQGTLYTDIVESG----TATAQTIKSHHNVGGLPED-MQFKLIE 362
Cdd:cd01997 81 GVTDPEEKRKIIGDTFIEVFDEVAKELnldPDDVYLAQGTLYPDLIESAsslaSSKADTIKTHHNVGGLPRElLKGKLVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 363 PLNTLFKDEVRVLGSELGIPDEIVWRQPFPGPGLGIRVLGEITEEKLEIVRESDAILREEIIKAGLDREIWQYFTALPGM 442
Cdd:cd01997 161 PLRDLFKDEVRELGRELGLPEELVWRHPFPGPGLAIRVLGEVTPEKLEILREADAIVEEELREAGLYDKISQAFAVLLPI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1812584946 443 RSVGVMGDERTYDYTVGIRAVTSIDGMTADWARIPWDVLEKISVRIVNEVKHVNRIVYDVTSKPPATIEWE 513
Cdd:cd01997 241 KSVGVQGDGRTYGYVVALRAVETEDFMTAEWARPPYEVLDKISNRITNEVPGVNRVVYDITSKPPATIEWE 311
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
9-195 |
9.92e-115 |
|
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: 336.59 E-value: 9.92e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 9 IIVLDFGSQYNQLIARRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPNSVYGEGALHCDEKIFELGLPIFGICYGM 88
Cdd:TIGR00888 1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGPSSVYAENAPRADEKIFELGVPVLGICYGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 89 QLMTQHFGGKVERANHREYGKAVLKVENESKLYANLPEEQVVWMSHGDLVTGLPEGFVVDATSESCPIAGMSNEAKNLYG 168
Cdd:TIGR00888 81 QLMAKQLGGEVGRAEKREYGKAELEILDEDDLFRGLPDESTVWMSHGDKVKELPEGFKVLATSDNCPVAAMAHEEKPIYG 160
|
170 180
....*....|....*....|....*..
gi 1812584946 169 VQFHPEVRHSEHGNDLIKNFVFGVCGC 195
Cdd:TIGR00888 161 VQFHPEVTHTEYGNELLENFVYDVCGC 187
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
9-189 |
1.36e-110 |
|
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: 325.64 E-value: 1.36e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 9 IIVLDFGSQYNQLIARRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPNSVYGEGALHCDEKIFELGLPIFGICYGM 88
Cdd:cd01742 1 ILILDFGSQYTHLIARRVRELGVYSEILPNTTPLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGICYGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 89 QLMTQHFGGKVERANHREYGKAVLKVENESKLYANLPEEQVVWMSHGDLVTGLPEGFVVDATSESCPIAGMSNEAKNLYG 168
Cdd:cd01742 81 QLIAKALGGKVERGDKREYGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVVKLPEGFKVIASSDNCPVAAIANEEKKIYG 160
|
170 180
....*....|....*....|.
gi 1812584946 169 VQFHPEVRHSEHGNDLIKNFV 189
Cdd:cd01742 161 VQFHPEVTHTEKGKEILKNFL 181
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
9-192 |
8.76e-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: 230.22 E-value: 8.76e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 9 IIVLD---FGSQYNQLIARRIRE-------FGVY-SELHPHTITAEeikamNPKGIIFSGGPNSVYGE-----GALHCDE 72
Cdd:COG0518 2 ILILDhdpFGGQYPGLIARRLREagieldvLRVYaGEILPYDPDLE-----DPDGLILSGGPMSVYDEdpwleDEPALIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 73 KIFELGLPIFGICYGMQLMTQHFGGKVERANHREYGKAVLKVENESKLYANLPEEQVVWMSHGDLVTGLPEGFVVDATSE 152
Cdd:COG0518 77 EAFELGKPVLGICYGAQLLAHALGGKVEPGPGREIGWAPVELTEADPLFAGLPDEFTVWMSHGDTVTELPEGAEVLASSD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 153 SCPIAGMSNEaKNLYGVQFHPEVRHS------------------------------EHGNDLIKNFVFGV 192
Cdd:COG0518 157 NCPNQAFRYG-RRVYGVQFHPEVTHTmmeawleeradelaaeellaeaslhdpelrEAGRRLLRNFLREI 225
|
|
| GMP_synt_C |
pfam00958 |
GMP synthase C terminal domain; GMP synthetase is a glutamine amidotransferase from the de ... |
421-512 |
6.61e-67 |
|
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: 210.34 E-value: 6.61e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 421 EEIIKAGLDREIWQYFTALPGMRSVGVMGDERTYDYTVGIRAVTSIDGMTADWARIPWDVLEKISVRIVNEVKHVNRIVY 500
Cdd:pfam00958 1 EEIKKAGLYRKIWQAFAVLLPVKSVGVMGDERTYEYVVALRAVTSTDGMTADWARLPYEVLEKISNRIVNEVPGVNRVVY 80
|
90
....*....|..
gi 1812584946 501 DVTSKPPATIEW 512
Cdd:pfam00958 81 DITSKPPATIEW 92
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
9-194 |
1.72e-64 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 207.40 E-value: 1.72e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 9 IIVLDFGSQYNQLIARRIREFGVYSELHPHTITAEEIKAMNpKGIIFSGGPNSvygEGALHCDEKIFELGLPIFGICYGM 88
Cdd:PRK00758 2 IVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTTPVEEIKAFE-DGLILSGGPDI---ERAGNCPEYLKELDVPILGICLGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 89 QLMTQHFGGKVERANHREYGKAVLKVENESKLYANLPEEQVVWMSHGDLVTGLPEGFVVDATSESCPIAGMSNEAKNLYG 168
Cdd:PRK00758 78 QLIAKAFGGEVGRGEYGEYALVEVEILDEDDILKGLPPEIRVWASHADEVKELPDGFEILARSDICEVEAMKHKEKPIYG 157
|
170 180
....*....|....*....|....*.
gi 1812584946 169 VQFHPEVRHSEHGNDLIKNFvFGVCG 194
Cdd:PRK00758 158 VQFHPEVAHTEYGEEIFKNF-LEICG 182
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
10-192 |
3.69e-58 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 190.91 E-value: 3.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 10 IVLDFGSQYNQLIARRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPNSVY-GEGALHCDEKIFELGLPIFGICYGM 88
Cdd:pfam00117 1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGaAGGAIEAIREARELKIPILGICLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 89 QLMTQHFGGKVERANHREYGKAVLKVEN-ESKLYANLPEEQVVWMSHGDLVTG--LPEGFVVDATSE-SCPIAGMSNEAK 164
Cdd:pfam00117 81 QLLALAFGGKVVKAKKFGHHGKNSPVGDdGCGLFYGLPNVFIVRRYHSYAVDPdtLPDGLEVTATSEnDGTIMGIRHKKL 160
|
170 180
....*....|....*....|....*...
gi 1812584946 165 NLYGVQFHPEVRHSEHGNDLIKNFVFGV 192
Cdd:pfam00117 161 PIFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
18-189 |
1.03e-30 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 117.92 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 18 YNqlIARRIREFG----VYSelhPHTITAEEIKAMNPKGIIFSGGPNSvyGEGALHCDEKIFELG--LPIFGICYGMQLM 91
Cdd:PRK05670 13 YN--LVQYLGELGaevvVYR---NDEITLEEIEALNPDAIVLSPGPGT--PAEAGISLELIREFAgkVPILGVCLGHQAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 92 TQHFGGKVERANHREYGKAVLKVENESKLYANLPEEQVVWMSHgDLV---TGLPEGFVVDATSESCPIAGMSNEAKNLYG 168
Cdd:PRK05670 86 GEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYH-SLVvdrESLPDCLEVTAWTDDGEIMGVRHKELPIYG 164
|
170 180
....*....|....*....|.
gi 1812584946 169 VQFHPEVRHSEHGNDLIKNFV 189
Cdd:PRK05670 165 VQFHPESILTEHGHKLLENFL 185
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
18-189 |
2.04e-28 |
|
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: 111.28 E-value: 2.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 18 YNqlIARRIREFGVYSELHPHT-ITAEEIKAMNPKGIIFSGGPnsvyG--EGALHCDEKIFELG--LPIFGICYGMQLMT 92
Cdd:COG0512 12 YN--LVQYLGELGAEVVVVRNDeITLEEIEALAPDGIVLSPGP----GtpEEAGISLEVIRAFAgkIPILGVCLGHQAIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 93 QHFGGKVERAN---HreyGKAVLKVENESKLYANLPEEQVVWMSH---GDLVTgLPEGFVVDATSESCPIAGMSNEAKNL 166
Cdd:COG0512 86 EAFGGKVVRAPepmH---GKTSPITHDGSGLFAGLPNPFTATRYHslvVDRET-LPDELEVTAWTEDGEIMGIRHRELPI 161
|
170 180
....*....|....*....|....*.
gi 1812584946 167 YGVQFHPEvrhS---EHGNDLIKNFV 189
Cdd:COG0512 162 EGVQFHPE---SiltEHGHQLLANFL 184
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
52-189 |
4.45e-25 |
|
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: 101.94 E-value: 4.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 52 GIIFSGGPNSVYGEGA--LHcDEK-----IFELGLPIFGICYGMQLMTQHFGGKVERANH-REYGKAVLKVENESK---L 120
Cdd:cd01741 49 GLVILGGPMSVDEDDYpwLK-KLKelirqALAAGKPVLGICLGHQLLARALGGKVGRNPKgWEIGWFPVTLTEAGKadpL 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1812584946 121 YANLPEEQVVWMSHGDLVTGLPEGFVVDATSESCPIAGMSNEaKNLYGVQFHPEvrhsehgNDLIKNFV 189
Cdd:cd01741 128 FAGLPDEFPVFHWHGDTVVELPPGAVLLASSEACPNQAFRYG-DRALGLQFHPE-------ERLLRNFL 188
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
18-189 |
1.41e-24 |
|
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: 100.69 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 18 YNqlIARRIREFGVYSE-LHPHTITAEEIKAMNPKGIIFSGGPNSVyGEGALHCD-EKIFELGLPIFGICYGMQLMTQHF 95
Cdd:cd01743 12 YN--LVQYLRELGAEVVvVRNDEITLEELELLNPDAIVISPGPGHP-EDAGISLEiIRALAGKVPILGVCLGHQAIAEAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 96 GGKVERANHREYGKAVLKVENESKLYANLPEE-QVV----WmsHGDLVTgLPEGFVVDATSESCPIAGMSNEAKNLYGVQ 170
Cdd:cd01743 89 GGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPfTVGryhsL--VVDPDP-LPDLLEVTASTEDGVIMALRHRDLPIYGVQ 165
|
170
....*....|....*....
gi 1812584946 171 FHPEVRHSEHGNDLIKNFV 189
Cdd:cd01743 166 FHPESILTEYGLRLLENFL 184
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
35-188 |
2.98e-21 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 96.71 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 35 LHPHTITAEEIKAMNPKGIIFSGGPNSvyGEGALHCDEKIFELG--LPIFGICYGMQLMTQHFGGKVERANHREYGKAVL 112
Cdd:PRK14607 30 VRNDEITIEEIEALNPSHIVISPGPGR--PEEAGISVEVIRHFSgkVPILGVCLGHQAIGYAFGGKIVHAKRILHGKTSP 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812584946 113 KVENESKLYANLPEEQVVWMSHGDLV--TGLPEGFVVDATSESCPIAGMSNEAKNLYGVQFHPEVRHSEHGNDLIKNF 188
Cdd:PRK14607 108 IDHNGKGLFRGIPNPTVATRYHSLVVeeASLPECLEVTAKSDDGEIMGIRHKEHPIFGVQFHPESILTEEGKRILKNF 185
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
40-189 |
3.04e-20 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 88.44 E-value: 3.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 40 ITAEEIKAMNPKGIIFSGGPNSVYGEGALHCDEKIFELGLPIFGICYGMQLMTQHFGGKVERANHREYGKAVLKVENESK 119
Cdd:PRK08007 34 LTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEG 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1812584946 120 LYANLPEEQVVWMSHGDLV--TGLPEGFVVDATSESCPIAGMSNEAKNLYGVQFHPEVRHSEHGNDLIKNFV 189
Cdd:PRK08007 114 VFRGLANPLTVTRYHSLVVepDSLPACFEVTAWSETREIMGIRHRQWDLEGVQFHPESILSEQGHQLLANFL 185
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
9-174 |
4.50e-20 |
|
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: 87.55 E-value: 4.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 9 IIVLDFGSQYNQLiaRRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPnsvyGEGAlHCDE------KIFELGLPIF 82
Cdd:cd01744 1 VVVIDFGVKHNIL--RELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGP----GDPA-LLDEaiktvrKLLGKKIPIF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 83 GICYGMQLMTQHFGGKVER-------ANHreygkAVLKVENesklyanlpeeQVVWMS---HGDLV--TGLPEGFVV--- 147
Cdd:cd01744 74 GICLGHQLLALALGAKTYKmkfghrgSNH-----PVKDLIT-----------GRVYITsqnHGYAVdpDSLPGGLEVthv 137
|
170 180 190
....*....|....*....|....*....|
gi 1812584946 148 ---DATsescpIAGMSNEAKNLYGVQFHPE 174
Cdd:cd01744 138 nlnDGT-----VEGIRHKDLPVFSVQFHPE 162
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
8-174 |
1.44e-18 |
|
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: 87.00 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 8 TIIVLDFGSQYNqlIARRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPnsvyGEGAlHCDE------KIFELGLPI 81
Cdd:COG0505 178 HVVALDFGVKRN--ILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGP----GDPA-ALDYaietirELLGKGIPI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 82 FGICYGMQLMTQHFGGKVER-------ANHreygkavlkvenesklyanlPeeqVVwmshgDLVTGLPE------GFVVD 148
Cdd:COG0505 251 FGICLGHQLLALALGAKTYKlkfghrgANH--------------------P---VK-----DLETGRVEitsqnhGFAVD 302
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1812584946 149 AtsESCP---------------IAGMSNEAKNLYGVQFHPE 174
Cdd:COG0505 303 E--DSLPatdlevthvnlndgtVEGLRHKDLPAFSVQYHPE 341
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
38-189 |
2.72e-18 |
|
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: 82.91 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 38 HTITAEEIKAMNPKGIIFSGGPNSVyGEGALHCDE-KIFELGLPIFGICYGMQLMTQHFGGKVERANHREYGKAVLKVEN 116
Cdd:TIGR00566 32 DSLTLQEIEALLPLLIVISPGPCTP-NEAGISLEAiRHFAGKLPILGVCLGHQAMGQAFGGDVVRANTVMHGKTSEIEHN 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1812584946 117 ESKLYANLPEEQVVWMSHGDLVT--GLPEGFVVDATS-ESCPIAGMSNEAKNLYGVQFHPEVRHSEHGNDLIKNFV 189
Cdd:TIGR00566 111 GAGIFRGLFNPLTATRYHSLVVEpeTLPTCFPVTAWEeENIEIMAIRHRDLPLEGVQFHPESILSEQGHQLLANFL 186
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
40-189 |
1.52e-17 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 81.00 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 40 ITAEEIKAMNPKGIIFSGGPNSVYGEGALHCDEKIFELGLPIFGICYGMQLMTQHFGGKVERANHREYGKAVLKVENESK 119
Cdd:PRK07649 34 VTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKT 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1812584946 120 LYANLPEEQVVWMSHGDLVTG--LPEGFVVDATSESCPIAGMSNEAKNLYGVQFHPEVRHSEHGNDLIKNFV 189
Cdd:PRK07649 114 IFSDIPNPFTATRYHSLIVKKetLPDCLEVTSWTEEGEIMAIRHKTLPIEGVQFHPESIMTSHGKELLQNFI 185
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
40-189 |
1.29e-16 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 78.23 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 40 ITAEEIKAMNPKGIIFSGGPNSVYGEGalHCDEKIFELG--LPIFGICYGMQLMTQHFGGKVERANHREYGKAVLKVENE 117
Cdd:CHL00101 34 IDLSKIKNLNIRHIIISPGPGHPRDSG--ISLDVISSYApyIPILGVCLGHQSIGYLFGGKIIKAPKPMHGKTSKIYHNH 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1812584946 118 SKLYANLPEEQVVWMSHGDLV--TGLPEGFVVDA-TSESCPIAGMSNEAKNLYGVQFHPEVRHSEHGNDLIKNFV 189
Cdd:CHL00101 112 DDLFQGLPNPFTATRYHSLIIdpLNLPSPLEITAwTEDGLIMACRHKKYKMLRGIQFHPESLLTTHGQQILRNFL 186
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
4-189 |
4.16e-16 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 77.53 E-value: 4.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 4 KQHDTIIVLDFGSQYNQLIARRIREFGVYSELHPH-TITAEEIKAMNPKGIIFSGGPNSVYGEG-ALhcdEKIFELG--L 79
Cdd:PLN02335 16 KQNGPIIVIDNYDSFTYNLCQYMGELGCHFEVYRNdELTVEELKRKNPRGVLISPGPGTPQDSGiSL---QTVLELGplV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 80 PIFGICYGMQLMTQHFGGKVERA-NHREYGKAVL---KVENESKLYANLPEEQVVWMSHGDLVT--GLPEGFV-VDATSE 152
Cdd:PLN02335 93 PLFGVCMGLQCIGEAFGGKIVRSpFGVMHGKSSPvhyDEKGEEGLFSGLPNPFTAGRYHSLVIEkdTFPSDELeVTAWTE 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1812584946 153 SCPIAGMSNEA-KNLYGVQFHPEVRHSEHGNDLIKNFV 189
Cdd:PLN02335 173 DGLIMAARHRKyKHIQGVQFHPESIITTEGKTIVRNFI 210
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
8-174 |
6.52e-16 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 78.96 E-value: 6.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 8 TIIVLDFGSQYNqlIARRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPnsvyGEGALhCDE------KIFELGLPI 81
Cdd:PRK12564 179 KVVAIDFGVKRN--ILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGP----GDPAA-LDYaiemirELLEKKIPI 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 82 FGICYGMQLMTQHFGGKVERAN--HReyGkavlkvenesklyANLPeeqVvwmshGDLVTGLPE------GFVVDAtsES 153
Cdd:PRK12564 252 FGICLGHQLLALALGAKTYKMKfgHR--G-------------ANHP---V-----KDLETGKVEitsqnhGFAVDE--DS 306
|
170 180 190
....*....|....*....|....*....|....*
gi 1812584946 154 CP--------------IAGMSNEAKNLYGVQFHPE 174
Cdd:PRK12564 307 LPanlevthvnlndgtVEGLRHKDLPAFSVQYHPE 341
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
76-189 |
1.19e-15 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 79.96 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 76 ELGLPIFGICYGMQLMTQHFGGKVERANHREYGKA-VLKVENESKLYANLPEEQVVWMSHGDLVT--GLPEGFVVDATSE 152
Cdd:PRK13566 596 ARNLPIFGVCLGLQAIVEAFGGELGQLAYPMHGKPsRIRVRGPGRLFSGLPEEFTVGRYHSLFADpeTLPDELLVTAETE 675
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1812584946 153 SCPIAGMSNEAKNLYGVQFHPEVRHS---EHGNDLIKNFV 189
Cdd:PRK13566 676 DGVIMAIEHKTLPVAAVQFHPESIMTlggDVGLRIIENVV 715
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
45-189 |
6.75e-15 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 72.99 E-value: 6.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 45 IKAMNPKGIIFSGGPNSVYGEGALHCDEKIFELGLPIFGICYGMQLMTQHFGGKVERANHREYGKAVLKVENESKLYANL 124
Cdd:PRK08857 39 IEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGL 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1812584946 125 PEEQVVWMSHGDLVTG--LPEGFVVDATSESC-----PIAGMSNEAKNLYGVQFHPEVRHSEHGNDLIKNFV 189
Cdd:PRK08857 119 NNPLTVTRYHSLVVKNdtLPECFELTAWTELEdgsmdEIMGFQHKTLPIEAVQFHPESIKTEQGHQLLANFL 190
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
40-189 |
7.41e-15 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 72.97 E-value: 7.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 40 ITAEEIKAMNPKGIIFSGGPNSVYGEGALHCDEKIFELGLPIFGICYGMQLMTQHFGGKVERANHREYGKAVLKVENESK 119
Cdd:PRK06774 34 LQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCLGHQALGQAFGARVVRARQVMHGKTSAICHSGQG 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1812584946 120 LYANLPEEQVVWMSHGDLV--TGLPEGFVVDATSESC----PIAGMSNEAKNLYGVQFHPEVRHSEHGNDLIKNFV 189
Cdd:PRK06774 114 VFRGLNQPLTVTRYHSLVIaaDSLPGCFELTAWSERGgemdEIMGIRHRTLPLEGVQFHPESILSEQGHQLLDNFL 189
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
8-174 |
8.59e-15 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 75.70 E-value: 8.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 8 TIIVLDFGsqYNQLIARRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPNSVygEGALHCDEKIFEL--GLPIFGIC 85
Cdd:PRK12838 169 HVALIDFG--YKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPGDP--KELQPYLPEIKKLisSYPILGIC 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 86 YGMQLMTQHFGGKVER-------ANHreygkAVLKVENesklyanlpeeQVVWMS---HGDLV-------TGLPEGFvVD 148
Cdd:PRK12838 245 LGHQLIALALGADTEKlpfghrgANH-----PVIDLTT-----------GRVWMTsqnHGYVVdedsldgTPLSVRF-FN 307
|
170 180
....*....|....*....|....*.
gi 1812584946 149 ATSEScpIAGMSNEAKNLYGVQFHPE 174
Cdd:PRK12838 308 VNDGS--IEGLRHKKKPVLSVQFHPE 331
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
9-189 |
1.40e-14 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 75.22 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 9 IIVLDFGSQYNqlIARRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPN--SVYGEGaLHCDEKIFELGLPIFGICY 86
Cdd:CHL00197 195 IIVIDFGVKYN--ILRRLKSFGCSITVVPATSPYQDILSYQPDGILLSNGPGdpSAIHYG-IKTVKKLLKYNIPIFGICM 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 87 GMQLMTQHFGGKV------ERA-NHREYGKAVLKVENESKLYA-NLPE--EQVVWMSHGDLvtglpegfvVDATsescpI 156
Cdd:CHL00197 272 GHQILSLALEAKTfklkfgHRGlNHPSGLNQQVEITSQNHGFAvNLESlaKNKFYITHFNL---------NDGT-----V 337
|
170 180 190
....*....|....*....|....*....|....
gi 1812584946 157 AGMSNEAKNLYGVQFHPEVRHSEHGND-LIKNFV 189
Cdd:CHL00197 338 AGISHSPKPYFSVQYHPEASPGPHDADyLFEYFI 371
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
9-183 |
2.02e-14 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 75.02 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 9 IIVLDFGSQYNqlIARRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPNSvygEGALHCD-EKIFEL--GLPIFGIC 85
Cdd:PLN02771 243 VIAYDFGIKHN--ILRRLASYGCKITVVPSTWPASEALKMKPDGVLFSNGPGD---PSAVPYAvETVKELlgKVPVFGIC 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 86 YGMQLMTQHFGGKVER-------ANH--REYGKAVLKVENESKLYANLPeeqvvwmshgdlvTGLPEGFVV---DATSES 153
Cdd:PLN02771 318 MGHQLLGQALGGKTFKmkfghhgGNHpvRNNRTGRVEISAQNHNYAVDP-------------ASLPEGVEVthvNLNDGS 384
|
170 180 190
....*....|....*....|....*....|
gi 1812584946 154 CpiAGMSNEAKNLYGVQFHPEVRHSEHGND 183
Cdd:PLN02771 385 C--AGLAFPALNVMSLQYHPEASPGPHDSD 412
|
|
| PRK09065 |
PRK09065 |
glutamine amidotransferase; Provisional |
76-174 |
9.01e-14 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181635 [Multi-domain] Cd Length: 237 Bit Score: 70.76 E-value: 9.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 76 ELGLPIFGICYGMQLMTQHFGGKVerANH---REYGKAVLKVENESK---LYANLPEEQVVWMSHGDLVTGLPEGFVVDA 149
Cdd:PRK09065 86 AAGMPLLGICYGHQLLAHALGGEV--GYNpagRESGTVTVELHPAAAddpLFAGLPAQFPAHLTHLQSVLRLPPGAVVLA 163
|
90 100
....*....|....*....|....*..
gi 1812584946 150 TS--ESCPIAGMSNEAknlYGVQFHPE 174
Cdd:PRK09065 164 RSaqDPHQAFRYGPHA---WGVQFHPE 187
|
|
| PRK07567 |
PRK07567 |
glutamine amidotransferase; Provisional |
52-174 |
2.37e-13 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181035 [Multi-domain] Cd Length: 242 Bit Score: 69.59 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 52 GIIFSGGPNSV------YGEGALHCDEKIFEL-------GLPIFGICYGMQLMTQHFGGKVERAnhreYGKAVLKVE--- 115
Cdd:PRK07567 54 GVIVGGSPFNVsdpaesKSPWQRRVEAELSGLldevvarDFPFLGACYGVGTLGHHQGGVVDRT----YGEPVGAVTvsl 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1812584946 116 -NESK---LYANLPEEQVVWMSHGDLVTGLPEGFVVDATSESCPIAgMSNEAKNLYGVQFHPE 174
Cdd:PRK07567 130 tDAGRadpLLAGLPDTFTAFVGHKEAVSALPPGAVLLATSPTCPVQ-MFRVGENVYATQFHPE 191
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
52-174 |
4.07e-13 |
|
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: 68.44 E-value: 4.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 52 GIIFSGGPN---SVYGE------GALHCDEKIFEL---------GLPIFGICYGMQLMTQHFGG--------KVERANHR 105
Cdd:pfam07722 61 GLLLTGGPNvdpHFYGEepsesgGPYDPARDAYELaliraalarGKPILGICRGFQLLNVALGGtlyqdiqeQPGFTDHR 140
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1812584946 106 EYGKAV-------LKVENESKLYANLPEEQVVWMS-HGDLVTGLPEGFVVDATSESCPIAGMS--NEAKNLYGVQFHPE 174
Cdd:pfam07722 141 EHCQVApyapshaVNVEPGSLLASLLGSEEFRVNSlHHQAIDRLAPGLRVEAVAPDGTIEAIEspNAKGFALGVQWHPE 219
|
|
| PuuD |
COG2071 |
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
52-189 |
4.07e-13 |
|
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: 68.66 E-value: 4.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 52 GIIFSGGPN---SVYGEGALHCDEKI------FEL---------GLPIFGICYGMQLMTQHFGG---------KVERANH 104
Cdd:COG2071 52 GLVLTGGADvdpALYGEEPHPELGPIdperdaFELaliraalerGKPVLGICRGMQLLNVALGGtlyqdlpdqVPGALDH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 105 REYGKAVL-----KVENESKLYANLPEEQV-VWMSHGDLVTGLPEGFVVDATSEScpiaGM-----SNEAKNLYGVQFHP 173
Cdd:COG2071 132 RQPAPRYAprhtvEIEPGSRLARILGEEEIrVNSLHHQAVKRLGPGLRVSARAPD----GVieaieSPGAPFVLGVQWHP 207
|
170
....*....|....*...
gi 1812584946 174 EVRHSEHGND--LIKNFV 189
Cdd:COG2071 208 EWLAASDPLSrrLFEAFV 225
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
52-194 |
2.07e-12 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 66.23 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 52 GIIFSGGPNSVYGEGAL-----HCDEKifelGLPIFGICYGMQLMTQHFGGKVERANHREYGKAVLKVENESKLYANLPE 126
Cdd:PRK07765 49 GVLLSPGPGTPERAGASidmvrACAAA----GTPLLGVCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPD 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 127 EQVVWMSHGDLV--TGLPEGFVVDATSESCPIAGMSNEAKNLYGVQFHPEVRHSEHGNDLIKNFVfGVCG 194
Cdd:PRK07765 125 PFTATRYHSLTIlpETLPAELEVTARTDSGVIMAVRHRELPIHGVQFHPESVLTEGGHRMLANWL-TVCG 193
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
81-189 |
4.77e-12 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 64.76 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 81 IFGICYGMQLMTQHFGGKVERANHREYGKA-VLKVENESKLYANLPEEQVVWMSHGDLVT--GLPEGFVVDATSESCPIA 157
Cdd:PRK06895 75 ILGVCLGHQTLCEFFGGELYNLNNVRHGQQrPLKVRSNSPLFDGLPEEFNIGLYHSWAVSeeNFPTPLEITAVCDENVVM 154
|
90 100 110
....*....|....*....|....*....|..
gi 1812584946 158 GMSNEAKNLYGVQFHPEVRHSEHGNDLIKNFV 189
Cdd:PRK06895 155 AMQHKTLPIYGVQFHPESYISEFGEQILRNWL 186
|
|
| PRK09522 |
PRK09522 |
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ... |
9-186 |
1.89e-11 |
|
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;
Pssm-ID: 181927 [Multi-domain] Cd Length: 531 Bit Score: 66.20 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 9 IIVLDFGSQYNQLIARRIREFG----VYSELHPHTITAEEIKAMNPKGIIFSGGPNSVYGEGALhcDEKIFEL--GLPIF 82
Cdd:PRK09522 4 ILLLDNIDSFTYNLADQLRSNGhnvvIYRNHIPAQTLIERLATMSNPVLMLSPGPGVPSEAGCM--PELLTRLrgKLPII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 83 GICYGMQLMTQHFGGKVERANHREYGKAVLKVENESKLYANLPEEQVVWMSHGDLVTGLPEGFVVDATSESCPIAgMSNE 162
Cdd:PRK09522 82 GICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSNIPAGLTINAHFNGMVMA-VRHD 160
|
170 180
....*....|....*....|....
gi 1812584946 163 AKNLYGVQFHPEVRHSEHGNDLIK 186
Cdd:PRK09522 161 ADRVCGFQFHPESILTTQGARLLE 184
|
|
| PRK05665 |
PRK05665 |
amidotransferase; Provisional |
72-177 |
7.49e-11 |
|
amidotransferase; Provisional
Pssm-ID: 168162 [Multi-domain] Cd Length: 240 Bit Score: 62.14 E-value: 7.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 72 EKIFELGLPIFGICYGMQLMTQHFGGKVERANhREYGKAVLKVENESKLYANLPE--EQVVWMSHGDLVTGLPEGFVVDA 149
Cdd:PRK05665 85 LKLYERGDKLLGVCFGHQLLALLLGGKAERAS-QGWGVGIHRYQLAAHAPWMSPAvtELTLLISHQDQVTALPEGATVIA 163
|
90 100
....*....|....*....|....*...
gi 1812584946 150 TSESCPIAGMSNEAKNLYgVQFHPEVRH 177
Cdd:PRK05665 164 SSDFCPFAAYHIGDQVLC-FQGHPEFVH 190
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
19-189 |
2.16e-10 |
|
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: 59.90 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 19 NQLIARRIREFGVYSELHPHTITAEEIKAM--NPKGIIFSGGPNSV---YGEGALHCDEKI------FEL---------G 78
Cdd:cd01745 21 NQYYVDAVRKAGGLPVLLPPVDDEEDLEQYleLLDGLLLTGGGDVDpplYGEEPHPELGPIdperdaFELallraalerG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 79 LPIFGICYGMQLMTQHFGGKVERanhreygkavlkvenesKLYANlpeeqvvwmS-HGDLVTGLPEGFVVDATSESCPIA 157
Cdd:cd01745 101 KPILGICRGMQLLNVALGGTLYQ-----------------DIRVN---------SlHHQAIKRLADGLRVEARAPDGVIE 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1812584946 158 GMSNEAKNLY-GVQFHPE--VRHSEHGNDLIKNFV 189
Cdd:cd01745 155 AIESPDRPFVlGVQWHPEwlADTDPDSLKLFEAFV 189
|
|
| PRK07053 |
PRK07053 |
glutamine amidotransferase; Provisional |
57-176 |
6.31e-10 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 235919 [Multi-domain] Cd Length: 234 Bit Score: 59.57 E-value: 6.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 57 GGPNSVYGEGA---LHCD----EKIFELGLPIFGICYGMQLMTQHFGGKVERANHREYGKAVLKVE---NESKLyANLPE 126
Cdd:PRK07053 55 GGPIGVYDDELypfLAPEiallRQRLAAGLPTLGICLGAQLIARALGARVYPGGQKEIGWAPLTLTdagRASPL-RHLGA 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1812584946 127 EQVVWMSHGDLVTgLPEGFVVDATSESCPiagmsNEA----KNLYGVQFHPEVR 176
Cdd:PRK07053 134 GTPVLHWHGDTFD-LPEGATLLASTPACR-----HQAfawgNHVLALQFHPEAR 181
|
|
| hisH |
PRK13181 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
76-188 |
9.83e-10 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 58.34 E-value: 9.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 76 ELGLPIFGICYGMQLMTQH-----------FGGKVERANHREY-----GKAVLKVENESKLYANLPEEQVVWMSHGDLVT 139
Cdd:PRK13181 70 EKKQPVLGICLGMQLLFESseegnvkglglIPGDVKRFRSEPLkvpqmGWNSVKPLKESPLFKGIEEGSYFYFVHSYYVP 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1812584946 140 GLPEGFVVdATSE-----SCPIagmsnEAKNLYGVQFHPEvRHSEHGNDLIKNF 188
Cdd:PRK13181 150 CEDPEDVL-ATTEygvpfCSAV-----AKDNIYAVQFHPE-KSGKAGLKLLKNF 196
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
78-189 |
3.64e-08 |
|
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: 53.66 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 78 GLPIFGICYGMQLMTQH------------FGGKVERANHREyGKAV-------LKVENESKLYANLPEEQVVWMSHGDLV 138
Cdd:cd01748 71 GKPFLGICLGMQLLFESseegggtkglglIPGKVVRFPASE-GLKVphmgwnqLEITKESPLFKGIPDGSYFYFVHSYYA 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1812584946 139 TGLPEGFVVDATSESCPIAGMsNEAKNLYGVQFHPEvRHSEHGNDLIKNFV 189
Cdd:cd01748 150 PPDDPDYILATTDYGGKFPAA-VEKDNIFGTQFHPE-KSGKAGLKLLKNFL 198
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
9-91 |
3.74e-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: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 9 IIVLDFGSQYN---QLIARRIREFGVYSELHPHTITAE--EIKAMNPKGIIFSGGPNSVYG----EGALHCDEKIFELGL 79
Cdd:cd03128 1 VAVLLFGGSEElelASPLDALREAGAEVDVVSPDGGPVesDVDLDDYDGLILPGGPGTPDDlawdEALLALLREAAAAGK 80
|
90
....*....|..
gi 1812584946 80 PIFGICYGMQLM 91
Cdd:cd03128 81 PVLGICLGAQLL 92
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
9-91 |
4.15e-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: 51.45 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 9 IIVLDFGSQYN---QLIARRIREFGVYSELHPHTITAE--EIKAMNPKGIIFSGGPNSVYG----EGALHCDEKIFELGL 79
Cdd:cd01653 1 VAVLLFPGFEElelASPLDALREAGAEVDVVSPDGGPVesDVDLDDYDGLILPGGPGTPDDlardEALLALLREAAAAGK 80
|
90
....*....|..
gi 1812584946 80 PIFGICYGMQLM 91
Cdd:cd01653 81 PILGICLGAQLL 92
|
|
| PRK05637 |
PRK05637 |
anthranilate synthase component II; Provisional |
38-174 |
7.47e-08 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 180178 [Multi-domain] Cd Length: 208 Bit Score: 52.92 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 38 HTITAEEIKAMNPKGIIFSGGPNSVYGEGalhCDEKIFE--LG-LPIFGICYGMQLMTQHFGGKVErANHREYGKAVLKV 114
Cdd:PRK05637 33 NTVPVEEILAANPDLICLSPGPGHPRDAG---NMMALIDrtLGqIPLLGICLGFQALLEHHGGKVE-PCGPVHGTTDNMI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 115 EN----ESKLYA-----------NLPEEQV-VWMSHGDLVTGLPEGFVVDATSESC--PIAgMSNEAKN--LYGVQFHPE 174
Cdd:PRK05637 109 LTdagvQSPVFAglatdvepdhpEIPGRKVpIARYHSLGCVVAPDGMESLGTCSSEigPVI-MAAETTDgkAIGLQFHPE 187
|
|
| NAD_synthase |
pfam02540 |
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ... |
202-439 |
8.98e-08 |
|
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: 53.15 E-value: 8.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 202 ENFIEVELEKiretVGDKKVLCALSGGVDSSVVAVLIHKAIG-DQLTCIFVDHGLLRKGEAEGVmKTFSEGFHMNVIKVD 280
Cdd:pfam02540 6 VDFLRDYVQK----AGFKGVVLGLSGGIDSSLVAYLAVKALGkENVLALIMPSSQSSEEDVQDA-LALAENLGIEYKTID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 281 ARD-------RFMDKLKGVEDPEQKRKI-------IGNEFIYVFDDEASKLQGMdfLAQGTLYTDIvesgtataqtiksh 346
Cdd:pfam02540 81 IKPivrafsqLFQDASEDFAKGNLKARIrmailyyIANKFNYLVLGTGNKSELA--VGYFTKYGDG-------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 347 hNVGglpedmqfklIEPLNTLFKDEVRVLGSELGIPDEIVWRQP----FPG----PGLGIRVlgEITEEKLEIVRESDAi 418
Cdd:pfam02540 145 -ACD----------IAPIGDLYKTQVYELARYLNVPERIIKKPPsadlWPGqtdeEELGIPY--DELDDILKLVEKKLS- 210
|
250 260
....*....|....*....|.
gi 1812584946 419 lREEIIKAGLDREIWQYFTAL 439
Cdd:pfam02540 211 -PEEIIGKGLPAEVVRRIENL 230
|
|
| IMP_synth_hisH |
TIGR01855 |
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ... |
72-189 |
1.24e-07 |
|
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: 51.94 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 72 EKIFELGLPIFGICYGMQLMTQH------------FGGKVERANHR---EYGKAVLKVENESKLYANLPEEQVVWMSHGD 136
Cdd:TIGR01855 65 ELVVRLGKPVLGICLGMQLLFERseegggvpglglIKGNVVKLEARkvpHMGWNEVHPVKESPLLNGIDEGAYFYFVHSY 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1812584946 137 LVTglPEGFVVDATSESCPIAGMSNEAKNLYGVQFHPEvRHSEHGNDLIKNFV 189
Cdd:TIGR01855 145 YAV--CEEEAVLAYADYGEKFPAAVQKGNIFGTQFHPE-KSGKTGLKLLENFL 194
|
|
| PRK06490 |
PRK06490 |
glutamine amidotransferase; Provisional |
53-178 |
2.65e-07 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 180590 [Multi-domain] Cd Length: 239 Bit Score: 51.50 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 53 IIFsGGPNSVYGEGALHCDEkIFELGLPI------FGICYGMQLMTQHFGGKVERANH--REYGKAVLKVENESKLYANL 124
Cdd:PRK06490 57 VIF-GGPMSANDPDDFIRRE-IDWISVPLkenkpfLGICLGAQMLARHLGARVAPHPDgrVEIGYYPLRPTEAGRALMHW 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1812584946 125 PEEQVVWMSHG-DlvtgLPEGFVVDATSESCPiagmsNEA----KNLYGVQFHPEVRHS 178
Cdd:PRK06490 135 PEMVYHWHREGfD----LPAGAELLATGDDFP-----NQAfrygDNAWGLQFHPEVTRA 184
|
|
| HisH |
COG0118 |
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
76-174 |
4.99e-07 |
|
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: 50.04 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 76 ELGLPIFGICYGMQLMTQH------------FGGKVERANHREY-----GKAVLKVENESKLYANLPEEQVVWMSHgdlv 138
Cdd:COG0118 71 AGGKPVLGICLGMQLLFERseengdteglglIPGEVVRFPASDLkvphmGWNTVEIAKDHPLFAGIPDGEYFYFVH---- 146
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1812584946 139 tglpeGFVVDATSEScPIAGMSN---------EAKNLYGVQFHPE 174
Cdd:COG0118 147 -----SYYVPPDDPE-DVVATTDygvpftaavERGNVFGTQFHPE 185
|
|
| LarE-like |
cd01990 |
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ... |
220-421 |
5.28e-07 |
|
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: 50.72 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 220 KVLCALSGGVDSSVVAVLIHKAIGDQLTCIFVDHGLLRKGEAEGVmKTFSEgfHMNV----IKVDardrFMDKLKGVEDP 295
Cdd:cd01990 1 KVVVAFSGGVDSSLLAKLAKEVLGDNVVAVTADSPLVPREELEEA-KRIAE--EIGIrheiIKTD----ELDDEEYVAND 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 296 EQK----RKIIGNEFIyvfddEASKLQGMDFLAQGTLYTDIVEsgtataqtikshHNVGGLP-EDMQFKLIEPLNTLFKD 370
Cdd:cd01990 74 PDRcyhcKKALYSTLK-----EIAKERGYDVVLDGTNADDLKD------------YRPGLLAaAELGIRSPLPELGLTKS 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1812584946 371 EVRVLGSELGIPdeiVWRQPfPGPGLGIRVL-GE-ITEEKLE-IVRESDAILRE 421
Cdd:cd01990 137 EIRELARELGLP---NWDKP-ASACLASRIPyGEeITPERLKrIEKAEELYLRL 186
|
|
| hisH |
PRK13141 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
78-189 |
6.17e-07 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 50.13 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 78 GLPIFGICYGMQLMTQH---FG---------GKVERANHREyGKAV-------LKVENESKLYANLPEEQVVWMSHGDLV 138
Cdd:PRK13141 72 GKPLLGICLGMQLLFESseeFGeteglgllpGRVRRFPPEE-GLKVphmgwnqLELKKESPLLKGIPDGAYVYFVHSYYA 150
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1812584946 139 TGLPEGFVVdATSE-SCPIAGMSnEAKNLYGVQFHPEvRHSEHGNDLIKNFV 189
Cdd:PRK13141 151 DPCDEEYVA-ATTDyGVEFPAAV-GKDNVFGAQFHPE-KSGDVGLKILKNFV 199
|
|
| tRNA_Me_trans |
pfam03054 |
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ... |
219-382 |
6.98e-07 |
|
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: 49.94 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 219 KKVLCALSGGVDSSVVAVLIHKAiGDQLTCIF----VDHGLLRKG----------EAEGVMKTFSEGFHmnviKVDARDR 284
Cdd:pfam03054 1 MKVVVAMSGGVDSSVAAYLLKEQ-GHNVIGVFmknwDEEQSLDEEgkccseedlaDAQRVCEQLGIPLY----VVNFEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 285 FMDKlkgVEDP---EQKR------KIIGNEFIY--VFDDEASKLQGMDFLAQGTlYTDIVESGTATA-----------QT 342
Cdd:pfam03054 76 YWED---VFEPfldEYKNgrtpnpDVLCNKEIKfgALLDYALENLGADYVATGH-YARVSLNKDGGSellraldknkdQS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1812584946 343 ikshHNVGGLPEDMQFKLIEPLNTLFKDEVRVLGSELGIP 382
Cdd:pfam03054 152 ----YFLSTLSQEQLEKLLFPLGELTKEEVRKIAKEAGLA 187
|
|
| hisH |
PRK13143 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
78-189 |
8.65e-07 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 49.48 E-value: 8.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 78 GLPIFGICYGMQLM----TQH--------FGGKVERANHRE----YGKAVLKVENESKLYANLPEEQVVWMsHgdlvtgl 141
Cdd:PRK13143 71 GKPFLGICLGMQLLfessEEGggvrglglFPGRVVRFPAGVkvphMGWNTVKVVKDCPLFEGIDGEYVYFV-H------- 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1812584946 142 peGFVVDATSESCpIAGMSN---------EAKNLYGVQFHPEvRHSEHGNDLIKNFV 189
Cdd:PRK13143 143 --SYYAYPDDEDY-VVATTDygiefpaavCNDNVFGTQFHPE-KSGETGLKILENFV 195
|
|
| nadE |
TIGR00552 |
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ... |
200-393 |
1.07e-06 |
|
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: 50.08 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 200 NMENFIEvELEK-IRETV---GDKKVLCALSGGVDSSVVAVLIHKAIGDQLTCIFVDHGLLRKGEAEGVMKTFSEGFHMN 275
Cdd:TIGR00552 1 NLIKYVE-EIEDfLRGYVqksGAKGVVLGLSGGIDSAVVAALCVEALGEQNHALLLPHSVQTPEQDVQDALALAEPLGIN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 276 VIKVDARDRFMDKLKGVEDPEQKRKII--GNE-------FIYVFddeASKlqgMDFLAQGTlytdivesGTATAQTIKSH 346
Cdd:TIGR00552 80 YKNIDIAPIAASFQAQTETGDELSDFLakGNLkarlrmaALYAI---ANK---HNLLVLGT--------GNKSELMLGYF 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1812584946 347 HNVGGLPEDmqfklIEPLNTLFKDEVRVLGSELGIPDEIVWRQP----FPG 393
Cdd:TIGR00552 146 TKYGDGGCD-----IAPIGDLFKTQVYELAKRLNVPERIIEKPPtadlFDG 191
|
|
| COG1606 |
COG1606 |
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only]; |
209-421 |
1.09e-06 |
|
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
Pssm-ID: 441214 [Multi-domain] Cd Length: 265 Bit Score: 50.11 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 209 LEKIRETVGD-KKVLCALSGGVDSSVVAVLIHKAIGDQLTCIFVDHGLLRKGEAEGVMKTFSE-GFHMNVIKVD--ARDR 284
Cdd:COG1606 5 LERLKAILKElGSVLVAFSGGVDSTLLAKVAHDVLGDRVLAVTADSPSLPERELEEAKELAKEiGIRHEVIETDelEDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 285 FmdklkgVEDPEQ-----KRKIIGnefiyVFDDEASKLqGMDFLAQGTLYTD----------IVESGtataqtIKShhnv 349
Cdd:COG1606 85 F------VANPPDrcyhcKKELFS-----KLKELAKEL-GYAVVADGTNADDlgdyrpglraAKELG------VRS---- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1812584946 350 gglPedmqfkLIEplNTLFKDEVRVLGSELGIPdeiVWRQPfPGPGLGIRV-LGE-ITEEKLEIVRESDAILRE 421
Cdd:COG1606 143 ---P------LAE--AGLTKAEIRELARELGLP---TWDKP-SSACLASRIpYGEeITPEKLRRVERAEAFLRS 201
|
|
| PRK08250 |
PRK08250 |
glutamine amidotransferase; Provisional |
81-174 |
1.56e-06 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181323 [Multi-domain] Cd Length: 235 Bit Score: 49.20 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 81 IFGICYGMQLMTQHFGGKVERANHREYGKAVLKVENESK---LYANLPEEQVVWMSHGDLvTGLPEGFVVDATSESCP-- 155
Cdd:PRK08250 87 VIGVCLGAQLIGEALGAKYEHSPEKEIGYFPITLTEAGLkdpLLSHFGSTLTVGHWHNDM-PGLTDQAKVLATSEGCPrq 165
|
90
....*....|....*....
gi 1812584946 156 IAGMSNEaknLYGVQFHPE 174
Cdd:PRK08250 166 IVQYSNL---VYGFQCHME 181
|
|
| hisH |
PRK13170 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
80-189 |
1.70e-06 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183877 [Multi-domain] Cd Length: 196 Bit Score: 48.70 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 80 PIFGICYGMQLMTQH------------FGGKVERanhreygkavLKVENESklyanLPE---EQVVWMSHGDLVTGLPEG 144
Cdd:PRK13170 72 PVLGICLGMQLLGERseesggvdclgiIDGPVKK----------MTDFGLP-----LPHmgwNQVTPQAGHPLFQGIEDG 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1812584946 145 ----FV------VD----ATSE-----SCPIAgmsneAKNLYGVQFHPEvRHSEHGNDLIKNFV 189
Cdd:PRK13170 137 syfyFVhsyampVNeytiAQCNygepfSAAIQ-----KDNFFGVQFHPE-RSGAAGAQLLKNFL 194
|
|
| PRK13980 |
PRK13980 |
NAD synthetase; Provisional |
203-421 |
2.91e-06 |
|
NAD synthetase; Provisional
Pssm-ID: 184435 [Multi-domain] Cd Length: 265 Bit Score: 48.67 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 203 NFIEVELEKiretVGDKKVLCALSGGVDSSVVAVLIHKAIG-DQLtcifvdHGLLRKGE---------AEGVMKTFseGF 272
Cdd:PRK13980 19 DFIREEVEK----AGAKGVVLGLSGGIDSAVVAYLAVKALGkENV------LALLMPSSvsppedledAELVAEDL--GI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 273 HMNVIKVDA-RDRFMDKLkgvedPEQKRKIIGN-------EFIYvfdDEASKLQGM---------DFLAQGTLYTDiveS 335
Cdd:PRK13980 87 EYKVIEITPiVDAFFSAI-----PDADRLRVGNimartrmVLLY---DYANRENRLvlgtgnkseLLLGYFTKYGD---G 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 336 GTAtaqtikshhnvgglpedmqfklIEPLNTLFKDEVRVLGSELGIPDEIVWRQPFPG--PG------LGI--RVLGEIT 405
Cdd:PRK13980 156 AVD----------------------LNPIGDLYKTQVRELARHLGVPEDIIEKPPSADlwEGqtdegeLGFsyETIDEIL 213
|
250
....*....|....*.
gi 1812584946 406 EEKLEIVRESDAILRE 421
Cdd:PRK13980 214 YLLFDKKMSREEILEE 229
|
|
| NAD_synthase |
cd00553 |
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ... |
210-396 |
5.94e-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: 47.55 E-value: 5.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 210 EKIRETvGDKKVLCALSGGVDSSVVAVLIHKAIG-DQLTCIFVDHGLLRKGEAEGVmKTFSEGFHMNVIKVD---ARDRF 285
Cdd:cd00553 16 DYLRKS-GAKGFVLGLSGGIDSAVVAALAVRALGaENVLALIMPSRYSSKETRDDA-KALAENLGIEYRTIDidpIVDAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 286 MDKLKGVEDPEQKRKIIGNE-------FIYVFddeASKLQGM---------DFLAQGTLYTDivesgtataqtikshHNV 349
Cdd:cd00553 94 LKALEHAGGSEAEDLALGNIqarlrmvLLYAL---ANLLGGLvlgtgnkseLLLGYFTKYGD---------------GAA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1812584946 350 GglpedmqfklIEPLNTLFKDEVRVLGSELGIPDEIVwRQPfPGPGL 396
Cdd:cd00553 156 D----------INPIGDLYKTQVRELARYLGVPEEII-EKP-PSAEL 190
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
212-439 |
1.51e-05 |
|
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: 47.53 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 212 IRETV---GDKKVLCALSGGVDSSVVAVLIHKAIG-DQLTCIF----------VDHgllrkgeAEGVMKTFseGFHMNVI 277
Cdd:COG0171 277 LRDYVrknGFKGVVLGLSGGIDSALVAALAVDALGpENVLGVTmpsrytsdesLED-------AEELAENL--GIEYEEI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 278 KV-DARDRFMDKLKGVEDPEQKRKIIGN-------EFIYvfdDEASKLQGM---------DFLAQGTLYTDivesgtata 340
Cdd:COG0171 348 DItPAVEAFLEALPHAFGGELDDVAEENlqarirmVILM---ALANKFGGLvlgtgnkseLAVGYFTKYGD--------- 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 341 qtikshHNVGglpedmqfklIEPLNTLFKDEVRVLGSELG-----IPDEIVWRQpfPGPGLgirVLGEITEEKLEIVRES 415
Cdd:COG0171 416 ------GAGD----------LAPIADLYKTQVYALARWLNrngevIPEDIIDKP--PSAEL---RPGQTDEDELGPYEVL 474
|
250 260 270
....*....|....*....|....*....|...
gi 1812584946 416 DAILR---------EEIIKAGLDREIWQYFTAL 439
Cdd:COG0171 475 DAILYayveeglspEEIAAAGYDREWVERVLRL 507
|
|
| hisH |
PRK14004 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
72-189 |
2.34e-05 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 172505 [Multi-domain] Cd Length: 210 Bit Score: 45.66 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 72 EKIFELGLPIFGICYGMQLM-------------------------TQHFGGKVERANHREYGKAVLKVENESKLYANLPE 126
Cdd:PRK14004 66 DKHVESGKPLFGICIGFQILfesseetnqgtkkeqieglgyikgkIKKFEGKDFKVPHIGWNRLQIRRKDKSKLLKGIGD 145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1812584946 127 EQVVWMSH--------GDLVTGLpegfvVDATSESCPIAgmsNEAKNLYGVQFHPEVRHSeHGNDLIKNFV 189
Cdd:PRK14004 146 QSFFYFIHsyrptgaeGNAITGL-----CDYYQEKFPAV---VEKENIFGTQFHPEKSHT-HGLKLLENFI 207
|
|
| mnmA |
PRK00143 |
tRNA-specific 2-thiouridylase MnmA; Reviewed |
219-241 |
3.71e-05 |
|
tRNA-specific 2-thiouridylase MnmA; Reviewed
Pssm-ID: 234664 [Multi-domain] Cd Length: 346 Bit Score: 45.83 E-value: 3.71e-05
|
| MnmA |
COG0482 |
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ... |
219-241 |
5.25e-05 |
|
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: 45.43 E-value: 5.25e-05
|
| puuD |
PRK11366 |
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional |
37-180 |
8.68e-05 |
|
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
Pssm-ID: 183101 [Multi-domain] Cd Length: 254 Bit Score: 44.12 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 37 PHTITAEEI-KAMNPK--GIIFSGGPNSV----YGEGALHCD-------------EKIFELGLPIFGICYGMQLMTQHFG 96
Cdd:PRK11366 46 PHALAEPSLlEQLLPKldGIYLPGSPSNVqphlYGENGDEPDadpgrdllsmaliNAALERRIPIFAICRGLQELVVATG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 97 GKVERA--------NHRE---------YGKA-VLKVENESKLYANLPEEQVVWMS--HGDLVTGLPEGFVVDATSESCPI 156
Cdd:PRK11366 126 GSLHRKlceqpellEHREdpelpveqqYAPShEVQVEEGGLLSALLPECSNFWVNslHGQGAKVVSPRLRVEARSPDGLV 205
|
170 180
....*....|....*....|....*
gi 1812584946 157 AGMS-NEAKNLYGVQFHPEVRHSEH 180
Cdd:PRK11366 206 EAVSvINHPFALGVQWHPEWNSSEY 230
|
|
| AANH-like |
cd01986 |
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ... |
224-289 |
8.82e-05 |
|
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: 40.90 E-value: 8.82e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1812584946 224 ALSGGVDSSVVAVLIHKAIGD-QLTCIFVDHGLLRKGEAEGVMKtfsegfhmnvikvDARDRFMDKL 289
Cdd:cd01986 4 GYSGGKDSSVALHLASRLGRKaEVAVVHIDHGIGFKEEAESVAS-------------IARRSILKKL 57
|
|
| TilS |
COG0037 |
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ... |
211-255 |
8.88e-05 |
|
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439807 [Multi-domain] Cd Length: 235 Bit Score: 44.05 E-value: 8.88e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1812584946 211 KIRETVGD-------KKVLCALSGGVDSSVVAVLIHK---AIGDQLTCIFVDHGL 255
Cdd:COG0037 1 KVRKAIRDyrllepgDRILVAVSGGKDSLALLHLLAKlrrRLGFELVAVHVDHGL 55
|
|
| TilS_N |
cd01992 |
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ... |
220-262 |
2.13e-04 |
|
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine synthase (EC 6.3.4.19), also called tRNA(Ile)-2-lysyl-cytidine synthase or tRNA(Ile)-lysidine synthetase, catalyzes the ligation of lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. This subfamily belongs to the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This domain has a strongly conserved motif SGGXD at the N-terminus.
Pssm-ID: 467496 [Multi-domain] Cd Length: 185 Bit Score: 42.20 E-value: 2.13e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1812584946 220 KVLCALSGGVDSSVVAVLIHKAI---GDQLTCIFVDHGlLRKGEAE 262
Cdd:cd01992 1 KILVAVSGGPDSMALLHLLKELRpklGLKLVAVHVDHG-LREESAE 45
|
|
| MnmA_TRMU-like |
cd01998 |
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
220-250 |
3.56e-04 |
|
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: 42.88 E-value: 3.56e-04
10 20 30
....*....|....*....|....*....|.
gi 1812584946 220 KVLCALSGGVDSSVVAVLIHKAiGDQLTCIF 250
Cdd:cd01998 1 KVAVAMSGGVDSSVAAALLKEQ-GYDVIGVF 30
|
|
| trmU |
TIGR00420 |
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ... |
219-382 |
1.77e-03 |
|
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase (trmU, asuE, or mnmA) is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine (mnm5s2U34) present in the wobble position of some tRNAs. This enzyme appears not to occur in the Archaea. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 273069 [Multi-domain] Cd Length: 352 Bit Score: 40.45 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 219 KKVLCALSGGVDSSVVAVLIHKAiGDQLTCIFVDHgLLRKGEAEGVMKTFSEGF--------HMNV--IKVDARDRFMDK 288
Cdd:TIGR00420 1 KKVIVGLSGGVDSSVSAYLLKQQ-GYEVVGVFMKN-WEEDDKNDGHGCTSAEDLrdaqaiceKLGIplEKVNFQKEYWNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 289 lkgVEDP---EQKR------KIIGNEFIY--VFDDEASKLQGMDFLAQGTlYTDI--VESGTATAQTIKSH-------HN 348
Cdd:TIGR00420 79 ---VFEPfiqEYKEgrtpnpDILCNKFIKfgAFLEYAAELLGNDKIATGH-YARIaeIEGKSLLLRALDKNkdqsyflYH 154
|
170 180 190
....*....|....*....|....*....|....
gi 1812584946 349 VGglPEDMQfKLIEPLNTLFKDEVRVLGSELGIP 382
Cdd:TIGR00420 155 LS--HEQLA-KLLFPLGELLKPEVRQIAKNAGLP 185
|
|
| hisH |
PRK13152 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
68-189 |
2.35e-03 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 171876 [Multi-domain] Cd Length: 201 Bit Score: 39.44 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 68 LHCDEKIFELGL----PIFGICYGMQLMTQ---HFG---------GKVERANHR------EYGKAVLKVENESKLYANLP 125
Cdd:PRK13152 59 LGFIEALKEQVLvqkkPILGICLGMQLFLErgyEGGvceglgfieGEVVKFEEDlnlkipHMGWNELEILKQSPLYQGIP 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1812584946 126 EEQVVWMSHGDLVTGLPEgfVVDATSESCPIAGMSNEAKNLYGVQFHPEvRHSEHGNDLIKNFV 189
Cdd:PRK13152 139 EKSDFYFVHSFYVKCKDE--FVSAKAQYGHKFVASLQKDNIFATQFHPE-KSQNLGLKLLENFA 199
|
|
| GATase1_Glutamyl_Hydrolase |
cd01747 |
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ... |
52-174 |
3.95e-03 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153218 [Multi-domain] Cd Length: 273 Bit Score: 39.23 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 52 GIIFSGGPNSVYGEGALHCDEKIFELGL---------PIFGICYGMQLMTQHFGGKVeraNHREYGKAV-----LKVEN- 116
Cdd:cd01747 57 GILFPGGAVDIDTSGYARTAKIIYNLALerndagdyfPVWGTCLGFELLTYLTSGET---LLLEATEATnsalpLNFTEd 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812584946 117 --ESKLYANLP--------EEQVVWMSHGDLVTglPEGFVV-DATSESCPIAGMSN-----------EAKN--LYGVQFH 172
Cdd:cd01747 134 alQSRLFKRFPpdllkslaTEPLTMNNHRYGIS--PENFTEnGLLSDFFNVLTTNDdwngvefistvEAYKypIYGVQWH 211
|
..
gi 1812584946 173 PE 174
Cdd:cd01747 212 PE 213
|
|
| ASS |
cd01999 |
argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle ... |
219-285 |
9.61e-03 |
|
argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle enzyme that catalyzes the penultimate step in arginine biosynthesis: the ATP-dependent ligation of citrulline to aspartate to form argininosuccinate, AMP and pyrophosphate. In humans, a defect in the ASS gene causes citrullinemia, a genetic disease characterized by severe vomiting spells and mental retardation. ASS is a homotetrameric enzyme of about 400 amino-acid residues. An arginine residue seems to be important for the enzyme's catalytic mechanism. The sequences of ASS from various prokaryotes, archaeabacteria and eukaryotes show significant similarity.
Pssm-ID: 467503 Cd Length: 386 Bit Score: 38.29 E-value: 9.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1812584946 219 KKVLCALSGGVDSSVVAVLIHKAIGDQLTCIFVDHGllRKGEAEGVMKTFSEGFHMNVIKVDARDRF 285
Cdd:cd01999 1 KKVVLAYSGGLDTSVILKWLKEEYGYEVIAFTADLG--QGDEEEEIEEKALKLGAVKVYVVDLREEF 65
|
|
| |
