|
Name |
Accession |
Description |
Interval |
E-value |
| guaA |
PRK00074 |
GMP synthase; Reviewed |
6-515 |
0e+00 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 1078.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 6 KQHDTIIVLDFGSQYNQLIARRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPNSVYGEGALHCDEKIFDLGLPIFG 85
Cdd:PRK00074 1 IHHDKILILDFGSQYTQLIARRVRELGVYSEIVPYDISAEEIRAFNPKGIILSGGPASVYEEGAPRADPEIFELGVPVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 86 ICYGMQLMTQQFGGTVERANHREYGKAVLKVENESKLYANLPEEQVVWMSHGDLVTGLPEGFVVDATSESCPIAGMSNEA 165
Cdd:PRK00074 81 ICYGMQLMAHQLGGKVERAGKREYGRAELEVDNDSPLFKGLPEEQDVWMSHGDKVTELPEGFKVIASTENCPIAAIANEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 166 KNLYGVQFHPEVRHSEHGNDLIKNFVFGVCGCSEGWNMENFIEVELEKIRETVGDKKVLCALSGGVDSSVVAVLIHKAIG 245
Cdd:PRK00074 161 RKFYGVQFHPEVTHTPQGKKLLENFVFDICGCKGDWTMENFIEEAIEEIREQVGDKKVILGLSGGVDSSVAAVLLHKAIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 246 DQLTCIFVDHGLLRKGEAEGVMKTFSEGFHMNVIKVDAKERFMNKLKGVEDPEQKRKIIGNEFIYVFDDEASKLEGMDFL 325
Cdd:PRK00074 241 DQLTCVFVDHGLLRKNEAEQVMEMFREHFGLNLIHVDASDRFLSALAGVTDPEEKRKIIGREFIEVFEEEAKKLGGVKFL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 326 AQGTLYTDIVESGTAT-AQTIKSHHNVGGLPEDMQFKLIEPLNTLFKDEVRVLGSELGIPDEIVWRQPFPGPGLGIRVLG 404
Cdd:PRK00074 321 AQGTLYPDVIESGGTKkAATIKSHHNVGGLPEDMKLKLVEPLRELFKDEVRKLGLELGLPEEIVYRHPFPGPGLAIRILG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 405 EITEEKLEIVRESDAILREEIIKAGLDREIWQYFTALPGMRSVGVMGDERTYDYTVGIRAVTSIDGMTADWARIPWDVLE 484
Cdd:PRK00074 401 EVTKEKLDILREADAIFIEELRKAGLYDKIWQAFAVLLPVKSVGVMGDGRTYDYVVALRAVTSIDGMTADWARLPYDFLE 480
|
490 500 510
....*....|....*....|....*....|.
gi 1259761698 485 KISVRIVNEVKHVNRIVYDVTSKPPATIEWE 515
Cdd:PRK00074 481 KISNRIINEVKGVNRVVYDITSKPPATIEWE 511
|
|
| GuaA2 |
COG0519 |
GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, ... |
6-515 |
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: 965.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 6 KQHDTIIVLDFGSQYNQLIARRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPNSVYGEGALHCDEKIFDLGLPIFG 85
Cdd:COG0519 1 MDKEIIIVLDFGGQYQQLIARRRREEGVYSEIIPPDTAAEEIKAKGPPGIILSGGPSSVYEEGAPPDDPELFELGGPILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 86 ICYGMQLMTQQFGGTVERANHREYGKAVLKVENESKLYANLPEEQVVWMSHGDLVTGLPEGFVVDATSESCPIAGMSNEA 165
Cdd:COG0519 81 ICYGGQLMLHLLGGGVVRAERREYGGALLLVDDESDLFAGGPEELQVWMSHGDRVTELPPGFEVIASTENCPVAAIANEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 166 KNLYGVQFHPEVRHSEHGNDLIKNFVFGVCGCSEGWNMENFIEVELEKIRETVGDKKVLCALSGGVDSSVVAVLIHKAIG 245
Cdd:COG0519 161 RKLYGVQFHPEVVHTEQGKEILKNFLFDICGCKGDWTMENFIEEAIEEIREQVGDGKVICALSGGVDSSVAAALLHKAIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 246 DQLTCIFVDHGLLRKGEAEGVMKTFSEGFHMNVIKVDAKERFMNKLKGVEDPEQKRKIIGNEFIYVFDDEASKLEGMDFL 325
Cdd:COG0519 241 DQLTCVFVDHGLLRKGEAEQVEETFKEHFGLNLIYVDASERFLSALKGVTDPEEKRKIIGEEFIEVFEEEAKKLGGAKFL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 326 AQGTLYTDIVESGTAT--AQTIKSHHNVGGLPEDMQFKLIEPLNTLFKDEVRVLGSELGIPDEIVWRQPFPGPGLGIRVL 403
Cdd:COG0519 321 AQGTLYPDVIESGSVKgpAATIKSHHNVGGLPEDMKFKLVEPLRELFKDEVRALGRELGLPEEIVYRHPFPGPGLAIRIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 404 GEITEEKLEIVRESDAILREEIIKAGLDREIWQYFTALPGMRSVGVMGDERTYDYTVGIRAVTSIDGMTADWARIPWDVL 483
Cdd:COG0519 401 GEVTKEKLEILREADAIFIEELRKAGLYDKVWQAFAVLLPVKSVGVMGDERTYEYVVALRAVTSVDGMTADWARLPYEVL 480
|
490 500 510
....*....|....*....|....*....|..
gi 1259761698 484 EKISVRIVNEVKHVNRIVYDVTSKPPATIEWE 515
Cdd:COG0519 481 ERISNRIINEVKGVNRVVYDITSKPPATIEWE 512
|
|
| PLN02347 |
PLN02347 |
GMP synthetase |
5-515 |
0e+00 |
|
GMP synthetase
Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 724.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 5 KKQHDTIIVLDFGSQYNQLIARRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPNSVYGEGALHCDEKIFDL----G 80
Cdd:PLN02347 7 KSYLDVVLILDYGSQYTHLITRRVRELGVYSLLLSGTASLDRIASLNPRVVILSGGPHSVHVEGAPTVPEGFFDYcrerG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 81 LPIFGICYGMQLMTQQFGGTVERANHREYGKAVLKVENESKLYANLPEE--QVVWMSHGDLVTGLPEGFVVDATSESCPI 158
Cdd:PLN02347 87 VPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCGSQLFGDLPSGetQTVWMSHGDEAVKLPEGFEVVAKSVQGAV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 159 AGMSNEAKNLYGVQFHPEVRHSEHGNDLIKNFVFGVCGCSEGWNMENFIEVELEKIRETVG-DKKVLCALSGGVDSSVVA 237
Cdd:PLN02347 167 VAIENRERRIYGLQYHPEVTHSPKGMETLRHFLFDVCGVTADWKMQDVLEEQIELIKATVGpDEHVICALSGGVDSTVAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 238 VLIHKAIGDQLTCIFVDHGLLRKGEAEGVMKTFSEGFHMNVIKVDAKERFMNKLKGVEDPEQKRKIIGNEFIYVFDDEAS 317
Cdd:PLN02347 247 TLVHKAIGDRLHCVFVDNGLLRYKEQERVMETFKRDLHLPVTCVDASERFLSKLKGVTDPEKKRKIIGAEFIEVFDEFAH 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 318 KLEGM-----DFLAQGTLYTDIVES------GTATAQTIKSHHNVGGLPEDMQFKLIEPLNTLFKDEVRVLGSELGIPDE 386
Cdd:PLN02347 327 KLEQKlgkkpAFLVQGTLYPDVIEScpppgsGRTHSHTIKSHHNVGGLPKDMKLKLIEPLKLLFKDEVRKLGRLLGVPEA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 387 IVWRQPFPGPGLGIRVLGEITEE-KLEIVRESDAILREEIIKAGLDREIWQYFTALPGMRSVGVMGDERTYDYTVGIRAV 465
Cdd:PLN02347 407 FLKRHPFPGPGLAVRVLGDVTEGnALDILRQVDEIFINSIKDAGLYDEIWQAFAVFLPVKSVGVQGDQRTHSHVVALRAV 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1259761698 466 TSIDGMTADWARIPWDVLEKISVRIVNEVKHVNRIVYDVTSKPPATIEWE 515
Cdd:PLN02347 487 TSEDGMTADWYHFEHKFLDDVSRKICNEVRGVNRVVYDITSKPPSTIEWE 536
|
|
| guaA_Cterm |
TIGR00884 |
GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; This protein of purine ... |
205-515 |
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: 573.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 205 NFIEVELEKIRETVGDKKVLCALSGGVDSSVVAVLIHKAIGDQLTCIFVDHGLLRKGEAEGVMKTFSEGFHMNVIKVDAK 284
Cdd:TIGR00884 1 NFIEEAVEEIREQVGDAKVIIALSGGVDSSVAAVLAHRAIGDRLTCVFVDHGLLRKGEAEQVVKTFGDRLGLNLVYVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 285 ERFMNKLKGVEDPEQKRKIIGNEFIYVFDDEASKLEGMDFLAQGTLYTDIVESGTATAQTIKSHHNVGGLPEDMQFKLIE 364
Cdd:TIGR00884 81 ERFLSALKGVTDPEEKRKIIGRVFIEVFEREAKKIGDAEYLAQGTIYPDVIESAAGTAHVIKSHHNVGGLPEDMKLKLVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 365 PLNTLFKDEVRVLGSELGIPDEIVWRQPFPGPGLGIRVLGEITEEKLEIVRESDAILREEIIKAGLDREIWQYFTALPGM 444
Cdd:TIGR00884 161 PLRELFKDEVRKLGKELGLPEEIVWRHPFPGPGLAVRVLGEVTKEKLEILRRADAIVIEELKKAGLYDKVWQAFAVLLPV 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1259761698 445 RSVGVMGDERTYDYTVGIRAVTSIDGMTADWARIPWDVLEKISVRIVNEVKHVNRIVYDVTSKPPATIEWE 515
Cdd:TIGR00884 241 KSVGVMGDGRTYGYVIALRAVESIDGMTADWARLPYDFLERISNRITNEVPGVNRVVYDITSKPPATIEWE 311
|
|
| GMP_synthase_C |
cd01997 |
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ... |
214-515 |
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: 511.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 214 IRETVGDKKVLCALSGGVDSSVVAVLIHKAIGD-QLTCIFVDHGLLRKGEAEGVMKTFSEGFHMNVIKVDAKERFMNKLK 292
Cdd:cd01997 1 IKRTVGDKKVLCLVSGGVDSTVCAALLHKALGDeRVIAVHIDNGLMRKNESEQVEEALKKLGVINLAKVDASKRFLKKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 293 GVEDPEQKRKIIGNEFIYVFDDEASKLE---GMDFLAQGTLYTDIVESG----TATAQTIKSHHNVGGLPED-MQFKLIE 364
Cdd:cd01997 81 GVTDPEEKRKIIGDTFIEVFDEVAKELNldpDDVYLAQGTLYPDLIESAsslaSSKADTIKTHHNVGGLPRElLKGKLVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 365 PLNTLFKDEVRVLGSELGIPDEIVWRQPFPGPGLGIRVLGEITEEKLEIVRESDAILREEIIKAGLDREIWQYFTALPGM 444
Cdd:cd01997 161 PLRDLFKDEVRELGRELGLPEELVWRHPFPGPGLAIRVLGEVTPEKLEILREADAIVEEELREAGLYDKISQAFAVLLPI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1259761698 445 RSVGVMGDERTYDYTVGIRAVTSIDGMTADWARIPWDVLEKISVRIVNEVKHVNRIVYDVTSKPPATIEWE 515
Cdd:cd01997 241 KSVGVQGDGRTYGYVVALRAVETEDFMTAEWARPPYEVLDKISNRITNEVPGVNRVVYDITSKPPATIEWE 311
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
11-197 |
7.38e-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: 336.98 E-value: 7.38e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 11 IIVLDFGSQYNQLIARRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPNSVYGEGALHCDEKIFDLGLPIFGICYGM 90
Cdd:TIGR00888 1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGPSSVYAENAPRADEKIFELGVPVLGICYGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 91 QLMTQQFGGTVERANHREYGKAVLKVENESKLYANLPEEQVVWMSHGDLVTGLPEGFVVDATSESCPIAGMSNEAKNLYG 170
Cdd:TIGR00888 81 QLMAKQLGGEVGRAEKREYGKAELEILDEDDLFRGLPDESTVWMSHGDKVKELPEGFKVLATSDNCPVAAMAHEEKPIYG 160
|
170 180
....*....|....*....|....*..
gi 1259761698 171 VQFHPEVRHSEHGNDLIKNFVFGVCGC 197
Cdd:TIGR00888 161 VQFHPEVTHTEYGNELLENFVYDVCGC 187
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
11-191 |
2.26e-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: 325.26 E-value: 2.26e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 11 IIVLDFGSQYNQLIARRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPNSVYGEGALHCDEKIFDLGLPIFGICYGM 90
Cdd:cd01742 1 ILILDFGSQYTHLIARRVRELGVYSEILPNTTPLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGICYGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 91 QLMTQQFGGTVERANHREYGKAVLKVENESKLYANLPEEQVVWMSHGDLVTGLPEGFVVDATSESCPIAGMSNEAKNLYG 170
Cdd:cd01742 81 QLIAKALGGKVERGDKREYGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVVKLPEGFKVIASSDNCPVAAIANEEKKIYG 160
|
170 180
....*....|....*....|.
gi 1259761698 171 VQFHPEVRHSEHGNDLIKNFV 191
Cdd:cd01742 161 VQFHPEVTHTEKGKEILKNFL 181
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
11-194 |
1.99e-72 |
|
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: 229.45 E-value: 1.99e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 11 IIVLD---FGSQYNQLIARRIRE-------FGVY-SELHPHTITAEeikamNPKGIIFSGGPNSVYGE-----GALHCDE 74
Cdd:COG0518 2 ILILDhdpFGGQYPGLIARRLREagieldvLRVYaGEILPYDPDLE-----DPDGLILSGGPMSVYDEdpwleDEPALIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 75 KIFDLGLPIFGICYGMQLMTQQFGGTVERANHREYGKAVLKVENESKLYANLPEEQVVWMSHGDLVTGLPEGFVVDATSE 154
Cdd:COG0518 77 EAFELGKPVLGICYGAQLLAHALGGKVEPGPGREIGWAPVELTEADPLFAGLPDEFTVWMSHGDTVTELPEGAEVLASSD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 155 SCPIAGMSNEaKNLYGVQFHPEVRHS------------------------------EHGNDLIKNFVFGV 194
Cdd:COG0518 157 NCPNQAFRYG-RRVYGVQFHPEVTHTmmeawleeradelaaeellaeaslhdpelrEAGRRLLRNFLREI 225
|
|
| GMP_synt_C |
pfam00958 |
GMP synthase C terminal domain; GMP synthetase is a glutamine amidotransferase from the de ... |
423-514 |
9.45e-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: 209.96 E-value: 9.45e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 423 EEIIKAGLDREIWQYFTALPGMRSVGVMGDERTYDYTVGIRAVTSIDGMTADWARIPWDVLEKISVRIVNEVKHVNRIVY 502
Cdd:pfam00958 1 EEIKKAGLYRKIWQAFAVLLPVKSVGVMGDERTYEYVVALRAVTSTDGMTADWARLPYEVLEKISNRIVNEVPGVNRVVY 80
|
90
....*....|..
gi 1259761698 503 DVTSKPPATIEW 514
Cdd:pfam00958 81 DITSKPPATIEW 92
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
11-196 |
3.00e-63 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 204.32 E-value: 3.00e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 11 IIVLDFGSQYNQLIARRIREFGVYSELHPHTITAEEIKAMNpKGIIFSGGPNSvygEGALHCDEKIFDLGLPIFGICYGM 90
Cdd:PRK00758 2 IVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTTPVEEIKAFE-DGLILSGGPDI---ERAGNCPEYLKELDVPILGICLGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 91 QLMTQQFGGTVERANHREYGKAVLKVENESKLYANLPEEQVVWMSHGDLVTGLPEGFVVDATSESCPIAGMSNEAKNLYG 170
Cdd:PRK00758 78 QLIAKAFGGEVGRGEYGEYALVEVEILDEDDILKGLPPEIRVWASHADEVKELPDGFEILARSDICEVEAMKHKEKPIYG 157
|
170 180
....*....|....*....|....*.
gi 1259761698 171 VQFHPEVRHSEHGNDLIKNFvFGVCG 196
Cdd:PRK00758 158 VQFHPEVAHTEYGEEIFKNF-LEICG 182
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
12-194 |
3.50e-58 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 191.30 E-value: 3.50e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 12 IVLDFGSQYNQLIARRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPNSVY-GEGALHCDEKIFDLGLPIFGICYGM 90
Cdd:pfam00117 1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGaAGGAIEAIREARELKIPILGICLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 91 QLMTQQFGGTVERANHREYGKAVLKVEN-ESKLYANLPEEQVVWMSHGDLVTG--LPEGFVVDATSE-SCPIAGMSNEAK 166
Cdd:pfam00117 81 QLLALAFGGKVVKAKKFGHHGKNSPVGDdGCGLFYGLPNVFIVRRYHSYAVDPdtLPDGLEVTATSEnDGTIMGIRHKKL 160
|
170 180
....*....|....*....|....*...
gi 1259761698 167 NLYGVQFHPEVRHSEHGNDLIKNFVFGV 194
Cdd:pfam00117 161 PIFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
20-191 |
1.15e-28 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 112.15 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 20 YNqlIARRIREFG----VYSelhPHTITAEEIKAMNPKGIIFSGGPNSvyGEGALHCDEKIFDLG--LPIFGICYGMQLM 93
Cdd:PRK05670 13 YN--LVQYLGELGaevvVYR---NDEITLEEIEALNPDAIVLSPGPGT--PAEAGISLELIREFAgkVPILGVCLGHQAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 94 TQQFGGTVERANHREYGKAVLKVENESKLYANLPEEQVVWMSHgDLV---TGLPEGFVVDATSESCPIAGMSNEAKNLYG 170
Cdd:PRK05670 86 GEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYH-SLVvdrESLPDCLEVTAWTDDGEIMGVRHKELPIYG 164
|
170 180
....*....|....*....|.
gi 1259761698 171 VQFHPEVRHSEHGNDLIKNFV 191
Cdd:PRK05670 165 VQFHPESILTEHGHKLLENFL 185
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
20-191 |
8.25e-27 |
|
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: 107.05 E-value: 8.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 20 YNqlIARRIREFGVYSELHPHT-ITAEEIKAMNPKGIIFSGGPnsvyG--EGALHCDEKI--FDLGLPIFGICYGMQLMT 94
Cdd:COG0512 12 YN--LVQYLGELGAEVVVVRNDeITLEEIEALAPDGIVLSPGP----GtpEEAGISLEVIraFAGKIPILGVCLGHQAIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 95 QQFGGTVERAN---HreyGKAVLKVENESKLYANLPEEQVVWMSH---GDLVTgLPEGFVVDATSESCPIAGMSNEAKNL 168
Cdd:COG0512 86 EAFGGKVVRAPepmH---GKTSPITHDGSGLFAGLPNPFTATRYHslvVDRET-LPDELEVTAWTEDGEIMGIRHRELPI 161
|
170 180
....*....|....*....|....*.
gi 1259761698 169 YGVQFHPEvrhS---EHGNDLIKNFV 191
Cdd:COG0512 162 EGVQFHPE---SiltEHGHQLLANFL 184
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
54-191 |
3.96e-24 |
|
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: 99.24 E-value: 3.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 54 GIIFSGGPNSVYGEGA--LHcDEK-----IFDLGLPIFGICYGMQLMTQQFGGTVERANH-REYGKAVLKVENESK---L 122
Cdd:cd01741 49 GLVILGGPMSVDEDDYpwLK-KLKelirqALAAGKPVLGICLGHQLLARALGGKVGRNPKgWEIGWFPVTLTEAGKadpL 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1259761698 123 YANLPEEQVVWMSHGDLVTGLPEGFVVDATSESCPIAGMSNEaKNLYGVQFHPEvrhsehgNDLIKNFV 191
Cdd:cd01741 128 FAGLPDEFPVFHWHGDTVVELPPGAVLLASSEACPNQAFRYG-DRALGLQFHPE-------ERLLRNFL 188
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
20-191 |
1.57e-23 |
|
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: 97.61 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 20 YNqlIARRIREFGVYSE-LHPHTITAEEIKAMNPKGIIFSGGPNSVyGEGALHCD-EKIFDLGLPIFGICYGMQLMTQQF 97
Cdd:cd01743 12 YN--LVQYLRELGAEVVvVRNDEITLEELELLNPDAIVISPGPGHP-EDAGISLEiIRALAGKVPILGVCLGHQAIAEAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 98 GGTVERANHREYGKAVLKVENESKLYANLPEE-QVV----WmsHGDLVTgLPEGFVVDATSESCPIAGMSNEAKNLYGVQ 172
Cdd:cd01743 89 GGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPfTVGryhsL--VVDPDP-LPDLLEVTASTEDGVIMALRHRDLPIYGVQ 165
|
170
....*....|....*....
gi 1259761698 173 FHPEVRHSEHGNDLIKNFV 191
Cdd:cd01743 166 FHPESILTEYGLRLLENFL 184
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
42-191 |
1.04e-20 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 89.59 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 42 ITAEEIKAMNPKGIIFSGGPNSVYGEGALHCDEKIFDLGLPIFGICYGMQLMTQQFGGTVERANHREYGKAVLKVENESK 121
Cdd:PRK08007 34 LTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEG 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1259761698 122 LYANLPEEQVVWMSHGDLV--TGLPEGFVVDATSESCPIAGMSNEAKNLYGVQFHPEVRHSEHGNDLIKNFV 191
Cdd:PRK08007 114 VFRGLANPLTVTRYHSLVVepDSLPACFEVTAWSETREIMGIRHRQWDLEGVQFHPESILSEQGHQLLANFL 185
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
37-190 |
1.50e-20 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 94.78 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 37 LHPHTITAEEIKAMNPKGIIFSGGPNSvyGEGALHCDEKI--FDLGLPIFGICYGMQLMTQQFGGTVERANHREYGKAVL 114
Cdd:PRK14607 30 VRNDEITIEEIEALNPSHIVISPGPGR--PEEAGISVEVIrhFSGKVPILGVCLGHQAIGYAFGGKIVHAKRILHGKTSP 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1259761698 115 KVENESKLYANLPEEQVVWMSHGDLV--TGLPEGFVVDATSESCPIAGMSNEAKNLYGVQFHPEVRHSEHGNDLIKNF 190
Cdd:PRK14607 108 IDHNGKGLFRGIPNPTVATRYHSLVVeeASLPECLEVTAKSDDGEIMGIRHKEHPIFGVQFHPESILTEEGKRILKNF 185
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
11-176 |
6.39e-19 |
|
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: 84.47 E-value: 6.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 11 IIVLDFGSQYNQLiaRRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPnsvyGEGAlHCDE------KIFDLGLPIF 84
Cdd:cd01744 1 VVVIDFGVKHNIL--RELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGP----GDPA-LLDEaiktvrKLLGKKIPIF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 85 GICYGMQLMTQQFGGTVER-------ANHreygkAVLKVENesklyanlpeeQVVWMS---HGDLV--TGLPEGFVV--- 149
Cdd:cd01744 74 GICLGHQLLALALGAKTYKmkfghrgSNH-----PVKDLIT-----------GRVYITsqnHGYAVdpDSLPGGLEVthv 137
|
170 180 190
....*....|....*....|....*....|
gi 1259761698 150 ---DATsescpIAGMSNEAKNLYGVQFHPE 176
Cdd:cd01744 138 nlnDGT-----VEGIRHKDLPVFSVQFHPE 162
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
40-191 |
5.91e-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: 81.76 E-value: 5.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 40 HTITAEEIKAMNPKGIIFSGGPNSVyGEGALHCDE-KIFDLGLPIFGICYGMQLMTQQFGGTVERANHREYGKAVLKVEN 118
Cdd:TIGR00566 32 DSLTLQEIEALLPLLIVISPGPCTP-NEAGISLEAiRHFAGKLPILGVCLGHQAMGQAFGGDVVRANTVMHGKTSEIEHN 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1259761698 119 ESKLYANLPEEQVVWMSHGDLVT--GLPEGFVVDATS-ESCPIAGMSNEAKNLYGVQFHPEVRHSEHGNDLIKNFV 191
Cdd:TIGR00566 111 GAGIFRGLFNPLTATRYHSLVVEpeTLPTCFPVTAWEeENIEIMAIRHRDLPLEGVQFHPESILSEQGHQLLANFL 186
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
10-176 |
6.71e-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: 85.07 E-value: 6.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 10 TIIVLDFGSQYNqlIARRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPnsvyGEGAlHCDE------KIFDLGLPI 83
Cdd:COG0505 178 HVVALDFGVKRN--ILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGP----GDPA-ALDYaietirELLGKGIPI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 84 FGICYGMQLMTQQFGGTVER-------ANHreygkavlkvenesklyanlPeeqVVwmshgDLVTGLPE------GFVVD 150
Cdd:COG0505 251 FGICLGHQLLALALGAKTYKlkfghrgANH--------------------P---VK-----DLETGRVEitsqnhGFAVD 302
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1259761698 151 AtsESCP---------------IAGMSNEAKNLYGVQFHPE 176
Cdd:COG0505 303 E--DSLPatdlevthvnlndgtVEGLRHKDLPAFSVQYHPE 341
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
42-191 |
2.68e-17 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 80.23 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 42 ITAEEIKAMNPKGIIFSGGPNSVYGEGALHCDEKIFDLGLPIFGICYGMQLMTQQFGGTVERANHREYGKAVLKVENESK 121
Cdd:PRK07649 34 VTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKT 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1259761698 122 LYANLPEEQVVWMSHGDLVTG--LPEGFVVDATSESCPIAGMSNEAKNLYGVQFHPEVRHSEHGNDLIKNFV 191
Cdd:PRK07649 114 IFSDIPNPFTATRYHSLIVKKetLPDCLEVTSWTEEGEIMAIRHKTLPIEGVQFHPESIMTSHGKELLQNFI 185
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
42-191 |
5.20e-16 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 76.31 E-value: 5.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 42 ITAEEIKAMNPKGIIFSGGPNSVYGEGalHCDEKIFDLG--LPIFGICYGMQLMTQQFGGTVERANHREYGKAVLKVENE 119
Cdd:CHL00101 34 IDLSKIKNLNIRHIIISPGPGHPRDSG--ISLDVISSYApyIPILGVCLGHQSIGYLFGGKIIKAPKPMHGKTSKIYHNH 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1259761698 120 SKLYANLPEEQVVWMSHGDLV--TGLPEGFVVDA-TSESCPIAGMSNEAKNLYGVQFHPEVRHSEHGNDLIKNFV 191
Cdd:CHL00101 112 DDLFQGLPNPFTATRYHSLIIdpLNLPSPLEITAwTEDGLIMACRHKKYKMLRGIQFHPESLLTTHGQQILRNFL 186
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
6-191 |
2.89e-15 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 74.83 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 6 KQHDTIIVLDFGSQYNQLIARRIREFGVYSELHPH-TITAEEIKAMNPKGIIFSGGPNSVYGEG-ALhcdEKIFDLG--L 81
Cdd:PLN02335 16 KQNGPIIVIDNYDSFTYNLCQYMGELGCHFEVYRNdELTVEELKRKNPRGVLISPGPGTPQDSGiSL---QTVLELGplV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 82 PIFGICYGMQLMTQQFGGTVERA-NHREYGKAVL---KVENESKLYANLPEEQVVWMSHGDLVT--GLPEGFV-VDATSE 154
Cdd:PLN02335 93 PLFGVCMGLQCIGEAFGGKIVRSpFGVMHGKSSPvhyDEKGEEGLFSGLPNPFTAGRYHSLVIEkdTFPSDELeVTAWTE 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1259761698 155 SCPIAGMSNEA-KNLYGVQFHPEVRHSEHGNDLIKNFV 191
Cdd:PLN02335 173 DGLIMAARHRKyKHIQGVQFHPESIITTEGKTIVRNFI 210
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
80-191 |
3.90e-15 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 78.42 E-value: 3.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 80 GLPIFGICYGMQLMTQQFGGTVERANHREYGKA-VLKVENESKLYANLPEEQVVWMSHGDLVT--GLPEGFVVDATSESC 156
Cdd:PRK13566 598 NLPIFGVCLGLQAIVEAFGGELGQLAYPMHGKPsRIRVRGPGRLFSGLPEEFTVGRYHSLFADpeTLPDELLVTAETEDG 677
|
90 100 110
....*....|....*....|....*....|....*...
gi 1259761698 157 PIAGMSNEAKNLYGVQFHPEVRHS---EHGNDLIKNFV 191
Cdd:PRK13566 678 VIMAIEHKTLPVAAVQFHPESIMTlggDVGLRIIENVV 715
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
10-176 |
4.40e-15 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 76.47 E-value: 4.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 10 TIIVLDFGsqYNQLIARRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPNSVygEGALHCDEKIFDL--GLPIFGIC 87
Cdd:PRK12838 169 HVALIDFG--YKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPGDP--KELQPYLPEIKKLisSYPILGIC 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 88 YGMQLMTQQFGGTVER-------ANHreygkAVLKVENesklyanlpeeQVVWMS---HGDLV-------TGLPEGFvVD 150
Cdd:PRK12838 245 LGHQLIALALGADTEKlpfghrgANH-----PVIDLTT-----------GRVWMTsqnHGYVVdedsldgTPLSVRF-FN 307
|
170 180
....*....|....*....|....*.
gi 1259761698 151 ATSEScpIAGMSNEAKNLYGVQFHPE 176
Cdd:PRK12838 308 VNDGS--IEGLRHKKKPVLSVQFHPE 331
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
10-176 |
5.37e-15 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 76.27 E-value: 5.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 10 TIIVLDFGSQYNqlIARRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPnsvyGEGALhCDE------KIFDLGLPI 83
Cdd:PRK12564 179 KVVAIDFGVKRN--ILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGP----GDPAA-LDYaiemirELLEKKIPI 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 84 FGICYGMQLMTQQFGGTVERAN--HReyGkavlkvenesklyANLPeeqVvwmshGDLVTGLPE------GFVVDAtsES 155
Cdd:PRK12564 252 FGICLGHQLLALALGAKTYKMKfgHR--G-------------ANHP---V-----KDLETGKVEitsqnhGFAVDE--DS 306
|
170 180 190
....*....|....*....|....*....|....*
gi 1259761698 156 CP--------------IAGMSNEAKNLYGVQFHPE 176
Cdd:PRK12564 307 LPanlevthvnlndgtVEGLRHKDLPAFSVQYHPE 341
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
11-191 |
9.55e-15 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 75.99 E-value: 9.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 11 IIVLDFGSQYNqlIARRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPN--SVYGEGaLHCDEKIFDLGLPIFGICY 88
Cdd:CHL00197 195 IIVIDFGVKYN--ILRRLKSFGCSITVVPATSPYQDILSYQPDGILLSNGPGdpSAIHYG-IKTVKKLLKYNIPIFGICM 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 89 GMQLMTQQFGGTV------ERA-NHREYGKAVLKVENESKLYA-NLPE--EQVVWMSHGDLvtglpegfvVDATsescpI 158
Cdd:CHL00197 272 GHQILSLALEAKTfklkfgHRGlNHPSGLNQQVEITSQNHGFAvNLESlaKNKFYITHFNL---------NDGT-----V 337
|
170 180 190
....*....|....*....|....*....|....
gi 1259761698 159 AGMSNEAKNLYGVQFHPEVRHSEHGND-LIKNFV 191
Cdd:CHL00197 338 AGISHSPKPYFSVQYHPEASPGPHDADyLFEYFI 371
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
42-191 |
1.46e-14 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 72.20 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 42 ITAEEIKAMNPKGIIFSGGPNSVYGEGALHCDEKIFDLGLPIFGICYGMQLMTQQFGGTVERANHREYGKAVLKVENESK 121
Cdd:PRK06774 34 LQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCLGHQALGQAFGARVVRARQVMHGKTSAICHSGQG 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1259761698 122 LYANLPEEQVVWMSHGDLV--TGLPEGFVVDATSESC----PIAGMSNEAKNLYGVQFHPEVRHSEHGNDLIKNFV 191
Cdd:PRK06774 114 VFRGLNQPLTVTRYHSLVIaaDSLPGCFELTAWSERGgemdEIMGIRHRTLPLEGVQFHPESILSEQGHQLLDNFL 189
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
47-191 |
1.59e-14 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 72.22 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 47 IKAMNPKGIIFSGGPNSVYGEGALHCDEKIFDLGLPIFGICYGMQLMTQQFGGTVERANHREYGKAVLKVENESKLYANL 126
Cdd:PRK08857 39 IEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGL 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1259761698 127 PEEQVVWMSHGDLVTG--LPEGFVVDATSESC-----PIAGMSNEAKNLYGVQFHPEVRHSEHGNDLIKNFV 191
Cdd:PRK08857 119 NNPLTVTRYHSLVVKNdtLPECFELTAWTELEdgsmdEIMGFQHKTLPIEAVQFHPESIKTEQGHQLLANFL 190
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
54-176 |
2.01e-14 |
|
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: 72.29 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 54 GIIFSGGPN---SVYGEGALHCDEKIF---------------DLGLPIFGICYGMQLMTQQFGGT--------VERANHR 107
Cdd:pfam07722 61 GLLLTGGPNvdpHFYGEEPSESGGPYDpardayelaliraalARGKPILGICRGFQLLNVALGGTlyqdiqeqPGFTDHR 140
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1259761698 108 EYGKAV-------LKVENESKLYANLPEEQVVWMS-HGDLVTGLPEGFVVDATSESCPIAGMS--NEAKNLYGVQFHPE 176
Cdd:pfam07722 141 EHCQVApyapshaVNVEPGSLLASLLGSEEFRVNSlHHQAIDRLAPGLRVEAVAPDGTIEAIEspNAKGFALGVQWHPE 219
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
54-196 |
1.20e-13 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 70.08 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 54 GIIFSGGPNSVYGEGAL-----HCDEKifdlGLPIFGICYGMQLMTQQFGGTVERANHREYGKAVLKVENESKLYANLPE 128
Cdd:PRK07765 49 GVLLSPGPGTPERAGASidmvrACAAA----GTPLLGVCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPD 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 129 EQVVWMSHGDLV--TGLPEGFVVDATSESCPIAGMSNEAKNLYGVQFHPEVRHSEHGNDLIKNFVfGVCG 196
Cdd:PRK07765 125 PFTATRYHSLTIlpETLPAELEVTARTDSGVIMAVRHRELPIHGVQFHPESVLTEGGHRMLANWL-TVCG 193
|
|
| PuuD |
COG2071 |
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
54-191 |
2.44e-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: 69.43 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 54 GIIFSGGPN---SVYGEGALHCDEKI------FDL---------GLPIFGICYGMQLMTQQFGGTV---------ERANH 106
Cdd:COG2071 52 GLVLTGGADvdpALYGEEPHPELGPIdperdaFELaliraalerGKPVLGICRGMQLLNVALGGTLyqdlpdqvpGALDH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 107 REYGKAVL-----KVENESKLYANLPEEQV-VWMSHGDLVTGLPEGFVVDATSEScpiaGM-----SNEAKNLYGVQFHP 175
Cdd:COG2071 132 RQPAPRYAprhtvEIEPGSRLARILGEEEIrVNSLHHQAVKRLGPGLRVSARAPD----GVieaieSPGAPFVLGVQWHP 207
|
170
....*....|....*...
gi 1259761698 176 EVRHSEHGND--LIKNFV 191
Cdd:COG2071 208 EWLAASDPLSrrLFEAFV 225
|
|
| PRK09065 |
PRK09065 |
glutamine amidotransferase; Provisional |
80-176 |
3.14e-13 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181635 [Multi-domain] Cd Length: 237 Bit Score: 69.22 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 80 GLPIFGICYGMQLMTQQFGGTVerANH---REYGKAVLKVENESK---LYANLPEEQVVWMSHGDLVTGLPEGFVVDATS 153
Cdd:PRK09065 88 GMPLLGICYGHQLLAHALGGEV--GYNpagRESGTVTVELHPAAAddpLFAGLPAQFPAHLTHLQSVLRLPPGAVVLARS 165
|
90 100
....*....|....*....|....*
gi 1259761698 154 --ESCPIAGMSNEAknlYGVQFHPE 176
Cdd:PRK09065 166 aqDPHQAFRYGPHA---WGVQFHPE 187
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
11-185 |
4.09e-13 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 71.16 E-value: 4.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 11 IIVLDFGSQYNqlIARRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPNSvygEGALHCD-EKIFDL--GLPIFGIC 87
Cdd:PLN02771 243 VIAYDFGIKHN--ILRRLASYGCKITVVPSTWPASEALKMKPDGVLFSNGPGD---PSAVPYAvETVKELlgKVPVFGIC 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 88 YGMQLMTQQFGGTVER-------ANH--REYGKAVLKVENESKLYANLPeeqvvwmshgdlvTGLPEGFVV---DATSES 155
Cdd:PLN02771 318 MGHQLLGQALGGKTFKmkfghhgGNHpvRNNRTGRVEISAQNHNYAVDP-------------ASLPEGVEVthvNLNDGS 384
|
170 180 190
....*....|....*....|....*....|
gi 1259761698 156 CpiAGMSNEAKNLYGVQFHPEVRHSEHGND 185
Cdd:PLN02771 385 C--AGLAFPALNVMSLQYHPEASPGPHDSD 412
|
|
| PRK07567 |
PRK07567 |
glutamine amidotransferase; Provisional |
54-176 |
1.10e-12 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181035 [Multi-domain] Cd Length: 242 Bit Score: 67.66 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 54 GIIFSGGPNSV------YGEGALHCDEKIFDL-------GLPIFGICYGMQLMTQQFGGTVERAnhreYGKAVLKVE--- 117
Cdd:PRK07567 54 GVIVGGSPFNVsdpaesKSPWQRRVEAELSGLldevvarDFPFLGACYGVGTLGHHQGGVVDRT----YGEPVGAVTvsl 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1259761698 118 -NESK---LYANLPEEQVVWMSHGDLVTGLPEGFVVDATSESCPIAgMSNEAKNLYGVQFHPE 176
Cdd:PRK07567 130 tDAGRadpLLAGLPDTFTAFVGHKEAVSALPPGAVLLATSPTCPVQ-MFRVGENVYATQFHPE 191
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
83-191 |
7.35e-12 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 64.37 E-value: 7.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 83 IFGICYGMQLMTQQFGGTVERANHREYGKA-VLKVENESKLYANLPEEQVVWMSHGDLVT--GLPEGFVVDATSESCPIA 159
Cdd:PRK06895 75 ILGVCLGHQTLCEFFGGELYNLNNVRHGQQrPLKVRSNSPLFDGLPEEFNIGLYHSWAVSeeNFPTPLEITAVCDENVVM 154
|
90 100 110
....*....|....*....|....*....|..
gi 1259761698 160 GMSNEAKNLYGVQFHPEVRHSEHGNDLIKNFV 191
Cdd:PRK06895 155 AMQHKTLPIYGVQFHPESYISEFGEQILRNWL 186
|
|
| PRK09522 |
PRK09522 |
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ... |
11-188 |
2.83e-11 |
|
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;
Pssm-ID: 181927 [Multi-domain] Cd Length: 531 Bit Score: 65.82 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 11 IIVLDFGSQYNQLIARRIREFG----VYSELHPHTITAEEIKAMNPKGIIFSGGPNSVYGEGALHCDEKIFDLGLPIFGI 86
Cdd:PRK09522 4 ILLLDNIDSFTYNLADQLRSNGhnvvIYRNHIPAQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 87 CYGMQLMTQQFGGTVERANHREYGKAVLKVENESKLYANLPEEQVVWMSHGDLVTGLPEGFVVDATSESCPIAgMSNEAK 166
Cdd:PRK09522 84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSNIPAGLTINAHFNGMVMA-VRHDAD 162
|
170 180
....*....|....*....|..
gi 1259761698 167 NLYGVQFHPEVRHSEHGNDLIK 188
Cdd:PRK09522 163 RVCGFQFHPESILTTQGARLLE 184
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
21-191 |
1.93e-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: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 21 NQLIARRIREFGVYSELHPHTITAEEIKAM--NPKGIIFSGGPNSV---YGEGALHCDEKIF---------------DLG 80
Cdd:cd01745 21 NQYYVDAVRKAGGLPVLLPPVDDEEDLEQYleLLDGLLLTGGGDVDpplYGEEPHPELGPIDperdafelallraalERG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 81 LPIFGICYGMQLMTQQFGGTVERanhreygkavlkvenesKLYANlpeeqvvwmS-HGDLVTGLPEGFVVDATSESCPIA 159
Cdd:cd01745 101 KPILGICRGMQLLNVALGGTLYQ-----------------DIRVN---------SlHHQAIKRLADGLRVEARAPDGVIE 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1259761698 160 GMSNEAKNLY-GVQFHPE--VRHSEHGNDLIKNFV 191
Cdd:cd01745 155 AIESPDRPFVlGVQWHPEwlADTDPDSLKLFEAFV 189
|
|
| PRK07053 |
PRK07053 |
glutamine amidotransferase; Provisional |
59-178 |
1.75e-09 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 235919 [Multi-domain] Cd Length: 234 Bit Score: 58.03 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 59 GGPNSVYGEGA---LHCD----EKIFDLGLPIFGICYGMQLMTQQFGGTVERANHREYGKAVLKVE---NESKLyANLPE 128
Cdd:PRK07053 55 GGPIGVYDDELypfLAPEiallRQRLAAGLPTLGICLGAQLIARALGARVYPGGQKEIGWAPLTLTdagRASPL-RHLGA 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1259761698 129 EQVVWMSHGDLVTgLPEGFVVDATSESCPiagmsNEA----KNLYGVQFHPEVR 178
Cdd:PRK07053 134 GTPVLHWHGDTFD-LPEGATLLASTPACR-----HQAfawgNHVLALQFHPEAR 181
|
|
| PRK05665 |
PRK05665 |
amidotransferase; Provisional |
74-179 |
2.00e-09 |
|
amidotransferase; Provisional
Pssm-ID: 168162 [Multi-domain] Cd Length: 240 Bit Score: 57.90 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 74 EKIFDLGLPIFGICYGMQLMTQQFGGTVERANhREYGKAVLKVENESKLYANLPE--EQVVWMSHGDLVTGLPEGFVVDA 151
Cdd:PRK05665 85 LKLYERGDKLLGVCFGHQLLALLLGGKAERAS-QGWGVGIHRYQLAAHAPWMSPAvtELTLLISHQDQVTALPEGATVIA 163
|
90 100
....*....|....*....|....*...
gi 1259761698 152 TSESCPIAGMSNEAKNLYgVQFHPEVRH 179
Cdd:PRK05665 164 SSDFCPFAAYHIGDQVLC-FQGHPEFVH 190
|
|
| hisH |
PRK13181 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
78-190 |
1.06e-08 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 55.26 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 78 DLGLPIFGICYGMQLMTQQ-----------FGGTVERANHREY-----GKAVLKVENESKLYANLPEEQVVWMSHGDLVT 141
Cdd:PRK13181 70 EKKQPVLGICLGMQLLFESseegnvkglglIPGDVKRFRSEPLkvpqmGWNSVKPLKESPLFKGIEEGSYFYFVHSYYVP 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1259761698 142 GLPEGFVVdATSE-----SCPIagmsnEAKNLYGVQFHPEvRHSEHGNDLIKNF 190
Cdd:PRK13181 150 CEDPEDVL-ATTEygvpfCSAV-----AKDNIYAVQFHPE-KSGKAGLKLLKNF 196
|
|
| NAD_synthase |
pfam02540 |
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ... |
204-441 |
1.25e-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: 55.85 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 204 ENFIEVELEKiretVGDKKVLCALSGGVDSSVVAVLIHKAIG-DQLTCIFVDHGLLRKGEAEGVmKTFSEGFHMNVIKVD 282
Cdd:pfam02540 6 VDFLRDYVQK----AGFKGVVLGLSGGIDSSLVAYLAVKALGkENVLALIMPSSQSSEEDVQDA-LALAENLGIEYKTID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 283 AKE---RFMNKLK----GVEDPEQKRKI-------IGNEFIYVFDDEASKLEGMdfLAQGTLYTDIvesgtataqtiksh 348
Cdd:pfam02540 81 IKPivrAFSQLFQdaseDFAKGNLKARIrmailyyIANKFNYLVLGTGNKSELA--VGYFTKYGDG-------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 349 hNVGglpedmqfklIEPLNTLFKDEVRVLGSELGIPDEIVWRQP----FPG----PGLGIRVlgEITEEKLEIVRESDAi 420
Cdd:pfam02540 145 -ACD----------IAPIGDLYKTQVYELARYLNVPERIIKKPPsadlWPGqtdeEELGIPY--DELDDILKLVEKKLS- 210
|
250 260
....*....|....*....|.
gi 1259761698 421 lREEIIKAGLDREIWQYFTAL 441
Cdd:pfam02540 211 -PEEIIGKGLPAEVVRRIENL 230
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
11-115 |
5.32e-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: 51.06 E-value: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 11 IIVLDFGSQYN---QLIARRIREFGVYSELHPHTITAE--EIKAMNPKGIIFSGGPNSVYG----EGALHCDEKIFDLGL 81
Cdd:cd01653 1 VAVLLFPGFEElelASPLDALREAGAEVDVVSPDGGPVesDVDLDDYDGLILPGGPGTPDDlardEALLALLREAAAAGK 80
|
90 100 110
....*....|....*....|....*....|....
gi 1259761698 82 PIFGICYGMQLMTQQFGGTVERANHREYGKAVLK 115
Cdd:cd01653 81 PILGICLGAQLLVLGVQFHPEAIDGAEAGARLLV 114
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
11-93 |
6.67e-08 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 50.28 E-value: 6.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 11 IIVLDFGSQYN---QLIARRIREFGVYSELHPHTITAE--EIKAMNPKGIIFSGGPNSVYG----EGALHCDEKIFDLGL 81
Cdd:cd03128 1 VAVLLFGGSEElelASPLDALREAGAEVDVVSPDGGPVesDVDLDDYDGLILPGGPGTPDDlawdEALLALLREAAAAGK 80
|
90
....*....|..
gi 1259761698 82 PIFGICYGMQLM 93
Cdd:cd03128 81 PVLGICLGAQLL 92
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
80-191 |
3.09e-07 |
|
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: 50.96 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 80 GLPIFGICYGMQLMTQQ------------FGGTVERANHREyGKAV-------LKVENESKLYANLPEEQVVWMSHGDLV 140
Cdd:cd01748 71 GKPFLGICLGMQLLFESseegggtkglglIPGKVVRFPASE-GLKVphmgwnqLEITKESPLFKGIPDGSYFYFVHSYYA 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1259761698 141 TGLPEGFVVDATSESCPIAGMsNEAKNLYGVQFHPEvRHSEHGNDLIKNFV 191
Cdd:cd01748 150 PPDDPDYILATTDYGGKFPAA-VEKDNIFGTQFHPE-KSGKAGLKLLKNFL 198
|
|
| PRK05637 |
PRK05637 |
anthranilate synthase component II; Provisional |
40-176 |
6.94e-07 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 180178 [Multi-domain] Cd Length: 208 Bit Score: 49.84 E-value: 6.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 40 HTITAEEIKAMNPKGIIFSGGPNSVYGEGalhCDEKIFD--LG-LPIFGICYGMQLMTQQFGGTVErANHREYGKAVLKV 116
Cdd:PRK05637 33 NTVPVEEILAANPDLICLSPGPGHPRDAG---NMMALIDrtLGqIPLLGICLGFQALLEHHGGKVE-PCGPVHGTTDNMI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 117 EN----ESKLYA-----------NLPEEQV-VWMSHGDLVTGLPEGFVVDATSESC--PIAgMSNEAKN--LYGVQFHPE 176
Cdd:PRK05637 109 LTdagvQSPVFAglatdvepdhpEIPGRKVpIARYHSLGCVVAPDGMESLGTCSSEigPVI-MAAETTDgkAIGLQFHPE 187
|
|
| tRNA_Me_trans |
pfam03054 |
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ... |
221-384 |
9.20e-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: 49.56 E-value: 9.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 221 KKVLCALSGGVDSSVVAVLIHKAiGDQLTCIF----VDHGLLRKG----------EAEGVMKTFSEGFHmnviKVDAKER 286
Cdd:pfam03054 1 MKVVVAMSGGVDSSVAAYLLKEQ-GHNVIGVFmknwDEEQSLDEEgkccseedlaDAQRVCEQLGIPLY----VVNFEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 287 FMNKlkgVEDP---EQKR------KIIGNEFI---YVFDDEASKLeGMDFLAQGTlYTDIVESGTATA-----------Q 343
Cdd:pfam03054 76 YWED---VFEPfldEYKNgrtpnpDVLCNKEIkfgALLDYALENL-GADYVATGH-YARVSLNKDGGSellraldknkdQ 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1259761698 344 TikshHNVGGLPEDMQFKLIEPLNTLFKDEVRVLGSELGIP 384
Cdd:pfam03054 151 S----YFLSTLSQEQLEKLLFPLGELTKEEVRKIAKEAGLA 187
|
|
| hisH |
PRK13143 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
80-191 |
9.55e-07 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 49.48 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 80 GLPIFGICYGMQLMTQQ------------FGGTVERANHRE----YGKAVLKVENESKLYANLPEEQVVWMsHgdlvtgl 143
Cdd:PRK13143 71 GKPFLGICLGMQLLFESseegggvrglglFPGRVVRFPAGVkvphMGWNTVKVVKDCPLFEGIDGEYVYFV-H------- 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1259761698 144 peGFVVDATSESCpIAGMSN---------EAKNLYGVQFHPEvRHSEHGNDLIKNFV 191
Cdd:PRK13143 143 --SYYAYPDDEDY-VVATTDygiefpaavCNDNVFGTQFHPE-KSGETGLKILENFV 195
|
|
| COG1606 |
COG1606 |
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only]; |
211-423 |
9.62e-07 |
|
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
Pssm-ID: 441214 [Multi-domain] Cd Length: 265 Bit Score: 50.11 E-value: 9.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 211 LEKIRETVGD-KKVLCALSGGVDSSVVAVLIHKAIGDQLTCIFVDHGLLRKGEAEGVMKTFSE-GFHMNVIKVD--AKER 286
Cdd:COG1606 5 LERLKAILKElGSVLVAFSGGVDSTLLAKVAHDVLGDRVLAVTADSPSLPERELEEAKELAKEiGIRHEVIETDelEDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 287 FmnklkgVEDPEQ-----KRKIIGnefiyVFDDEASKLeGMDFLAQGTLYTD----------IVESGtataqtIKShhnv 351
Cdd:COG1606 85 F------VANPPDrcyhcKKELFS-----KLKELAKEL-GYAVVADGTNADDlgdyrpglraAKELG------VRS---- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1259761698 352 gglPedmqfkLIEplNTLFKDEVRVLGSELGIPdeiVWRQPfPGPGLGIRV-LGE-ITEEKLEIVRESDAILRE 423
Cdd:COG1606 143 ---P------LAE--AGLTKAEIRELARELGLP---TWDKP-SSACLASRIpYGEeITPEKLRRVERAEAFLRS 201
|
|
| nadE |
TIGR00552 |
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ... |
202-395 |
1.47e-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: 49.69 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 202 NMENFIEvELEK-IRETV---GDKKVLCALSGGVDSSVVAVLIHKAIGDQLTCIFVDHGLLRKGEAEGVMKTFSEGFHMN 277
Cdd:TIGR00552 1 NLIKYVE-EIEDfLRGYVqksGAKGVVLGLSGGIDSAVVAALCVEALGEQNHALLLPHSVQTPEQDVQDALALAEPLGIN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 278 VIKVDAKERFMNKLKGVEDPEQKRKII--GNE-------FIYVFDDEASKL--------EGMdfLAQGTLYTDIvesGTA 340
Cdd:TIGR00552 80 YKNIDIAPIAASFQAQTETGDELSDFLakGNLkarlrmaALYAIANKHNLLvlgtgnksELM--LGYFTKYGDG---GCD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1259761698 341 taqtikshhnvgglpedmqfklIEPLNTLFKDEVRVLGSELGIPDEIVWRQP----FPG 395
Cdd:TIGR00552 155 ----------------------IAPIGDLFKTQVYELAKRLNVPERIIEKPPtadlFDG 191
|
|
| hisH |
PRK13141 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
80-191 |
1.61e-06 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 48.97 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 80 GLPIFGICYGMQLMTQQ---FG---------GTVERANHREyGKAV-------LKVENESKLYANLPEEQVVWMSHGDLV 140
Cdd:PRK13141 72 GKPLLGICLGMQLLFESseeFGeteglgllpGRVRRFPPEE-GLKVphmgwnqLELKKESPLLKGIPDGAYVYFVHSYYA 150
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1259761698 141 TGLPEGFVVdATSE-SCPIAGMSnEAKNLYGVQFHPEvRHSEHGNDLIKNFV 191
Cdd:PRK13141 151 DPCDEEYVA-ATTDyGVEFPAAV-GKDNVFGAQFHPE-KSGDVGLKILKNFV 199
|
|
| LarE-like |
cd01990 |
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ... |
222-423 |
1.79e-06 |
|
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: 48.79 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 222 KVLCALSGGVDSSVVAVLIHKAIGDQLTCIFVDHGLLRKGEAEGVMKTFSEgfhmnvIKVDAKERFMNKLKG---VEDPE 298
Cdd:cd01990 1 KVVVAFSGGVDSSLLAKLAKEVLGDNVVAVTADSPLVPREELEEAKRIAEE------IGIRHEIIKTDELDDeeyVANDP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 299 QK----RKIIGNEFIyvfddEASKLEGMDFLAQGTLYTDIVEsgtataqtikshHNVGGLP-EDMQFKLIEPLNTLFKDE 373
Cdd:cd01990 75 DRcyhcKKALYSTLK-----EIAKERGYDVVLDGTNADDLKD------------YRPGLLAaAELGIRSPLPELGLTKSE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1259761698 374 VRVLGSELGIPdeiVWRQPfPGPGLGIRVL-GE-ITEEKLE-IVRESDAILRE 423
Cdd:cd01990 138 IRELARELGLP---NWDKP-ASACLASRIPyGEeITPERLKrIEKAEELYLRL 186
|
|
| hisH |
PRK13170 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
82-191 |
1.79e-06 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183877 [Multi-domain] Cd Length: 196 Bit Score: 48.70 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 82 PIFGICYGMQLMTQ--QFGGTVERANhreygkaVLKVENESKLYANLPE-----EQVVWMSHGDLVTGLPEG----FV-- 148
Cdd:PRK13170 72 PVLGICLGMQLLGErsEESGGVDCLG-------IIDGPVKKMTDFGLPLphmgwNQVTPQAGHPLFQGIEDGsyfyFVhs 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1259761698 149 ----VD----ATSE-----SCPIAgmsneAKNLYGVQFHPEvRHSEHGNDLIKNFV 191
Cdd:PRK13170 145 yampVNeytiAQCNygepfSAAIQ-----KDNFFGVQFHPE-RSGAAGAQLLKNFL 194
|
|
| PRK06490 |
PRK06490 |
glutamine amidotransferase; Provisional |
55-180 |
2.68e-06 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 180590 [Multi-domain] Cd Length: 239 Bit Score: 48.80 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 55 IIFsGGPNSVYGEGALHCDEkIFDLGLPI------FGICYGMQLMTQQFGGTVERANH--REYGKAVLKVENESKLYANL 126
Cdd:PRK06490 57 VIF-GGPMSANDPDDFIRRE-IDWISVPLkenkpfLGICLGAQMLARHLGARVAPHPDgrVEIGYYPLRPTEAGRALMHW 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1259761698 127 PEEQVVWMSHG-DLvtglPEGFVVDATSESCPiagmsNEA----KNLYGVQFHPEVRHS 180
Cdd:PRK06490 135 PEMVYHWHREGfDL----PAGAELLATGDDFP-----NQAfrygDNAWGLQFHPEVTRA 184
|
|
| HisH |
COG0118 |
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
78-176 |
5.42e-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: 46.96 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 78 DLGLPIFGICYGMQLMTQQ------------FGGTVERanhreYGKAVLKV----------ENESKLYANLPEEQVVWMS 135
Cdd:COG0118 71 AGGKPVLGICLGMQLLFERseengdteglglIPGEVVR-----FPASDLKVphmgwntveiAKDHPLFAGIPDGEYFYFV 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1259761698 136 HGdlvtglpegFVVDATSEScPIAGMSN---------EAKNLYGVQFHPE 176
Cdd:COG0118 146 HS---------YYVPPDDPE-DVVATTDygvpftaavERGNVFGTQFHPE 185
|
|
| IMP_synth_hisH |
TIGR01855 |
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ... |
74-191 |
8.65e-06 |
|
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: 46.55 E-value: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 74 EKIFDLGLPIFGICYGMQLMTQQ------------FGGTVERANHR---EYGKAVLKVENESKLYANLPEEQVVWMSHGD 138
Cdd:TIGR01855 65 ELVVRLGKPVLGICLGMQLLFERseegggvpglglIKGNVVKLEARkvpHMGWNEVHPVKESPLLNGIDEGAYFYFVHSY 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1259761698 139 LVTglPEGFVVDATSESCPIAGMSNEAKNLYGVQFHPEvRHSEHGNDLIKNFV 191
Cdd:TIGR01855 145 YAV--CEEEAVLAYADYGEKFPAAVQKGNIFGTQFHPE-KSGKTGLKLLENFL 194
|
|
| PRK08250 |
PRK08250 |
glutamine amidotransferase; Provisional |
83-176 |
8.81e-06 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181323 [Multi-domain] Cd Length: 235 Bit Score: 46.88 E-value: 8.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 83 IFGICYGMQLMTQQFGGTVERANHREYGKAVLKVENESK---LYANLPEEQVVWMSHGDLvTGLPEGFVVDATSESCP-- 157
Cdd:PRK08250 87 VIGVCLGAQLIGEALGAKYEHSPEKEIGYFPITLTEAGLkdpLLSHFGSTLTVGHWHNDM-PGLTDQAKVLATSEGCPrq 165
|
90
....*....|....*....
gi 1259761698 158 IAGMSNEaknLYGVQFHPE 176
Cdd:PRK08250 166 IVQYSNL---VYGFQCHME 181
|
|
| PRK13980 |
PRK13980 |
NAD synthetase; Provisional |
205-423 |
9.42e-06 |
|
NAD synthetase; Provisional
Pssm-ID: 184435 [Multi-domain] Cd Length: 265 Bit Score: 47.13 E-value: 9.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 205 NFIEVELEKiretVGDKKVLCALSGGVDSSVVAVLIHKAIG-DQLtcifvdHGLLRKGE---------AEGVMKTFseGF 274
Cdd:PRK13980 19 DFIREEVEK----AGAKGVVLGLSGGIDSAVVAYLAVKALGkENV------LALLMPSSvsppedledAELVAEDL--GI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 275 HMNVIK----VDAkerFMNKLkgvedPEQKRKIIGN-------EFIYvfdDEASKLEGM---------DFLAQGTLYTDi 334
Cdd:PRK13980 87 EYKVIEitpiVDA---FFSAI-----PDADRLRVGNimartrmVLLY---DYANRENRLvlgtgnkseLLLGYFTKYGD- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 335 veSGTAtaqtikshhnvgglpedmqfklIEPLNTLFKDEVRVLGSELGIPDEIVWRQPFPG--PG------LGI--RVLG 404
Cdd:PRK13980 155 --GAVD----------------------LNPIGDLYKTQVRELARHLGVPEDIIEKPPSADlwEGqtdegeLGFsyETID 210
|
250
....*....|....*....
gi 1259761698 405 EITEEKLEIVRESDAILRE 423
Cdd:PRK13980 211 EILYLLFDKKMSREEILEE 229
|
|
| puuD |
PRK11366 |
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional |
39-182 |
1.21e-05 |
|
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
Pssm-ID: 183101 [Multi-domain] Cd Length: 254 Bit Score: 46.82 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 39 PHTITAEEI-KAMNPK--GIIFSGGPNSV----YGEGAlhcDEKIFDLG----------------LPIFGICYGMQLMTQ 95
Cdd:PRK11366 46 PHALAEPSLlEQLLPKldGIYLPGSPSNVqphlYGENG---DEPDADPGrdllsmalinaalerrIPIFAICRGLQELVV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 96 QFGGTVERA--------NHRE---------YGKA-VLKVENESKLYANLPEEQVVWMS--HGDLVTGLPEGFVVDATSES 155
Cdd:PRK11366 123 ATGGSLHRKlceqpellEHREdpelpveqqYAPShEVQVEEGGLLSALLPECSNFWVNslHGQGAKVVSPRLRVEARSPD 202
|
170 180
....*....|....*....|....*...
gi 1259761698 156 CPIAGMS-NEAKNLYGVQFHPEVRHSEH 182
Cdd:PRK11366 203 GLVEAVSvINHPFALGVQWHPEWNSSEY 230
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
214-441 |
3.06e-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: 46.76 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 214 IRETV---GDKKVLCALSGGVDSSVVAVLIHKAIG-DQLTCIF----------VDHgllrkgeAEGVMKTFseGFHMNVI 279
Cdd:COG0171 277 LRDYVrknGFKGVVLGLSGGIDSALVAALAVDALGpENVLGVTmpsrytsdesLED-------AEELAENL--GIEYEEI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 280 KV-DAKERFMNKLKGVEDPEQK-----------RKII---------------GNefiyvfddeasKLEgmdfLAQG--TL 330
Cdd:COG0171 348 DItPAVEAFLEALPHAFGGELDdvaeenlqariRMVIlmalankfgglvlgtGN-----------KSE----LAVGyfTK 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 331 YTDivesgtataqtikshHNVGglpedmqfklIEPLNTLFKDEVRVLGSELG-----IPDEIVWRQpfPGPGLgirVLGE 405
Cdd:COG0171 413 YGD---------------GAGD----------LAPIADLYKTQVYALARWLNrngevIPEDIIDKP--PSAEL---RPGQ 462
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1259761698 406 ITEEKLEIVRESDAILR---------EEIIKAGLDREIWQYFTAL 441
Cdd:COG0171 463 TDEDELGPYEVLDAILYayveeglspEEIAAAGYDREWVERVLRL 507
|
|
| mnmA |
PRK00143 |
tRNA-specific 2-thiouridylase MnmA; Reviewed |
221-243 |
3.57e-05 |
|
tRNA-specific 2-thiouridylase MnmA; Reviewed
Pssm-ID: 234664 [Multi-domain] Cd Length: 346 Bit Score: 45.83 E-value: 3.57e-05
|
| MnmA |
COG0482 |
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ... |
221-243 |
5.18e-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: 5.18e-05
|
| NAD_synthase |
cd00553 |
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ... |
212-398 |
7.29e-05 |
|
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: 44.47 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 212 EKIRETvGDKKVLCALSGGVDSSVVAVLIHKAIG-DQLTCIFVDHGLLRKGEAEGVmKTFSEGFHMNVIKVDAK---ERF 287
Cdd:cd00553 16 DYLRKS-GAKGFVLGLSGGIDSAVVAALAVRALGaENVLALIMPSRYSSKETRDDA-KALAENLGIEYRTIDIDpivDAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 288 MNKLKGVEDPEQKRKIIGNE-------FIYVFddeASKLEGM---------DFLAQGTLYTDivesgtataqtikshHNV 351
Cdd:cd00553 94 LKALEHAGGSEAEDLALGNIqarlrmvLLYAL---ANLLGGLvlgtgnkseLLLGYFTKYGD---------------GAA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1259761698 352 GglpedmqfklIEPLNTLFKDEVRVLGSELGIPDEIVwRQPfPGPGL 398
Cdd:cd00553 156 D----------INPIGDLYKTQVRELARYLGVPEEII-EKP-PSAEL 190
|
|
| TilS |
COG0037 |
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ... |
213-295 |
8.68e-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: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 213 KIRETVGD-------KKVLCALSGGVDSSVVAVLIHK---AIGDQLTCIFVDHGL--LRKGEAEGVmKTFSE--GFHMNV 278
Cdd:COG0037 1 KVRKAIRDyrllepgDRILVAVSGGKDSLALLHLLAKlrrRLGFELVAVHVDHGLreESDEDAEFV-AELCEelGIPLHV 79
|
90
....*....|....*..
gi 1259761698 279 IKVDAKERFMNKLKGVE 295
Cdd:COG0037 80 VRVDVPAIAKKEGKSPE 96
|
|
| AANH-like |
cd01986 |
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ... |
226-291 |
8.94e-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: 8.94e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1259761698 226 ALSGGVDSSVVAVLIHKAIGD-QLTCIFVDHGLLRKGEAEGVMKtfsegfhmnvikvDAKERFMNKL 291
Cdd:cd01986 4 GYSGGKDSSVALHLASRLGRKaEVAVVHIDHGIGFKEEAESVAS-------------IARRSILKKL 57
|
|
| hisH |
PRK14004 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
80-191 |
1.17e-04 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 172505 [Multi-domain] Cd Length: 210 Bit Score: 43.35 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 80 GLPIFGICYGMQLM-------------------------TQQFGGTVERANHREYGKAVLKVENESKLYANLPEEQVVWM 134
Cdd:PRK14004 72 GKPLFGICIGFQILfesseetnqgtkkeqieglgyikgkIKKFEGKDFKVPHIGWNRLQIRRKDKSKLLKGIGDQSFFYF 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1259761698 135 SH--------GDLVTGLpegfvVDATSESCPIAgmsNEAKNLYGVQFHPEVRHSeHGNDLIKNFV 191
Cdd:PRK14004 152 IHsyrptgaeGNAITGL-----CDYYQEKFPAV---VEKENIFGTQFHPEKSHT-HGLKLLENFI 207
|
|
| TilS_N |
cd01992 |
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ... |
222-264 |
2.14e-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: 2.14e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1259761698 222 KVLCALSGGVDSSVVAVLIHKAI---GDQLTCIFVDHGlLRKGEAE 264
Cdd:cd01992 1 KILVAVSGGPDSMALLHLLKELRpklGLKLVAVHVDHG-LREESAE 45
|
|
| MnmA_TRMU-like |
cd01998 |
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
222-252 |
3.46e-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: 3.46e-04
10 20 30
....*....|....*....|....*....|.
gi 1259761698 222 KVLCALSGGVDSSVVAVLIHKAiGDQLTCIF 252
Cdd:cd01998 1 KVAVAMSGGVDSSVAAALLKEQ-GYDVIGVF 30
|
|
| GATase1_Glutamyl_Hydrolase |
cd01747 |
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ... |
54-176 |
1.20e-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: 40.77 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 54 GIIFSGGPNSVYGEGALHCDEKIFDLGL---------PIFGICYGMQLMTQQfggTVERANHREYGKAV-----LKVEN- 118
Cdd:cd01747 57 GILFPGGAVDIDTSGYARTAKIIYNLALerndagdyfPVWGTCLGFELLTYL---TSGETLLLEATEATnsalpLNFTEd 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 119 --ESKLYANLP--------EEQVVWMSHGDLVTglPEGFVV-DATSESCPIAGMSN-----------EAKN--LYGVQFH 174
Cdd:cd01747 134 alQSRLFKRFPpdllkslaTEPLTMNNHRYGIS--PENFTEnGLLSDFFNVLTTNDdwngvefistvEAYKypIYGVQWH 211
|
..
gi 1259761698 175 PE 176
Cdd:cd01747 212 PE 213
|
|
| trmU |
TIGR00420 |
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ... |
221-384 |
1.78e-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: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 221 KKVLCALSGGVDSSVVAVLIHKAiGDQLTCIFVDHgLLRKGEAEGVMKTFSEGF--------HMNV--IKVDAKERFMNK 290
Cdd:TIGR00420 1 KKVIVGLSGGVDSSVSAYLLKQQ-GYEVVGVFMKN-WEEDDKNDGHGCTSAEDLrdaqaiceKLGIplEKVNFQKEYWNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 291 lkgVEDP---EQKR------KIIGNEFIY--VFDDEASKLEGMDFLAQGTlYTDI--VESGTATAQTIKSH-------HN 350
Cdd:TIGR00420 79 ---VFEPfiqEYKEgrtpnpDILCNKFIKfgAFLEYAAELLGNDKIATGH-YARIaeIEGKSLLLRALDKNkdqsyflYH 154
|
170 180 190
....*....|....*....|....*....|....
gi 1259761698 351 VGglPEDMQfKLIEPLNTLFKDEVRVLGSELGIP 384
Cdd:TIGR00420 155 LS--HEQLA-KLLFPLGELLKPEVRQIAKNAGLP 185
|
|
| ASS |
cd01999 |
argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle ... |
221-328 |
5.93e-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: 39.06 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 221 KKVLCALSGGVDSSVVAVLIHKAIGDQLTCIFVDHGllRKGEAEGVMKTFSEGFHMNVIKVDAKERFMNK-----LKGVE 295
Cdd:cd01999 1 KKVVLAYSGGLDTSVILKWLKEEYGYEVIAFTADLG--QGDEEEEIEEKALKLGAVKVYVVDLREEFAEDyifpaIKANA 78
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1259761698 296 DPEQK--------RKIIGNEFIyvfddEASKLEGMDFLAQG 328
Cdd:cd01999 79 IYEGRyplgtalaRPLIAKKLV-----EVAREEGATAVAHG 114
|
|
| hisH |
PRK13152 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
82-191 |
9.03e-03 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 171876 [Multi-domain] Cd Length: 201 Bit Score: 37.51 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1259761698 82 PIFGICYGMQLMTQ---QFG-----GTVERANHREYGKAVLKV----------ENESKLYANLPEEQVVWMSHGDLVTGL 143
Cdd:PRK13152 75 PILGICLGMQLFLErgyEGGvceglGFIEGEVVKFEEDLNLKIphmgwneleiLKQSPLYQGIPEKSDFYFVHSFYVKCK 154
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1259761698 144 PEgfVVDATSESCPIAGMSNEAKNLYGVQFHPEvRHSEHGNDLIKNFV 191
Cdd:PRK13152 155 DE--FVSAKAQYGHKFVASLQKDNIFATQFHPE-KSQNLGLKLLENFA 199
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
220-247 |
9.87e-03 |
|
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: 37.64 E-value: 9.87e-03
10 20
....*....|....*....|....*...
gi 1259761698 220 DKKVLCALSGGVDSSVVAVLIHKAIGDQ 247
Cdd:cd01991 2 DVPVGVLLSGGLDSSLIAALAARLLPET 29
|
|
| |
