|
Name |
Accession |
Description |
Interval |
E-value |
| guaA |
PRK00074 |
GMP synthase; Reviewed |
14-528 |
0e+00 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 746.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 14 DRIVILDFGSQTTHLIGRRIREQGIFAEIVAGTAPMEDWIDEGVRGVILSGSPSSIHDEDAPLPDRRIYSRGIPLLGICY 93
Cdd:PRK00074 4 DKILILDFGSQYTQLIARRVRELGVYSEIVPYDISAEEIRAFNPKGIILSGGPASVYEEGAPRADPEIFELGVPVLGICY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 94 GLHVTAHLLGGEISRAETREYGPAPVEVVTNHEITSGVSRRFTSWMSHGDAIRRLPPGAREIATTSHGVTAIVTIPEASF 173
Cdd:PRK00074 84 GMQLMAHQLGGKVERAGKREYGRAELEVDNDSPLFKGLPEEQDVWMSHGDKVTELPEGFKVIASTENCPIAAIANEERKF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 174 VGLQFHPEVTHSEQGLQILDNFAAGVCQARRQWSVENYLEQLQGELRGQAGDKPILLLISGGVDSSVVAALLLQTFPpEQ 253
Cdd:PRK00074 164 YGVQFHPEVTHTPQGKKLLENFVFDICGCKGDWTMENFIEEAIEEIREQVGDKKVILGLSGGVDSSVAAVLLHKAIG-DQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 254 IHLMYIDTGLMRKDESVEIGAALRKLGARNLYLIDAEERFLSALAGAVDPEKKRHIIGDLFISVQEDEiASRLSGDYLLA 333
Cdd:PRK00074 243 LTCVFVDHGLLRKNEAEQVMEMFREHFGLNLIHVDASDRFLSALAGVTDPEEKRKIIGREFIEVFEEE-AKKLGGVKFLA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 334 QGTLYTDLIESGhGSGGTAKsIKSHHNVAsplvrkkreaGL-------ILEPLAALYKDEVRDLGRLLGLPEEIVGRHPF 406
Cdd:PRK00074 322 QGTLYPDVIESG-GTKKAAT-IKSHHNVG----------GLpedmklkLVEPLRELFKDEVRKLGLELGLPEEIVYRHPF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 407 PGPGLGVRVLGEVTRERCDILREADAIFIRELRKAGLYDAIWQAFAVLLPIQSVGVAGDSRAYGNVVALRAVTSTDGMTA 486
Cdd:PRK00074 390 PGPGLAIRILGEVTKEKLDILREADAIFIEELRKAGLYDKIWQAFAVLLPVKSVGVMGDGRTYDYVVALRAVTSIDGMTA 469
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1339315715 487 DVYGFEPAFLRTVSAAITNGIPQVGRVVYDCSGKPPATIEWE 528
Cdd:PRK00074 470 DWARLPYDFLEKISNRIINEVKGVNRVVYDITSKPPATIEWE 511
|
|
| GuaA2 |
COG0519 |
GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, ... |
16-528 |
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: 661.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 16 IVILDFGSQTTHLIGRRIREQGIFAEIVAGTAPMEDWIDEGVRGVILSGSPSSIHDEDAPLPDRRIYSRGIPLLGICYGL 95
Cdd:COG0519 6 IIVLDFGGQYQQLIARRRREEGVYSEIIPPDTAAEEIKAKGPPGIILSGGPSSVYEEGAPPDDPELFELGGPILGICYGG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 96 HVTAHLLGGEISRAETREYGPAPVEVVTNHEITSGVSRRFTSWMSHGDAIRRLPPGAREIATTSHGVTAIVTIPEASFVG 175
Cdd:COG0519 86 QLMLHLLGGGVVRAERREYGGALLLVDDESDLFAGGPEELQVWMSHGDRVTELPPGFEVIASTENCPVAAIANEERKLYG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 176 LQFHPEVTHSEQGLQILDNFAAGVCQARRQWSVENYLEQLQGELRGQAGDKPILLLISGGVDSSVVAALLLQTFPpEQIH 255
Cdd:COG0519 166 VQFHPEVVHTEQGKEILKNFLFDICGCKGDWTMENFIEEAIEEIREQVGDGKVICALSGGVDSSVAAALLHKAIG-DQLT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 256 LMYIDTGLMRKDESVEIGAALR-KLGArNLYLIDAEERFLSALAGAVDPEKKRHIIGDLFISVQEDEiASRLSGDYLLAQ 334
Cdd:COG0519 245 CVFVDHGLLRKGEAEQVEETFKeHFGL-NLIYVDASERFLSALKGVTDPEEKRKIIGEEFIEVFEEE-AKKLGGAKFLAQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 335 GTLYTDLIESGhGSGGTAKSIKSHHNVASPLVRKKREaglILEPLAALYKDEVRDLGRLLGLPEEIVGRHPFPGPGLGVR 414
Cdd:COG0519 323 GTLYPDVIESG-SVKGPAATIKSHHNVGGLPEDMKFK---LVEPLRELFKDEVRALGRELGLPEEIVYRHPFPGPGLAIR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 415 VLGEVTRERCDILREADAIFIRELRKAGLYDAIWQAFAVLLPIQSVGVAGDSRAYGNVVALRAVTSTDGMTADVYGFEPA 494
Cdd:COG0519 399 ILGEVTKEKLEILREADAIFIEELRKAGLYDKVWQAFAVLLPVKSVGVMGDERTYEYVVALRAVTSVDGMTADWARLPYE 478
|
490 500 510
....*....|....*....|....*....|....
gi 1339315715 495 FLRTVSAAITNGIPQVGRVVYDCSGKPPATIEWE 528
Cdd:COG0519 479 VLERISNRIINEVKGVNRVVYDITSKPPATIEWE 512
|
|
| PLN02347 |
PLN02347 |
GMP synthetase |
10-528 |
0e+00 |
|
GMP synthetase
Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 568.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 10 PSGTDRIVILDFGSQTTHLIGRRIREQGIFAEIVAGTAPMEDWIDEGVRGVILSGSPSSIHDEDAP-LPD---RRIYSRG 85
Cdd:PLN02347 7 KSYLDVVLILDYGSQYTHLITRRVRELGVYSLLLSGTASLDRIASLNPRVVILSGGPHSVHVEGAPtVPEgffDYCRERG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 86 IPLLGICYGLHVTAHLLGGEISRAETREYGPAPVEVVTNHEI--TSGVSRRFTSWMSHGDAIRRLPPGAREIATTSHGVT 163
Cdd:PLN02347 87 VPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCGSQLfgDLPSGETQTVWMSHGDEAVKLPEGFEVVAKSVQGAV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 164 AIVTIPEASFVGLQFHPEVTHSEQGLQILDNFAAGVCQARRQWSVENYLEQLQGELRGQAG-DKPILLLISGGVDSSVvA 242
Cdd:PLN02347 167 VAIENRERRIYGLQYHPEVTHSPKGMETLRHFLFDVCGVTADWKMQDVLEEQIELIKATVGpDEHVICALSGGVDSTV-A 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 243 ALLLQTFPPEQIHLMYIDTGLMRKDESVEIGAALRklgaRNLYL----IDAEERFLSALAGAVDPEKKRHIIGDLFISVQ 318
Cdd:PLN02347 246 ATLVHKAIGDRLHCVFVDNGLLRYKEQERVMETFK----RDLHLpvtcVDASERFLSKLKGVTDPEKKRKIIGAEFIEVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 319 eDEIASRL---SG---DYLLaQGTLYTDLIES--GHGSGGT-AKSIKSHHNVAS-PLVRKKReaglILEPLAALYKDEVR 388
Cdd:PLN02347 322 -DEFAHKLeqkLGkkpAFLV-QGTLYPDVIEScpPPGSGRThSHTIKSHHNVGGlPKDMKLK----LIEPLKLLFKDEVR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 389 DLGRLLGLPEEIVGRHPFPGPGLGVRVLGEVTRERC-DILREADAIFIRELRKAGLYDAIWQAFAVLLPIQSVGVAGDSR 467
Cdd:PLN02347 396 KLGRLLGVPEAFLKRHPFPGPGLAVRVLGDVTEGNAlDILRQVDEIFINSIKDAGLYDEIWQAFAVFLPVKSVGVQGDQR 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1339315715 468 AYGNVVALRAVTSTDGMTADVYGFEPAFLRTVSAAITNGIPQVGRVVYDCSGKPPATIEWE 528
Cdd:PLN02347 476 THSHVVALRAVTSEDGMTADWYHFEHKFLDDVSRKICNEVRGVNRVVYDITSKPPSTIEWE 536
|
|
| GMP_synthase_C |
cd01997 |
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ... |
219-528 |
4.93e-155 |
|
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: 444.68 E-value: 4.93e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 219 LRGQAGDKPILLLISGGVDSSVVAALLLQTFPPEQIHLMYIDTGLMRKDESVEIGAALRKLGARNLYLIDAEERFLSALA 298
Cdd:cd01997 1 IKRTVGDKKVLCLVSGGVDSTVCAALLHKALGDERVIAVHIDNGLMRKNESEQVEEALKKLGVINLAKVDASKRFLKKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 299 GAVDPEKKRHIIGDLFISVQEDEIAS--RLSGDYLLAQGTLYTDLIESG-HGSGGTAKSIKSHHNVaSPLVRKKrEAGLI 375
Cdd:cd01997 81 GVTDPEEKRKIIGDTFIEVFDEVAKElnLDPDDVYLAQGTLYPDLIESAsSLASSKADTIKTHHNV-GGLPREL-LKGKL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 376 LEPLAALYKDEVRDLGRLLGLPEEIVGRHPFPGPGLGVRVLGEVTRERCDILREADAIFIRELRKAGLYDAIWQAFAVLL 455
Cdd:cd01997 159 VEPLRDLFKDEVRELGRELGLPEELVWRHPFPGPGLAIRVLGEVTPEKLEILREADAIVEEELREAGLYDKISQAFAVLL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1339315715 456 PIQSVGVAGDSRAYGNVVALRAVTSTDGMTADVYGFEPAFLRTVSAAITNGIPQVGRVVYDCSGKPPATIEWE 528
Cdd:cd01997 239 PIKSVGVQGDGRTYGYVVALRAVETEDFMTAEWARPPYEVLDKISNRITNEVPGVNRVVYDITSKPPATIEWE 311
|
|
| guaA_Cterm |
TIGR00884 |
GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; This protein of purine ... |
210-528 |
1.54e-134 |
|
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: 392.47 E-value: 1.54e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 210 NYLEQLQGELRGQAGDKPILLLISGGVDSSVvAALLLQTFPPEQIHLMYIDTGLMRKDESVEIGAALRKLGARNLYLIDA 289
Cdd:TIGR00884 1 NFIEEAVEEIREQVGDAKVIIALSGGVDSSV-AAVLAHRAIGDRLTCVFVDHGLLRKGEAEQVVKTFGDRLGLNLVYVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 290 EERFLSALAGAVDPEKKRHIIGDLFISVQEDEiASRLSGDYLLAQGTLYTDLIESGhgsGGTAKSIKSHHNVASPLVRKK 369
Cdd:TIGR00884 80 KERFLSALKGVTDPEEKRKIIGRVFIEVFERE-AKKIGDAEYLAQGTIYPDVIESA---AGTAHVIKSHHNVGGLPEDMK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 370 REaglILEPLAALYKDEVRDLGRLLGLPEEIVGRHPFPGPGLGVRVLGEVTRERCDILREADAIFIRELRKAGLYDAIWQ 449
Cdd:TIGR00884 156 LK---LVEPLRELFKDEVRKLGKELGLPEEIVWRHPFPGPGLAVRVLGEVTKEKLEILRRADAIVIEELKKAGLYDKVWQ 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1339315715 450 AFAVLLPIQSVGVAGDSRAYGNVVALRAVTSTDGMTADVYGFEPAFLRTVSAAITNGIPQVGRVVYDCSGKPPATIEWE 528
Cdd:TIGR00884 233 AFAVLLPVKSVGVMGDGRTYGYVIALRAVESIDGMTADWARLPYDFLERISNRITNEVPGVNRVVYDITSKPPATIEWE 311
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
16-196 |
1.13e-73 |
|
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: 231.66 E-value: 1.13e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 16 IVILDFGSQTTHLIGRRIREQGIFAEIVAGTAPMEDWIDEGVRGVILSGSPSSIHDEDAPLPDRRIYSRGIPLLGICYGL 95
Cdd:cd01742 1 ILILDFGSQYTHLIARRVRELGVYSEILPNTTPLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGICYGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 96 HVTAHLLGGEISRAETREYGPAPVEVVTNHEITSGVSRRFTSWMSHGDAIRRLPPGAREIATTSHGVTAIVTIPEASFVG 175
Cdd:cd01742 81 QLIAKALGGKVERGDKREYGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVVKLPEGFKVIASSDNCPVAAIANEEKKIYG 160
|
170 180
....*....|....*....|.
gi 1339315715 176 LQFHPEVTHSEQGLQILDNFA 196
Cdd:cd01742 161 VQFHPEVTHTEKGKEILKNFL 181
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
16-202 |
1.51e-72 |
|
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: 228.74 E-value: 1.51e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 16 IVILDFGSQTTHLIGRRIREQGIFAEIVAGTAPMEDWIDEGVRGVILSGSPSSIHDEDAPLPDRRIYSRGIPLLGICYGL 95
Cdd:TIGR00888 1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGPSSVYAENAPRADEKIFELGVPVLGICYGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 96 HVTAHLLGGEISRAETREYGPAPVEVVTNHEITSGVSRRFTSWMSHGDAIRRLPPGAREIATTSHGVTAIVTIPEASFVG 175
Cdd:TIGR00888 81 QLMAKQLGGEVGRAEKREYGKAELEILDEDDLFRGLPDESTVWMSHGDKVKELPEGFKVLATSDNCPVAAMAHEEKPIYG 160
|
170 180
....*....|....*....|....*..
gi 1339315715 176 LQFHPEVTHSEQGLQILDNFAAGVCQA 202
Cdd:TIGR00888 161 VQFHPEVTHTEYGNELLENFVYDVCGC 187
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
15-199 |
1.17e-52 |
|
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: 178.22 E-value: 1.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 15 RIVILD---FGSQTTHLIGRRIREQGIFAEIV---AGTAPMEDWIDEGVRGVILSGSPSSIHDEDAPLPD-----RRIYS 83
Cdd:COG0518 1 KILILDhdpFGGQYPGLIARRLREAGIELDVLrvyAGEILPYDPDLEDPDGLILSGGPMSVYDEDPWLEDepaliREAFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 84 RGIPLLGICYGLHVTAHLLGGEISRAETREYGPAPVEVVTNHEITSGVSRRFTSWMSHGDAIRRLPPGAREIATTSHGVT 163
Cdd:COG0518 81 LGKPVLGICYGAQLLAHALGGKVEPGPGREIGWAPVELTEADPLFAGLPDEFTVWMSHGDTVTELPEGAEVLASSDNCPN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1339315715 164 AIVTIpEASFVGLQFHPEVTHS------------------------------EQGLQILDNFAAGV 199
Cdd:COG0518 161 QAFRY-GRRVYGVQFHPEVTHTmmeawleeradelaaeellaeaslhdpelrEAGRRLLRNFLREI 225
|
|
| GMP_synt_C |
pfam00958 |
GMP synthase C terminal domain; GMP synthetase is a glutamine amidotransferase from the de ... |
437-527 |
5.36e-51 |
|
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: 169.13 E-value: 5.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 437 ELRKAGLYDAIWQAFAVLLPIQSVGVAGDSRAYGNVVALRAVTSTDGMTADVYGFEPAFLRTVSAAITNGIPQVGRVVYD 516
Cdd:pfam00958 2 EIKKAGLYRKIWQAFAVLLPVKSVGVMGDERTYEYVVALRAVTSTDGMTADWARLPYEVLEKISNRIVNEVPGVNRVVYD 81
|
90
....*....|.
gi 1339315715 517 CSGKPPATIEW 527
Cdd:pfam00958 82 ITSKPPATIEW 92
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
15-201 |
3.98e-42 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 148.85 E-value: 3.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 15 RIVILDFGSQTTHLIGRRIREQGIFAEIVAGTAPMEDwIDEGVRGVILSGSPSSihdEDAPLPDRRIYSRGIPLLGICYG 94
Cdd:PRK00758 1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTTPVEE-IKAFEDGLILSGGPDI---ERAGNCPEYLKELDVPILGICLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 95 LHVTAHLLGGEISRAETREYGPAPVEVVTNHEITSGVSRRFTSWMSHGDAIRRLPPGAREIATTSH-GVTAIVTiPEASF 173
Cdd:PRK00758 77 HQLIAKAFGGEVGRGEYGEYALVEVEILDEDDILKGLPPEIRVWASHADEVKELPDGFEILARSDIcEVEAMKH-KEKPI 155
|
170 180
....*....|....*....|....*...
gi 1339315715 174 VGLQFHPEVTHSEQGLQILDNFAAgVCQ 201
Cdd:PRK00758 156 YGVQFHPEVAHTEYGEEIFKNFLE-ICG 182
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
17-195 |
1.36e-33 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 125.81 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 17 VILDFGSQTTHLIGRRIREQGIFAEIVAGTAPMEDWIDEGVRGVILSGSPSSIHD-EDAPLPDRRIYSRGIPLLGICYGL 95
Cdd:pfam00117 1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAaGGAIEAIREARELKIPILGICLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 96 HVTAHLLGGEISRAETREYGPAPVEVV-TNHEITSGVSRRFTSWMSHGDAIRR--LPPGAREIATTSHGVT--AIVTIPE 170
Cdd:pfam00117 81 QLLALAFGGKVVKAKKFGHHGKNSPVGdDGCGLFYGLPNVFIVRRYHSYAVDPdtLPDGLEVTATSENDGTimGIRHKKL 160
|
170 180
....*....|....*....|....*
gi 1339315715 171 AsFVGLQFHPEVTHSEQGLQILDNF 195
Cdd:pfam00117 161 P-IFGVQFHPESILTPHGPEILFNF 184
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
55-181 |
9.11e-23 |
|
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: 95.78 E-value: 9.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 55 EGVRGVILSGSPSSIHDEDAP-LPD-----RRIYSRGIPLLGICYGLHVTAHLLGGEISRAET-REYGPAPVEVV---TN 124
Cdd:cd01741 45 DDYDGLVILGGPMSVDEDDYPwLKKlkeliRQALAAGKPVLGICLGHQLLARALGGKVGRNPKgWEIGWFPVTLTeagKA 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1339315715 125 HEITSGVSRRFTSWMSHGDAIRRLPPGAREIATTSHGVTAIVTIPEaSFVGLQFHPE 181
Cdd:cd01741 125 DPLFAGLPDEFPVFHWHGDTVVELPPGAVLLASSEACPNQAFRYGD-RALGLQFHPE 180
|
|
| PRK07567 |
PRK07567 |
glutamine amidotransferase; Provisional |
55-181 |
1.27e-13 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181035 [Multi-domain] Cd Length: 242 Bit Score: 70.74 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 55 EGVRGVILSGSPSSIHD---EDAPLPDR----------RIYSRGIPLLGICYGLHVTAHLLGGEISRAETREYGPAPVEv 121
Cdd:PRK07567 50 DDYSGVIVGGSPFNVSDpaeSKSPWQRRveaelsglldEVVARDFPFLGACYGVGTLGHHQGGVVDRTYGEPVGAVTVS- 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 122 VTNH----EITSGVSRRFTSWMSHGDAIRRLPPGAREIATTShgvtaivTIPEASF-VG-----LQFHPE 181
Cdd:PRK07567 129 LTDAgradPLLAGLPDTFTAFVGHKEAVSALPPGAVLLATSP-------TCPVQMFrVGenvyaTQFHPE 191
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
59-195 |
5.68e-13 |
|
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: 67.17 E-value: 5.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 59 GVILS---GSPssihDEDAPLPD-RRIYSRGIPLLGICYGLHVTAHLLGGEISRAETREYGPAPVEVVTNHEITSGVSRR 134
Cdd:cd01743 45 AIVISpgpGHP----EDAGISLEiIRALAGKVPILGVCLGHQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQP 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1339315715 135 FT-----SWMSHGDairRLPPGAREIATTSHGVTAIVTIPEASFVGLQFHPEVTHSEQGLQILDNF 195
Cdd:cd01743 121 FTvgryhSLVVDPD---PLPDLLEVTASTEDGVIMALRHRDLPIYGVQFHPESILTEYGLRLLENF 183
|
|
| PRK09065 |
PRK09065 |
glutamine amidotransferase; Provisional |
55-184 |
2.89e-12 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181635 [Multi-domain] Cd Length: 237 Bit Score: 66.52 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 55 EGVRGVILSGSPSSIHDEdAPLPD------RRIYSRGIPLLGICYGLHVTAHLLGGEIS-RAETREYGPAPVEVVT---N 124
Cdd:PRK09065 53 DDFAGVIITGSWAMVTDR-LDWSErtadwlRQAAAAGMPLLGICYGHQLLAHALGGEVGyNPAGRESGTVTVELHPaaaD 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1339315715 125 HEITSGVSRRFTSWMSHGDAIRRLPPGAREIATTSH-GVTAIVTIPEAsfVGLQFHPEVTH 184
Cdd:PRK09065 132 DPLFAGLPAQFPAHLTHLQSVLRLPPGAVVLARSAQdPHQAFRYGPHA--WGVQFHPEFTA 190
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
57-195 |
1.97e-10 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 60.13 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 57 VRGVILSGSPSSIHDEDAPLPDRRIYSRGIPLLGICYGLHVTAHLLGGEISRAETREYGPAPVEVVTNHEITSGVSRRFT 136
Cdd:CHL00101 44 IRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCLGHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFT 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1339315715 137 SWMSHGDAIRRL-PPGARE-IATTSHGVtaIVTIPEASF---VGLQFHPEVTHSEQGLQILDNF 195
Cdd:CHL00101 124 ATRYHSLIIDPLnLPSPLEiTAWTEDGL--IMACRHKKYkmlRGIQFHPESLLTTHGQQILRNF 185
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
16-181 |
4.11e-10 |
|
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: 59.05 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 16 IVILDFGSQttHLIGRRIREQGIFAEIVAGTAPMEDWIDEGVRGVILS---GSPSSIHDEDAPLpdRRIYSRGIPLLGIC 92
Cdd:cd01744 1 VVVIDFGVK--HNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSngpGDPALLDEAIKTV--RKLLGKKIPIFGIC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 93 YGLHVTAHLLGGEISRAetrEYG------PApVEVVTNH-EITSgvsrrftswMSHGDAIRR--LPPGAREiattSH--- 160
Cdd:cd01744 77 LGHQLLALALGAKTYKM---KFGhrgsnhPV-KDLITGRvYITS---------QNHGYAVDPdsLPGGLEV----THvnl 139
|
170 180
....*....|....*....|...
gi 1339315715 161 --GVTAIVTIPEASFVGLQFHPE 181
Cdd:cd01744 140 ndGTVEGIRHKDLPVFSVQFHPE 162
|
|
| NAD_synthase |
cd00553 |
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ... |
215-405 |
6.08e-10 |
|
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: 59.88 E-value: 6.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 215 LQGELRgQAGDKPILLLISGGVDSSVVAALLLQTFPPEQIH---LMYIDTGlmrkDESVEIGAAL-RKLGARnLYLID-- 288
Cdd:cd00553 14 LRDYLR-KSGAKGFVLGLSGGIDSAVVAALAVRALGAENVLaliMPSRYSS----KETRDDAKALaENLGIE-YRTIDid 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 289 -AEERFLSALAGAVDPEKKRHIIGDlfisvqedeIASRLSGD--YLLAQ-------GTlyTDLIES--------GHGSGG 350
Cdd:cd00553 88 pIVDAFLKALEHAGGSEAEDLALGN---------IQARLRMVllYALANllgglvlGT--GNKSELllgyftkyGDGAAD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1339315715 351 taksikshhnvasplvrkkreagliLEPLAALYKDEVRDLGRLLGLPEEIVGRHP 405
Cdd:cd00553 157 -------------------------INPIGDLYKTQVRELARYLGVPEEIIEKPP 186
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
59-195 |
9.75e-09 |
|
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: 55.04 E-value: 9.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 59 GVILS---GSPssihdEDAPLPDR--RIYSRGIPLLGICYGLHVTAHLLGGEISRAetreygPAPV-----EV-VTNHEI 127
Cdd:COG0512 45 GIVLSpgpGTP-----EEAGISLEviRAFAGKIPILGVCLGHQAIGEAFGGKVVRA------PEPMhgktsPItHDGSGL 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1339315715 128 TSGVSRRFT-----SWmshgdAIRR--LPPGAREIATTSHGVTAIVTIPEASFVGLQFHPEVTHSEQGLQILDNF 195
Cdd:COG0512 114 FAGLPNPFTatryhSL-----VVDRetLPDELEVTAWTEDGEIMGIRHRELPIEGVQFHPESILTEHGHQLLANF 183
|
|
| nadE |
TIGR00552 |
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ... |
209-408 |
1.34e-08 |
|
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: 55.86 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 209 ENYLEQLQGELRG---QAGDKPILLLISGGVDSSVVAALLLQTFpPEQIHLMYIDTGLMRKDESVEIGAALRKLGARNLY 285
Cdd:TIGR00552 3 IKYVEEIEDFLRGyvqKSGAKGVVLGLSGGIDSAVVAALCVEAL-GEQNHALLLPHSVQTPEQDVQDALALAEPLGINYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 286 LIDAEE--RFLSALAGAVDPEKKRHIIGDL----------FISVQEDEIASRLS--GDYLLAQGTLYtdliesghGSGGT 351
Cdd:TIGR00552 82 NIDIAPiaASFQAQTETGDELSDFLAKGNLkarlrmaalyAIANKHNLLVLGTGnkSELMLGYFTKY--------GDGGC 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1339315715 352 AksikshhnvasplvrkkreagliLEPLAALYKDEVRDLGRLLGLPEEIVGRHP----FPG 408
Cdd:TIGR00552 154 D-----------------------IAPIGDLFKTQVYELAKRLNVPERIIEKPPtadlFDG 191
|
|
| PuuD |
COG2071 |
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
55-197 |
1.88e-08 |
|
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: 55.17 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 55 EGVRGVILSGSP---------SSIHDEDAPLPDR---------RIYSRGIPLLGICYGLHVTAHLLGG----EIS----- 107
Cdd:COG2071 48 DRLDGLVLTGGAdvdpalygeEPHPELGPIDPERdafelalirAALERGKPVLGICRGMQLLNVALGGtlyqDLPdqvpg 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 108 ----RAETREYGPA-PVEVVTN---HEITSGVSRRFTSWmsHGDAIRRLPPGAREIATTSHGVTAIVTIPEASFV-GLQF 178
Cdd:COG2071 128 aldhRQPAPRYAPRhTVEIEPGsrlARILGEEEIRVNSL--HHQAVKRLGPGLRVSARAPDGVIEAIESPGAPFVlGVQW 205
|
170 180
....*....|....*....|.
gi 1339315715 179 HPE--VTHSEQGLQILDNFAA 197
Cdd:COG2071 206 HPEwlAASDPLSRRLFEAFVE 226
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
86-195 |
2.47e-08 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 53.98 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 86 IPLLGICYGLHVTAHLLGGEISRAETREYGPA-PVEVvTNHEITSGVSRRFTSWMSHGDAIRR--LPPGAREIATTSHGV 162
Cdd:PRK05670 73 VPILGVCLGHQAIGEAFGGKVVRAKEIMHGKTsPIEH-DGSGIFAGLPNPFTVTRYHSLVVDResLPDCLEVTAWTDDGE 151
|
90 100 110
....*....|....*....|....*....|...
gi 1339315715 163 TAIVTIPEASFVGLQFHPEVTHSEQGLQILDNF 195
Cdd:PRK05670 152 IMGVRHKELPIYGVQFHPESILTEHGHKLLENF 184
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
59-181 |
5.18e-08 |
|
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: 53.41 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 59 GVILSGSPS---------SIHDEDAPLPDRRIYS---------RGIPLLGICYGLHVTAHLLGG----EIS----RAETR 112
Cdd:pfam07722 61 GLLLTGGPNvdphfygeePSESGGPYDPARDAYElaliraalaRGKPILGICRGFQLLNVALGGtlyqDIQeqpgFTDHR 140
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1339315715 113 E------YGPA-PVEVVTNHEITSGVSRRFTSWMS-HGDAIRRLPPGAREIATTSHG-VTAIVTIPEASFV-GLQFHPE 181
Cdd:pfam07722 141 EhcqvapYAPShAVNVEPGSLLASLLGSEEFRVNSlHHQAIDRLAPGLRVEAVAPDGtIEAIESPNAKGFAlGVQWHPE 219
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
50-200 |
1.60e-07 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 51.97 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 50 EDWIDEGVRGVILSGSPSSIHDEDAPLPDRRIY-SRGIPLLGICYGLHVTAHLLGGEISRAETREYGPAPVEVVTNHEIT 128
Cdd:PRK07765 40 EAAVAAQFDGVLLSPGPGTPERAGASIDMVRACaAAGTPLLGVCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVL 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1339315715 129 SGVSRRFTSWMSHGDAI--RRLPPGAREIATTSHGVTAIVTIPEASFVGLQFHPEVTHSEQGLQILDNFAAgVC 200
Cdd:PRK07765 120 AGLPDPFTATRYHSLTIlpETLPAELEVTARTDSGVIMAVRHRELPIHGVQFHPESVLTEGGHRMLANWLT-VC 192
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
51-181 |
1.79e-07 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153216 [Multi-domain] Cd Length: 189 Bit Score: 51.42 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 51 DWIDegvrGVILSGSPS---------SIHDEDAPLPDRRIYS---------RGIPLLGICYGLHVTAHLLGGEISRAEtr 112
Cdd:cd01745 52 ELLD----GLLLTGGGDvdpplygeePHPELGPIDPERDAFElallraaleRGKPILGICRGMQLLNVALGGTLYQDI-- 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 113 eygpapvevvtnhEITSGvsrrftswmsHGDAIRRLPPGAREIATTSHG-VTAIVTIPEASFVGLQFHPE 181
Cdd:cd01745 126 -------------RVNSL----------HHQAIKRLADGLRVEARAPDGvIEAIESPDRPFVLGVQWHPE 172
|
|
| PRK13980 |
PRK13980 |
NAD synthetase; Provisional |
208-408 |
1.96e-07 |
|
NAD synthetase; Provisional
Pssm-ID: 184435 [Multi-domain] Cd Length: 265 Bit Score: 52.52 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 208 VENYLEQ-LQGELRGqAGDKPILLLISGGVDSSVVAALLLQTFPPEQIH--LM-YIDTglmrKDESVEigAALR---KLG 280
Cdd:PRK13980 13 VREIIVDfIREEVEK-AGAKGVVLGLSGGIDSAVVAYLAVKALGKENVLalLMpSSVS----PPEDLE--DAELvaeDLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 281 ARnlY-LIDAE---ERFLSALagavdPEKKRHIIGDL----------FISVQEDeiasRL---SGD---YLLAQGTLYtd 340
Cdd:PRK13980 86 IE--YkVIEITpivDAFFSAI-----PDADRLRVGNImartrmvllyDYANREN----RLvlgTGNkseLLLGYFTKY-- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1339315715 341 liesghGSGGTAksikshhnvasplvrkkreagliLEPLAALYKDEVRDLGRLLGLPEEIVGRHPFPG 408
Cdd:PRK13980 153 ------GDGAVD-----------------------LNPIGDLYKTQVRELARHLGVPEDIIEKPPSAD 191
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
225-291 |
6.68e-07 |
|
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: 50.35 E-value: 6.68e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1339315715 225 DKPILLLISGGVDSSVVAALLLQTFPPEQIHLMYIDTGLMRKDESVEIGAALRKLGAR-NLYLIDAEE 291
Cdd:cd01991 2 DVPVGVLLSGGLDSSLIAALAARLLPETPIDLFTVGFEGSPTPDRAAARRVAEELGTEhHEVEVTIEE 69
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
60-195 |
8.50e-07 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 49.53 E-value: 8.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 60 VILSGSPSSIHDEDAPLPDRRIYSRGIPLLGICYGLHVTAHLLGGEISRAETREYGPAPVEVVTNHEITSGVSRRFTSWM 139
Cdd:PRK08007 47 IVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTR 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1339315715 140 SHGDAIR--RLPPGAREIATTSHGVTAIVTIPEASFVGLQFHPEVTHSEQGLQILDNF 195
Cdd:PRK08007 127 YHSLVVEpdSLPACFEVTAWSETREIMGIRHRQWDLEGVQFHPESILSEQGHQLLANF 184
|
|
| puuD |
PRK11366 |
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional |
59-189 |
1.53e-06 |
|
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
Pssm-ID: 183101 [Multi-domain] Cd Length: 254 Bit Score: 49.51 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 59 GVILSGSPSSIH--------DEDAPLPDRRIYS---------RGIPLLGICYGLHVTAHLLGGEISRA--------ETRE 113
Cdd:PRK11366 64 GIYLPGSPSNVQphlygengDEPDADPGRDLLSmalinaaleRRIPIFAICRGLQELVVATGGSLHRKlceqpellEHRE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 114 YGPAPVE--VVTNHEIT---SGVSRRF-----TSWMS--HGDAIRRLPPGAREIATTSHGVTAIVTIPEASFV-GLQFHP 180
Cdd:PRK11366 144 DPELPVEqqYAPSHEVQveeGGLLSALlpecsNFWVNslHGQGAKVVSPRLRVEARSPDGLVEAVSVINHPFAlGVQWHP 223
|
....*....
gi 1339315715 181 EVTHSEQGL 189
Cdd:PRK11366 224 EWNSSEYAL 232
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
60-195 |
2.62e-06 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 48.26 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 60 VILSGSPSSIHDEDAPLPDRRIYSRGIPLLGICYGLHVTAHLLGGEISRAETREYGPAPVEVVTNHEITSGVSRRFTSWM 139
Cdd:PRK07649 47 LMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATR 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1339315715 140 SHGDAIRR--LPPGAREIATTSHGVTAIVTIPEASFVGLQFHPEVTHSEQGLQILDNF 195
Cdd:PRK07649 127 YHSLIVKKetLPDCLEVTSWTEEGEIMAIRHKTLPIEGVQFHPESIMTSHGKELLQNF 184
|
|
| PRK05665 |
PRK05665 |
amidotransferase; Provisional |
82-184 |
2.99e-06 |
|
amidotransferase; Provisional
Pssm-ID: 168162 [Multi-domain] Cd Length: 240 Bit Score: 48.65 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 82 YSRGIPLLGICYGLHVTAHLLGGEISRAE------TREYGPAPVEVVTNHEITSgvsrrFTSWMSHGDAIRRLPPGAREI 155
Cdd:PRK05665 88 YERGDKLLGVCFGHQLLALLLGGKAERASqgwgvgIHRYQLAAHAPWMSPAVTE-----LTLLISHQDQVTALPEGATVI 162
|
90 100
....*....|....*....|....*....
gi 1339315715 156 ATTSHGVTAIVTIpEASFVGLQFHPEVTH 184
Cdd:PRK05665 163 ASSDFCPFAAYHI-GDQVLCFQGHPEFVH 190
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
60-197 |
3.37e-06 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 47.95 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 60 VILSGSPSSIHDEDAPLPDRRIYSRGIPLLGICYGLHVTAHLLGGEISRAETREYGPAPVEVVTNHEITSGVSRRFTSWM 139
Cdd:PRK08857 47 LVISPGPCTPNEAGISLQAIEHFAGKLPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTR 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1339315715 140 SHGDAIRR--LPPGAREIATTSH---GVTAIVTIPEASFV--GLQFHPEVTHSEQGLQILDNFAA 197
Cdd:PRK08857 127 YHSLVVKNdtLPECFELTAWTELedgSMDEIMGFQHKTLPieAVQFHPESIKTEQGHQLLANFLA 191
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
60-195 |
3.78e-06 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 47.55 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 60 VILSGSPSSIHDEDAPLPDRRIYSRGIPLLGICYGLHVTAHLLGGEISRAETREYGPAPVEVVTNHEITSGVSRRFTSWM 139
Cdd:PRK06774 47 LVISPGPCTPNEAGISLAVIRHFADKLPILGVCLGHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTR 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1339315715 140 SHGDAI--RRLPPGAREIATTSHG--VTAIVTIPEASFV--GLQFHPEVTHSEQGLQILDNF 195
Cdd:PRK06774 127 YHSLVIaaDSLPGCFELTAWSERGgeMDEIMGIRHRTLPleGVQFHPESILSEQGHQLLDNF 188
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
15-181 |
1.37e-05 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 47.48 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 15 RIVILDFGSQTThlIGRRIREQGIFAEIVAGTAPMEDWIDEGVRGVILS---GSPSSIHDEDAPLpdRRIYSRGIPLLGI 91
Cdd:CHL00197 194 KIIVIDFGVKYN--ILRRLKSFGCSITVVPATSPYQDILSYQPDGILLSngpGDPSAIHYGIKTV--KKLLKYNIPIFGI 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 92 CYGLHVTAHLLGGEISRAETREYG-PAPVEVVTNHEITS---GVSRRFTSWMSHGDAIRRLPPGAREIATTSHGVTAIVT 167
Cdd:CHL00197 270 CMGHQILSLALEAKTFKLKFGHRGlNHPSGLNQQVEITSqnhGFAVNLESLAKNKFYITHFNLNDGTVAGISHSPKPYFS 349
|
170
....*....|....
gi 1339315715 168 IpeasfvglQFHPE 181
Cdd:CHL00197 350 V--------QYHPE 355
|
|
| hisH |
PRK13141 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
84-199 |
2.69e-05 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 45.12 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 84 RGIPLLGIC------------YGLHVTAHLLGGEISRAETREYGPAP------VEVVTNHEITSGVSRRftSWM--SHGD 143
Cdd:PRK13141 71 SGKPLLGIClgmqllfesseeFGETEGLGLLPGRVRRFPPEEGLKVPhmgwnqLELKKESPLLKGIPDG--AYVyfVHSY 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1339315715 144 AIRRLPPGAReIATTSHG--VTAIVTIPeaSFVGLQFHPEVTHsEQGLQILDNFAAGV 199
Cdd:PRK13141 149 YADPCDEEYV-AATTDYGveFPAAVGKD--NVFGAQFHPEKSG-DVGLKILKNFVEMV 202
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
37-405 |
3.37e-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: 46.38 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 37 GIFAEIVAGTAPMEDWIDEGVRGVILSGSPSSIHDEDAPLPDRRIYSRGIPLLGICYGLHVTAHLLGGEISRAETREYGP 116
Cdd:COG0171 118 VVEEEEEEFVGGPPPPPAALGGAGVLLILSSSSSAVGAAAAAAALAAALLSSLSSAAYYAAAGGGESTTDLARGGGGGLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 117 APVEVVTNHEITSGVSRRFTSWMSHGDAIRRLPPGAREIATTSHGVTAIVTIPEASFVGLQFHPEVTHSEQGLQILDNFa 196
Cdd:COG0171 198 LVVLLLVGGGDDDFFDGGSAAVDDDDLLLLLRRRREEELLLARARDADGGRRVAAEAAPPPPEEEEMDLEEVYDALVLG- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 197 agvcqarrqwsVENYLEQlqgelrgqAGDKPILLLISGGVDSSVVAALLLQTFPPEQIH--LM-YIDTGlmrkDESVEIG 273
Cdd:COG0171 277 -----------LRDYVRK--------NGFKGVVLGLSGGIDSALVAALAVDALGPENVLgvTMpSRYTS----DESLEDA 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 274 AAL-RKLGARnLYLID---AEERFLSALAGAVDPEKKRhiigdlfisVQEDEIASRLSGDYL------------------ 331
Cdd:COG0171 334 EELaENLGIE-YEEIDitpAVEAFLEALPHAFGGELDD---------VAEENLQARIRMVILmalankfgglvlgtgnks 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 332 -LAQG--TLYTDliesgHGSGgtaksikshhnvasplvrkkreagliLEPLAALYKDEVRDLGRLLG-----LPEEIVGR 403
Cdd:COG0171 404 eLAVGyfTKYGD-----GAGD--------------------------LAPIADLYKTQVYALARWLNrngevIPEDIIDK 452
|
..
gi 1339315715 404 HP 405
Cdd:COG0171 453 PP 454
|
|
| PRK06490 |
PRK06490 |
glutamine amidotransferase; Provisional |
55-185 |
3.94e-05 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 180590 [Multi-domain] Cd Length: 239 Bit Score: 45.34 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 55 EGVRGVILSGSPSSIHDEDA-----------PLPDRRiysrgiPLLGICYGLHVTAHLLGGEIS-RAETR-EYGPAPVEV 121
Cdd:PRK06490 51 EDHAGAVIFGGPMSANDPDDfirreidwisvPLKENK------PFLGICLGAQMLARHLGARVApHPDGRvEIGYYPLRP 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1339315715 122 vTNHeitsgvSRRFTSWMSHGDAIRR----LPPGAREIATTSH-GVTAIVTIPEAsfVGLQFHPEVTHS 185
Cdd:PRK06490 125 -TEA------GRALMHWPEMVYHWHRegfdLPAGAELLATGDDfPNQAFRYGDNA--WGLQFHPEVTRA 184
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
224-329 |
4.28e-05 |
|
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 46.17 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 224 GDKPILLLISGGVDSSVVAALLLQTFPPEQIHLMYIDTGLMRK-DESVEIGAALRKLGARN-LYLIDAEErFLSALAGAV 301
Cdd:TIGR01536 251 ADVPVGVLLSGGLDSSLVAAIARREAPRGPVHTFSIGFEGSPDfDESKYARKVADHLGTEHhEVLFSVEE-GLDALPEVI 329
|
90 100 110
....*....|....*....|....*....|....
gi 1339315715 302 ----DPEKKRHIIGDLFIS--VQEDEIASRLSGD 329
Cdd:TIGR01536 330 yhleEPTTIRASIPLYLLSklAREDGVKVVLSGE 363
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
86-245 |
7.02e-05 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 45.48 E-value: 7.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 86 IPLLGICYGLHVTAHLLGGEISRAETREYGPAPVEVVTNHEITSGVSRRFTSWMSHGDAIRR--LPPGAREIATTSHGVT 163
Cdd:PRK14607 74 VPILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEasLPECLEVTAKSDDGEI 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 164 AIVTIPEASFVGLQFHPEVTHSEQGLQILDNFAAGvcqARRQWSVENYLEQL-QGE-LRGQAGDKPILLLISGGVDSSVV 241
Cdd:PRK14607 154 MGIRHKEHPIFGVQFHPESILTEEGKRILKNFLNY---QREEIDIKSYLKKLvEGEdLSFEEAEDVMEDITDGNATDAQI 230
|
....
gi 1339315715 242 AALL 245
Cdd:PRK14607 231 AGFL 234
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
16-97 |
9.65e-05 |
|
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: 41.82 E-value: 9.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 16 IVILDFGSQTT---HLIGRRIREQGIFAEIVA--GTAPMEDWIDEGVRGVILSGSPSSIHDEDAPLPD----RRIYSRGI 86
Cdd:cd01653 1 VAVLLFPGFEElelASPLDALREAGAEVDVVSpdGGPVESDVDLDDYDGLILPGGPGTPDDLARDEALlallREAAAAGK 80
|
90
....*....|.
gi 1339315715 87 PLLGICYGLHV 97
Cdd:cd01653 81 PILGICLGAQL 91
|
|
| hisH |
PRK13181 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
84-196 |
9.77e-05 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 43.32 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 84 RGIPLLGICYGLHVTAHL--------LGgeISRAETREYGPAP----------VEVVTNHEITSGVS--RRFtsWMSHGd 143
Cdd:PRK13181 71 KKQPVLGICLGMQLLFESseegnvkgLG--LIPGDVKRFRSEPlkvpqmgwnsVKPLKESPLFKGIEegSYF--YFVHS- 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1339315715 144 aiRRLPPGARE--IATTSHGVTAIVTIPEASFVGLQFHPEVTHsEQGLQILDNFA 196
Cdd:PRK13181 146 --YYVPCEDPEdvLATTEYGVPFCSAVAKDNIYAVQFHPEKSG-KAGLKLLKNFA 197
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
84-195 |
1.17e-04 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153219 [Multi-domain] Cd Length: 198 Bit Score: 43.26 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 84 RGIPLLGICYGLHVTAH------------LLGGEISRAETREYGPAP------VEVVTNHEITSGVSRRftSWM----SH 141
Cdd:cd01748 70 SGKPFLGICLGMQLLFEsseegggtkglgLIPGKVVRFPASEGLKVPhmgwnqLEITKESPLFKGIPDG--SYFyfvhSY 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1339315715 142 gdairRLPPGARE--IATTSHGVTAIVTIPEASFVGLQFHPEVTHsEQGLQILDNF 195
Cdd:cd01748 148 -----YAPPDDPDyiLATTDYGGKFPAAVEKDNIFGTQFHPEKSG-KAGLKLLKNF 197
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
16-97 |
1.32e-04 |
|
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: 41.03 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 16 IVILDFGSQTT---HLIGRRIREQGIFAEIVAGTAPMEDWID--EGVRGVILSGSPSSIHDEDAPLPD----RRIYSRGI 86
Cdd:cd03128 1 VAVLLFGGSEElelASPLDALREAGAEVDVVSPDGGPVESDVdlDDYDGLILPGGPGTPDDLAWDEALlallREAAAAGK 80
|
90
....*....|.
gi 1339315715 87 PLLGICYGLHV 97
Cdd:cd03128 81 PVLGICLGAQL 91
|
|
| PRK09522 |
PRK09522 |
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ... |
16-215 |
1.53e-04 |
|
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;
Pssm-ID: 181927 [Multi-domain] Cd Length: 531 Bit Score: 44.25 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 16 IVILDFGSQTTHLIGRRIREQGIFAEIVAGTAPMEDWID--EGVRGVILSGSPSSIHDEDAP-LPDRRIYSRG-IPLLGI 91
Cdd:PRK09522 4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIErlATMSNPVLMLSPGPGVPSEAGcMPELLTRLRGkLPIIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 92 CYGLHVTAHLLGGEISRAETREYGPAPVEVVTNHEITSGVSRRFTSWMSHGDAIRRLPPGArEIATTSHGVTAIVTIPEA 171
Cdd:PRK09522 84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSNIPAGL-TINAHFNGMVMAVRHDAD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1339315715 172 SFVGLQFHPEVTHSEQGLQILDN-FAAGVCQARRQWSVENYLEQL 215
Cdd:PRK09522 163 RVCGFQFHPESILTTQGARLLEQtLAWAQQKLEPTNTLQPILEKL 207
|
|
| hisH |
PRK13170 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
147-195 |
3.62e-04 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183877 [Multi-domain] Cd Length: 196 Bit Score: 41.77 E-value: 3.62e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1339315715 147 RLPPGAREIATTSHGVTAIVTIPEASFVGLQFHPEVThSEQGLQILDNF 195
Cdd:PRK13170 146 AMPVNEYTIAQCNYGEPFSAAIQKDNFFGVQFHPERS-GAAGAQLLKNF 193
|
|
| PRK07053 |
PRK07053 |
glutamine amidotransferase; Provisional |
60-183 |
4.91e-04 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 235919 [Multi-domain] Cd Length: 234 Bit Score: 41.85 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 60 VILsGSPSSIHDEDA-P-LPD------RRIYSRGiPLLGICYGLHVTAHLLGGEISRAETREYGPAPVeVVTNH------ 125
Cdd:PRK07053 52 VVL-GGPIGVYDDELyPfLAPeiallrQRLAAGL-PTLGICLGAQLIARALGARVYPGGQKEIGWAPL-TLTDAgraspl 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1339315715 126 -EITSGVSrrFTSWmsHGDAIrRLPPGAREIATTShgvtaivTIPEASF------VGLQFHPEVT 183
Cdd:PRK07053 129 rHLGAGTP--VLHW--HGDTF-DLPEGATLLASTP-------ACRHQAFawgnhvLALQFHPEAR 181
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
2-106 |
5.37e-04 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 42.19 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 2 TTGSALTPPSGTDRIVILDFGSQttHLIGRRIREQGIFAEIVAGTAPMEDWIDEGVRGVILSGSPSSIHDEDAPLPDRRI 81
Cdd:PRK12838 156 STKEPYTYGNGGKHVALIDFGYK--KSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKK 233
|
90 100
....*....|....*....|....*
gi 1339315715 82 YSRGIPLLGICYGLHVTAHLLGGEI 106
Cdd:PRK12838 234 LISSYPILGICLGHQLIALALGADT 258
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
60-194 |
5.93e-04 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 42.60 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 60 VILSGSPSSIHDEDAPLPDRRIYSRGIPLLGICYGLHVTAHLLGGEISRAETREYG-PAPVEVVTNHEITSGVSRRFTSW 138
Cdd:PRK13566 573 VVLSPGPGRPSDFDCKATIDAALARNLPIFGVCLGLQAIVEAFGGELGQLAYPMHGkPSRIRVRGPGRLFSGLPEEFTVG 652
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1339315715 139 MSHGDAIRR--LPPGAREIATTSHGVTAIVTIPEASFVGLQFHPEVTHS---EQGLQILDN 194
Cdd:PRK13566 653 RYHSLFADPetLPDELLVTAETEDGVIMAIEHKTLPVAAVQFHPESIMTlggDVGLRIIEN 713
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
15-183 |
7.65e-04 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 41.89 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 15 RIVILDFGSQttHLIGRRIREQGIFAEIVAGTAPMEDWIDEGVRGVILS---GSPSSIhdEDAPLPDRRIYSRgIPLLGI 91
Cdd:PLN02771 242 HVIAYDFGIK--HNILRRLASYGCKITVVPSTWPASEALKMKPDGVLFSngpGDPSAV--PYAVETVKELLGK-VPVFGI 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 92 CYGLHVTAHLLGGEISRAETREYGpapvevvTNHEITSGVSRRF-TSWMSHGDAI--RRLPPGArEIA--TTSHGVTAIV 166
Cdd:PLN02771 317 CMGHQLLGQALGGKTFKMKFGHHG-------GNHPVRNNRTGRVeISAQNHNYAVdpASLPEGV-EVThvNLNDGSCAGL 388
|
170
....*....|....*..
gi 1339315715 167 TIPEASFVGLQFHPEVT 183
Cdd:PLN02771 389 AFPALNVMSLQYHPEAS 405
|
|
| nadE |
PRK00876 |
NAD(+) synthase; |
215-405 |
1.15e-03 |
|
NAD(+) synthase;
Pssm-ID: 179150 [Multi-domain] Cd Length: 326 Bit Score: 41.09 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 215 LQGELRGQAGDKPILLLISGGVDSSVVAALLLQTFPPEQIHlmyidtGLM-----RKDESVEIGAAL-RKLGARNLylid 288
Cdd:PRK00876 23 IREQVRGTLRRRGVVLGLSGGIDSSVTAALCVRALGKERVY------GLLmperdSSPESLRLGREVaEHLGVEYV---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 289 aEERFLSALAGAVDPEKKRHIIGDLFISVQED-----EIASRLSGD-----YLLAQ---GTL---------YTDLIESGH 346
Cdd:PRK00876 93 -VEDITPALEALGCYRRRDEAIRRVVPEYGPGwkskiVLPNLLDGDglnvfSLVVQdpdGEVtrkrlpanaYLQIVAATN 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1339315715 347 GSGGTAKSIKSHH----NVA---SP---------LVrKKREAGLILEPLAALYKDEVRDLGRLLGLPEEIVGRHP 405
Cdd:PRK00876 172 FKQRTRKMVEYYHadrlNYAvagTPnrleydqgfFV-KNGDGAADLKPIAHLYKTQVYALAEHLGVPEEIRRRPP 245
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
224-301 |
1.27e-03 |
|
Asparagine synthase; This family is always found associated with pfam00310. Members of this family catalyze the conversion of aspartate to asparagine.
Pssm-ID: 395594 [Multi-domain] Cd Length: 279 Bit Score: 40.68 E-value: 1.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1339315715 224 GDKPILLLISGGVDSSVVAAlLLQTFPPEQIHLMYIDTGLMRKDESVEIGAALRKLGARNLYLIDAEERFLSALAGAV 301
Cdd:pfam00733 16 ADVPVGAFLSGGLDSSSIAA-LAARQSPSPLHTFSIGFEGRGYDEAPYAREVAEHLGTDHHELVVTPEDLLDALPDVI 92
|
|
| mnmA |
PRK00143 |
tRNA-specific 2-thiouridylase MnmA; Reviewed |
228-247 |
1.60e-03 |
|
tRNA-specific 2-thiouridylase MnmA; Reviewed
Pssm-ID: 234664 [Multi-domain] Cd Length: 346 Bit Score: 40.82 E-value: 1.60e-03
|
| QueC |
COG0603 |
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ... |
226-299 |
1.67e-03 |
|
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; 7-cyano-7-deazaguanine synthase (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440368 [Multi-domain] Cd Length: 223 Bit Score: 40.14 E-value: 1.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1339315715 226 KPILLLISGGVDSSVVAALLLQTFppEQIHLMYIDTGLmRkdESVEIGAA---LRKLGARNLYLIDAeeRFLSALAG 299
Cdd:COG0603 3 KKAVVLLSGGLDSTTCLAWALARG--YEVYALSFDYGQ-R--HRKELEAArriAKALGVGEHKVIDL--DFLGEIGG 72
|
|
| MnmA_TRMU-like |
cd01998 |
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
228-247 |
1.90e-03 |
|
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.
Pssm-ID: 467502 [Multi-domain] Cd Length: 349 Bit Score: 40.57 E-value: 1.90e-03
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
82-195 |
1.95e-03 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 39.34 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 82 YSRGIPLLGICYGLHVTAHLLGGEISRAETREYGPA-PVEVVTNHEITSGVSRRFTSWMSHGDAIRR--LPPGAREIATT 158
Cdd:PRK06895 69 YHQHKSILGVCLGHQTLCEFFGGELYNLNNVRHGQQrPLKVRSNSPLFDGLPEEFNIGLYHSWAVSEenFPTPLEITAVC 148
|
90 100 110
....*....|....*....|....*....|....*..
gi 1339315715 159 SHGVTAIVTIPEASFVGLQFHPEVTHSEQGLQILDNF 195
Cdd:PRK06895 149 DENVVMAMQHKTLPIYGVQFHPESYISEFGEQILRNW 185
|
|
| MnmA |
COG0482 |
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ... |
228-247 |
1.97e-03 |
|
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: 40.42 E-value: 1.97e-03
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
9-106 |
2.42e-03 |
|
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: 40.39 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 9 PPSGTDRIVILDFGsqTTHLIGRRIREQGIFAEIVAGTAPMEDWIDEGVRGVILS---GSPssihdedAPLPD-----RR 80
Cdd:COG0505 172 APGAGFHVVALDFG--VKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSngpGDP-------AALDYaietiRE 242
|
90 100
....*....|....*....|....*.
gi 1339315715 81 IYSRGIPLLGICYGLHVTAHLLGGEI 106
Cdd:COG0505 243 LLGKGIPIFGICLGHQLLALALGAKT 268
|
|
| AANH-like |
cd01986 |
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ... |
228-278 |
3.54e-03 |
|
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: 36.28 E-value: 3.54e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1339315715 228 ILLLISGGVDSSVVAALLLQTFPPEQIHLMYIDTGLMRKDESVEIGAALRK 278
Cdd:cd01986 1 VVVGYSGGKDSSVALHLASRLGRKAEVAVVHIDHGIGFKEEAESVASIARR 51
|
|
| ASS |
cd01999 |
argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle ... |
226-293 |
4.76e-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: 39.44 E-value: 4.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1339315715 226 KPILLLISGGVDSSVVAALLLQTFPPEQIHLMyIDTGlmRKDESVEIGAALRKLGARNLYLIDAEERF 293
Cdd:cd01999 1 KKVVLAYSGGLDTSVILKWLKEEYGYEVIAFT-ADLG--QGDEEEEIEEKALKLGAVKVYVVDLREEF 65
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
8-106 |
8.28e-03 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 38.52 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339315715 8 TPPSGTDRIVILDFGSQTThlIGRRIREQGIFAEIVAGTAPMEDWIDEGVRGVILS---GSPssihdedAPLPD-----R 79
Cdd:PRK12564 172 PGGELKYKVVAIDFGVKRN--ILRELAERGCRVTVVPATTTAEEILALNPDGVFLSngpGDP-------AALDYaiemiR 242
|
90 100
....*....|....*....|....*..
gi 1339315715 80 RIYSRGIPLLGICYGLHVTAHLLGGEI 106
Cdd:PRK12564 243 ELLEKKIPIFGICLGHQLLALALGAKT 269
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
224-273 |
9.11e-03 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 38.54 E-value: 9.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1339315715 224 GDKPILLLISGGVDSSVVAALLLQTFPPEQIHLMYIDtglMRKDESVEIG 273
Cdd:PTZ00077 236 GDVPFGLFLSGGLDSSIVAAIVAKLIKNGEIDLSKRG---MPKLHSFCIG 282
|
|
| |
