|
Name |
Accession |
Description |
Interval |
E-value |
| guaA |
PRK00074 |
GMP synthase; Reviewed |
9-525 |
0e+00 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 928.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 9 NMFDTILVLDFGSQYSHLITRRLREFNIYAEMLPCTQKISEL-GWTPKGVILSGGPYSVYAEDAPHVDHAIFDLNVPILG 87
Cdd:PRK00074 1 IHHDKILILDFGSQYTQLIARRVRELGVYSEIVPYDISAEEIrAFNPKGIILSGGPASVYEEGAPRADPEIFELGVPVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 88 ICYGMQELAWINGKQVGRGDKREYGPATLKVIDDSnSLFKGMND-STVWMSHGDKLHGLPTGYKTIATSDNSPYCGIVHE 166
Cdd:PRK00074 81 ICYGMQLMAHQLGGKVERAGKREYGRAELEVDNDS-PLFKGLPEeQDVWMSHGDKVTELPEGFKVIASTENCPIAAIANE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 167 TKPIYGIQFHPEVTHSTQGKTLLKNFAVDLCHAKQNWTMENFIDTEINRIRKLVGpTAEVIGAVSGGVDSTVASKLMTEA 246
Cdd:PRK00074 160 ERKFYGVQFHPEVTHTPQGKKLLENFVFDICGCKGDWTMENFIEEAIEEIREQVG-DKKVILGLSGGVDSSVAAVLLHKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 247 IGDRFHAILVDNGVLRLNEAANVKKTLVEGLGINLMVVDASEEFLSKLKGVTDPEKKRKIIGNTFIHVFEREAEKIKPkd 326
Cdd:PRK00074 239 IGDQLTCVFVDHGLLRKNEAEQVMEMFREHFGLNLIHVDASDRFLSALAGVTDPEEKRKIIGREFIEVFEEEAKKLGG-- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 327 gkeIQFLLQGTLYPDVIESISFKgPSQTIKTHHNVGGLLENMKLKLIEPLRELFKDEVRHLGELLGIPHDLVWRHPFPGP 406
Cdd:PRK00074 317 ---VKFLAQGTLYPDVIESGGTK-KAATIKSHHNVGGLPEDMKLKLVEPLRELFKDEVRKLGLELGLPEEIVYRHPFPGP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 407 GIAIRVLGEVTKEQVEIARKADNIYIEEIKKAGLYNQISQAFACLLPVKSVGVMGDQRTYDQVIALRAIETTDFMTADWF 486
Cdd:PRK00074 393 GLAIRILGEVTKEKLDILREADAIFIEELRKAGLYDKIWQAFAVLLPVKSVGVMGDGRTYDYVVALRAVTSIDGMTADWA 472
|
490 500 510
....*....|....*....|....*....|....*....
gi 285814221 487 PFEHSFLKKVASRIVNEVDGVARVTYDITSKPPATVEWE 525
Cdd:PRK00074 473 RLPYDFLEKISNRIINEVKGVNRVVYDITSKPPATIEWE 511
|
|
| GuaA2 |
COG0519 |
GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, ... |
10-525 |
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: 842.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 10 MFDTILVLDFGSQYSHLITRRLREFNIYAEMLPCT---QKISELGwtPKGVILSGGPYSVYAEDAPHVDHAIFDLNVPIL 86
Cdd:COG0519 2 DKEIIIVLDFGGQYQQLIARRRREEGVYSEIIPPDtaaEEIKAKG--PPGIILSGGPSSVYEEGAPPDDPELFELGGPIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 87 GICYGMQELAWINGKQVGRGDKREYGPATLKVIDDSNSLFKGMNDSTVWMSHGDKLHGLPTGYKTIATSDNSPYCGIVHE 166
Cdd:COG0519 80 GICYGGQLMLHLLGGGVVRAERREYGGALLLVDDESDLFAGGPEELQVWMSHGDRVTELPPGFEVIASTENCPVAAIANE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 167 TKPIYGIQFHPEVTHSTQGKTLLKNFAVDLCHAKQNWTMENFIDTEINRIRKLVGpTAEVIGAVSGGVDSTVASKLMTEA 246
Cdd:COG0519 160 ERKLYGVQFHPEVVHTEQGKEILKNFLFDICGCKGDWTMENFIEEAIEEIREQVG-DGKVICALSGGVDSSVAAALLHKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 247 IGDRFHAILVDNGVLRLNEAANVKKTLVEGLGINLMVVDASEEFLSKLKGVTDPEKKRKIIGNTFIHVFEREAEKIKPkd 326
Cdd:COG0519 239 IGDQLTCVFVDHGLLRKGEAEQVEETFKEHFGLNLIYVDASERFLSALKGVTDPEEKRKIIGEEFIEVFEEEAKKLGG-- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 327 gkeIQFLLQGTLYPDVIESISFKGPSQTIKTHHNVGGLLENMKLKLIEPLRELFKDEVRHLGELLGIPHDLVWRHPFPGP 406
Cdd:COG0519 317 ---AKFLAQGTLYPDVIESGSVKGPAATIKSHHNVGGLPEDMKFKLVEPLRELFKDEVRALGRELGLPEEIVYRHPFPGP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 407 GIAIRVLGEVTKEQVEIARKADNIYIEEIKKAGLYNQISQAFACLLPVKSVGVMGDQRTYDQVIALRAIETTDFMTADWF 486
Cdd:COG0519 394 GLAIRILGEVTKEKLEILREADAIFIEELRKAGLYDKVWQAFAVLLPVKSVGVMGDERTYEYVVALRAVTSVDGMTADWA 473
|
490 500 510
....*....|....*....|....*....|....*....
gi 285814221 487 PFEHSFLKKVASRIVNEVDGVARVTYDITSKPPATVEWE 525
Cdd:COG0519 474 RLPYEVLERISNRIINEVKGVNRVVYDITSKPPATIEWE 512
|
|
| PLN02347 |
PLN02347 |
GMP synthetase |
12-525 |
0e+00 |
|
GMP synthetase
Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 759.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 12 DTILVLDFGSQYSHLITRRLREFNIYAEMLPCTQKISEL-GWTPKGVILSGGPYSVYAEDAPHVDHAIFDL----NVPIL 86
Cdd:PLN02347 11 DVVLILDYGSQYTHLITRRVRELGVYSLLLSGTASLDRIaSLNPRVVILSGGPHSVHVEGAPTVPEGFFDYcrerGVPVL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 87 GICYGMQELAWINGKQVGRGDKREYGPATLKVIDDSnSLFKGMNDS---TVWMSHGDKLHGLPTGYKTIATSDNSPYCGI 163
Cdd:PLN02347 91 GICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCGS-QLFGDLPSGetqTVWMSHGDEAVKLPEGFEVVAKSVQGAVVAI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 164 VHETKPIYGIQFHPEVTHSTQGKTLLKNFAVDLCHAKQNWTMENFIDTEINRIRKLVGPTAEVIGAVSGGVDSTVASKLM 243
Cdd:PLN02347 170 ENRERRIYGLQYHPEVTHSPKGMETLRHFLFDVCGVTADWKMQDVLEEQIELIKATVGPDEHVICALSGGVDSTVAATLV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 244 TEAIGDRFHAILVDNGVLRLNEAANVKKTLVEGLGINLMVVDASEEFLSKLKGVTDPEKKRKIIGNTFIHVFEREAEKIK 323
Cdd:PLN02347 250 HKAIGDRLHCVFVDNGLLRYKEQERVMETFKRDLHLPVTCVDASERFLSKLKGVTDPEKKRKIIGAEFIEVFDEFAHKLE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 324 PKDGKEIQFLLQGTLYPDVIESISFKGP----SQTIKTHHNVGGLLENMKLKLIEPLRELFKDEVRHLGELLGIPHDLVW 399
Cdd:PLN02347 330 QKLGKKPAFLVQGTLYPDVIESCPPPGSgrthSHTIKSHHNVGGLPKDMKLKLIEPLKLLFKDEVRKLGRLLGVPEAFLK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 400 RHPFPGPGIAIRVLGEVTKE-QVEIARKADNIYIEEIKKAGLYNQISQAFACLLPVKSVGVMGDQRTYDQVIALRAIETT 478
Cdd:PLN02347 410 RHPFPGPGLAVRVLGDVTEGnALDILRQVDEIFINSIKDAGLYDEIWQAFAVFLPVKSVGVQGDQRTHSHVVALRAVTSE 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 285814221 479 DFMTADWFPFEHSFLKKVASRIVNEVDGVARVTYDITSKPPATVEWE 525
Cdd:PLN02347 490 DGMTADWYHFEHKFLDDVSRKICNEVRGVNRVVYDITSKPPSTIEWE 536
|
|
| guaA_Cterm |
TIGR00884 |
GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; This protein of purine ... |
207-525 |
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: 562.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 207 NFIDTEINRIRKLVGPtAEVIGAVSGGVDSTVASKLMTEAIGDRFHAILVDNGVLRLNEAANVKKTLVEGLGINLMVVDA 286
Cdd:TIGR00884 1 NFIEEAVEEIREQVGD-AKVIIALSGGVDSSVAAVLAHRAIGDRLTCVFVDHGLLRKGEAEQVVKTFGDRLGLNLVYVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 287 SEEFLSKLKGVTDPEKKRKIIGNTFIHVFEREAEKIKPkdgkeIQFLLQGTLYPDVIESISfkGPSQTIKTHHNVGGLLE 366
Cdd:TIGR00884 80 KERFLSALKGVTDPEEKRKIIGRVFIEVFEREAKKIGD-----AEYLAQGTIYPDVIESAA--GTAHVIKSHHNVGGLPE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 367 NMKLKLIEPLRELFKDEVRHLGELLGIPHDLVWRHPFPGPGIAIRVLGEVTKEQVEIARKADNIYIEEIKKAGLYNQISQ 446
Cdd:TIGR00884 153 DMKLKLVEPLRELFKDEVRKLGKELGLPEEIVWRHPFPGPGLAVRVLGEVTKEKLEILRRADAIVIEELKKAGLYDKVWQ 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 285814221 447 AFACLLPVKSVGVMGDQRTYDQVIALRAIETTDFMTADWFPFEHSFLKKVASRIVNEVDGVARVTYDITSKPPATVEWE 525
Cdd:TIGR00884 233 AFAVLLPVKSVGVMGDGRTYGYVIALRAVESIDGMTADWARLPYDFLERISNRITNEVPGVNRVVYDITSKPPATIEWE 311
|
|
| GMP_synthase_C |
cd01997 |
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ... |
216-525 |
0e+00 |
|
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP synthetase (glutamine-hydrolyzing, EC 6.3.5.2) contains two subdomains: the ATP pyrophosphatase domain at the N-terminal and the dimerization domain at the C-terminal end. The ATP-PPase domain is a twisted, five-stranded parallel beta-sheet sandwiched between helical layers. It has a signature nucleotide-binding motif, or PP-loop, at the end of the first-beta strand. GMP synthetase is a homodimer, but in some archaea, it is a heterodimer made up of ATP pyrophosphatase (ATP-PPase) and a GATase subunit. In eukaryotes and bacteria, the two catalytic units are encoded by a single gene producing a two-domain-type GMP with a GATase domain in the N-terminus and an ATP-PPase domain in the C-terminus.
Pssm-ID: 467501 [Multi-domain] Cd Length: 311 Bit Score: 512.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 216 IRKLVGpTAEVIGAVSGGVDSTVASKLMTEAIGD-RFHAILVDNGVLRLNEAANVKKTLVEGLGINLMVVDASEEFLSKL 294
Cdd:cd01997 1 IKRTVG-DKKVLCLVSGGVDSTVCAALLHKALGDeRVIAVHIDNGLMRKNESEQVEEALKKLGVINLAKVDASKRFLKKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 295 KGVTDPEKKRKIIGNTFIHVFEREAEKIKPKDgkEIQFLLQGTLYPDVIESISFKG--PSQTIKTHHNVGGLLEN-MKLK 371
Cdd:cd01997 80 KGVTDPEEKRKIIGDTFIEVFDEVAKELNLDP--DDVYLAQGTLYPDLIESASSLAssKADTIKTHHNVGGLPRElLKGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 372 LIEPLRELFKDEVRHLGELLGIPHDLVWRHPFPGPGIAIRVLGEVTKEQVEIARKADNIYIEEIKKAGLYNQISQAFACL 451
Cdd:cd01997 158 LVEPLRDLFKDEVRELGRELGLPEELVWRHPFPGPGLAIRVLGEVTPEKLEILREADAIVEEELREAGLYDKISQAFAVL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 285814221 452 LPVKSVGVMGDQRTYDQVIALRAIETTDFMTADWFPFEHSFLKKVASRIVNEVDGVARVTYDITSKPPATVEWE 525
Cdd:cd01997 238 LPIKSVGVQGDGRTYGYVVALRAVETEDFMTAEWARPPYEVLDKISNRITNEVPGVNRVVYDITSKPPATIEWE 311
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
14-200 |
9.87e-112 |
|
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: 329.28 E-value: 9.87e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 14 ILVLDFGSQYSHLITRRLREFNIYAEMLPCTQKISELG-WTPKGVILSGGPYSVYAEDAPHVDHAIFDLNVPILGICYGM 92
Cdd:TIGR00888 1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTTPLEEIReKNPKGIILSGGPSSVYAENAPRADEKIFELGVPVLGICYGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 93 QELAWINGKQVGRGDKREYGPATLKVIDDSnSLFKGM-NDSTVWMSHGDKLHGLPTGYKTIATSDNSPYCGIVHETKPIY 171
Cdd:TIGR00888 81 QLMAKQLGGEVGRAEKREYGKAELEILDED-DLFRGLpDESTVWMSHGDKVKELPEGFKVLATSDNCPVAAMAHEEKPIY 159
|
170 180
....*....|....*....|....*....
gi 285814221 172 GIQFHPEVTHSTQGKTLLKNFAVDLCHAK 200
Cdd:TIGR00888 160 GVQFHPEVTHTEYGNELLENFVYDVCGCE 188
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
14-193 |
4.89e-105 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153213 [Multi-domain] Cd Length: 181 Bit Score: 312.16 E-value: 4.89e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 14 ILVLDFGSQYSHLITRRLREFNIYAEMLPCTQKI-SELGWTPKGVILSGGPYSVYAEDAPHVDHAIFDLNVPILGICYGM 92
Cdd:cd01742 1 ILILDFGSQYTHLIARRVRELGVYSEILPNTTPLeEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGICYGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 93 QELAWINGKQVGRGDKREYGPATLKvIDDSNSLFKGMNDS-TVWMSHGDKLHGLPTGYKTIATSDNSPYCGIVHETKPIY 171
Cdd:cd01742 81 QLIAKALGGKVERGDKREYGKAEIE-IDDSSPLFEGLPDEqTVWMSHGDEVVKLPEGFKVIASSDNCPVAAIANEEKKIY 159
|
170 180
....*....|....*....|..
gi 285814221 172 GIQFHPEVTHSTQGKTLLKNFA 193
Cdd:cd01742 160 GVQFHPEVTHTEKGKEILKNFL 181
|
|
| GMP_synt_C |
pfam00958 |
GMP synthase C terminal domain; GMP synthetase is a glutamine amidotransferase from the de ... |
433-524 |
5.46e-63 |
|
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: 200.33 E-value: 5.46e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 433 EEIKKAGLYNQISQAFACLLPVKSVGVMGDQRTYDQVIALRAIETTDFMTADWFPFEHSFLKKVASRIVNEVDGVARVTY 512
Cdd:pfam00958 1 EEIKKAGLYRKIWQAFAVLLPVKSVGVMGDERTYEYVVALRAVTSTDGMTADWARLPYEVLEKISNRIVNEVPGVNRVVY 80
|
90
....*....|..
gi 285814221 513 DITSKPPATVEW 524
Cdd:pfam00958 81 DITSKPPATIEW 92
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
14-183 |
3.74e-56 |
|
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: 187.46 E-value: 3.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 14 ILVLD---FGSQYSHLITRRLRE-------FNIYA-EMLPCTQKISElgwtPKGVILSGGPYSVYAED-----APHVDHA 77
Cdd:COG0518 2 ILILDhdpFGGQYPGLIARRLREagieldvLRVYAgEILPYDPDLED----PDGLILSGGPMSVYDEDpwledEPALIRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 78 IFDLNVPILGICYGMQELAWINGKQVGRGDKREYGPATLKVIDDSnSLFKGMNDS-TVWMSHGDKLHGLPTGYKTIATSD 156
Cdd:COG0518 78 AFELGKPVLGICYGAQLLAHALGGKVEPGPGREIGWAPVELTEAD-PLFAGLPDEfTVWMSHGDTVTELPEGAEVLASSD 156
|
170 180
....*....|....*....|....*..
gi 285814221 157 NSPYCGIVHEtKPIYGIQFHPEVTHST 183
Cdd:COG0518 157 NCPNQAFRYG-RRVYGVQFHPEVTHTM 182
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
15-196 |
2.15e-53 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 178.97 E-value: 2.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 15 LVLDFGSQYSHLITRRLREFNIYAEMLPCTQKISELGWT-PKGVILSGGPYSVYA-EDAPHVDHAIFDLNVPILGICYGM 92
Cdd:pfam00117 1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEEnPDGIILSGGPGSPGAaGGAIEAIREARELKIPILGICLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 93 QELAWINGKQVGRGDKREYGPATLKVIDDSNSLFKGM-NDSTVWMSHGDKLHG--LPTGYKTIATSDN-SPYCGIVHETK 168
Cdd:pfam00117 81 QLLALAFGGKVVKAKKFGHHGKNSPVGDDGCGLFYGLpNVFIVRRYHSYAVDPdtLPDGLEVTATSENdGTIMGIRHKKL 160
|
170 180
....*....|....*....|....*...
gi 285814221 169 PIYGIQFHPEVTHSTQGKTLLKNFAVDL 196
Cdd:pfam00117 161 PIFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
14-197 |
1.51e-50 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 171.19 E-value: 1.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 14 ILVLDFGSQYSHLITRRLREFNIYAEMLPCTQKISELGWTPKGVILSGGPYsvyAEDAPHVDHAIFDLNVPILGICYGMQ 93
Cdd:PRK00758 2 IVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTTPVEEIKAFEDGLILSGGPD---IERAGNCPEYLKELDVPILGICLGHQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 94 ELAWINGKQVGRGDKREYGPATLKVIDDsNSLFKGMNDST-VWMSHGDKLHGLPTGYKTIATSDNSPYCGIVHETKPIYG 172
Cdd:PRK00758 79 LIAKAFGGEVGRGEYGEYALVEVEILDE-DDILKGLPPEIrVWASHADEVKELPDGFEILARSDICEVEAMKHKEKPIYG 157
|
170 180
....*....|....*....|....*
gi 285814221 173 IQFHPEVTHSTQGKTLLKNFAvDLC 197
Cdd:PRK00758 158 VQFHPEVAHTEYGEEIFKNFL-EIC 181
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
56-193 |
4.73e-19 |
|
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: 84.99 E-value: 4.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 56 GVILSGGPYSVYAEDAPHVDH------AIFDLNVPILGICYGMQELAWINGKQVGRG-DKREYGPATLKVIDD--SNSLF 126
Cdd:cd01741 49 GLVILGGPMSVDEDDYPWLKKlkelirQALAAGKPVLGICLGHQLLARALGGKVGRNpKGWEIGWFPVTLTEAgkADPLF 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 285814221 127 KGMNDS-TVWMSHGDKLHGLPTGYKTIATSDNSPYCGIVHETKpIYGIQFHPEvthstqgKTLLKNFA 193
Cdd:cd01741 129 AGLPDEfPVFHWHGDTVVELPPGAVLLASSEACPNQAFRYGDR-ALGLQFHPE-------ERLLRNFL 188
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
54-192 |
4.31e-15 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 73.63 E-value: 4.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 54 PKGVILSGGPYSvyAEDA----PHVDHaiFDLNVPILGICYGMQELAWINGKQVGRGDKREYGPATlKVIDDSNSLFKGM 129
Cdd:PRK05670 44 PDAIVLSPGPGT--PAEAgislELIRE--FAGKVPILGVCLGHQAIGEAFGGKVVRAKEIMHGKTS-PIEHDGSGIFAGL 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 285814221 130 NDS-TVWMSH---GDKLHgLPTGYKTIATSDNSPYCGIVHETKPIYGIQFHPEVTHSTQGKTLLKNF 192
Cdd:PRK05670 119 PNPfTVTRYHslvVDRES-LPDCLEVTAWTDDGEIMGVRHKELPIYGVQFHPESILTEHGHKLLENF 184
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
54-192 |
5.47e-15 |
|
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: 73.34 E-value: 5.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 54 PKGVILSGGPYSvyAEDAPHVDHAI--FDLNVPILGICYGMQELAWINGKQVGRGDKREYGPATlKVIDDSNSLFKGMND 131
Cdd:cd01743 43 PDAIVISPGPGH--PEDAGISLEIIraLAGKVPILGVCLGHQAIAEAFGGKVVRAPEPMHGKTS-EIHHDGSGLFKGLPQ 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 285814221 132 STVWM---S-HGDKLHgLPTGYKTIATSDNspycGIV----HETKPIYGIQFHPEVTHSTQGKTLLKNF 192
Cdd:cd01743 120 PFTVGryhSlVVDPDP-LPDLLEVTASTED----GVImalrHRDLPIYGVQFHPESILTEYGLRLLENF 183
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
14-178 |
3.78e-14 |
|
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: 70.60 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 14 ILVLDFGSQYShlITRRLREFNIYAEMLPCTQKISE-LGWTPKGVILSGGPysvyaEDAPHVDHAI------FDLNVPIL 86
Cdd:cd01744 1 VVVIDFGVKHN--ILRELLKRGCEVTVVPYNTDAEEiLKLDPDGIFLSNGP-----GDPALLDEAIktvrklLGKKIPIF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 87 GICYGMQELAWINGKQvgrgdkreygpaTLKVIddsnslF--KGMN-------DSTVWM-SHGdklHG-------LPTGY 149
Cdd:cd01744 74 GICLGHQLLALALGAK------------TYKMK------FghRGSNhpvkdliTGRVYItSQN---HGyavdpdsLPGGL 132
|
170 180 190
....*....|....*....|....*....|.
gi 285814221 150 KTIATS--DNSPyCGIVHETKPIYGIQFHPE 178
Cdd:cd01744 133 EVTHVNlnDGTV-EGIRHKDLPVFSVQFHPE 162
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
54-192 |
1.30e-13 |
|
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: 69.30 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 54 PKGVILSGGPYSvyAEDAPHVDHAI--FDLNVPILGICYGMQELAWINGKQVGRGDKREYGPATLKVIDDSnSLFKGMND 131
Cdd:COG0512 43 PDGIVLSPGPGT--PEEAGISLEVIraFAGKIPILGVCLGHQAIGEAFGGKVVRAPEPMHGKTSPITHDGS-GLFAGLPN 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 285814221 132 S-TVWMSH---GDKlHGLPTGYKTIATSDNspycGIV----HETKPIYGIQFHPEVTHSTQGKTLLKNF 192
Cdd:COG0512 120 PfTATRYHslvVDR-ETLPDELEVTAWTED----GEImgirHRELPIEGVQFHPESILTEHGHQLLANF 183
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
46-192 |
5.66e-13 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 67.45 E-value: 5.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 46 KISELgwTPKGVILSGGPYsvYAEDAPHVDHAI--FDLNVPILGICYGMQELAWINGKQVGRGDKREYGPATlKVIDDSN 123
Cdd:CHL00101 38 KIKNL--NIRHIIISPGPG--HPRDSGISLDVIssYAPYIPILGVCLGHQSIGYLFGGKIIKAPKPMHGKTS-KIYHNHD 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 285814221 124 SLFKGM-NDSTVWMSHG---DKLHgLPTGYKTIATSDNSPYCGIVHET-KPIYGIQFHPEVTHSTQGKTLLKNF 192
Cdd:CHL00101 113 DLFQGLpNPFTATRYHSliiDPLN-LPSPLEITAWTEDGLIMACRHKKyKMLRGIQFHPESLLTTHGQQILRNF 185
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
54-192 |
1.00e-12 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 70.52 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 54 PKGVILSGGPYSvyAEDAPHVDHAI--FDLNVPILGICYGMQELAWINGKQVGRGDKREYGPATlKVIDDSNSLFKGMND 131
Cdd:PRK14607 45 PSHIVISPGPGR--PEEAGISVEVIrhFSGKVPILGVCLGHQAIGYAFGGKIVHAKRILHGKTS-PIDHNGKGLFRGIPN 121
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 285814221 132 STV---WMSHGDKLHGLPTGYKTIATSDNSPYCGIVHETKPIYGIQFHPEVTHSTQGKTLLKNF 192
Cdd:PRK14607 122 PTVatrYHSLVVEEASLPECLEVTAKSDDGEIMGIRHKEHPIFGVQFHPESILTEEGKRILKNF 185
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
15-192 |
1.14e-12 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 66.75 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 15 LVLDFGSQYSHLITRRLREFNIyaemlpctQKISELgwTPKGVILSGGPYSvyAEDAPHVDHAI--FDLNVPILGICYGM 92
Cdd:PRK07649 15 LVQFLGELGQELVVKRNDEVTI--------SDIENM--KPDFLMISPGPCS--PNEAGISMEVIryFAGKIPIFGVCLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 93 QELAWINGKQVGRGDKREYGpATLKVIDDSNSLFKGMND---STVWMSHGDKLHGLPTGYKTIATSDNSPYCGIVHETKP 169
Cdd:PRK07649 83 QSIAQVFGGEVVRAERLMHG-KTSLMHHDGKTIFSDIPNpftATRYHSLIVKKETLPDCLEVTSWTEEGEIMAIRHKTLP 161
|
170 180
....*....|....*....|...
gi 285814221 170 IYGIQFHPEVTHSTQGKTLLKNF 192
Cdd:PRK07649 162 IEGVQFHPESIMTSHGKELLQNF 184
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
54-192 |
4.45e-12 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 64.90 E-value: 4.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 54 PKGVILSGGPYSvyAEDAPHVDHAI--FDLNVPILGICYGMQELAWINGKQVGRGDKREYGpATLKVIDDSNSLFKGMND 131
Cdd:PRK08857 44 PTHLVISPGPCT--PNEAGISLQAIehFAGKLPILGVCLGHQAIAQVFGGQVVRARQVMHG-KTSPIRHTGRSVFKGLNN 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 285814221 132 S-TVWMSHG--DKLHGLPTGYKTIATSDNS-----PYCGIVHETKPIYGIQFHPEVTHSTQGKTLLKNF 192
Cdd:PRK08857 121 PlTVTRYHSlvVKNDTLPECFELTAWTELEdgsmdEIMGFQHKTLPIEAVQFHPESIKTEQGHQLLANF 189
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
83-192 |
5.37e-12 |
|
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: 64.81 E-value: 5.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 83 VPILGICYGMQELAWINGKQVGRGDKREYGpATLKVIDDSNSLFKGMND---STVWMSHGDKLHGLPTGYKTIATSD-NS 158
Cdd:TIGR00566 73 LPILGVCLGHQAMGQAFGGDVVRANTVMHG-KTSEIEHNGAGIFRGLFNpltATRYHSLVVEPETLPTCFPVTAWEEeNI 151
|
90 100 110
....*....|....*....|....*....|....
gi 285814221 159 PYCGIVHETKPIYGIQFHPEVTHSTQGKTLLKNF 192
Cdd:TIGR00566 152 EIMAIRHRDLPLEGVQFHPESILSEQGHQLLANF 185
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
54-192 |
4.65e-11 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 61.86 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 54 PKGVILSGGPYSvyaEDAPHVDHAI---FDLNVPILGICYGMQELAWINGKQVGRGDKREYGpATLKVIDDSNSLFKGMN 130
Cdd:PRK08007 44 PQKIVISPGPCT---PDEAGISLDVirhYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHG-KTSPITHNGEGVFRGLA 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 285814221 131 DS-TVWMSHGDKLH--GLPTGYKTIATSDNSPYCGIVHETKPIYGIQFHPEVTHSTQGKTLLKNF 192
Cdd:PRK08007 120 NPlTVTRYHSLVVEpdSLPACFEVTAWSETREIMGIRHRQWDLEGVQFHPESILSEQGHQLLANF 184
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
53-192 |
6.50e-10 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 58.72 E-value: 6.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 53 TPKGVILSGGPYSvyAEDAPHVDHAI--FDLNVPILGICYGMQELAWINGKQVGRGDKREYGPATLkVIDDSNSLFKGMN 130
Cdd:PRK06774 43 APSHLVISPGPCT--PNEAGISLAVIrhFADKLPILGVCLGHQALGQAFGARVVRARQVMHGKTSA-ICHSGQGVFRGLN 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 285814221 131 DS-TVWMSHGDKLHG--LPTGYKTIATSDNS----PYCGIVHETKPIYGIQFHPEVTHSTQGKTLLKNF 192
Cdd:PRK06774 120 QPlTVTRYHSLVIAAdsLPGCFELTAWSERGgemdEIMGIRHRTLPLEGVQFHPESILSEQGHQLLDNF 188
|
|
| hisH |
PRK13181 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
80-193 |
7.27e-10 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 58.72 E-value: 7.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 80 DLNVPILGICYGMQELA------------WINgkqvgrGDKREYGPATLKV-------IDDSNS--LFKGMND-STVWMS 137
Cdd:PRK13181 70 EKKQPVLGICLGMQLLFesseegnvkglgLIP------GDVKRFRSEPLKVpqmgwnsVKPLKEspLFKGIEEgSYFYFV 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 285814221 138 H------GDKLHglptgykTIATSD-NSPYCGIVHETKpIYGIQFHPEVTHSTqGKTLLKNFA 193
Cdd:PRK13181 144 HsyyvpcEDPED-------VLATTEyGVPFCSAVAKDN-IYAVQFHPEKSGKA-GLKLLKNFA 197
|
|
| PRK09065 |
PRK09065 |
glutamine amidotransferase; Provisional |
56-181 |
1.52e-09 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181635 [Multi-domain] Cd Length: 237 Bit Score: 58.43 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 56 GVILSGG--------PYSVYAED-APHVDHAifdlNVPILGICYGMQELAWINGKQVG---RGdkREYGPATLKVID--D 121
Cdd:PRK09065 57 GVIITGSwamvtdrlDWSERTADwLRQAAAA----GMPLLGICYGHQLLAHALGGEVGynpAG--RESGTVTVELHPaaA 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285814221 122 SNSLFKGMnDSTVW--MSHGDKLHGLPTGYKTIATSDNSPyCGIVHETKPIYGIQFHPEVTH 181
Cdd:PRK09065 131 DDPLFAGL-PAQFPahLTHLQSVLRLPPGAVVLARSAQDP-HQAFRYGPHAWGVQFHPEFTA 190
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
13-178 |
1.87e-09 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 59.32 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 13 TILVLDFGSQYShlITRRLREFNIYAEMLPCTQKISE-LGWTPKGVILSGGPysvyaEDAPHVDHAI------FDLNVPI 85
Cdd:PRK12564 179 KVVAIDFGVKRN--ILRELAERGCRVTVVPATTTAEEiLALNPDGVFLSNGP-----GDPAALDYAIemirelLEKKIPI 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 86 LGICYGMQELAWINGkqvGRGDKREYG------PatlkVID-----------------DSNSL-------FKGMNDSTVw 135
Cdd:PRK12564 252 FGICLGHQLLALALG---AKTYKMKFGhrganhP----VKDletgkveitsqnhgfavDEDSLpanlevtHVNLNDGTV- 323
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 285814221 136 mshgdklhglptgyktiatsdnspyCGIVHETKPIYGIQFHPE 178
Cdd:PRK12564 324 -------------------------EGLRHKDLPAFSVQYHPE 341
|
|
| PRK09522 |
PRK09522 |
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ... |
14-210 |
1.90e-09 |
|
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;
Pssm-ID: 181927 [Multi-domain] Cd Length: 531 Bit Score: 60.04 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 14 ILVLDFGSQYSHLITRRLREFN----IYAEMLPCTQKISELGWTPKGVI-LSGGPYSvyAEDAPHVDHAIFDL--NVPIL 86
Cdd:PRK09522 4 ILLLDNIDSFTYNLADQLRSNGhnvvIYRNHIPAQTLIERLATMSNPVLmLSPGPGV--PSEAGCMPELLTRLrgKLPII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 87 GICYGMQELAWINGKQVGRGDKREYGPATlKVIDDSNSLFKG-MNDSTVWMSHGDKLHGLPTGYkTIATSDNSPYCGIVH 165
Cdd:PRK09522 82 GICLGHQAIVEAYGGYVGQAGEILHGKAS-SIEHDGQAMFAGlTNPLPVARYHSLVGSNIPAGL-TINAHFNGMVMAVRH 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 285814221 166 ETKPIYGIQFHPEVTHSTQGKTLL-KNFAVDLCHAKQNWTMENFID 210
Cdd:PRK09522 160 DADRVCGFQFHPESILTTQGARLLeQTLAWAQQKLEPTNTLQPILE 205
|
|
| PRK07567 |
PRK07567 |
glutamine amidotransferase; Provisional |
56-178 |
4.38e-09 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181035 [Multi-domain] Cd Length: 242 Bit Score: 57.26 E-value: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 56 GVILSGGPYSV---YAEDAP---HVDHAIFDL-------NVPILGICYGMQELAWINGKQVGRGDKREYGPATLKVIDD- 121
Cdd:PRK07567 54 GVIVGGSPFNVsdpAESKSPwqrRVEAELSGLldevvarDFPFLGACYGVGTLGHHQGGVVDRTYGEPVGAVTVSLTDAg 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 122 -SNSLFKGMNDS-TVWMSHGDKLHGLPTGYKTIATSDNSPYCGI-VHETkpIYGIQFHPE 178
Cdd:PRK07567 134 rADPLLAGLPDTfTAFVGHKEAVSALPPGAVLLATSPTCPVQMFrVGEN--VYATQFHPE 191
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
57-192 |
4.55e-09 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 56.28 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 57 VILSGGPysvyaeDAPHVDHAIFDL------NVPILGICYGMQEL------AWINGKQVGRGDKReygpaTLKVIDDsNS 124
Cdd:PRK06895 47 ILISPGP------DVPRAYPQLFAMleryhqHKSILGVCLGHQTLceffggELYNLNNVRHGQQR-----PLKVRSN-SP 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285814221 125 LFKGMNDS---TVWMSHGDKLHGLPTGYKTIATSDNSPYCGIVHETKPIYGIQFHPEVTHSTQGKTLLKNF 192
Cdd:PRK06895 115 LFDGLPEEfniGLYHSWAVSEENFPTPLEITAVCDENVVMAMQHKTLPIYGVQFHPESYISEFGEQILRNW 185
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
14-178 |
7.03e-09 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 57.88 E-value: 7.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 14 ILVLDFGSQYShlITRRLREFNIYAEMLPCTQKISE-LGWTPKGVILSGGPYSVYA-EDAPHVDHAIFDLNVPILGICYG 91
Cdd:CHL00197 195 IIVIDFGVKYN--ILRRLKSFGCSITVVPATSPYQDiLSYQPDGILLSNGPGDPSAiHYGIKTVKKLLKYNIPIFGICMG 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 92 MQELAWING------KQVGRGDKREYGPATLKVIDDSN--------SLFKgmndSTVWMSHGDkLHGLptgykTIAtsdn 157
Cdd:CHL00197 273 HQILSLALEaktfklKFGHRGLNHPSGLNQQVEITSQNhgfavnleSLAK----NKFYITHFN-LNDG-----TVA---- 338
|
170 180
....*....|....*....|.
gi 285814221 158 spycGIVHETKPIYGIQFHPE 178
Cdd:CHL00197 339 ----GISHSPKPYFSVQYHPE 355
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
13-178 |
1.26e-08 |
|
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: 56.95 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 13 TILVLDFGSQYShlITRRLREFNIYAEMLPCTQKISE-LGWTPKGVILSGGPysvyaEDAPHVDHAI------FDLNVPI 85
Cdd:COG0505 178 HVVALDFGVKRN--ILRELAERGCRVTVVPATTSAEEiLALNPDGVFLSNGP-----GDPAALDYAIetirelLGKGIPI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 86 LGICYGMQELAWINGkqvGRGDKREYG------PatlkVID-----------------DSNSL--------FKGMNDSTV 134
Cdd:COG0505 251 FGICLGHQLLALALG---AKTYKLKFGhrganhP----VKDletgrveitsqnhgfavDEDSLpatdlevtHVNLNDGTV 323
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 285814221 135 wmshgdklhglptgyktiatsdnspyCGIVHETKPIYGIQFHPE 178
Cdd:COG0505 324 --------------------------EGLRHKDLPAFSVQYHPE 341
|
|
| PRK13980 |
PRK13980 |
NAD synthetase; Provisional |
213-405 |
1.34e-08 |
|
NAD synthetase; Provisional
Pssm-ID: 184435 [Multi-domain] Cd Length: 265 Bit Score: 55.99 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 213 INRIRKLV---GPTAEVIGaVSGGVDSTVASKLMTEAIG-DRFHAILVDNgvlRLNEAANVK--KTLVEGLGINLMVVDA 286
Cdd:PRK13980 18 VDFIREEVekaGAKGVVLG-LSGGIDSAVVAYLAVKALGkENVLALLMPS---SVSPPEDLEdaELVAEDLGIEYKVIEI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 287 S---EEFLSKLkgvtdPEKKRKIIGNtfihvfereaekIKP------------KDGK---------EIqFLLQGTLYPDv 342
Cdd:PRK13980 94 TpivDAFFSAI-----PDADRLRVGN------------IMArtrmvllydyanRENRlvlgtgnksEL-LLGYFTKYGD- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 285814221 343 iesisfkGPSQtikthhnvggllenmklklIEPLRELFKDEVRHLGELLGIPHDLVWRHPFPG 405
Cdd:PRK13980 155 -------GAVD-------------------LNPIGDLYKTQVRELARHLGVPEDIIEKPPSAD 191
|
|
| hisH |
PRK13170 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
84-192 |
3.97e-08 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183877 [Multi-domain] Cd Length: 196 Bit Score: 53.32 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 84 PILGICYGMQELawingkqvGRGDKREYGPATLKVID------------------------DSNSLFKGMND-STVWMSH 138
Cdd:PRK13170 72 PVLGICLGMQLL--------GERSEESGGVDCLGIIDgpvkkmtdfglplphmgwnqvtpqAGHPLFQGIEDgSYFYFVH 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 285814221 139 GdklHGLPTGYKTIATSDNS-PYCGIVHEtKPIYGIQFHPEVThSTQGKTLLKNF 192
Cdd:PRK13170 144 S---YAMPVNEYTIAQCNYGePFSAAIQK-DNFFGVQFHPERS-GAAGAQLLKNF 193
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
77-178 |
4.34e-08 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 56.08 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 77 AIFDLNVPILGICYGMQELAWINGKQVGRGDKREYG-PATLKVIDdSNSLFKGMNDS-TVWMSHgdKLH----GLPTGYK 150
Cdd:PRK13566 593 AALARNLPIFGVCLGLQAIVEAFGGELGQLAYPMHGkPSRIRVRG-PGRLFSGLPEEfTVGRYH--SLFadpeTLPDELL 669
|
90 100
....*....|....*....|....*...
gi 285814221 151 TIATSDNSPYCGIVHETKPIYGIQFHPE 178
Cdd:PRK13566 670 VTAETEDGVIMAIEHKTLPVAAVQFHPE 697
|
|
| hisH |
PRK13143 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
56-197 |
6.38e-08 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 52.95 E-value: 6.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 56 GVILSG-GPYSVYAEDAPHVDHAIFDL---NVPILGICYGMQ-------E------LAWINGKqVGRGDKREYGP----A 114
Cdd:PRK13143 41 GIVLPGvGAFGAAMENLSPLRDVILEAarsGKPFLGICLGMQllfesseEgggvrgLGLFPGR-VVRFPAGVKVPhmgwN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 115 TLKVIDDSNsLFKGMNDSTVWMSHgdKLHGLPTGYK-TIATSD-NSPYCGIVhETKPIYGIQFHPEVThSTQGKTLLKNF 192
Cdd:PRK13143 120 TVKVVKDCP-LFEGIDGEYVYFVH--SYYAYPDDEDyVVATTDyGIEFPAAV-CNDNVFGTQFHPEKS-GETGLKILENF 194
|
....*
gi 285814221 193 aVDLC 197
Cdd:PRK13143 195 -VELI 198
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
14-97 |
1.22e-07 |
|
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: 50.29 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 14 ILVLDFGSQYS---HLITRRLREFNIYAEMLPCTQKISELGWTPK---GVILSGGPYSVYA----EDAPHVDHAIFDLNV 83
Cdd:cd01653 1 VAVLLFPGFEElelASPLDALREAGAEVDVVSPDGGPVESDVDLDdydGLILPGGPGTPDDlardEALLALLREAAAAGK 80
|
90
....*....|....
gi 285814221 84 PILGICYGMQELAW 97
Cdd:cd01653 81 PILGICLGAQLLVL 94
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
13-178 |
1.64e-07 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 53.36 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 13 TILVLDFGsqYSHLITRRLREFNIYAEMLP---CTQKISELgwTPKGVILSGGPYSvyAEDAPHVDHAIFDL--NVPILG 87
Cdd:PRK12838 169 HVALIDFG--YKKSILRSLSKRGCKVTVLPydtSLEEIKNL--NPDGIVLSNGPGD--PKELQPYLPEIKKLisSYPILG 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 88 ICYGMQELAWING------KQVGRGdkreygpATLKVIDdsnslfkgMNDSTVWMS---HG-----DKLHGLPTGYKTIA 153
Cdd:PRK12838 243 ICLGHQLIALALGadteklPFGHRG-------ANHPVID--------LTTGRVWMTsqnHGyvvdeDSLDGTPLSVRFFN 307
|
170 180
....*....|....*....|....*
gi 285814221 154 TSDNSpYCGIVHETKPIYGIQFHPE 178
Cdd:PRK12838 308 VNDGS-IEGLRHKKKPVLSVQFHPE 331
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
83-192 |
4.28e-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: 50.57 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 83 VPILGICYGMQELA-------------WINGKqVGRGDKREYGP------ATLKVIDDSNSLFKGMNDSTVWMSHgdKLH 143
Cdd:cd01748 72 KPFLGICLGMQLLFesseegggtkglgLIPGK-VVRFPASEGLKvphmgwNQLEITKESPLFKGIPDGSYFYFVH--SYY 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 285814221 144 GLPTGYK-TIATSD-NSPYCGIVhETKPIYGIQFHPEVTHSTqGKTLLKNF 192
Cdd:cd01748 149 APPDDPDyILATTDyGGKFPAAV-EKDNIFGTQFHPEKSGKA-GLKLLKNF 197
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
56-191 |
4.82e-07 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 50.43 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 56 GVILSGGPYSVYAEDA--PHVdHAIFDLNVPILGICYGMQELAWINGKQVGRGDKREYGpATLKVIDDSNSLFKGMND-- 131
Cdd:PRK07765 49 GVLLSPGPGTPERAGAsiDMV-RACAAAGTPLLGVCLGHQAIGVAFGATVDRAPELLHG-KTSSVHHTGVGVLAGLPDpf 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285814221 132 -STVWMSHGDKLHGLPTGYKTIATSDNSPYCGIVHETKPIYGIQFHPEVTHSTQGKTLLKN 191
Cdd:PRK07765 127 tATRYHSLTILPETLPAELEVTARTDSGVIMAVRHRELPIHGVQFHPESVLTEGGHRMLAN 187
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
14-95 |
1.67e-06 |
|
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: 46.42 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 14 ILVLDFGSQYS---HLITRRLREFNIYAEMLPCTQKISELGWTPK---GVILSGGPYSVYA----EDAPHVDHAIFDLNV 83
Cdd:cd03128 1 VAVLLFGGSEElelASPLDALREAGAEVDVVSPDGGPVESDVDLDdydGLILPGGPGTPDDlawdEALLALLREAAAAGK 80
|
90
....*....|..
gi 285814221 84 PILGICYGMQEL 95
Cdd:cd03128 81 PVLGICLGAQLL 92
|
|
| COG1606 |
COG1606 |
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only]; |
229-288 |
1.82e-06 |
|
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
Pssm-ID: 441214 [Multi-domain] Cd Length: 265 Bit Score: 49.34 E-value: 1.82e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 229 AVSGGVDSTVASKLMTEAIGDRFHAILVDNGVLRLNEAANVKKtLVEGLGINLMVVDASE 288
Cdd:COG1606 21 AFSGGVDSTLLAKVAHDVLGDRVLAVTADSPSLPERELEEAKE-LAKEIGIRHEVIETDE 79
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
56-178 |
2.77e-06 |
|
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: 48.41 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 56 GVILSGGPY---SVYAEDaPHVDHAIFDL----------------NVPILGICYGMQELAWING--------KQVGRGDK 108
Cdd:pfam07722 61 GLLLTGGPNvdpHFYGEE-PSESGGPYDPardayelaliraalarGKPILGICRGFQLLNVALGgtlyqdiqEQPGFTDH 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 109 RE------YGPA-TLKVidDSNSLFKGM---NDSTVWMSHGDKLHGLPTGYKTIATSDNspycGIVH------ETKPIYG 172
Cdd:pfam07722 140 REhcqvapYAPShAVNV--EPGSLLASLlgsEEFRVNSLHHQAIDRLAPGLRVEAVAPD----GTIEaiespnAKGFALG 213
|
....*.
gi 285814221 173 IQFHPE 178
Cdd:pfam07722 214 VQWHPE 219
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
82-192 |
6.37e-06 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 49.08 E-value: 6.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 82 NVPILGICYGMQELAWINGKQV--------GRGDKREYGPATL------------KV------IDDSNSLFKGMNdSTVW 135
Cdd:PLN02889 162 DIPILGVCLGHQALGYVHGARIvhapepvhGRLSEIEHNGCRLfddipsgrnsgfKVvryhslVIDAESLPKELV-PIAW 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 136 MSHGDKLHGL--------PTGYKTI----------------ATSDNSPYC----------GIVHETKPIYGIQFHPEVTH 181
Cdd:PLN02889 241 TSSSDTLSFLesqksglvPDAYESQigqsgssdpfssklknGTSWPSSHSermqngkilmGIMHSTRPHYGLQFHPESIA 320
|
170
....*....|.
gi 285814221 182 STQGKTLLKNF 192
Cdd:PLN02889 321 TCYGRQIFKNF 331
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
56-178 |
7.74e-06 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153216 [Multi-domain] Cd Length: 189 Bit Score: 46.80 E-value: 7.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 56 GVILSGGPySV----YAEDAPHVDHAIF---------------DLNVPILGICYGMQELAwingkqvgrgdkrEYGPATL 116
Cdd:cd01745 56 GLLLTGGG-DVdpplYGEEPHPELGPIDperdafelallraalERGKPILGICRGMQLLN-------------VALGGTL 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285814221 117 ----KViddsNSLfkgmndstvwmsHGDKLHGLPTGYKTIATSDNspycGIV----HETKP-IYGIQFHPE 178
Cdd:cd01745 122 yqdiRV----NSL------------HHQAIKRLADGLRVEARAPD----GVIeaieSPDRPfVLGVQWHPE 172
|
|
| NAD_synthase |
cd00553 |
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ... |
226-309 |
8.99e-06 |
|
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de novo nicotinamide adenine dinucleotide (NAD(+)) biosynthesis, an amide transfer from either ammonia or glutamine to nicotinic acid adenine dinucleotide (NaAD). The conversion of NaAD to NAD(+) occurs via a NAD-adenylate intermediate and requires ATP and Mg(2+). The intermediate is subsequently cleaved into NAD(+) and AMP. In many prokaryotes, such as Escherichia coli, NAD synthase consists of a single domain and is strictly ammonia dependent. In contrast, eukaryotes and other prokaryotes have an additional N-terminal amidohydrolase domain that prefer glutamine. Interestingly, NAD(+) synthases in these prokaryotes, can also utilize ammonia as an amide source.
Pssm-ID: 467484 [Multi-domain] Cd Length: 248 Bit Score: 47.16 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 226 VIGaVSGGVDSTVASKLMTEAIG-DRFHAILVDNGVLRlNEAANVKKTLVEGLGINLMVVD---ASEEFLSKLKGVTDPE 301
Cdd:cd00553 27 VLG-LSGGIDSAVVAALAVRALGaENVLALIMPSRYSS-KETRDDAKALAENLGIEYRTIDidpIVDAFLKALEHAGGSE 104
|
....*...
gi 285814221 302 KKRKIIGN 309
Cdd:cd00553 105 AEDLALGN 112
|
|
| hisH |
PRK13146 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
84-192 |
2.61e-05 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237290 [Multi-domain] Cd Length: 209 Bit Score: 45.16 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 84 PILGICYGMQELAwingkqvGRGdkREYG--------PATLKVIDDSNSLFK----GMNdsTVWMSHGDKL-HGLPTG-- 148
Cdd:PRK13146 79 PFLGICVGMQLLF-------ERG--LEHGdtpglgliPGEVVRFQPDGPALKvphmGWN--TVDQTRDHPLfAGIPDGar 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 285814221 149 -Y-------------KTIATSD-NSPYCGIVhETKPIYGIQFHPEVTHsTQGKTLLKNF 192
Cdd:PRK13146 148 fYfvhsyyaqpanpaDVVAWTDyGGPFTAAV-ARDNLFATQFHPEKSQ-DAGLALLRNF 204
|
|
| LarE-like |
cd01990 |
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ... |
226-402 |
4.18e-05 |
|
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: 44.94 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 226 VIGAVSGGVDSTVASKLMTEAIGDRFHAILVDNGVL---RLNEAanvkKTLVEGLGINLMVVDASEefLSKLKGVTDPEK 302
Cdd:cd01990 2 VVVAFSGGVDSSLLAKLAKEVLGDNVVAVTADSPLVpreELEEA----KRIAEEIGIRHEIIKTDE--LDDEEYVANDPD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 303 K----RKIIGNTFIHVfereaekikpKDGKEIQFLLQGTLYPDVIEsisfkgpsqtikthHNVGGL-LENMKLKLIEPLR 377
Cdd:cd01990 76 RcyhcKKALYSTLKEI----------AKERGYDVVLDGTNADDLKD--------------YRPGLLaAAELGIRSPLPEL 131
|
170 180
....*....|....*....|....*
gi 285814221 378 ELFKDEVRHLGELLGIPhdlVWRHP 402
Cdd:cd01990 132 GLTKSEIRELARELGLP---NWDKP 153
|
|
| PRK07053 |
PRK07053 |
glutamine amidotransferase; Provisional |
57-180 |
5.94e-05 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 235919 [Multi-domain] Cd Length: 234 Bit Score: 44.55 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 57 VILsGGPYSVYAEDA-PHVDHAI------FDLNVPILGICYGMQELAWINGKQVGRGDKREYGPATLKVIDDSN-SLFKG 128
Cdd:PRK07053 52 VVL-GGPIGVYDDELyPFLAPEIallrqrLAAGLPTLGICLGAQLIARALGARVYPGGQKEIGWAPLTLTDAGRaSPLRH 130
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 285814221 129 MNDST-VWMSHGDKLHgLPTGYKTIATSDNSPycgivHET----KPIYGIQFHPEVT 180
Cdd:PRK07053 131 LGAGTpVLHWHGDTFD-LPEGATLLASTPACR-----HQAfawgNHVLALQFHPEAR 181
|
|
| PRK05665 |
PRK05665 |
amidotransferase; Provisional |
85-181 |
9.52e-05 |
|
amidotransferase; Provisional
Pssm-ID: 168162 [Multi-domain] Cd Length: 240 Bit Score: 44.03 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 85 ILGICYGMQELAWINGKQVGRGDKR-EYGPATLKVIDDSNSLFKGMNDSTVWMSHGDKLHGLPTGYKTIATSDNSPYcGI 163
Cdd:PRK05665 94 LLGVCFGHQLLALLLGGKAERASQGwGVGIHRYQLAAHAPWMSPAVTELTLLISHQDQVTALPEGATVIASSDFCPF-AA 172
|
90
....*....|....*...
gi 285814221 164 VHETKPIYGIQFHPEVTH 181
Cdd:PRK05665 173 YHIGDQVLCFQGHPEFVH 190
|
|
| TtuA-like |
cd01993 |
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ... |
218-395 |
1.46e-04 |
|
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) 2-sulfurtransferase, also called tRNA thiouridine synthetase TtuA, catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T). TtuA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus.
Pssm-ID: 467497 [Multi-domain] Cd Length: 190 Bit Score: 42.70 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 218 KLVGPTAEVIGAVSGGVDSTVASKLMTEaIGDRFHAILVDNGVLRL-NEAANVKKTLVEGLGINLMVVDASEEFlskLKG 296
Cdd:cd01993 3 KMFEKDDKILVAVSGGKDSLALLAVLKK-LGYNVEALYINLGIGEYsEKSEEVVKKLAEKLNLPLHVVDLKEEY---GLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 297 VTDPEKKRK-----IIGNTFIHVFEREAEKIKPK---------DgkEIQFLLQGTLYPDvIESISFKGPsqtiKTHHNVG 362
Cdd:cd01993 79 IPELAKKSRrppcsVCGLVKRYIMNKFAVENGFDvvatghnldD--EAAFLLGNILNWN-EEYLAKQGP----FLLPEHG 151
|
170 180 190
....*....|....*....|....*....|...
gi 285814221 363 GLLENMKlkliePLRELFKDEVRHLGELLGIPH 395
Cdd:cd01993 152 GLVTRVK-----PLYEITEEEIALYALLNGIPY 179
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
226-310 |
1.56e-04 |
|
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: 44.45 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 226 VIGaVSGGVDSTVASKLMTEAIG-DRFHAIL----------VDNGvlrlneaanvkKTLVEGLGINLMVVD---ASEEFL 291
Cdd:COG0171 290 VLG-LSGGIDSALVAALAVDALGpENVLGVTmpsrytsdesLEDA-----------EELAENLGIEYEEIDitpAVEAFL 357
|
90
....*....|....*....
gi 285814221 292 SKLKGVTDPEKKRKIIGNT 310
Cdd:COG0171 358 EALPHAFGGELDDVAEENL 376
|
|
| IMP_synth_hisH |
TIGR01855 |
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ... |
83-193 |
1.68e-04 |
|
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: 42.70 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 83 VPILGICYGMQ-------E------LAWINGKqVGRGDKR---EYGPATLKVIDDSNsLFKGMN-DSTVWMSHgdKLHGL 145
Cdd:TIGR01855 72 KPVLGICLGMQllferseEgggvpgLGLIKGN-VVKLEARkvpHMGWNEVHPVKESP-LLNGIDeGAYFYFVH--SYYAV 147
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 285814221 146 PTGYKTIATSD-NSPYCGIVhETKPIYGIQFHPEVTHSTqGKTLLKNFA 193
Cdd:TIGR01855 148 CEEEAVLAYADyGEKFPAAV-QKGNIFGTQFHPEKSGKT-GLKLLENFL 194
|
|
| PuuD |
COG2071 |
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
56-96 |
3.68e-04 |
|
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: 42.08 E-value: 3.68e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285814221 56 GVILSGG----PYSvYAEDaPHVDHAIFD----------------LNVPILGICYGMQELA 96
Cdd:COG2071 52 GLVLTGGadvdPAL-YGEE-PHPELGPIDperdafelaliraaleRGKPVLGICRGMQLLN 110
|
|
| hisH |
PRK14004 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
84-192 |
8.84e-04 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 172505 [Multi-domain] Cd Length: 210 Bit Score: 40.66 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 84 PILGICYGMQEL-------------AWINGKQVGRGDKREYGPATLKVI-----------DDSNSLFKGM-NDSTVWMSH 138
Cdd:PRK14004 74 PLFGICIGFQILfesseetnqgtkkEQIEGLGYIKGKIKKFEGKDFKVPhigwnrlqirrKDKSKLLKGIgDQSFFYFIH 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 285814221 139 GDKlhglPTGYKTIATSDNSPYCG----IVHETKPIYGIQFHPEVTHsTQGKTLLKNF 192
Cdd:PRK14004 154 SYR----PTGAEGNAITGLCDYYQekfpAVVEKENIFGTQFHPEKSH-THGLKLLENF 206
|
|
| TilS |
COG0037 |
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ... |
218-296 |
1.36e-03 |
|
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: 40.59 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285814221 218 KLVGPTAEVIGAVSGGVDSTV---ASKLMTEAIGDRFHAILVDNGvLRLN---EAANVKKtLVEGLGINLMVVDASEEFL 291
Cdd:COG0037 10 RLLEPGDRILVAVSGGKDSLAllhLLAKLRRRLGFELVAVHVDHG-LREEsdeDAEFVAE-LCEELGIPLHVVRVDVPAI 87
|
....*
gi 285814221 292 SKLKG 296
Cdd:COG0037 88 AKKEG 92
|
|
| TilS_N |
cd01992 |
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ... |
229-281 |
3.61e-03 |
|
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: 38.73 E-value: 3.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 285814221 229 AVSGGVDSTVASKLMTEAI---GDRFHAILVDNGvLRLN---EAANVKKtLVEGLGINL 281
Cdd:cd01992 5 AVSGGPDSMALLHLLKELRpklGLKLVAVHVDHG-LREEsaeEAQFVAK-LCKKLGIPL 61
|
|
| AANH_WbpG-like |
cd01996 |
Rhizobium leguminosarum WbpG protein and similar proteins; This subfamily includes Rhizobium ... |
226-282 |
3.94e-03 |
|
Rhizobium leguminosarum WbpG protein and similar proteins; This subfamily includes Rhizobium leguminosarum WbpG and Campylobacter jejuni PseA proteins. They belong to the of adenine nucleotide alpha hydrolase (AANH) superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus.
Pssm-ID: 467500 [Multi-domain] Cd Length: 158 Bit Score: 38.12 E-value: 3.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 285814221 226 VIGaVSGGVDSTVASKLMTEAIGDRFHAILVDNGVLRLNEAANVKKtLVEGLGINLM 282
Cdd:cd01996 9 IIG-VSGGKDSTYAAHKAKEKYGLRPLLVTVDAGWNSPEAVKNIEK-LVRALGVDLI 63
|
|
| |
