|
Name |
Accession |
Description |
Interval |
E-value |
| guaA |
PRK00074 |
GMP synthase; Reviewed |
5-525 |
0e+00 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 1105.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 5 IHKHRILILDFGSQYTQLVARRVRELGVYCELWAWDVTEAQIRDFNPSGIILSGGPESTTEENSPRAPQYVFEAGVPVFG 84
Cdd:PRK00074 1 IHHDKILILDFGSQYTQLIARRVRELGVYSEIVPYDISAEEIRAFNPKGIILSGGPASVYEEGAPRADPEIFELGVPVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 85 VCYGMQTMAMQLGGHVEGSNEREFGYAQVEVLTDSALVRGIEDSLtadgkpllDVWMSHGDKVTAIPSDFVTVASTESCP 164
Cdd:PRK00074 81 ICYGMQLMAHQLGGKVERAGKREYGRAELEVDNDSPLFKGLPEEQ--------DVWMSHGDKVTELPEGFKVIASTENCP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 165 FAIMANEEKRFYGVQFHPEVTHTRQGMRMLERFVRDICQCEALWTPAKIIDDAVARIREQVGDDKVILGLSGGVDSSVTA 244
Cdd:PRK00074 153 IAAIANEERKFYGVQFHPEVTHTPQGKKLLENFVFDICGCKGDWTMENFIEEAIEEIREQVGDKKVILGLSGGVDSSVAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 245 MLLHRAIGKNLTCVFVDNGLLRLNEAEQVMDMFGDHFGLNIVHVPAEERFLSALAGENDPEAKRKIIGRVFVEVFDEEAL 324
Cdd:PRK00074 233 VLLHKAIGDQLTCVFVDHGLLRKNEAEQVMEMFREHFGLNLIHVDASDRFLSALAGVTDPEEKRKIIGREFIEVFEEEAK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 325 KLEDVKWLAQGTIYPDVIESAasATGKAHVIKSHHNVGGLPKEMKMGLVEPLKELFKDEVRKIGLELGLPYDMLYRHPFP 404
Cdd:PRK00074 313 KLGGVKFLAQGTLYPDVIESG--GTKKAATIKSHHNVGGLPEDMKLKLVEPLRELFKDEVRKLGLELGLPEEIVYRHPFP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 405 GPGLGVRVLGEVKKEYCDLLRRADAIFIEELRKADLYDKVSQAFTVFLPVRSVGVMGDGRKYDWVVSLRAVETIDFMTAH 484
Cdd:PRK00074 391 GPGLAIRILGEVTKEKLDILREADAIFIEELRKAGLYDKIWQAFAVLLPVKSVGVMGDGRTYDYVVALRAVTSIDGMTAD 470
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 446060441 485 WAHLPYDFLGRVSNRIINEVNGISRVVYDISGKPPATIEWE 525
Cdd:PRK00074 471 WARLPYDFLEKISNRIINEVKGVNRVVYDITSKPPATIEWE 511
|
|
| GuaA2 |
COG0519 |
GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, ... |
5-525 |
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: 940.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 5 IHKHRILILDFGSQYTQLVARRVRELGVYCELWAWDVTEAQIRDFNPSGIILSGGPESTTEENSPRAPQYVFEAGVPVFG 84
Cdd:COG0519 1 MDKEIIIVLDFGGQYQQLIARRRREEGVYSEIIPPDTAAEEIKAKGPPGIILSGGPSSVYEEGAPPDDPELFELGGPILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 85 VCYGMQTMAMQLGGHVEGSNEREFGYAqvevltdsALVRGIEDSLTADGKPLLDVWMSHGDKVTAIPSDFVTVASTESCP 164
Cdd:COG0519 81 ICYGGQLMLHLLGGGVVRAERREYGGA--------LLLVDDESDLFAGGPEELQVWMSHGDRVTELPPGFEVIASTENCP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 165 FAIMANEEKRFYGVQFHPEVTHTRQGMRMLERFVRDICQCEALWTPAKIIDDAVARIREQVGDDKVILGLSGGVDSSVTA 244
Cdd:COG0519 153 VAAIANEERKLYGVQFHPEVVHTEQGKEILKNFLFDICGCKGDWTMENFIEEAIEEIREQVGDGKVICALSGGVDSSVAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 245 MLLHRAIGKNLTCVFVDNGLLRLNEAEQVMDMFGDHFGLNIVHVPAEERFLSALAGENDPEAKRKIIGRVFVEVFDEEAL 324
Cdd:COG0519 233 ALLHKAIGDQLTCVFVDHGLLRKGEAEQVEETFKEHFGLNLIYVDASERFLSALKGVTDPEEKRKIIGEEFIEVFEEEAK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 325 KLEDVKWLAQGTIYPDVIESaASATGKAHVIKSHHNVGGLPKEMKMGLVEPLKELFKDEVRKIGLELGLPYDMLYRHPFP 404
Cdd:COG0519 313 KLGGAKFLAQGTLYPDVIES-GSVKGPAATIKSHHNVGGLPEDMKFKLVEPLRELFKDEVRALGRELGLPEEIVYRHPFP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 405 GPGLGVRVLGEVKKEYCDLLRRADAIFIEELRKADLYDKVSQAFTVFLPVRSVGVMGDGRKYDWVVSLRAVETIDFMTAH 484
Cdd:COG0519 392 GPGLAIRILGEVTKEKLEILREADAIFIEELRKAGLYDKVWQAFAVLLPVKSVGVMGDERTYEYVVALRAVTSVDGMTAD 471
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 446060441 485 WAHLPYDFLGRVSNRIINEVNGISRVVYDISGKPPATIEWE 525
Cdd:COG0519 472 WARLPYEVLERISNRIINEVKGVNRVVYDITSKPPATIEWE 512
|
|
| PLN02347 |
PLN02347 |
GMP synthetase |
6-525 |
0e+00 |
|
GMP synthetase
Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 687.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 6 HKHRILILDFGSQYTQLVARRVRELGVYCELWAWDVTEAQIRDFNPSGIILSGGPESTTEENSPRAP----QYVFEAGVP 81
Cdd:PLN02347 9 YLDVVLILDYGSQYTHLITRRVRELGVYSLLLSGTASLDRIASLNPRVVILSGGPHSVHVEGAPTVPegffDYCRERGVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 82 VFGVCYGMQTMAMQLGGHVEGSNEREFGYAQVEVLTDSALVRGIEDSLTADgkplldVWMSHGDKVTAIPSDFVTVASTE 161
Cdd:PLN02347 89 VLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCGSQLFGDLPSGETQT------VWMSHGDEAVKLPEGFEVVAKSV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 162 SCPFAIMANEEKRFYGVQFHPEVTHTRQGMRMLERFVRDICQCEALWTPAKIIDDAVARIREQVG-DDKVILGLSGGVDS 240
Cdd:PLN02347 163 QGAVVAIENRERRIYGLQYHPEVTHSPKGMETLRHFLFDVCGVTADWKMQDVLEEQIELIKATVGpDEHVICALSGGVDS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 241 SVTAMLLHRAIGKNLTCVFVDNGLLRLNEAEQVMDMFGDHFGLNIVHVPAEERFLSALAGENDPEAKRKIIGRVFVEVFD 320
Cdd:PLN02347 243 TVAATLVHKAIGDRLHCVFVDNGLLRYKEQERVMETFKRDLHLPVTCVDASERFLSKLKGVTDPEKKRKIIGAEFIEVFD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 321 EEALKLED-----VKWLAQGTIYPDVIESA---ASATGKAHVIKSHHNVGGLPKEMKMGLVEPLKELFKDEVRKIGLELG 392
Cdd:PLN02347 323 EFAHKLEQklgkkPAFLVQGTLYPDVIESCpppGSGRTHSHTIKSHHNVGGLPKDMKLKLIEPLKLLFKDEVRKLGRLLG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 393 LPYDMLYRHPFPGPGLGVRVLGEVKKE-YCDLLRRADAIFIEELRKADLYDKVSQAFTVFLPVRSVGVMGDGRKYDWVVS 471
Cdd:PLN02347 403 VPEAFLKRHPFPGPGLAVRVLGDVTEGnALDILRQVDEIFINSIKDAGLYDEIWQAFAVFLPVKSVGVQGDQRTHSHVVA 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 446060441 472 LRAVETIDFMTAHWAHLPYDFLGRVSNRIINEVNGISRVVYDISGKPPATIEWE 525
Cdd:PLN02347 483 LRAVTSEDGMTADWYHFEHKFLDDVSRKICNEVRGVNRVVYDITSKPPSTIEWE 536
|
|
| guaA_Cterm |
TIGR00884 |
GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; This protein of purine ... |
212-525 |
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: 589.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 212 KIIDDAVARIREQVGDDKVILGLSGGVDSSVTAMLLHRAIGKNLTCVFVDNGLLRLNEAEQVMDMFGDHFGLNIVHVPAE 291
Cdd:TIGR00884 1 NFIEEAVEEIREQVGDAKVIIALSGGVDSSVAAVLAHRAIGDRLTCVFVDHGLLRKGEAEQVVKTFGDRLGLNLVYVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 292 ERFLSALAGENDPEAKRKIIGRVFVEVFDEEALKLEDVKWLAQGTIYPDVIESAAsatGKAHVIKSHHNVGGLPKEMKMG 371
Cdd:TIGR00884 81 ERFLSALKGVTDPEEKRKIIGRVFIEVFEREAKKIGDAEYLAQGTIYPDVIESAA---GTAHVIKSHHNVGGLPEDMKLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 372 LVEPLKELFKDEVRKIGLELGLPYDMLYRHPFPGPGLGVRVLGEVKKEYCDLLRRADAIFIEELRKADLYDKVSQAFTVF 451
Cdd:TIGR00884 158 LVEPLRELFKDEVRKLGKELGLPEEIVWRHPFPGPGLAVRVLGEVTKEKLEILRRADAIVIEELKKAGLYDKVWQAFAVL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446060441 452 LPVRSVGVMGDGRKYDWVVSLRAVETIDFMTAHWAHLPYDFLGRVSNRIINEVNGISRVVYDISGKPPATIEWE 525
Cdd:TIGR00884 238 LPVKSVGVMGDGRTYGYVIALRAVESIDGMTADWARLPYDFLERISNRITNEVPGVNRVVYDITSKPPATIEWE 311
|
|
| GMP_synthase_C |
cd01997 |
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ... |
221-525 |
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: 532.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 221 IREQVGDDKVILGLSGGVDSSVTAMLLHRAIGK-NLTCVFVDNGLLRLNEAEQVMDMFGDHFGLNIVHVPAEERFLSALA 299
Cdd:cd01997 1 IKRTVGDKKVLCLVSGGVDSTVCAALLHKALGDeRVIAVHIDNGLMRKNESEQVEEALKKLGVINLAKVDASKRFLKKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 300 GENDPEAKRKIIGRVFVEVFDEEALKLE---DVKWLAQGTIYPDVIESAAS-ATGKAHVIKSHHNVGGLPKE-MKMGLVE 374
Cdd:cd01997 81 GVTDPEEKRKIIGDTFIEVFDEVAKELNldpDDVYLAQGTLYPDLIESASSlASSKADTIKTHHNVGGLPRElLKGKLVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 375 PLKELFKDEVRKIGLELGLPYDMLYRHPFPGPGLGVRVLGEVKKEYCDLLRRADAIFIEELRKADLYDKVSQAFTVFLPV 454
Cdd:cd01997 161 PLRDLFKDEVRELGRELGLPEELVWRHPFPGPGLAIRVLGEVTPEKLEILREADAIVEEELREAGLYDKISQAFAVLLPI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446060441 455 RSVGVMGDGRKYDWVVSLRAVETIDFMTAHWAHLPYDFLGRVSNRIINEVNGISRVVYDISGKPPATIEWE 525
Cdd:cd01997 241 KSVGVQGDGRTYGYVVALRAVETEDFMTAEWARPPYEVLDKISNRITNEVPGVNRVVYDITSKPPATIEWE 311
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
10-205 |
1.34e-113 |
|
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: 334.28 E-value: 1.34e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 10 ILILDFGSQYTQLVARRVRELGVYCELWAWDVTEAQIRDFNPSGIILSGGPESTTEENSPRAPQYVFEAGVPVFGVCYGM 89
Cdd:TIGR00888 1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGPSSVYAENAPRADEKIFELGVPVLGICYGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 90 QTMAMQLGGHVEGSNEREFGYAQVEVLTDSALVRGIEDsltadgkpLLDVWMSHGDKVTAIPSDFVTVASTESCPFAIMA 169
Cdd:TIGR00888 81 QLMAKQLGGEVGRAEKREYGKAELEILDEDDLFRGLPD--------ESTVWMSHGDKVKELPEGFKVLATSDNCPVAAMA 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 446060441 170 NEEKRFYGVQFHPEVTHTRQGMRMLERFVRDICQCE 205
Cdd:TIGR00888 153 HEEKPIYGVQFHPEVTHTEYGNELLENFVYDVCGCE 188
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
10-198 |
1.08e-101 |
|
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: 303.30 E-value: 1.08e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 10 ILILDFGSQYTQLVARRVRELGVYCELWAWDVTEAQIRDFNPSGIILSGGPESTTEENSPRAPQYVFEAGVPVFGVCYGM 89
Cdd:cd01742 1 ILILDFGSQYTHLIARRVRELGVYSEILPNTTPLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGICYGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 90 QTMAMQLGGHVEGSNEREFGYAQVEVLTDSALVRGIEDSLTadgkplldVWMSHGDKVTAIPSDFVTVASTESCPFAIMA 169
Cdd:cd01742 81 QLIAKALGGKVERGDKREYGKAEIEIDDSSPLFEGLPDEQT--------VWMSHGDEVVKLPEGFKVIASSDNCPVAAIA 152
|
170 180
....*....|....*....|....*....
gi 446060441 170 NEEKRFYGVQFHPEVTHTRQGMRMLERFV 198
Cdd:cd01742 153 NEEKKIYGVQFHPEVTHTEKGKEILKNFL 181
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
9-201 |
1.20e-66 |
|
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: 214.81 E-value: 1.20e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 9 RILILD---FGSQYTQLVARRVRELG-------VY-CELWAWDVTEAqirdfNPSGIILSGGPESTTEE-----NSPRAP 72
Cdd:COG0518 1 KILILDhdpFGGQYPGLIARRLREAGieldvlrVYaGEILPYDPDLE-----DPDGLILSGGPMSVYDEdpwleDEPALI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 73 QYVFEAGVPVFGVCYGMQTMAMQLGGHVEGSNEREFGYAQVEVLTDSALVRGIEDSLTadgkplldVWMSHGDKVTAIPS 152
Cdd:COG0518 76 REAFELGKPVLGICYGAQLLAHALGGKVEPGPGREIGWAPVELTEADPLFAGLPDEFT--------VWMSHGDTVTELPE 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446060441 153 DFVTVASTESCPFAIMANeEKRFYGVQFHPEVTHT------------------------------RQGMRMLERFVRDI 201
Cdd:COG0518 148 GAEVLASSDNCPNQAFRY-GRRVYGVQFHPEVTHTmmeawleeradelaaeellaeaslhdpelrEAGRRLLRNFLREI 225
|
|
| GMP_synt_C |
pfam00958 |
GMP synthase C terminal domain; GMP synthetase is a glutamine amidotransferase from the de ... |
433-524 |
2.67e-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: 201.10 E-value: 2.67e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 433 EELRKADLYDKVSQAFTVFLPVRSVGVMGDGRKYDWVVSLRAVETIDFMTAHWAHLPYDFLGRVSNRIINEVNGISRVVY 512
Cdd:pfam00958 1 EEIKKAGLYRKIWQAFAVLLPVKSVGVMGDERTYEYVVALRAVTSTDGMTADWARLPYEVLEKISNRIVNEVPGVNRVVY 80
|
90
....*....|..
gi 446060441 513 DISGKPPATIEW 524
Cdd:pfam00958 81 DITSKPPATIEW 92
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
11-201 |
1.68e-49 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 168.57 E-value: 1.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 11 LILDFGSQYTQLVARRVRELGVYCELWAWDVTEAQIRDFNPSGIILSGGPES-TTEENSPRAPQYVFEAGVPVFGVCYGM 89
Cdd:pfam00117 1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSpGAAGGAIEAIREARELKIPILGICLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 90 QTMAMQLGGHVEGSNEREFGYAQVEVLTDSAlvrgiedSLTADGKPLLDVWMSHGDKVTA--IPSDF-VTVASTESCPFA 166
Cdd:pfam00117 81 QLLALAFGGKVVKAKKFGHHGKNSPVGDDGC-------GLFYGLPNVFIVRRYHSYAVDPdtLPDGLeVTATSENDGTIM 153
|
170 180 190
....*....|....*....|....*....|....*
gi 446060441 167 IMANEEKRFYGVQFHPEVTHTRQGMRMLERFVRDI 201
Cdd:pfam00117 154 GIRHKKLPIFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
9-203 |
1.70e-47 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 163.10 E-value: 1.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 9 RILILDFGSQYTQLVARRVRELGVYCELWAWDVTEAQIRDfNPSGIILSGGPEStteENSPRAPQYVFEAGVPVFGVCYG 88
Cdd:PRK00758 1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTTPVEEIKA-FEDGLILSGGPDI---ERAGNCPEYLKELDVPILGICLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 89 MQTMAMQLGGHVEGSNEREFGYAQVEVLTDSALVRGIEDSLTadgkplldVWMSHGDKVTAIPSDFVTVASTESCPFAIM 168
Cdd:PRK00758 77 HQLIAKAFGGEVGRGEYGEYALVEVEILDEDDILKGLPPEIR--------VWASHADEVKELPDGFEILARSDICEVEAM 148
|
170 180 190
....*....|....*....|....*....|....*
gi 446060441 169 ANEEKRFYGVQFHPEVTHTRQGMRMLERFVrDICQ 203
Cdd:PRK00758 149 KHKEKPIYGVQFHPEVAHTEYGEEIFKNFL-EICG 182
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
9-198 |
4.48e-26 |
|
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: 105.02 E-value: 4.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 9 RILILDFGSQYTQ-LVARRVRELGVycELWAWDVTEAQIRDFNPS-----GIILSGGPESTTEENSP------RAPQYVF 76
Cdd:cd01741 1 RILILQHDTPEGPgLFEDLLREAGA--ETIEIDVVDVYAGELLPDlddydGLVILGGPMSVDEDDYPwlkklkELIRQAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 77 EAGVPVFGVCYGMQTMAMQLGGHVE-GSNEREFGYAQVEvLTDsalvRGIEDSLTADGKPLLDVWMSHGDKVTAIPSDFV 155
Cdd:cd01741 79 AAGKPVLGICLGHQLLARALGGKVGrNPKGWEIGWFPVT-LTE----AGKADPLFAGLPDEFPVFHWHGDTVVELPPGAV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446060441 156 TVASTESCPFAIMANEEkRFYGVQFHPEvthtrqgMRMLERFV 198
Cdd:cd01741 154 LLASSEACPNQAFRYGD-RALGLQFHPE-------ERLLRNFL 188
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
10-198 |
2.79e-19 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.
Pssm-ID: 153214 [Multi-domain] Cd Length: 184 Bit Score: 85.66 E-value: 2.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 10 ILILD-FGSqYTQLVARRVRELGVYCELWAWD-VTEAQIRDFNPSGIILSGGPES-TTEENSPRAPQYvFEAGVPVFGVC 86
Cdd:cd01743 1 ILLIDnYDS-FTYNLVQYLRELGAEVVVVRNDeITLEELELLNPDAIVISPGPGHpEDAGISLEIIRA-LAGKVPILGVC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 87 YGMQTMAMQLGGHVEGSNEREFGYAQVEVLTDSALVRGIED--------SLTADGKPLldvwmshgdkvtaiPSDFVTVA 158
Cdd:cd01743 79 LGHQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQpftvgryhSLVVDPDPL--------------PDLLEVTA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446060441 159 STESCpfAIMA--NEEKRFYGVQFHPEVTHTRQGMRMLERFV 198
Cdd:cd01743 145 STEDG--VIMAlrHRDLPIYGVQFHPESILTEYGLRLLENFL 184
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
10-199 |
2.66e-18 |
|
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: 82.78 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 10 ILILD-FGS------QYtqlvarrVRELGVYCELWAWD-VTEAQIRDFNPSGIILSGGPEstTEENSPRAPQYV--FEAG 79
Cdd:COG0512 1 ILLIDnYDSftynlvQY-------LGELGAEVVVVRNDeITLEEIEALAPDGIVLSPGPG--TPEEAGISLEVIraFAGK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 80 VPVFGVCYGMQTMAMQLGGHVEGSNEREFGYA-QVEVlTDSALVRGIED--------SLTADGKPLldvwmshgdkvtai 150
Cdd:COG0512 72 IPILGVCLGHQAIGEAFGGKVVRAPEPMHGKTsPITH-DGSGLFAGLPNpftatryhSLVVDRETL-------------- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446060441 151 PSDFVTVASTESCpfAIMA--NEEKRFYGVQFHPEVTHTRQGMRMLERFVR 199
Cdd:COG0512 137 PDELEVTAWTEDG--EIMGirHRELPIEGVQFHPESILTEHGHQLLANFLE 185
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
10-199 |
1.13e-15 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 75.17 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 10 ILILD-FGS------QYtqlvarrVRELGVYCELWAWD-VTEAQIRDFNPSGIILSGGPeSTTEE--NSPRAPQYvFEAG 79
Cdd:PRK05670 2 ILLIDnYDSftynlvQY-------LGELGAEVVVYRNDeITLEEIEALNPDAIVLSPGP-GTPAEagISLELIRE-FAGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 80 VPVFGVCYGMQTMAMQLGGHVEGSNEREFGYAQVEVLTDSALVRGIED--------SLTADGKPLLDVWmshgdKVTAIP 151
Cdd:PRK05670 73 VPILGVCLGHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNpftvtryhSLVVDRESLPDCL-----EVTAWT 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446060441 152 SDFVtvastescpfaIMA--NEEKRFYGVQFHPEVTHTRQGMRMLERFVR 199
Cdd:PRK05670 148 DDGE-----------IMGvrHKELPIYGVQFHPESILTEHGHKLLENFLE 186
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
40-199 |
3.20e-14 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 71.37 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 40 DVTEAQIRDFNPSGIILSGGPESTTEENSPRAPQYVFEAGVPVFGVCYGMQTMAMQLGGHVEGSnEREFGYAQVEVLTDS 119
Cdd:PRK07649 33 EVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCLGHQSIAQVFGGEVVRA-ERLMHGKTSLMHHDG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 120 ALV-RGIEDSLTADGKPLLDVwmshgdKVTAIPSDFVTVASTESCPFAIMANEEKRFYGVQFHPEVTHTRQGMRMLERFV 198
Cdd:PRK07649 112 KTIfSDIPNPFTATRYHSLIV------KKETLPDCLEVTSWTEEGEIMAIRHKTLPIEGVQFHPESIMTSHGKELLQNFI 185
|
.
gi 446060441 199 R 199
Cdd:PRK07649 186 R 186
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
9-226 |
9.45e-14 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 70.46 E-value: 9.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 9 RILILDfgsQYTQLVARRVR---ELGVYCELWAWD---VTEAQIRDFNPSGIILSGGPeSTTEENSPRAP--QYVFEAGV 80
Cdd:PRK07765 2 RILVVD---NYDSFVFNLVQylgQLGVEAEVWRNDdprLADEAAVAAQFDGVLLSPGP-GTPERAGASIDmvRACAAAGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 81 PVFGVCYGMQTMAMQLGGHVEGSNEREFGYAQVEVLTDSALVRGIEDSLTADGKPLLDVwmshgdKVTAIPSDFVTVAST 160
Cdd:PRK07765 78 PLLGVCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTI------LPETLPAELEVTART 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446060441 161 ESCPFAIMANEEKRFYGVQFHPEVTHTRQGMRMLERFVrDICQcealWTPAkiiDDAVARIREQVG 226
Cdd:PRK07765 152 DSGVIMAVRHRELPIHGVQFHPESVLTEGGHRMLANWL-TVCG----WAPD---EALVRRLENEVA 209
|
|
| PRK09065 |
PRK09065 |
glutamine amidotransferase; Provisional |
53-199 |
1.61e-12 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181635 [Multi-domain] Cd Length: 237 Bit Score: 67.29 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 53 GIILSGGPESTTE--ENSPRAPQYVFEA---GVPVFGVCYGMQTMAMQLGGHVeGSNE--REFGYAQVEvLTDSAlvrgI 125
Cdd:PRK09065 57 GVIITGSWAMVTDrlDWSERTADWLRQAaaaGMPLLGICYGHQLLAHALGGEV-GYNPagRESGTVTVE-LHPAA----A 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 126 EDSLTADGKPLLDVWMSHGDKVTAIPSDFVTVASTESCPFAIMANEEkRFYGVQFHPE---------------------- 183
Cdd:PRK09065 131 DDPLFAGLPAQFPAHLTHLQSVLRLPPGAVVLARSAQDPHQAFRYGP-HAWGVQFHPEftahimraylraradclrregl 209
|
170 180
....*....|....*....|....
gi 446060441 184 --------VTHTRQGMRMLERFVR 199
Cdd:PRK09065 210 dartllreVSEAPWARKLLRRFVR 233
|
|
| PRK07567 |
PRK07567 |
glutamine amidotransferase; Provisional |
52-183 |
6.42e-12 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181035 [Multi-domain] Cd Length: 242 Bit Score: 65.35 E-value: 6.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 52 SGIILSGGPESTT---EENSP---RAPQ-------YVFEAGVPVFGVCYGMQTMAMQLGGHVEGSNEREFGYAQVEvLTD 118
Cdd:PRK07567 53 SGVIVGGSPFNVSdpaESKSPwqrRVEAelsglldEVVARDFPFLGACYGVGTLGHHQGGVVDRTYGEPVGAVTVS-LTD 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446060441 119 SalvrGIEDSLTADGKPLLDVWMSHGDKVTAIPSDFVTVASTESCPF-AIMANEekRFYGVQFHPE 183
Cdd:PRK07567 132 A----GRADPLLAGLPDTFTAFVGHKEAVSALPPGAVLLATSPTCPVqMFRVGE--NVYATQFHPE 191
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
10-207 |
8.64e-12 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 64.82 E-value: 8.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 10 ILILDFGSQYTQLVARRVRELGVYCELWAWD-VTEAQIRDFNPSGIILSGGPesTTEENSPRAPQYVFEAG--VPVFGVC 86
Cdd:PLN02335 21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRNDeLTVEELKRKNPRGVLISPGP--GTPQDSGISLQTVLELGplVPLFGVC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 87 YGMQTMAMQLGG----------HVEGS--NEREFGyaqvevltDSALVRGIEDSLTADGKPLLDVwmshgdKVTAIPSDF 154
Cdd:PLN02335 99 MGLQCIGEAFGGkivrspfgvmHGKSSpvHYDEKG--------EEGLFSGLPNPFTAGRYHSLVI------EKDTFPSDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446060441 155 VTV-ASTESCpfAIMANEEKRF---YGVQFHPEVTHTRQGMRMLERFVRDICQCEAL 207
Cdd:PLN02335 165 LEVtAWTEDG--LIMAARHRKYkhiQGVQFHPESIITTEGKTIVRNFIKIIEKKESE 219
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
8-199 |
4.54e-11 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 65.32 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 8 HRILILDFGSQYTQLVARRVRELGVYCELWAWDVTEAQIRDFNPSGIILSGGPESTTEENSPRAPQYVFEAGVPVFGVCY 87
Cdd:PRK13566 527 KRVLLVDHEDSFVHTLANYFRQTGAEVTTVRYGFAEEMLDRVNPDLVVLSPGPGRPSDFDCKATIDAALARNLPIFGVCL 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 88 GMQTMAMQLGGHVEGSNEREFGYA-QVEVLTDSALVRGIEDSLTAdGKplldvWMS-HGDKVTaIPSDFVTVASTESCpf 165
Cdd:PRK13566 607 GLQAIVEAFGGELGQLAYPMHGKPsRIRVRGPGRLFSGLPEEFTV-GR-----YHSlFADPET-LPDELLVTAETEDG-- 677
|
170 180 190
....*....|....*....|....*....|....*....
gi 446060441 166 AIMANEEK--RFYGVQFHPEVTHT---RQGMRMLERFVR 199
Cdd:PRK13566 678 VIMAIEHKtlPVAAVQFHPESIMTlggDVGLRIIENVVR 716
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
10-198 |
7.16e-11 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 61.29 E-value: 7.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 10 ILILDFGSQYTQLVARRVRELGV-YCELWAWDVTEAQIRDFNPSGIILSGGPESTTEenSPRAPQYV--FEAGVPVFGVC 86
Cdd:CHL00101 2 ILIIDNYDSFTYNLVQSLGELNSdVLVCRNDEIDLSKIKNLNIRHIIISPGPGHPRD--SGISLDVIssYAPYIPILGVC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 87 YGMQTMAMQLGGHVEGSNEREFGYAQVEVLTDSALVRGIEDSLTADGKPLLDVwmshgDKVTaIPSDFVTVASTESCpfA 166
Cdd:CHL00101 80 LGHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLII-----DPLN-LPSPLEITAWTEDG--L 151
|
170 180 190
....*....|....*....|....*....|....*
gi 446060441 167 IMANEEKRF---YGVQFHPEVTHTRQGMRMLERFV 198
Cdd:CHL00101 152 IMACRHKKYkmlRGIQFHPESLLTTHGQQILRNFL 186
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
10-183 |
1.12e-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: 60.59 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 10 ILILDFGSQYTQLvaRRVRELGVYCELWAWDVTEAQIRDFNPSGIILSGGPestteeNSPRAPQY-------VFEAGVPV 82
Cdd:cd01744 1 VVVIDFGVKHNIL--RELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGP------GDPALLDEaiktvrkLLGKKIPI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 83 FGVCYGMQTMAMQLG--------GHvEGSNerefgYAQVEVLTDSALVrgiedslTAdgkplldvwMSHGDKVTA--IPS 152
Cdd:cd01744 73 FGICLGHQLLALALGaktykmkfGH-RGSN-----HPVKDLITGRVYI-------TS---------QNHGYAVDPdsLPG 130
|
170 180 190
....*....|....*....|....*....|..
gi 446060441 153 DF-VTVASTESCPFAIMANEEKRFYGVQFHPE 183
Cdd:cd01744 131 GLeVTHVNLNDGTVEGIRHKDLPVFSVQFHPE 162
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
33-198 |
2.86e-10 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 59.55 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 33 YCELWAW-------DVTEAQIRDFNPSGIILSGGPESTTEENSPRAPQYVFEAGVPVFGVCYGMQTMAMQLGGHVEGSNE 105
Cdd:PRK08007 19 FCELGADvlvkrndALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 106 REFGYAQVEVLTDSALVRGIEDSLTADGKPLLDVwmshgDKVTaIPSDFVTVASTESCPFAIMANEEKRFYGVQFHPEVT 185
Cdd:PRK08007 99 VMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVV-----EPDS-LPACFEVTAWSETREIMGIRHRQWDLEGVQFHPESI 172
|
170
....*....|...
gi 446060441 186 HTRQGMRMLERFV 198
Cdd:PRK08007 173 LSEQGHQLLANFL 185
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
41-197 |
4.16e-10 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 62.04 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 41 VTEAQIRDFNPSGIILSGGPeSTTEE--NSPRAPQYvFEAGVPVFGVCYGMQTMAMQLGGHVEGSNEREFGYAQVEVLTD 118
Cdd:PRK14607 35 ITIEEIEALNPSHIVISPGP-GRPEEagISVEVIRH-FSGKVPILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 119 SALVRGIEDSLTADGKPLLDVwmshgdKVTAIPSDF-VTVASTEScpfAIMANEEKRF--YGVQFHPEVTHTRQGMRMLE 195
Cdd:PRK14607 113 KGLFRGIPNPTVATRYHSLVV------EEASLPECLeVTAKSDDG---EIMGIRHKEHpiFGVQFHPESILTEEGKRILK 183
|
..
gi 446060441 196 RF 197
Cdd:PRK14607 184 NF 185
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
15-198 |
6.62e-10 |
|
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: 58.65 E-value: 6.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 15 FGSQYTQLVARRVRELgvycelwawdvTEAQIRDFNPSGIILSGGPESTTEENSPRAPQYVFEAGVPVFGVCYGMQTMAM 94
Cdd:TIGR00566 19 FCELGAEVVVKRNDSL-----------TLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCLGHQAMGQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 95 QLGGHVEGSNEREFGYAQVEVLTDSALVRGIEDSLTADGKPLLDVwmshgdKVTAIPSDFvTVASTESCPFAIMA--NEE 172
Cdd:TIGR00566 88 AFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVV------EPETLPTCF-PVTAWEEENIEIMAirHRD 160
|
170 180
....*....|....*....|....*.
gi 446060441 173 KRFYGVQFHPEVTHTRQGMRMLERFV 198
Cdd:TIGR00566 161 LPLEGVQFHPESILSEQGHQLLANFL 186
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
10-198 |
1.11e-09 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 57.96 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 10 ILILDFGSQYTQLVARRVRELGVYCELWAWD-VTEAQIRDFNPSGIILSGGPESTTEENSPRAPQYVFEAGVPVFGVCYG 88
Cdd:PRK08857 2 LLMIDNYDSFTYNLYQYFCELGAQVKVVRNDeIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 89 MQTMAMQLGGHVEGSNEREFGYAQVEVLTDSALVRGIEDSLTADGKPLLDVwmshgdKVTAIPSDFVTVASTESCPFA-- 166
Cdd:PRK08857 82 HQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVV------KNDTLPECFELTAWTELEDGSmd 155
|
170 180 190
....*....|....*....|....*....|....*
gi 446060441 167 -IMANEEKRF--YGVQFHPEVTHTRQGMRMLERFV 198
Cdd:PRK08857 156 eIMGFQHKTLpiEAVQFHPESIKTEQGHQLLANFL 190
|
|
| PRK08250 |
PRK08250 |
glutamine amidotransferase; Provisional |
50-185 |
3.48e-09 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181323 [Multi-domain] Cd Length: 235 Bit Score: 57.28 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 50 NPSGI---ILSGGPES--TTEENSP----RAPQYVF----EAGVPVFGVCYGMQTMAMQLGGHVEGSNEREFGYAQVEvL 116
Cdd:PRK08250 42 NADGFdllIVMGGPQSprTTREECPyfdsKAEQRLInqaiKAGKAVIGVCLGAQLIGEALGAKYEHSPEKEIGYFPIT-L 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446060441 117 TDSalvrGIEDSLTADGKPLLDVWMSHGDkVTAIPSDFVTVASTESCPFAIMANEEKrFYGVQFHPEVT 185
Cdd:PRK08250 121 TEA----GLKDPLLSHFGSTLTVGHWHND-MPGLTDQAKVLATSEGCPRQIVQYSNL-VYGFQCHMEFT 183
|
|
| hisH |
PRK13181 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
77-199 |
4.51e-09 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 56.41 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 77 EAGVPVFGVCYGMQTMAmqlGGHVEGSNE---------REF----------GYAQVEVLTDSALVRGIEDSLtadgkpll 137
Cdd:PRK13181 70 EKKQPVLGICLGMQLLF---ESSEEGNVKglglipgdvKRFrseplkvpqmGWNSVKPLKESPLFKGIEEGS-------- 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446060441 138 DVWMSHGDKVTAIPSDFVtVASTE-SCPFAiMANEEKRFYGVQFHPEVTHtRQGMRMLERFVR 199
Cdd:PRK13181 139 YFYFVHSYYVPCEDPEDV-LATTEyGVPFC-SAVAKDNIYAVQFHPEKSG-KAGLKLLKNFAE 198
|
|
| tRNA_Me_trans |
pfam03054 |
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ... |
228-394 |
6.69e-09 |
|
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.
Pssm-ID: 460787 [Multi-domain] Cd Length: 202 Bit Score: 55.72 E-value: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 228 DKVILGLSGGVDSSVTAMLLHRAiGKNLTCVFvdnglLRLNEAEQVMDMFGdhfglnivHVPAEERFlsalageNDPEAK 307
Cdd:pfam03054 1 MKVVVAMSGGVDSSVAAYLLKEQ-GHNVIGVF-----MKNWDEEQSLDEEG--------KCCSEEDL-------ADAQRV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 308 RKIIGrVFVEVFDEEALKLEDV------KWLAQGTIYPDV-----------IESAAS-------ATGkaHVIKSHHNVGG 363
Cdd:pfam03054 60 CEQLG-IPLYVVNFEKEYWEDVfepfldEYKNGRTPNPDVlcnkeikfgalLDYALEnlgadyvATG--HYARVSLNKDG 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446060441 364 LPkEMKMG---------------------LVEPLKELFKDEVRKIGLELGLP 394
Cdd:pfam03054 137 GS-ELLRAldknkdqsyflstlsqeqlekLLFPLGELTKEEVRKIAKEAGLA 187
|
|
| NAD_synthase |
cd00553 |
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ... |
210-314 |
9.28e-09 |
|
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: 56.02 E-value: 9.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 210 PAKIIDDAVARIREQV---GDDKVILGLSGGVDSSVTAMLLHRAIGK-NLTCVFVDNGLLR---LNEAEQVMDMFGD-HF 281
Cdd:cd00553 3 PEEIIEALVCFLRDYLrksGAKGFVLGLSGGIDSAVVAALAVRALGAeNVLALIMPSRYSSketRDDAKALAENLGIeYR 82
|
90 100 110
....*....|....*....|....*....|...
gi 446060441 282 GLNIvhVPAEERFLSALAGENDPEAKRKIIGRV 314
Cdd:cd00553 83 TIDI--DPIVDAFLKALEHAGGSEAEDLALGNI 113
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
10-109 |
1.49e-08 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 52.99 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 10 ILILDFGSQYT---QLVARRVRELGVYCELWAWD--VTEAQIRDFNPSGIILSGGPESTTEENSPRAP----QYVFEAGV 80
Cdd:cd01653 1 VAVLLFPGFEElelASPLDALREAGAEVDVVSPDggPVESDVDLDDYDGLILPGGPGTPDDLARDEALlallREAAAAGK 80
|
90 100
....*....|....*....|....*....
gi 446060441 81 PVFGVCYGMQTMAMQLGGHVEGSNEREFG 109
Cdd:cd01653 81 PILGICLGAQLLVLGVQFHPEAIDGAEAG 109
|
|
| PRK07053 |
PRK07053 |
glutamine amidotransferase; Provisional |
77-185 |
5.45e-08 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 235919 [Multi-domain] Cd Length: 234 Bit Score: 53.80 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 77 EAGVPVFGVCYGMQTMAMQLGGHVEGSNEREFGYAQVeVLTDSALvrgieDSLTA---DGKPLLDvWmsHGDKVTaIPSD 153
Cdd:PRK07053 81 AAGLPTLGICLGAQLIARALGARVYPGGQKEIGWAPL-TLTDAGR-----ASPLRhlgAGTPVLH-W--HGDTFD-LPEG 150
|
90 100 110
....*....|....*....|....*....|....*
gi 446060441 154 FVTVASTESCP---FAIMANeekrFYGVQFHPEVT 185
Cdd:PRK07053 151 ATLLASTPACRhqaFAWGNH----VLALQFHPEAR 181
|
|
| PRK05637 |
PRK05637 |
anthranilate synthase component II; Provisional |
31-203 |
6.56e-08 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 180178 [Multi-domain] Cd Length: 208 Bit Score: 52.92 E-value: 6.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 31 GVYCELWAWDVTEAQIRDFNPSGIILSGGPESTTEENSPRAPQYVFEAGVPVFGVCYGMQTMAMQLGGHVEGSNEREfGY 110
Cdd:PRK05637 25 GYKCTVFRNTVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLGFQALLEHHGGKVEPCGPVH-GT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 111 AQVEVLTDSALVRGIEDSLTADGKPllDVWMSHGDKV----------TAIPSDFVTVASTESC--PfAIMANE--EKRFY 176
Cdd:PRK05637 104 TDNMILTDAGVQSPVFAGLATDVEP--DHPEIPGRKVpiaryhslgcVVAPDGMESLGTCSSEigP-VIMAAEttDGKAI 180
|
170 180
....*....|....*....|....*..
gi 446060441 177 GVQFHPEVTHTRQGMRMLERFVRDICQ 203
Cdd:PRK05637 181 GLQFHPESVLSPTGPIILSRCVEQLLA 207
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
7-98 |
1.10e-07 |
|
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 53.87 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 7 KHRILILDFGSQYTQLvaRRVRELGVYCELWAWDVTEAQIRDFNPSGIILSGGPestteeNSPRAPQY-------VFEAG 79
Cdd:COG0505 176 GFHVVALDFGVKRNIL--RELAERGCRVTVVPATTSAEEILALNPDGVFLSNGP------GDPAALDYaietireLLGKG 247
|
90
....*....|....*....
gi 446060441 80 VPVFGVCYGMQTMAMQLGG 98
Cdd:COG0505 248 IPIFGICLGHQLLALALGA 266
|
|
| hisH |
PRK13143 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
77-202 |
1.39e-07 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 51.79 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 77 EAGVPVFGVCYGMQTM--AMQLGGHVE------GSNER--------EFGYAQVEVLTDSALVRGIEDSltadgkpllDVW 140
Cdd:PRK13143 69 RSGKPFLGICLGMQLLfeSSEEGGGVRglglfpGRVVRfpagvkvpHMGWNTVKVVKDCPLFEGIDGE---------YVY 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446060441 141 MSHGDKVTAIPSDfVTVASTE-SCPF-AIMANEekRFYGVQFHPEVThTRQGMRMLERFVRDIC 202
Cdd:PRK13143 140 FVHSYYAYPDDED-YVVATTDyGIEFpAAVCND--NVFGTQFHPEKS-GETGLKILENFVELIK 199
|
|
| PRK13980 |
PRK13980 |
NAD synthetase; Provisional |
211-253 |
1.59e-07 |
|
NAD synthetase; Provisional
Pssm-ID: 184435 [Multi-domain] Cd Length: 265 Bit Score: 52.52 E-value: 1.59e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 446060441 211 AKIIDDAVARIREQV---GDDKVILGLSGGVDSSVTAMLLHRAIGK 253
Cdd:PRK13980 11 EKVREIIVDFIREEVekaGAKGVVLGLSGGIDSAVVAYLAVKALGK 56
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
205-305 |
1.82e-07 |
|
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: 53.70 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 205 EALWTPAKIIDDAVARIREQV---GDDKVILGLSGGVDSSVTAMLLHRAIGK-NLTCVF----------VDNgllrlneA 270
Cdd:COG0171 261 EEEMDLEEVYDALVLGLRDYVrknGFKGVVLGLSGGIDSALVAALAVDALGPeNVLGVTmpsrytsdesLED-------A 333
|
90 100 110
....*....|....*....|....*....|....*.
gi 446060441 271 EQVMDMFG-DHFGLNIvhVPAEERFLSALAGENDPE 305
Cdd:COG0171 334 EELAENLGiEYEEIDI--TPAVEAFLEALPHAFGGE 367
|
|
| PRK05665 |
PRK05665 |
amidotransferase; Provisional |
76-186 |
2.41e-07 |
|
amidotransferase; Provisional
Pssm-ID: 168162 [Multi-domain] Cd Length: 240 Bit Score: 51.74 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 76 FEAGVPVFGVCYGMQTMAMQLGGHVEGSNErefGYAQvevltdsalvrGIEDSLTADGKPlldvWM-----------SHG 144
Cdd:PRK05665 88 YERGDKLLGVCFGHQLLALLLGGKAERASQ---GWGV-----------GIHRYQLAAHAP----WMspavteltlliSHQ 149
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 446060441 145 DKVTAIPSDFVTVASTESCPFAIMANEEKrFYGVQFHPEVTH 186
Cdd:PRK05665 150 DQVTALPEGATVIASSDFCPFAAYHIGDQ-VLCFQGHPEFVH 190
|
|
| PRK09522 |
PRK09522 |
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ... |
10-196 |
3.75e-07 |
|
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;
Pssm-ID: 181927 [Multi-domain] Cd Length: 531 Bit Score: 52.72 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 10 ILILDFGSQYTQLVARRVRELG----VYCELWAWDVTEAQIRDFNPSGIILSGGPESTTEENSPRAPQYVFEAGVPVFGV 85
Cdd:PRK09522 4 ILLLDNIDSFTYNLADQLRSNGhnvvIYRNHIPAQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 86 CYGMQTMAMQLGGHVEGSNErefgyaqvevltdsaLVRGIEDSLTADGKPL-------LDVWMSHGDKVTAIPSDFVTVA 158
Cdd:PRK09522 84 CLGHQAIVEAYGGYVGQAGE---------------ILHGKASSIEHDGQAMfagltnpLPVARYHSLVGSNIPAGLTINA 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 446060441 159 STESCPFAIMaNEEKRFYGVQFHPEVTHTRQGMRMLER 196
Cdd:PRK09522 149 HFNGMVMAVR-HDADRVCGFQFHPESILTTQGARLLEQ 185
|
|
| PuuD |
COG2071 |
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
53-199 |
3.83e-07 |
|
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: 50.94 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 53 GIILSGG----PESTTEENSPRAP--------------QYVFEAGVPVFGVCYGMQTMAMQLGG---------------H 99
Cdd:COG2071 52 GLVLTGGadvdPALYGEEPHPELGpidperdafelaliRAALERGKPVLGICRGMQLLNVALGGtlyqdlpdqvpgaldH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 100 VEgSNEREFGYAQVEVLTDSALvrgieDSLTadGKPLLDVWMSH-------GD--KVTAIPSDFVtvasTEscpfAIMAN 170
Cdd:COG2071 132 RQ-PAPRYAPRHTVEIEPGSRL-----ARIL--GEEEIRVNSLHhqavkrlGPglRVSARAPDGV----IE----AIESP 195
|
170 180 190
....*....|....*....|....*....|.
gi 446060441 171 EEKRFYGVQFHPE--VTHTRQGMRMLERFVR 199
Cdd:COG2071 196 GAPFVLGVQWHPEwlAASDPLSRRLFEAFVE 226
|
|
| AANH-like |
cd01986 |
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ... |
230-276 |
4.04e-07 |
|
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide alpha hydrolase (AANH)-like proteins includes N-type ATP PPases and ATP sulfurylases. The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.
Pssm-ID: 467490 [Multi-domain] Cd Length: 74 Bit Score: 47.45 E-value: 4.04e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 446060441 230 VILGLSGGVDSSVTAMLLHRAIGK-NLTCVFVDNGLLRLNEAEQVMDM 276
Cdd:cd01986 1 VVVGYSGGKDSSVALHLASRLGRKaEVAVVHIDHGIGFKEEAESVASI 48
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
2-98 |
6.05e-07 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 51.61 E-value: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 2 TENIHKHRILILDFGSQYTQLvaRRVRELGVYCELWAWDVTEAQIRDFNPSGIILSGGP---ESTTEENSprAPQYVFEA 78
Cdd:PRK12564 172 PGGELKYKVVAIDFGVKRNIL--RELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPgdpAALDYAIE--MIRELLEK 247
|
90 100
....*....|....*....|
gi 446060441 79 GVPVFGVCYGMQTMAMQLGG 98
Cdd:PRK12564 248 KIPIFGICLGHQLLALALGA 267
|
|
| LarE-like |
cd01990 |
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ... |
229-394 |
6.15e-07 |
|
Lactate racemization operon protein LarE and similar proteins; This subfamily includes Lactiplantibacillus plantarum LarE, a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family. LarE is part of the lar operon, encoding five Lar proteins (LarA-E) that collaboratively synthesize and incorporate a niacin-derived Ni-containing cofactor into LarA, an Ni-dependent lactate racemase. It catalyzes successive thiolation reactions by donating the sulfur atom of their exclusive cysteine residues to the substrate. The LarE-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. Proteins from this subfamily probably binds ATP. This domain is about 200 amino acids long with a strongly conserved motif SGGxDS at the N-terminus.
Pssm-ID: 467494 [Multi-domain] Cd Length: 222 Bit Score: 50.33 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 229 KVILGLSGGVDSSVTAMLLHRAIGKNLTCVFVDNGLL---RLNEAEQVMDMFG-DHFGLNIVHVPAEERflsalaGENDP 304
Cdd:cd01990 1 KVVVAFSGGVDSSLLAKLAKEVLGDNVVAVTADSPLVpreELEEAKRIAEEIGiRHEIIKTDELDDEEY------VANDP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 305 EakrkiigRVFV---EVFD---EEALKLeDVKWLAQGTIYPDVIEsaasatgkahvikshHNVGGLP-KEMKMGLVEPLK 377
Cdd:cd01990 75 D-------RCYHckkALYStlkEIAKER-GYDVVLDGTNADDLKD---------------YRPGLLAaAELGIRSPLPEL 131
|
170
....*....|....*..
gi 446060441 378 ELFKDEVRKIGLELGLP 394
Cdd:cd01990 132 GLTKSEIRELARELGLP 148
|
|
| hisH |
PRK13146 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
75-199 |
8.00e-07 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237290 [Multi-domain] Cd Length: 209 Bit Score: 49.78 E-value: 8.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 75 VFEAGVPVFGVCYGMQTMAM------------QLGGHVE---GSNERE----FGYAQVEVLTDSALVRGIEDS------- 128
Cdd:PRK13146 73 VLAAGRPFLGICVGMQLLFErglehgdtpglgLIPGEVVrfqPDGPALkvphMGWNTVDQTRDHPLFAGIPDGarfyfvh 152
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446060441 129 ---LTADGKPLLDVWMSHGDKVTAIpsdfvtVAstescpfaimanEEKRFyGVQFHPEVTHtRQGMRMLERFVR 199
Cdd:PRK13146 153 syyAQPANPADVVAWTDYGGPFTAA------VA------------RDNLF-ATQFHPEKSQ-DAGLALLRNFLA 206
|
|
| COG1606 |
COG1606 |
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only]; |
214-395 |
1.53e-06 |
|
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
Pssm-ID: 441214 [Multi-domain] Cd Length: 265 Bit Score: 49.72 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 214 IDDAVARIREQvgdDKVILGLSGGVDSSVTAMLLHRAIGKNLTCVFVDNGLLR---LNEAEQVMDMFGdhfglnIVHVPA 290
Cdd:COG1606 5 LERLKAILKEL---GSVLVAFSGGVDSTLLAKVAHDVLGDRVLAVTADSPSLPereLEEAKELAKEIG------IRHEVI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 291 EERFLS--ALAgENDPE----AKRKIIGRVfvevfDEEALKLEdVKWLAQGTIYPDVIE-----SAAsatgkahvikshh 359
Cdd:COG1606 76 ETDELEdpEFV-ANPPDrcyhCKKELFSKL-----KELAKELG-YAVVADGTNADDLGDyrpglRAA------------- 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 446060441 360 nvgglpKEmkMGLVEPLKE--LFKDEVRKIGLELGLPY 395
Cdd:COG1606 136 ------KE--LGVRSPLAEagLTKAEIRELARELGLPT 165
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
77-198 |
1.56e-06 |
|
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: 48.65 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 77 EAGVPVFGVCYGMQTMAM--QLGGHVEG-----------SNEREF-----GYAQVEVLTDSALVRGIED--------SLT 130
Cdd:cd01748 69 ASGKPFLGICLGMQLLFEssEEGGGTKGlglipgkvvrfPASEGLkvphmGWNQLEITKESPLFKGIPDgsyfyfvhSYY 148
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 131 ADGKPLLDVWMS--HGDKVTAipsdfvtvastescpfaimANEEKRFYGVQFHPEVTHtRQGMRMLERFV 198
Cdd:cd01748 149 APPDDPDYILATtdYGGKFPA-------------------AVEKDNIFGTQFHPEKSG-KAGLKLLKNFL 198
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
53-183 |
2.22e-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: 48.79 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 53 GIILSGGP--------ESTTEENSPRAPQ----------YVFEAGVPVFGVCYGMQTMAMQLGG--------------HV 100
Cdd:pfam07722 61 GLLLTGGPnvdphfygEEPSESGGPYDPArdayelalirAALARGKPILGICRGFQLLNVALGGtlyqdiqeqpgftdHR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 101 EGSNEREFGYAQ-VEVLTDSALvrgieDSLTADGKPllDVWMSHGDKVTAIPSDFVTVAST-----EscpfAI-MANEEK 173
Cdd:pfam07722 141 EHCQVAPYAPSHaVNVEPGSLL-----ASLLGSEEF--RVNSLHHQAIDRLAPGLRVEAVApdgtiE----AIeSPNAKG 209
|
170
....*....|
gi 446060441 174 RFYGVQFHPE 183
Cdd:pfam07722 210 FALGVQWHPE 219
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
1-98 |
2.24e-06 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 49.80 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 1 MTENIHKH-----RILILDFGSQYTQLvaRRVRELGVYCELWAWDVTEAQIRDFNPSGIILSGGPestteeNSPRAPQYV 75
Cdd:CHL00197 181 LADNKRPHssyqlKIIVIDFGVKYNIL--RRLKSFGCSITVVPATSPYQDILSYQPDGILLSNGP------GDPSAIHYG 252
|
90 100 110
....*....|....*....|....*....|
gi 446060441 76 -------FEAGVPVFGVCYGMQTMAMQLGG 98
Cdd:CHL00197 253 iktvkklLKYNIPIFGICMGHQILSLALEA 282
|
|
| nadE |
PRK00876 |
NAD(+) synthase; |
210-317 |
2.74e-06 |
|
NAD(+) synthase;
Pssm-ID: 179150 [Multi-domain] Cd Length: 326 Bit Score: 49.18 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 210 PAKIIDDAVARIREQVGDD----KVILGLSGGVDSSVTAMLLHRAIGK-NLTCVFV-----DNGLLRLNEaeqvmdMFGD 279
Cdd:PRK00876 12 AAAEAERIRAAIREQVRGTlrrrGVVLGLSGGIDSSVTAALCVRALGKeRVYGLLMperdsSPESLRLGR------EVAE 85
|
90 100 110
....*....|....*....|....*....|....*...
gi 446060441 280 HFGLNivhvPAEERFLSALAGENDPEAKRKIIGRVFVE 317
Cdd:PRK00876 86 HLGVE----YVVEDITPALEALGCYRRRDEAIRRVVPE 119
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
10-90 |
3.04e-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: 45.65 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 10 ILILDFGSQYT---QLVARRVRELGVYCELWAWD--VTEAQIRDFNPSGIILSGGPESTTEENSPRAP----QYVFEAGV 80
Cdd:cd03128 1 VAVLLFGGSEElelASPLDALREAGAEVDVVSPDggPVESDVDLDDYDGLILPGGPGTPDDLAWDEALlallREAAAAGK 80
|
90
....*....|
gi 446060441 81 PVFGVCYGMQ 90
Cdd:cd03128 81 PVLGICLGAQ 90
|
|
| hisH |
PRK13170 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
81-198 |
4.11e-06 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183877 [Multi-domain] Cd Length: 196 Bit Score: 47.54 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 81 PVFGVCYGMQTMAmqlgghvEGSNEREF------------------------GYAQVEVLTDSALVRGIEDSLTadgkpl 136
Cdd:PRK13170 72 PVLGICLGMQLLG-------ERSEESGGvdclgiidgpvkkmtdfglplphmGWNQVTPQAGHPLFQGIEDGSY------ 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446060441 137 ldVWMSHGdkvTAIPSDFVTVASTE-SCPF-AIMANeeKRFYGVQFHPEVTHTrQGMRMLERFV 198
Cdd:PRK13170 139 --FYFVHS---YAMPVNEYTIAQCNyGEPFsAAIQK--DNFFGVQFHPERSGA-AGAQLLKNFL 194
|
|
| IMP_synth_hisH |
TIGR01855 |
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ... |
75-199 |
4.69e-06 |
|
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273836 [Multi-domain] Cd Length: 196 Bit Score: 47.32 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 75 VFEAGVPVFGVCYGMQTM--------AMQLGGHVEGSNER-------EFGYAQVEVLTDSALVRGIEDSLtadgkpllDV 139
Cdd:TIGR01855 67 VVRLGKPVLGICLGMQLLferseeggGVPGLGLIKGNVVKlearkvpHMGWNEVHPVKESPLLNGIDEGA--------YF 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 140 WMSHgdKVTAIPSDFVTVASTESCPFAIMANEEKRFYGVQFHPEVTHtRQGMRMLERFVR 199
Cdd:TIGR01855 139 YFVH--SYYAVCEEEAVLAYADYGEKFPAAVQKGNIFGTQFHPEKSG-KTGLKLLENFLE 195
|
|
| MnmA |
COG0482 |
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ... |
229-250 |
7.53e-06 |
|
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: 48.13 E-value: 7.53e-06
|
| HisH |
COG0118 |
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
77-195 |
7.70e-06 |
|
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 439888 [Multi-domain] Cd Length: 196 Bit Score: 46.57 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 77 EAGVPVFGVCYGMQTMAMQ---------LG---GHVEGSNEREF-----GYAQVEVLTDSALVRGIEDsltadgkplldv 139
Cdd:COG0118 71 AGGKPVLGICLGMQLLFERseengdtegLGlipGEVVRFPASDLkvphmGWNTVEIAKDHPLFAGIPD------------ 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446060441 140 wmshGDKV------TAIPSDF-VTVASTE-SCPF-AIMANEekRFYGVQFHPEVTHtRQGMRMLE 195
Cdd:COG0118 139 ----GEYFyfvhsyYVPPDDPeDVVATTDyGVPFtAAVERG--NVFGTQFHPEKSG-AAGLRLLK 196
|
|
| MnmA_TRMU-like |
cd01998 |
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
229-259 |
8.46e-06 |
|
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: 47.89 E-value: 8.46e-06
10 20 30
....*....|....*....|....*....|.
gi 446060441 229 KVILGLSGGVDSSVTAMLLHRAiGKNLTCVF 259
Cdd:cd01998 1 KVAVAMSGGVDSSVAAALLKEQ-GYDVIGVF 30
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
9-194 |
9.57e-06 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 46.27 E-value: 9.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 9 RILILDFGSQYTQLVARRVRELGVycelwAWDVTEAQIRDFNP----SGIILSGGPestteeNSPRA-PQYV-----FEA 78
Cdd:PRK06895 3 KLLIINNHDSFTFNLVDLIRKLGV-----PMQVVNVEDLDLDEvenfSHILISPGP------DVPRAyPQLFamlerYHQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 79 GVPVFGVCYGMQTMAMQLGGHVEGSNEREFGYA-QVEVLTDSALVRGIedsltadgKPLLDVWMSHGDKVTaiPSDFVT- 156
Cdd:PRK06895 72 HKSILGVCLGHQTLCEFFGGELYNLNNVRHGQQrPLKVRSNSPLFDGL--------PEEFNIGLYHSWAVS--EENFPTp 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446060441 157 -VASTESCPFAIMANEEKRF--YGVQFHPEVTHTRQGMRML 194
Cdd:PRK06895 142 lEITAVCDENVVMAMQHKTLpiYGVQFHPESYISEFGEQIL 182
|
|
| mnmA |
PRK00143 |
tRNA-specific 2-thiouridylase MnmA; Reviewed |
229-259 |
1.00e-05 |
|
tRNA-specific 2-thiouridylase MnmA; Reviewed
Pssm-ID: 234664 [Multi-domain] Cd Length: 346 Bit Score: 47.76 E-value: 1.00e-05
10 20 30
....*....|....*....|....*....|.
gi 446060441 229 KVILGLSGGVDSSVTAMLLHRAiGKNLTCVF 259
Cdd:PRK00143 2 RVVVGMSGGVDSSVAAALLKEQ-GYEVIGVF 31
|
|
| trmU |
TIGR00420 |
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ... |
228-262 |
2.86e-05 |
|
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase (trmU, asuE, or mnmA) is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine (mnm5s2U34) present in the wobble position of some tRNAs. This enzyme appears not to occur in the Archaea. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 273069 [Multi-domain] Cd Length: 352 Bit Score: 46.23 E-value: 2.86e-05
10 20 30
....*....|....*....|....*....|....*
gi 446060441 228 DKVILGLSGGVDSSVTAMLLHRAiGKNLTCVFVDN 262
Cdd:TIGR00420 1 KKVIVGLSGGVDSSVSAYLLKQQ-GYEVVGVFMKN 34
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
4-98 |
4.46e-05 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 45.65 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 4 NIHKHrILILDFGsqYTQLVARRVRELGVYCELWAWDVTEAQIRDFNPSGIILSGGPeSTTEENSPRAPQ-YVFEAGVPV 82
Cdd:PRK12838 165 NGGKH-VALIDFG--YKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGP-GDPKELQPYLPEiKKLISSYPI 240
|
90
....*....|....*.
gi 446060441 83 FGVCYGMQTMAMQLGG 98
Cdd:PRK12838 241 LGICLGHQLIALALGA 256
|
|
| NAD_synthase |
pfam02540 |
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ... |
213-253 |
6.16e-05 |
|
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is induced by stress factors such as heat shock and glucose limitation.
Pssm-ID: 396888 [Multi-domain] Cd Length: 241 Bit Score: 44.68 E-value: 6.16e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 446060441 213 IIDDAVARIREQV---GDDKVILGLSGGVDSSVTAMLLHRAIGK 253
Cdd:pfam02540 1 EINALVDFLRDYVqkaGFKGVVLGLSGGIDSSLVAYLAVKALGK 44
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
8-98 |
6.61e-05 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 45.36 E-value: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 8 HRILILDFGSQYTQLvaRRVRELGvyCELW----AWDVTEAQirDFNPSGIILSGGPestteeNSPRAPQYVFE------ 77
Cdd:PLN02771 241 YHVIAYDFGIKHNIL--RRLASYG--CKITvvpsTWPASEAL--KMKPDGVLFSNGP------GDPSAVPYAVEtvkell 308
|
90 100
....*....|....*....|.
gi 446060441 78 AGVPVFGVCYGMQTMAMQLGG 98
Cdd:PLN02771 309 GKVPVFGICMGHQLLGQALGG 329
|
|
| PRK13794 |
PRK13794 |
hypothetical protein; Provisional |
229-292 |
8.93e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237509 [Multi-domain] Cd Length: 479 Bit Score: 45.04 E-value: 8.93e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446060441 229 KVILGLSGGVDSSVTAMLLHRAIGKNLTCVFVDNGlLRLNEAEQVMDMFGDHFGLNIVHVPAEE 292
Cdd:PRK13794 249 PVTVAYSGGKDSLATLLLALKALGINFPVLFNDTG-LEFPETLENVEDVEKHYGLEIIRTKSEE 311
|
|
| hisH |
PRK13141 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
77-204 |
9.58e-05 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 43.58 E-value: 9.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 77 EAGVPVFGVCYGMQTMAMQ---------LG---GHV----EGSNER--EFGYAQVEVLTDSALVRGIEDSLtadgkpllD 138
Cdd:PRK13141 70 ASGKPLLGICLGMQLLFESseefgetegLGllpGRVrrfpPEEGLKvpHMGWNQLELKKESPLLKGIPDGA--------Y 141
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446060441 139 VWMSHGDKVTAIPSDFVTVASTESCPF-AIMANeeKRFYGVQFHPEVTHTrQGMRMLERFVRDICQC 204
Cdd:PRK13141 142 VYFVHSYYADPCDEEYVAATTDYGVEFpAAVGK--DNVFGAQFHPEKSGD-VGLKILKNFVEMVEEC 205
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
53-98 |
2.35e-04 |
|
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: 42.18 E-value: 2.35e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446060441 53 GIILSGGP---------ESTTEENSPRAPQYVFE---------AGVPVFGVCYGMQTMAMQLGG 98
Cdd:cd01745 56 GLLLTGGGdvdpplygeEPHPELGPIDPERDAFElallraaleRGKPILGICRGMQLLNVALGG 119
|
|
| TilS |
COG0037 |
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ... |
227-306 |
5.70e-04 |
|
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: 41.74 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 227 DDKVILGLSGGVDSSVTAMLLH---RAIGKNLTCVFVDNGL--LRLNEAEQVMDmFGDHFGLNIVHVPAEERFLSALAGE 301
Cdd:COG0037 15 GDRILVAVSGGKDSLALLHLLAklrRRLGFELVAVHVDHGLreESDEDAEFVAE-LCEELGIPLHVVRVDVPAIAKKEGK 93
|
....*
gi 446060441 302 NdPEA 306
Cdd:COG0037 94 S-PEA 97
|
|
| CysD |
COG0175 |
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
211-304 |
7.61e-04 |
|
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439945 [Multi-domain] Cd Length: 232 Bit Score: 40.99 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446060441 211 AKIIDDAVARIREQVGD--DKVILGLSGGVDSSVtamLLH--RAIGKNLTCVFVDNGLLrLNEAEQVMDMFGDHFGLNIV 286
Cdd:COG0175 15 AELEAEAIEILREAAAEfgGRVVVSSSGGKDSTV---LLHlaAKFKPPIPVLFLDTGYE-FPETYEFRDRLAERLGLDLI 90
|
90
....*....|....*...
gi 446060441 287 HVPAEERFLSALAGENDP 304
Cdd:COG0175 91 VVRPEDAFAEQLAEFGPP 108
|
|
| AANH_superfamily |
cd01984 |
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ... |
230-261 |
1.37e-03 |
|
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase (AANH) superfamily includes N-type ATP PPases, ATP sulfurylases, universal stress response proteins (USPs), and electron transfer flavoproteins (ETFs). The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.
Pssm-ID: 467489 [Multi-domain] Cd Length: 56 Bit Score: 37.07 E-value: 1.37e-03
10 20 30
....*....|....*....|....*....|....*
gi 446060441 230 VILGLSGGVDSSVTAMLLHRAIG---KNLTCVFVD 261
Cdd:cd01984 1 ILVPLSGGEDSSIALKHAKKFKTskaEEVVVVHVG 35
|
|
| nadE |
TIGR00552 |
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ... |
221-254 |
1.96e-03 |
|
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: 40.06 E-value: 1.96e-03
10 20 30
....*....|....*....|....*....|....*..
gi 446060441 221 IREQV---GDDKVILGLSGGVDSSVTAMLLHRAIGKN 254
Cdd:TIGR00552 13 LRGYVqksGAKGVVLGLSGGIDSAVVAALCVEALGEQ 49
|
|
| CTU1-like |
cd01713 |
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ... |
228-263 |
2.29e-03 |
|
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human cytoplasmic tRNA 2-thiolation protein 1, also called cytosolic thiouridylase subunit 1 (CTU1), ATP-binding domain-containing protein 3 (ATPBD3), cancer-associated gene protein, or cytoplasmic tRNA adenylyltransferase 1. CTU1 plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). It directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. The CTU1-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.
Pssm-ID: 467486 Cd Length: 208 Bit Score: 39.49 E-value: 2.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 446060441 228 DKVILGLSGGVDSSVTAMLLH-----RAIGKNLTCVFVDNG 263
Cdd:cd01713 19 DRVAVGLSGGKDSTVLLYVLKelnkrHDYGVELIAVTIDEG 59
|
|
| PRK13981 |
PRK13981 |
NAD synthetase; Provisional |
229-259 |
4.86e-03 |
|
NAD synthetase; Provisional
Pssm-ID: 237577 [Multi-domain] Cd Length: 540 Bit Score: 39.37 E-value: 4.86e-03
10 20 30
....*....|....*....|....*....|..
gi 446060441 229 KVILGLSGGVDSSVTAMLLHRAIGK-NLTCVF 259
Cdd:PRK13981 282 GVVLGLSGGIDSALVAAIAVDALGAeRVRAVM 313
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
227-292 |
8.44e-03 |
|
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or synthetase) B is always associated with an N-terminal amidotransferase domain. Family members that contain this domain catalyze the conversion of aspartate to asparagine. Asparagine synthase B catalyzes the synthesis of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase.
Pssm-ID: 467495 [Multi-domain] Cd Length: 224 Bit Score: 38.02 E-value: 8.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446060441 227 DDKVILGLSGGVDSSVTAMLLHRAIGK-NLTCVFVDNGLLRLNE---AEQVMDMFG-DHfglNIVHVPAEE 292
Cdd:cd01991 2 DVPVGVLLSGGLDSSLIAALAARLLPEtPIDLFTVGFEGSPTPDraaARRVAEELGtEH---HEVEVTIEE 69
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