|
Name |
Accession |
Description |
Interval |
E-value |
| guaA |
PRK00074 |
GMP synthase; Reviewed |
7-516 |
0e+00 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 1032.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 7 QKIIVLDYGSQYNQLISRRIREFGVFSELKNHKITAEEVRAINPIGIVLSGGPNSVYAENAFDIDPEIFELGIPILGICY 86
Cdd:PRK00074 4 DKILILDFGSQYTQLIARRVRELGVYSEIVPYDISAEEIRAFNPKGIILSGGPASVYEEGAPRADPEIFELGVPVLGICY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 87 GMQLITHKLGGKVVPAGeagNREYGQSNLQLKTESALFAGTPEEQLVLMSHGDAVTEIPADFHLVGLSADCPFAAIENTE 166
Cdd:PRK00074 84 GMQLMAHQLGGKVERAG---KREYGRAELEVDNDSPLFKGLPEEQDVWMSHGDKVTELPEGFKVIASTENCPIAAIANEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 167 RRIYGIQFHPEVRHSVYGNDILKNFAFGICGAKGDWTMENFIETEIEKIRQTVGDKKVLLGLSGGVDSSVVGVLLQRAIG 246
Cdd:PRK00074 161 RKFYGVQFHPEVTHTPQGKKLLENFVFDICGCKGDWTMENFIEEAIEEIREQVGDKKVILGLSGGVDSSVAAVLLHKAIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 247 DQLTCIFVDHGLLRKNEGDQVMEMLGGKFGLNIIRVDAAKRFLDLLAGVSDPEKKRKIIGNEFVYVFDDEASKLTDVEFL 326
Cdd:PRK00074 241 DQLTCVFVDHGLLRKNEAEQVMEMFREHFGLNLIHVDASDRFLSALAGVTDPEEKRKIIGREFIEVFEEEAKKLGGVKFL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 327 AQGTLYTDIIES-GTDTAETIKSHHNVGGLPEDMQFKLIEPLNTLFKDEVRALGTALGMPDEVVWRQPFPGPGLAIRVMG 405
Cdd:PRK00074 321 AQGTLYPDVIESgGTKKAATIKSHHNVGGLPEDMKLKLVEPLRELFKDEVRKLGLELGLPEEIVYRHPFPGPGLAIRILG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 406 EITEEKLQTVRESDAILREEIAKAGLDRDVWQYFTVNTGVRSVGVMGDGRTYDYTIAIRAITSIDGMTADFAKLPWDVLQ 485
Cdd:PRK00074 401 EVTKEKLDILREADAIFIEELRKAGLYDKIWQAFAVLLPVKSVGVMGDGRTYDYVVALRAVTSIDGMTADWARLPYDFLE 480
|
490 500 510
....*....|....*....|....*....|.
gi 636941923 486 KISVRIVNEVDHVNRIVYDITSKPPATVEWE 516
Cdd:PRK00074 481 KISNRIINEVKGVNRVVYDITSKPPATIEWE 511
|
|
| GuaA2 |
COG0519 |
GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, ... |
4-516 |
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: 928.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 4 QDVQKIIVLDYGSQYNQLISRRIREFGVFSELKNHKITAEEVRAINPIGIVLSGGPNSVYAENAFDIDPEIFELGIPILG 83
Cdd:COG0519 1 MDKEIIIVLDFGGQYQQLIARRRREEGVYSEIIPPDTAAEEIKAKGPPGIILSGGPSSVYEEGAPPDDPELFELGGPILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 84 ICYGMQLITHKLGGKVVPAGEagnREYGQSNLQLKTESALFAGTPEEQLVLMSHGDAVTEIPADFHLVGLSADCPFAAIE 163
Cdd:COG0519 81 ICYGGQLMLHLLGGGVVRAER---REYGGALLLVDDESDLFAGGPEELQVWMSHGDRVTELPPGFEVIASTENCPVAAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 164 NTERRIYGIQFHPEVRHSVYGNDILKNFAFGICGAKGDWTMENFIETEIEKIRQTVGDKKVLLGLSGGVDSSVVGVLLQR 243
Cdd:COG0519 158 NEERKLYGVQFHPEVVHTEQGKEILKNFLFDICGCKGDWTMENFIEEAIEEIREQVGDGKVICALSGGVDSSVAAALLHK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 244 AIGDQLTCIFVDHGLLRKNEGDQVMEMLGGKFGLNIIRVDAAKRFLDLLAGVSDPEKKRKIIGNEFVYVFDDEASKLTDV 323
Cdd:COG0519 238 AIGDQLTCVFVDHGLLRKGEAEQVEETFKEHFGLNLIYVDASERFLSALKGVTDPEEKRKIIGEEFIEVFEEEAKKLGGA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 324 EFLAQGTLYTDIIESGT--DTAETIKSHHNVGGLPEDMQFKLIEPLNTLFKDEVRALGTALGMPDEVVWRQPFPGPGLAI 401
Cdd:COG0519 318 KFLAQGTLYPDVIESGSvkGPAATIKSHHNVGGLPEDMKFKLVEPLRELFKDEVRALGRELGLPEEIVYRHPFPGPGLAI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 402 RVMGEITEEKLQTVRESDAILREEIAKAGLDRDVWQYFTVNTGVRSVGVMGDGRTYDYTIAIRAITSIDGMTADFAKLPW 481
Cdd:COG0519 398 RILGEVTKEKLEILREADAIFIEELRKAGLYDKVWQAFAVLLPVKSVGVMGDERTYEYVVALRAVTSVDGMTADWARLPY 477
|
490 500 510
....*....|....*....|....*....|....*
gi 636941923 482 DVLQKISVRIVNEVDHVNRIVYDITSKPPATVEWE 516
Cdd:COG0519 478 EVLERISNRIINEVKGVNRVVYDITSKPPATIEWE 512
|
|
| PLN02347 |
PLN02347 |
GMP synthetase |
2-516 |
0e+00 |
|
GMP synthetase
Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 682.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 2 TKQDVQKIIVLDYGSQYNQLISRRIREFGVFSELKNHKITAEEVRAINPIGIVLSGGPNSVYAENAFDIDPEIFEL---- 77
Cdd:PLN02347 6 AKSYLDVVLILDYGSQYTHLITRRVRELGVYSLLLSGTASLDRIASLNPRVVILSGGPHSVHVEGAPTVPEGFFDYcrer 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 78 GIPILGICYGMQLITHKLGGKVVPAGeagNREYGQSNLQLKTESALFAGTPEE--QLVLMSHGDAVTEIPADFHLVGLSA 155
Cdd:PLN02347 86 GVPVLGICYGMQLIVQKLGGEVKPGE---KQEYGRMEIRVVCGSQLFGDLPSGetQTVWMSHGDEAVKLPEGFEVVAKSV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 156 DCPFAAIENTERRIYGIQFHPEVRHSVYGNDILKNFAFGICGAKGDWTMENFIETEIEKIRQTVG-DKKVLLGLSGGVDS 234
Cdd:PLN02347 163 QGAVVAIENRERRIYGLQYHPEVTHSPKGMETLRHFLFDVCGVTADWKMQDVLEEQIELIKATVGpDEHVICALSGGVDS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 235 SVVGVLLQRAIGDQLTCIFVDHGLLRKNEGDQVMEMLGGKFGLNIIRVDAAKRFLDLLAGVSDPEKKRKIIGNEFVYVFD 314
Cdd:PLN02347 243 TVAATLVHKAIGDRLHCVFVDNGLLRYKEQERVMETFKRDLHLPVTCVDASERFLSKLKGVTDPEKKRKIIGAEFIEVFD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 315 DEASKL-----TDVEFLAQGTLYTDIIES------GTDTAETIKSHHNVGGLPEDMQFKLIEPLNTLFKDEVRALGTALG 383
Cdd:PLN02347 323 EFAHKLeqklgKKPAFLVQGTLYPDVIEScpppgsGRTHSHTIKSHHNVGGLPKDMKLKLIEPLKLLFKDEVRKLGRLLG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 384 MPDEVVWRQPFPGPGLAIRVMGEITEE-KLQTVRESDAILREEIAKAGLDRDVWQYFTVNTGVRSVGVMGDGRTYDYTIA 462
Cdd:PLN02347 403 VPEAFLKRHPFPGPGLAVRVLGDVTEGnALDILRQVDEIFINSIKDAGLYDEIWQAFAVFLPVKSVGVQGDQRTHSHVVA 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 636941923 463 IRAITSIDGMTADFAKLPWDVLQKISVRIVNEVDHVNRIVYDITSKPPATVEWE 516
Cdd:PLN02347 483 LRAVTSEDGMTADWYHFEHKFLDDVSRKICNEVRGVNRVVYDITSKPPSTIEWE 536
|
|
| guaA_Cterm |
TIGR00884 |
GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; This protein of purine ... |
206-516 |
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: 551.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 206 NFIETEIEKIRQTVGDKKVLLGLSGGVDSSVVGVLLQRAIGDQLTCIFVDHGLLRKNEGDQVMEMLGGKFGLNIIRVDAA 285
Cdd:TIGR00884 1 NFIEEAVEEIREQVGDAKVIIALSGGVDSSVAAVLAHRAIGDRLTCVFVDHGLLRKGEAEQVVKTFGDRLGLNLVYVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 286 KRFLDLLAGVSDPEKKRKIIGNEFVYVFDDEASKLTDVEFLAQGTLYTDIIESGTDTAETIKSHHNVGGLPEDMQFKLIE 365
Cdd:TIGR00884 81 ERFLSALKGVTDPEEKRKIIGRVFIEVFEREAKKIGDAEYLAQGTIYPDVIESAAGTAHVIKSHHNVGGLPEDMKLKLVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 366 PLNTLFKDEVRALGTALGMPDEVVWRQPFPGPGLAIRVMGEITEEKLQTVRESDAILREEIAKAGLDRDVWQYFTVNTGV 445
Cdd:TIGR00884 161 PLRELFKDEVRKLGKELGLPEEIVWRHPFPGPGLAVRVLGEVTKEKLEILRRADAIVIEELKKAGLYDKVWQAFAVLLPV 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 636941923 446 RSVGVMGDGRTYDYTIAIRAITSIDGMTADFAKLPWDVLQKISVRIVNEVDHVNRIVYDITSKPPATVEWE 516
Cdd:TIGR00884 241 KSVGVMGDGRTYGYVIALRAVESIDGMTADWARLPYDFLERISNRITNEVPGVNRVVYDITSKPPATIEWE 311
|
|
| GMP_synthase_C |
cd01997 |
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ... |
215-516 |
1.46e-174 |
|
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: 493.60 E-value: 1.46e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 215 IRQTVGDKKVLLGLSGGVDSSVVGVLLQRAIGD-QLTCIFVDHGLLRKNEGDQVMEMLGGKFGLNIIRVDAAKRFLDLLA 293
Cdd:cd01997 1 IKRTVGDKKVLCLVSGGVDSTVCAALLHKALGDeRVIAVHIDNGLMRKNESEQVEEALKKLGVINLAKVDASKRFLKKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 294 GVSDPEKKRKIIGNEFVYVFDDEASKL---TDVEFLAQGTLYTDIIESG----TDTAETIKSHHNVGGLPED-MQFKLIE 365
Cdd:cd01997 81 GVTDPEEKRKIIGDTFIEVFDEVAKELnldPDDVYLAQGTLYPDLIESAsslaSSKADTIKTHHNVGGLPRElLKGKLVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 366 PLNTLFKDEVRALGTALGMPDEVVWRQPFPGPGLAIRVMGEITEEKLQTVRESDAILREEIAKAGLDRDVWQYFTVNTGV 445
Cdd:cd01997 161 PLRDLFKDEVRELGRELGLPEELVWRHPFPGPGLAIRVLGEVTPEKLEILREADAIVEEELREAGLYDKISQAFAVLLPI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 636941923 446 RSVGVMGDGRTYDYTIAIRAITSIDGMTADFAKLPWDVLQKISVRIVNEVDHVNRIVYDITSKPPATVEWE 516
Cdd:cd01997 241 KSVGVQGDGRTYGYVVALRAVETEDFMTAEWARPPYEVLDKISNRITNEVPGVNRVVYDITSKPPATIEWE 311
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
9-192 |
4.34e-96 |
|
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: 288.67 E-value: 4.34e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 9 IIVLDYGSQYNQLISRRIREFGVFSELKNHKITAEEVRAINPIGIVLSGGPNSVYAENAFDIDPEIFELGIPILGICYGM 88
Cdd:cd01742 1 ILILDFGSQYTHLIARRVRELGVYSEILPNTTPLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGICYGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 89 QLITHKLGGKVVPageAGNREYGQSNLQLKTESALFAGTPEEQLVLMSHGDAVTEIPADFHLVGLSADCPFAAIENTERR 168
Cdd:cd01742 81 QLIAKALGGKVER---GDKREYGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVVKLPEGFKVIASSDNCPVAAIANEEKK 157
|
170 180
....*....|....*....|....
gi 636941923 169 IYGIQFHPEVRHSVYGNDILKNFA 192
Cdd:cd01742 158 IYGVQFHPEVTHTEKGKEILKNFL 181
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
9-199 |
7.05e-96 |
|
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: 288.44 E-value: 7.05e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 9 IIVLDYGSQYNQLISRRIREFGVFSELKNHKITAEEVRAINPIGIVLSGGPNSVYAENAFDIDPEIFELGIPILGICYGM 88
Cdd:TIGR00888 1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGPSSVYAENAPRADEKIFELGVPVLGICYGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 89 QLITHKLGGKVvpaGEAGNREYGQSNLQLKTESALFAGTPEEQLVLMSHGDAVTEIPADFHLVGLSADCPFAAIENTERR 168
Cdd:TIGR00888 81 QLMAKQLGGEV---GRAEKREYGKAELEILDEDDLFRGLPDESTVWMSHGDKVKELPEGFKVLATSDNCPVAAMAHEEKP 157
|
170 180 190
....*....|....*....|....*....|.
gi 636941923 169 IYGIQFHPEVRHSVYGNDILKNFAFGICGAK 199
Cdd:TIGR00888 158 IYGVQFHPEVTHTEYGNELLENFVYDVCGCE 188
|
|
| GMP_synt_C |
pfam00958 |
GMP synthase C terminal domain; GMP synthetase is a glutamine amidotransferase from the de ... |
424-515 |
1.67e-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: 201.49 E-value: 1.67e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 424 EEIAKAGLDRDVWQYFTVNTGVRSVGVMGDGRTYDYTIAIRAITSIDGMTADFAKLPWDVLQKISVRIVNEVDHVNRIVY 503
Cdd:pfam00958 1 EEIKKAGLYRKIWQAFAVLLPVKSVGVMGDERTYEYVVALRAVTSTDGMTADWARLPYEVLEKISNRIVNEVPGVNRVVY 80
|
90
....*....|..
gi 636941923 504 DITSKPPATVEW 515
Cdd:pfam00958 81 DITSKPPATIEW 92
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
8-195 |
1.93e-63 |
|
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: 206.34 E-value: 1.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 8 KIIVLD---YGSQYNQLISRRIRE-------FGVF-SELKNHKITAEevraiNPIGIVLSGGPNSVYAE-----NAFDID 71
Cdd:COG0518 1 KILILDhdpFGGQYPGLIARRLREagieldvLRVYaGEILPYDPDLE-----DPDGLILSGGPMSVYDEdpwleDEPALI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 72 PEIFELGIPILGICYGMQLITHKLGGKVVPAGEagnREYGQSNLQLKTESALFAGTPEEQLVLMSHGDAVTEIPADFHLV 151
Cdd:COG0518 76 REAFELGKPVLGICYGAQLLAHALGGKVEPGPG---REIGWAPVELTEADPLFAGLPDEFTVWMSHGDTVTELPEGAEVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 636941923 152 GLSADCPFAAIENtERRIYGIQFHPEVRHSV------------------------------YGNDILKNFAFGI 195
Cdd:COG0518 153 ASSDNCPNQAFRY-GRRVYGVQFHPEVTHTMmeawleeradelaaeellaeaslhdpelreAGRRLLRNFLREI 225
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
8-197 |
7.94e-52 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 174.27 E-value: 7.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 8 KIIVLDYGSQYNQLISRRIREFGVFSELKNHKITAEEVRAiNPIGIVLSGGPNSVYAENAFDIdpeIFELGIPILGICYG 87
Cdd:PRK00758 1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTTPVEEIKA-FEDGLILSGGPDIERAGNCPEY---LKELDVPILGICLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 88 MQLITHKLGGKVVpAGEAGnrEYGQSNLQLKTESALFAGTPEEQLVLMSHGDAVTEIPADFHLVGLSADCPFAAIENTER 167
Cdd:PRK00758 77 HQLIAKAFGGEVG-RGEYG--EYALVEVEILDEDDILKGLPPEIRVWASHADEVKELPDGFEILARSDICEVEAMKHKEK 153
|
170 180 190
....*....|....*....|....*....|
gi 636941923 168 RIYGIQFHPEVRHSVYGNDILKNFaFGICG 197
Cdd:PRK00758 154 PIYGVQFHPEVAHTEYGEEIFKNF-LEICG 182
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
10-195 |
5.96e-51 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 172.04 E-value: 5.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 10 IVLDYGSQYNQLISRRIREFGVFSELKNHKITAEEVRAINPIGIVLSGGPNSVYA-ENAFDIDPEIFELGIPILGICYGM 88
Cdd:pfam00117 1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAaGGAIEAIREARELKIPILGICLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 89 QLITHKLGGKVVPAGEagnREYGQSNLQLK-TESALFAGTPEEQLVLMSHGDAVTE--IPADFHLVGLSA-DCPFAAIEN 164
Cdd:pfam00117 81 QLLALAFGGKVVKAKK---FGHHGKNSPVGdDGCGLFYGLPNVFIVRRYHSYAVDPdtLPDGLEVTATSEnDGTIMGIRH 157
|
170 180 190
....*....|....*....|....*....|.
gi 636941923 165 TERRIYGIQFHPEVRHSVYGNDILKNFAFGI 195
Cdd:pfam00117 158 KKLPIFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
35-192 |
3.45e-29 |
|
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: 113.49 E-value: 3.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 35 LKNHKITAEEVRAINPI------------GIVLSGGPNSVYAENAFDIDPEI------FELGIPILGICYGMQLITHKLG 96
Cdd:cd01741 20 LREAGAETIEIDVVDVYagellpdlddydGLVILGGPMSVDEDDYPWLKKLKelirqaLAAGKPVLGICLGHQLLARALG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 97 GKVVPAGEAgnREYGQSNLQL---KTESALFAGTPEEQLVLMSHGDAVTEIPADFHLVGLSADCPFAAIEnTERRIYGIQ 173
Cdd:cd01741 100 GKVGRNPKG--WEIGWFPVTLteaGKADPLFAGLPDEFPVFHWHGDTVVELPPGAVLLASSEACPNQAFR-YGDRALGLQ 176
|
170
....*....|....*....
gi 636941923 174 FHPEvrhsvygNDILKNFA 192
Cdd:cd01741 177 FHPE-------ERLLRNFL 188
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
8-191 |
5.69e-22 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 93.27 E-value: 5.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 8 KIIVLD-YGS-QYNqlISRRIREFG----VFselKNHKITAEEVRAINPIGIVLSGGP-------NSVYAenafdidpeI 74
Cdd:PRK05670 1 MILLIDnYDSfTYN--LVQYLGELGaevvVY---RNDEITLEEIEALNPDAIVLSPGPgtpaeagISLEL---------I 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 75 FELG--IPILGICYGMQLITHKLGGKVVPAGEAgnrEYGQSNLQLKTESALFAGTPEEQLVLMSHGDAV--TEIPADFHL 150
Cdd:PRK05670 67 REFAgkVPILGVCLGHQAIGEAFGGKVVRAKEI---MHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVdrESLPDCLEV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 636941923 151 VGLSADCPFAAIENTERRIYGIQFHPEVRHSVYGNDILKNF 191
Cdd:PRK05670 144 TAWTDDGEIMGVRHKELPIYGVQFHPESILTEHGHKLLENF 184
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
9-191 |
5.11e-21 |
|
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: 90.48 E-value: 5.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 9 IIVLD-YGS-QYNqlISRRIREFG----VFselKNHKITAEEVRAINPIGIVLSGGPNSvyAENAfDIDPEI---FELGI 79
Cdd:COG0512 1 ILLIDnYDSfTYN--LVQYLGELGaevvVV---RNDEITLEEIEALAPDGIVLSPGPGT--PEEA-GISLEViraFAGKI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 80 PILGICYGMQLITHKLGGKVVPAGEA--GnreygqsnlqlKT------ESALFAGTPEE-------QLVLmshgdAVTEI 144
Cdd:COG0512 73 PILGVCLGHQAIGEAFGGKVVRAPEPmhG-----------KTspithdGSGLFAGLPNPftatryhSLVV-----DRETL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 636941923 145 PADFHLVGLSADCPFAAIENTERRIYGIQFHPEvrhSV---YGNDILKNF 191
Cdd:COG0512 137 PDELEVTAWTEDGEIMGIRHRELPIEGVQFHPE---SIlteHGHQLLANF 183
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
35-191 |
2.19e-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: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 35 LKNHKITAEEVRAINPIGIVLSGGPNSVyAENAFDID-PEIFELGIPILGICYGMQLITHKLGGKVVPAGEA--GnreyG 111
Cdd:cd01743 28 VRNDEITLEELELLNPDAIVISPGPGHP-EDAGISLEiIRALAGKVPILGVCLGHQAIAEAFGGKVVRAPEPmhG----K 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 112 QSNLQLkTESALFAGTPEEQLVLMSHGDAVTEIPADFHLVgLSADCP---FAAIENTERRIYGIQFHPEvrhSV---YGN 185
Cdd:cd01743 103 TSEIHH-DGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLLE-VTASTEdgvIMALRHRDLPIYGVQFHPE---SIlteYGL 177
|
....*.
gi 636941923 186 DILKNF 191
Cdd:cd01743 178 RLLENF 183
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
8-191 |
1.03e-16 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 82.84 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 8 KIIVLD-YGS-QYN--QLISRRirEFGVFSELKNHKITAEEVRAINPIGIVLSGGPNSvyAENAfDIDPEI---FELGIP 80
Cdd:PRK14607 1 MIILIDnYDSfTYNiyQYIGEL--GPEEIEVVRNDEITIEEIEALNPSHIVISPGPGR--PEEA-GISVEVirhFSGKVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 81 ILGICYGMQLITHKLGGKVVpagEAGNREYGQSNLQLKTESALFAGTPEEQLVLMSHGDAVTE--IPADFHLVGLSADCP 158
Cdd:PRK14607 76 ILGVCLGHQAIGYAFGGKIV---HAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVEEasLPECLEVTAKSDDGE 152
|
170 180 190
....*....|....*....|....*....|...
gi 636941923 159 FAAIENTERRIYGIQFHPEVRHSVYGNDILKNF 191
Cdd:PRK14607 153 IMGIRHKEHPIFGVQFHPESILTEEGKRILKNF 185
|
|
| PRK09065 |
PRK09065 |
glutamine amidotransferase; Provisional |
52-177 |
4.69e-16 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181635 [Multi-domain] Cd Length: 237 Bit Score: 77.69 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 52 GIVLSGGPNSV-----YAENAFDIDPEIFELGIPILGICYGMQLITHKLGGKVV--PAGeagnREYGQSNLQLKTESA-- 122
Cdd:PRK09065 57 GVIITGSWAMVtdrldWSERTADWLRQAAAAGMPLLGICYGHQLLAHALGGEVGynPAG----RESGTVTVELHPAAAdd 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 636941923 123 -LFAGTPEEQLVLMSHGDAVTEIPADFHLVGLSADCPFAAIENTErRIYGIQFHPE 177
Cdd:PRK09065 133 pLFAGLPAQFPAHLTHLQSVLRLPPGAVVLARSAQDPHQAFRYGP-HAWGVQFHPE 187
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
52-177 |
3.00e-13 |
|
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.
Pssm-ID: 429620 [Multi-domain] Cd Length: 219 Bit Score: 68.82 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 52 GIVLSGGPN---SVYAENAF----DIDPE--IFEL---------GIPILGICYGMQLITHKLGGKVVPA-----GEAGNR 108
Cdd:pfam07722 61 GLLLTGGPNvdpHFYGEEPSesggPYDPArdAYELaliraalarGKPILGICRGFQLLNVALGGTLYQDiqeqpGFTDHR 140
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 636941923 109 EYGQS-------NLQLKTESALFAGTPEEQLVLMS-HGDAVTEIPADFHLVGLSADCPFAAIE--NTERRIYGIQFHPE 177
Cdd:pfam07722 141 EHCQVapyapshAVNVEPGSLLASLLGSEEFRVNSlHHQAIDRLAPGLRVEAVAPDGTIEAIEspNAKGFALGVQWHPE 219
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
9-191 |
6.79e-13 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 67.90 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 9 IIVLD-YGS-QYNqlISRRIREFGVFSEL-KNHKITAEEVRAINPIGIVLSGGP-----NSVYAENAFDIDPEIfelgiP 80
Cdd:PLN02335 21 IIVIDnYDSfTYN--LCQYMGELGCHFEVyRNDELTVEELKRKNPRGVLISPGPgtpqdSGISLQTVLELGPLV-----P 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 81 ILGICYGMQLITHKLGGKVV--PAGEAgnreYGQSNL---QLKTESALFAGTPEEQLVLMSHGDAVTE--IPAD-FHLVG 152
Cdd:PLN02335 94 LFGVCMGLQCIGEAFGGKIVrsPFGVM----HGKSSPvhyDEKGEEGLFSGLPNPFTAGRYHSLVIEKdtFPSDeLEVTA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 636941923 153 LSADCPFAAIENTE-RRIYGIQFHPEVRHSVYGNDILKNF 191
Cdd:PLN02335 170 WTEDGLIMAARHRKyKHIQGVQFHPESIITTEGKTIVRNF 209
|
|
| PRK07053 |
PRK07053 |
glutamine amidotransferase; Provisional |
53-179 |
7.88e-13 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 235919 [Multi-domain] Cd Length: 234 Bit Score: 68.05 E-value: 7.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 53 IVLsGGPNSVYAENAFD-IDPEI------FELGIPILGICYGMQLITHKLGGKVVPAGEagnREYGQSNLQLKTE----- 120
Cdd:PRK07053 52 VVL-GGPIGVYDDELYPfLAPEIallrqrLAAGLPTLGICLGAQLIARALGARVYPGGQ---KEIGWAPLTLTDAgrasp 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 121 -SALFAGTPeeqlVLMSHGDAVtEIPADFHLVGLSADCPFAAIEnTERRIYGIQFHPEVR 179
Cdd:PRK07053 128 lRHLGAGTP----VLHWHGDTF-DLPEGATLLASTPACRHQAFA-WGNHVLALQFHPEAR 181
|
|
| hisH |
PRK13181 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
72-192 |
2.29e-12 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 66.04 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 72 PEIFELGIPILGICYGMQLITHK--------LG---GKVV--PAGEAGNREYGQSNLQLKTESALFAGTPEEQLVLMSHG 138
Cdd:PRK13181 66 KEHVEKKQPVLGICLGMQLLFESseegnvkgLGlipGDVKrfRSEPLKVPQMGWNSVKPLKESPLFKGIEEGSYFYFVHS 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 636941923 139 DAVteIPADFHLVGLSAD--CPF-AAIENteRRIYGIQFHPEVRHSVyGNDILKNFA 192
Cdd:PRK13181 146 YYV--PCEDPEDVLATTEygVPFcSAVAK--DNIYAVQFHPEKSGKA-GLKLLKNFA 197
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
36-191 |
5.81e-12 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 64.55 E-value: 5.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 36 KNHKITAEEVRAINPIGIVLSGGPNSVyAENAFDIDPEIFELG-IPILGICYGMQLITHKLGGKVVPAGEAgnrEYGQSN 114
Cdd:PRK08007 30 RNDALTLADIDALKPQKIVISPGPCTP-DEAGISLDVIRHYAGrLPILGVCLGHQAMAQAFGGKVVRAAKV---MHGKTS 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 636941923 115 LQLKTESALFAGTPEEQLVLMSHGDAV--TEIPADFHLVGLSADCPFAAIENTERRIYGIQFHPEVRHSVYGNDILKNF 191
Cdd:PRK08007 106 PITHNGEGVFRGLANPLTVTRYHSLVVepDSLPACFEVTAWSETREIMGIRHRQWDLEGVQFHPESILSEQGHQLLANF 184
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
35-191 |
8.54e-12 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 63.98 E-value: 8.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 35 LKNHKITAEEVRAINPIGIVLSGGPNsvYAENAFDIDPEIFELG--IPILGICYGMQLITHKLGGKVVPAGEAgnrEYGQ 112
Cdd:CHL00101 29 CRNDEIDLSKIKNLNIRHIIISPGPG--HPRDSGISLDVISSYApyIPILGVCLGHQSIGYLFGGKIIKAPKP---MHGK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 113 SNLQLKTESALFAGTPEEQLVLMSHG---DAVTeIPADFHLVGLSADCPFAAIENTE-RRIYGIQFHPEVRHSVYGNDIL 188
Cdd:CHL00101 104 TSKIYHNHDDLFQGLPNPFTATRYHSliiDPLN-LPSPLEITAWTEDGLIMACRHKKyKMLRGIQFHPESLLTTHGQQIL 182
|
...
gi 636941923 189 KNF 191
Cdd:CHL00101 183 RNF 185
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
9-98 |
9.37e-12 |
|
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: 63.67 E-value: 9.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 9 IIVLDYGSQYNQLisRRIREFGVFSELKNHKITAEEVRAINPIGIVLSGGPNsvyaeNAFDIDP------EIFELGIPIL 82
Cdd:cd01744 1 VVVIDFGVKHNIL--RELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPG-----DPALLDEaiktvrKLLGKKIPIF 73
|
90
....*....|....*.
gi 636941923 83 GICYGMQLITHKLGGK 98
Cdd:cd01744 74 GICLGHQLLALALGAK 89
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
36-191 |
1.90e-11 |
|
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: 62.88 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 36 KNHKITAEEVRAINPIGIVLSGGPnsVYAENAfDIDPEIFEL---GIPILGICYGMQLITHKLGGKVVpagEAGNREYGQ 112
Cdd:TIGR00566 30 RNDSLTLQEIEALLPLLIVISPGP--CTPNEA-GISLEAIRHfagKLPILGVCLGHQAMGQAFGGDVV---RANTVMHGK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 113 -SNLQLKTEsALFAGTPEEQLVLMSHGDAVT--EIPADFHLVGLS-ADCPFAAIENTERRIYGIQFHPEVRHSVYGNDIL 188
Cdd:TIGR00566 104 tSEIEHNGA-GIFRGLFNPLTATRYHSLVVEpeTLPTCFPVTAWEeENIEIMAIRHRDLPLEGVQFHPESILSEQGHQLL 182
|
...
gi 636941923 189 KNF 191
Cdd:TIGR00566 183 ANF 185
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
36-191 |
4.78e-11 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 62.13 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 36 KNHKITAEEVRAINPIGIVLSGGPNSvyaENAFDIDPEI---FELGIPILGICYGMQLITHKLGGKVVpagEAGNREYGQ 112
Cdd:PRK07649 30 RNDEVTISDIENMKPDFLMISPGPCS---PNEAGISMEViryFAGKIPIFGVCLGHQSIAQVFGGEVV---RAERLMHGK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 113 SNLQLKTESALFAGTPEEQLVLMSHGDAVTE--IPADFHLVGLSADCPFAAIENTERRIYGIQFHPEVRHSVYGNDILKN 190
Cdd:PRK07649 104 TSLMHHDGKTIFSDIPNPFTATRYHSLIVKKetLPDCLEVTSWTEEGEIMAIRHKTLPIEGVQFHPESIMTSHGKELLQN 183
|
.
gi 636941923 191 F 191
Cdd:PRK07649 184 F 184
|
|
| hisH |
PRK13141 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
66-192 |
5.97e-11 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 62.07 E-value: 5.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 66 NAFDIDPEIFEL---GIPILGICYGMQLI--------THK-LG---GKVVPAGEAGNR---EYGQSNLQLKTESALFAGT 127
Cdd:PRK13141 57 RERGLDEVIKEAvasGKPLLGICLGMQLLfesseefgETEgLGllpGRVRRFPPEEGLkvpHMGWNQLELKKESPLLKGI 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 128 PEEQLVLMSHGDAVTEIPADFhlvgLSADCPF-----AAIENteRRIYGIQFHPEvRHSVYGNDILKNFA 192
Cdd:PRK13141 137 PDGAYVYFVHSYYADPCDEEY----VAATTDYgvefpAAVGK--DNVFGAQFHPE-KSGDVGLKILKNFV 199
|
|
| PRK07567 |
PRK07567 |
glutamine amidotransferase; Provisional |
72-177 |
8.19e-11 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181035 [Multi-domain] Cd Length: 242 Bit Score: 62.27 E-value: 8.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 72 PEIFELGIPILGICYGMQLITHKLGGKVvpageagNREYGQ----SNLQLKTESA---LFAGTPEEQLVLMSHGDAVTEI 144
Cdd:PRK07567 87 DEVVARDFPFLGACYGVGTLGHHQGGVV-------DRTYGEpvgaVTVSLTDAGRadpLLAGLPDTFTAFVGHKEAVSAL 159
|
90 100 110
....*....|....*....|....*....|...
gi 636941923 145 PADFHLVGLSADCPFAAIENTErRIYGIQFHPE 177
Cdd:PRK07567 160 PPGAVLLATSPTCPVQMFRVGE-NVYATQFHPE 191
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
8-98 |
1.20e-10 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 63.28 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 8 KIIVLDYGSQYNqlISRRIREFGVFSELKNHKITAEEVRAINPIGIVLSGGPNSVYAEN-AFDIDPEIFELGIPILGICY 86
Cdd:CHL00197 194 KIIVIDFGVKYN--ILRRLKSFGCSITVVPATSPYQDILSYQPDGILLSNGPGDPSAIHyGIKTVKKLLKYNIPIFGICM 271
|
90
....*....|..
gi 636941923 87 GMQLITHKLGGK 98
Cdd:CHL00197 272 GHQILSLALEAK 283
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
53-191 |
1.44e-10 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 60.52 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 53 IVLSGGPN--SVYaenafdidPEIFEL------GIPILGICYGMQLITHKLGGKVVPAGEAgnREYGQSNLQLKTESALF 124
Cdd:PRK06895 47 ILISPGPDvpRAY--------PQLFAMleryhqHKSILGVCLGHQTLCEFFGGELYNLNNV--RHGQQRPLKVRSNSPLF 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 636941923 125 AGTPEEQLVLMSHGDAVTEI--PADFHLVGLSADCPFAAIENTERRIYGIQFHPEVRHSVYGNDILKNF 191
Cdd:PRK06895 117 DGLPEEFNIGLYHSWAVSEEnfPTPLEITAVCDENVVMAMQHKTLPIYGVQFHPESYISEFGEQILRNW 185
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
8-100 |
1.91e-10 |
|
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: 62.35 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 8 KIIVLDYGSQYNqlISRRIREFG----VFselkNHKITAEEVRAINPIGIVLSGGP----NSVYAENAFDidpEIFELGI 79
Cdd:COG0505 178 HVVALDFGVKRN--ILRELAERGcrvtVV----PATTSAEEILALNPDGVFLSNGPgdpaALDYAIETIR---ELLGKGI 248
|
90 100
....*....|....*....|.
gi 636941923 80 PILGICYGMQLITHKLGGKVV 100
Cdd:COG0505 249 PIFGICLGHQLLALALGAKTY 269
|
|
| nadE |
TIGR00552 |
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ... |
204-396 |
2.29e-10 |
|
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: 60.87 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 204 MENFIEtEIEK-IRQTV---GDKKVLLGLSGGVDSSVVGVLLQRAIGDQLTCIFVDHGLLRKNEGDQVMEMLGGKFGLNI 279
Cdd:TIGR00552 2 LIKYVE-EIEDfLRGYVqksGAKGVVLGLSGGIDSAVVAALCVEALGEQNHALLLPHSVQTPEQDVQDALALAEPLGINY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 280 IRVDAAK--RFLDLLAGVSDPEKKRKIIGNE-------FVYVFDDEASKL---TD--VEF-LAQGTLYTDIiesGTDtae 344
Cdd:TIGR00552 81 KNIDIAPiaASFQAQTETGDELSDFLAKGNLkarlrmaALYAIANKHNLLvlgTGnkSELmLGYFTKYGDG---GCD--- 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 636941923 345 tikshhnvgglpedmqfklIEPLNTLFKDEVRALGTALGMPDEVVWRQP----FPG 396
Cdd:TIGR00552 155 -------------------IAPIGDLFKTQVYELAKRLNVPERIIEKPPtadlFDG 191
|
|
| PuuD |
COG2071 |
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
52-177 |
6.17e-10 |
|
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: 59.41 E-value: 6.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 52 GIVLSGGPN---SVYAENAF----DIDPE--IFEL---------GIPILGICYGMQLITHKLGGKV---VPAGEAGNREY 110
Cdd:COG2071 52 GLVLTGGADvdpALYGEEPHpelgPIDPErdAFELaliraalerGKPVLGICRGMQLLNVALGGTLyqdLPDQVPGALDH 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 636941923 111 GQSN--------LQLKTESALFAGTPEEQLVLMS-HGDAVTEIPADFHLVGLSADcpfaAIENTERR-IYGIQFHPE 177
Cdd:COG2071 132 RQPApryaprhtVEIEPGSRLARILGEEEIRVNSlHHQAVKRLGPGLRVSARAPDgvieAIESPGAPfVLGVQWHPE 208
|
|
| PRK05665 |
PRK05665 |
amidotransferase; Provisional |
73-180 |
7.35e-10 |
|
amidotransferase; Provisional
Pssm-ID: 168162 [Multi-domain] Cd Length: 240 Bit Score: 59.44 E-value: 7.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 73 EIFELGIPILGICYGMQLITHKLGGKVvpagEAGNREYGQSNLQLKTESALFAGTPE--EQLVLMSHGDAVTEIPADFHL 150
Cdd:PRK05665 86 KLYERGDKLLGVCFGHQLLALLLGGKA----ERASQGWGVGIHRYQLAAHAPWMSPAvtELTLLISHQDQVTALPEGATV 161
|
90 100 110
....*....|....*....|....*....|
gi 636941923 151 VGLSADCPFAAIeNTERRIYGIQFHPEVRH 180
Cdd:PRK05665 162 IASSDFCPFAAY-HIGDQVLCFQGHPEFVH 190
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
8-100 |
1.03e-09 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 60.09 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 8 KIIVLDYGSQYNqlISRRIREFGVFSELKNHKITAEEVRAINPIGIVLSGGP----NSVYAENAFDidpEIFELGIPILG 83
Cdd:PRK12564 179 KVVAIDFGVKRN--ILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPgdpaALDYAIEMIR---ELLEKKIPIFG 253
|
90
....*....|....*..
gi 636941923 84 ICYGMQLITHKLGGKVV 100
Cdd:PRK12564 254 ICLGHQLLALALGAKTY 270
|
|
| PRK05637 |
PRK05637 |
anthranilate synthase component II; Provisional |
40-188 |
4.14e-09 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 180178 [Multi-domain] Cd Length: 208 Bit Score: 56.78 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 40 ITAEEVRAINPIGIVLSGGP-NSVYAENAFD-IDPEIFElgIPILGICYGMQLITHKLGGKVVPAGEAgnreYGQSNLQL 117
Cdd:PRK05637 35 VPVEEILAANPDLICLSPGPgHPRDAGNMMAlIDRTLGQ--IPLLGICLGFQALLEHHGGKVEPCGPV----HGTTDNMI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 118 KT----ESALFAG-----TPEEQ-------LVLMSHGDAVTEIPADFHLVGlsaDCPFA------AIENTERRIYGIQFH 175
Cdd:PRK05637 109 LTdagvQSPVFAGlatdvEPDHPeipgrkvPIARYHSLGCVVAPDGMESLG---TCSSEigpvimAAETTDGKAIGLQFH 185
|
170
....*....|...
gi 636941923 176 PEVRHSVYGNDIL 188
Cdd:PRK05637 186 PESVLSPTGPIIL 198
|
|
| NAD_synthase |
pfam02540 |
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ... |
205-438 |
6.98e-09 |
|
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: 56.62 E-value: 6.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 205 ENFIETEIEKirqtVGDKKVLLGLSGGVDSSVVGVLLQRAIGDQLTcifvdHGLL----RKNEGD-QVMEMLGGKFGLNI 279
Cdd:pfam02540 6 VDFLRDYVQK----AGFKGVVLGLSGGIDSSLVAYLAVKALGKENV-----LALImpssQSSEEDvQDALALAENLGIEY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 280 IRVD---AAKRFLDLLagvsDPEKKRKIIGNE-------FVYVFDDEASKL---TD--VEF-LAQGTLYTDIiesGTDta 343
Cdd:pfam02540 77 KTIDikpIVRAFSQLF----QDASEDFAKGNLkarirmaILYYIANKFNYLvlgTGnkSELaVGYFTKYGDG---ACD-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 344 etikshhnvgglpedmqfklIEPLNTLFKDEVRALGTALGMPDEVVWRQP----FPgpglairvmGEITEEKL-QTVRES 418
Cdd:pfam02540 148 --------------------IAPIGDLYKTQVYELARYLNVPERIIKKPPsadlWP---------GQTDEEELgIPYDEL 198
|
250 260
....*....|....*....|....*...
gi 636941923 419 DAIL--------REEIAKAGLDRDVWQY 438
Cdd:pfam02540 199 DDILklvekklsPEEIIGKGLPAEVVRR 226
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
52-201 |
7.16e-09 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 55.83 E-value: 7.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 52 GIVLSGGPNSVYAENA-FDIDPEIFELGIPILGICYGMQLITHKLGGKVVPAGEAgnrEYGQSNLQLKTESALFAGTPEE 130
Cdd:PRK07765 49 GVLLSPGPGTPERAGAsIDMVRACAAAGTPLLGVCLGHQAIGVAFGATVDRAPEL---LHGKTSSVHHTGVGVLAGLPDP 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 636941923 131 QLVLMSHGDAVTE--IPADFHLVGLSADCPFAAIENTERRIYGIQFHPEVRHSVYGNDILKNFaFGICGAKGD 201
Cdd:PRK07765 126 FTATRYHSLTILPetLPAELEVTARTDSGVIMAVRHRELPIHGVQFHPESVLTEGGHRMLANW-LTVCGWAPD 197
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
35-191 |
7.55e-09 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 55.65 E-value: 7.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 35 LKNHKITAEEVRAINPIGIVLSGGPNSVYAENAFDIDPEIFELGIPILGICYGMQLITHKLGGKVVPAGEAgnrEYGQSN 114
Cdd:PRK08857 29 VRNDEIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCLGHQAIAQVFGGQVVRARQV---MHGKTS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 115 LQLKTESALFAGTPEEQLVLMSHGDAVTE--IPADFHLVGLS--ADCPFAAIENTERR---IYGIQFHPEVRHSVYGNDI 187
Cdd:PRK08857 106 PIRHTGRSVFKGLNNPLTVTRYHSLVVKNdtLPECFELTAWTelEDGSMDEIMGFQHKtlpIEAVQFHPESIKTEQGHQL 185
|
....
gi 636941923 188 LKNF 191
Cdd:PRK08857 186 LANF 189
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
36-191 |
8.05e-09 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 55.25 E-value: 8.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 36 KNHKITAEEVRAINPIGIVLSGGPNSvyaENAFDIDPEI---FELGIPILGICYGMQLITHKLGGKVVPAGEAgnrEYGQ 112
Cdd:PRK06774 30 RNDELQLTDIEQLAPSHLVISPGPCT---PNEAGISLAVirhFADKLPILGVCLGHQALGQAFGARVVRARQV---MHGK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 113 SNLQLKTESALFAGTPEEQLVLMSHG--DAVTEIPADFHLVGLSA-DCPFAAIENTERR---IYGIQFHPEVRHSVYGND 186
Cdd:PRK06774 104 TSAICHSGQGVFRGLNQPLTVTRYHSlvIAADSLPGCFELTAWSErGGEMDEIMGIRHRtlpLEGVQFHPESILSEQGHQ 183
|
....*
gi 636941923 187 ILKNF 191
Cdd:PRK06774 184 LLDNF 188
|
|
| NAD_synthase |
cd00553 |
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ... |
205-307 |
9.66e-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: 9.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 205 ENFIETEIEKIRQTV---GDKKVLLGLSGGVDSSVVGVLLQRAIG-DQLTCIFVDHGLLRKNEGD---QVMEMLGGKFgl 277
Cdd:cd00553 4 EEIIEALVCFLRDYLrksGAKGFVLGLSGGIDSAVVAALAVRALGaENVLALIMPSRYSSKETRDdakALAENLGIEY-- 81
|
90 100 110
....*....|....*....|....*....|.
gi 636941923 278 NIIRVDAA-KRFLDLLAGVSDPEKKRKIIGN 307
Cdd:cd00553 82 RTIDIDPIvDAFLKALEHAGGSEAEDLALGN 112
|
|
| PRK06490 |
PRK06490 |
glutamine amidotransferase; Provisional |
52-181 |
1.12e-08 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 180590 [Multi-domain] Cd Length: 239 Bit Score: 55.74 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 52 GIVLSGGPNSVYAENAFdIDPEIFELGIPI------LGICYGMQLITHKLGGKVVPAGEaGNREYGQSNLQLKTESALFA 125
Cdd:PRK06490 55 GAVIFGGPMSANDPDDF-IRREIDWISVPLkenkpfLGICLGAQMLARHLGARVAPHPD-GRVEIGYYPLRPTEAGRALM 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 636941923 126 GTPEeqLVLMSHGDAVtEIPADFHLVGLSADCPFAAIENTErRIYGIQFHPEVRHS 181
Cdd:PRK06490 133 HWPE--MVYHWHREGF-DLPAGAELLATGDDFPNQAFRYGD-NAWGLQFHPEVTRA 184
|
|
| PRK09522 |
PRK09522 |
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ... |
49-218 |
1.64e-08 |
|
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;
Pssm-ID: 181927 [Multi-domain] Cd Length: 531 Bit Score: 56.96 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 49 NPIgIVLSGGPNsvyAENAFDIDPEIFEL---GIPILGICYGMQLITHKLGGKVvpaGEAGNREYGQSNLQLKTESALFA 125
Cdd:PRK09522 49 NPV-LMLSPGPG---VPSEAGCMPELLTRlrgKLPIIGICLGHQAIVEAYGGYV---GQAGEILHGKASSIEHDGQAMFA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 126 GTPEEQLVLMSHGDAVTEIPAdfhlvGLSADCPF----AAIENTERRIYGIQFHPEVRHSVYGNDILKNfafGICGAKGD 201
Cdd:PRK09522 122 GLTNPLPVARYHSLVGSNIPA-----GLTINAHFngmvMAVRHDADRVCGFQFHPESILTTQGARLLEQ---TLAWAQQK 193
|
170
....*....|....*..
gi 636941923 202 WTMENFIETEIEKIRQT 218
Cdd:PRK09522 194 LEPTNTLQPILEKLYQA 210
|
|
| PRK13980 |
PRK13980 |
NAD synthetase; Provisional |
206-396 |
1.98e-08 |
|
NAD synthetase; Provisional
Pssm-ID: 184435 [Multi-domain] Cd Length: 265 Bit Score: 55.22 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 206 NFIETEIEKirqtVGDKKVLLGLSGGVDSSVVGVLLQRAIG-DQLtcifvdHGLL-------RKNEGD--QVMEMLGGKF 275
Cdd:PRK13980 19 DFIREEVEK----AGAKGVVLGLSGGIDSAVVAYLAVKALGkENV------LALLmpssvspPEDLEDaeLVAEDLGIEY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 276 glNIIR----VDAakrFLDLLagvsdPEKKRKIIGNEFVYVfddEASKLTDV---------------EFL-AQGTLYTDi 335
Cdd:PRK13980 89 --KVIEitpiVDA---FFSAI-----PDADRLRVGNIMART---RMVLLYDYanrenrlvlgtgnksELLlGYFTKYGD- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 636941923 336 ieSGTDtaetikshhnvgglpedmqfklIEPLNTLFKDEVRALGTALGMPDEVVWRQPFPG 396
Cdd:PRK13980 155 --GAVD----------------------LNPIGDLYKTQVRELARHLGVPEDIIEKPPSAD 191
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
8-95 |
3.75e-08 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 55.28 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 8 KIIVLDYGsqYNQLISRRIREFGVFSELKNHKITAEEVRAINPIGIVLSGGPNSvyAENAFDIDPEIFEL--GIPILGIC 85
Cdd:PRK12838 169 HVALIDFG--YKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPGD--PKELQPYLPEIKKLisSYPILGIC 244
|
90
....*....|....*..
gi 636941923 86 YGMQLI-------THKL 95
Cdd:PRK12838 245 LGHQLIalalgadTEKL 261
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
78-191 |
4.43e-08 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153219 [Multi-domain] Cd Length: 198 Bit Score: 53.27 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 78 GIPILGICYGMQLI---------THKLG---GKVVPAGEAGNR---EYGQSNLQLKTESALFAGTPEEQLVLMSHGDAVT 142
Cdd:cd01748 71 GKPFLGICLGMQLLfesseegggTKGLGlipGKVVRFPASEGLkvpHMGWNQLEITKESPLFKGIPDGSYFYFVHSYYAP 150
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 636941923 143 EIPADFHLvglsADC----PF-AAIENteRRIYGIQFHPEVRHSVyGNDILKNF 191
Cdd:cd01748 151 PDDPDYIL----ATTdyggKFpAAVEK--DNIFGTQFHPEKSGKA-GLKLLKNF 197
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
42-177 |
5.05e-08 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 55.69 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 42 AEEVRA-INPIGIVLSGGPNSvyaENAFDIDPEI---FELGIPILGICYGMQLITHKLGGKV----VPAgeagnreYGQ- 112
Cdd:PRK13566 561 AEEMLDrVNPDLVVLSPGPGR---PSDFDCKATIdaaLARNLPIFGVCLGLQAIVEAFGGELgqlaYPM-------HGKp 630
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636941923 113 SNLQLKTESALFAGTPEEQLVLMSH---GDAVTeIPADFHLVGLSADCPFAAIENTERRIYGIQFHPE 177
Cdd:PRK13566 631 SRIRVRGPGRLFSGLPEEFTVGRYHslfADPET-LPDELLVTAETEDGVIMAIEHKTLPVAAVQFHPE 697
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
52-177 |
8.11e-08 |
|
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: 52.58 E-value: 8.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 52 GIVLSGGPNSV---YAENAF----DIDPE--IFEL---------GIPILGICYGMQLITHKLGGKVVPageagnreygqs 113
Cdd:cd01745 56 GLLLTGGGDVDpplYGEEPHpelgPIDPErdAFELallraalerGKPILGICRGMQLLNVALGGTLYQ------------ 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 636941923 114 nlQLKTESAlfagtpeeqlvlmsHGDAVTEIPADFHLVGLSADCPFAAIENTERR-IYGIQFHPE 177
Cdd:cd01745 124 --DIRVNSL--------------HHQAIKRLADGLRVEARAPDGVIEAIESPDRPfVLGVQWHPE 172
|
|
| IMP_synth_hisH |
TIGR01855 |
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ... |
9-192 |
8.11e-08 |
|
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: 52.71 E-value: 8.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 9 IIVLDYGSQYNQLISRRIREFGVFSElknhkITAEEVRAINPIGIVLSG-GPNSVYAENAFDIDPEIF-----ELGIPIL 82
Cdd:TIGR01855 1 IVIIDYGVGNLGSVKRALKRVGAEPV-----VVKDSKEAELADKLILPGvGAFGAAMARLRENGLDLFvelvvRLGKPVL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 83 GICYGMQLITHK------------LGGKVVPAGEAGNREYGQSNLQLKTESALFAGTPEEQLVLMSHGDAVteIPADFHL 150
Cdd:TIGR01855 76 GICLGMQLLFERseegggvpglglIKGNVVKLEARKVPHMGWNEVHPVKESPLLNGIDEGAYFYFVHSYYA--VCEEEAV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 636941923 151 VGlSAD--CPFAAIENtERRIYGIQFHPEvRHSVYGNDILKNFA 192
Cdd:TIGR01855 154 LA-YADygEKFPAAVQ-KGNIFGTQFHPE-KSGKTGLKLLENFL 194
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
9-91 |
4.57e-06 |
|
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: 45.67 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 9 IIVLDYGSQYN---QLISRRIREFGVFSEL--KNHKITAEEVRAINPIGIVLSGGPNSVYA----ENAFDIDPEIFELGI 79
Cdd:cd01653 1 VAVLLFPGFEElelASPLDALREAGAEVDVvsPDGGPVESDVDLDDYDGLILPGGPGTPDDlardEALLALLREAAAAGK 80
|
90
....*....|..
gi 636941923 80 PILGICYGMQLI 91
Cdd:cd01653 81 PILGICLGAQLL 92
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
5-98 |
5.62e-06 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 48.82 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 5 DVQKIIVLDYGSQYNqlISRRIREFGVFSELKNHKITAEEVRAINPIGIVLSGGPNSVYA-ENAFDIDPEIfeLG-IPIL 82
Cdd:PLN02771 239 ESYHVIAYDFGIKHN--ILRRLASYGCKITVVPSTWPASEALKMKPDGVLFSNGPGDPSAvPYAVETVKEL--LGkVPVF 314
|
90
....*....|....*.
gi 636941923 83 GICYGMQLITHKLGGK 98
Cdd:PLN02771 315 GICMGHQLLGQALGGK 330
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
9-91 |
5.96e-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: 44.88 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 9 IIVLDYGSQYN---QLISRRIREFGVFSEL--KNHKITAEEVRAINPIGIVLSGGPNSVYA----ENAFDIDPEIFELGI 79
Cdd:cd03128 1 VAVLLFGGSEElelASPLDALREAGAEVDVvsPDGGPVESDVDLDDYDGLILPGGPGTPDDlawdEALLALLREAAAAGK 80
|
90
....*....|..
gi 636941923 80 PILGICYGMQLI 91
Cdd:cd03128 81 PVLGICLGAQLL 92
|
|
| AANH-like |
cd01986 |
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ... |
224-292 |
1.06e-05 |
|
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide alpha hydrolase (AANH)-like proteins includes N-type ATP PPases and ATP sulfurylases. The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.
Pssm-ID: 467490 [Multi-domain] Cd Length: 74 Bit Score: 43.60 E-value: 1.06e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 636941923 224 VLLGLSGGVDSSVVGVLLQRAIGD-QLTCIFVDHGLLRKNEGDQVME----MLGGKFGLNIIRVDAAKRFLDLL 292
Cdd:cd01986 1 VVVGYSGGKDSSVALHLASRLGRKaEVAVVHIDHGIGFKEEAESVASiarrSILKKLAEKGARAIATGVLRPLL 74
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
206-435 |
1.38e-05 |
|
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 439941 [Multi-domain] Cd Length: 542 Bit Score: 47.53 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 206 NFIETEIEKIRQtvgdKKVLLGLSGGVDSSVVGVLLQRAIG-DQLTCIF----------VDHGLlrknegdQVMEMLGGK 274
Cdd:COG0171 275 LGLRDYVRKNGF----KGVVLGLSGGIDSALVAALAVDALGpENVLGVTmpsrytsdesLEDAE-------ELAENLGIE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 275 FG-LNIirVDAAKRFLDLLAGVSDPEKK-----------RKII----GNEFVYVFddeaskLT--D-VEfLAQG--TLYT 333
Cdd:COG0171 344 YEeIDI--TPAVEAFLEALPHAFGGELDdvaeenlqariRMVIlmalANKFGGLV------LGtgNkSE-LAVGyfTKYG 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 334 DiiesgtdtaetikshHNVGglpedmqfklIEPLNTLFKDEVRALGTALGM-----PDEVVWRQpfPGPGLAIrvmGEIT 408
Cdd:COG0171 415 D---------------GAGD----------LAPIADLYKTQVYALARWLNRngeviPEDIIDKP--PSAELRP---GQTD 464
|
250 260 270
....*....|....*....|....*....|....*.
gi 636941923 409 EEKLQTVRESDAILR---------EEIAKAGLDRDV 435
Cdd:COG0171 465 EDELGPYEVLDAILYayveeglspEEIAAAGYDREW 500
|
|
| hisH |
PRK13146 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
78-191 |
1.76e-05 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237290 [Multi-domain] Cd Length: 209 Bit Score: 45.93 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 78 GIPILGICYGMQL---------ITHKLG---GKVVPAGEAGNRE----YGQSNLQLKTESALFAGTPEEQLVLMSHGDAV 141
Cdd:PRK13146 77 GRPFLGICVGMQLlferglehgDTPGLGlipGEVVRFQPDGPALkvphMGWNTVDQTRDHPLFAGIPDGARFYFVHSYYA 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 636941923 142 -TEIPAdfHLVGlSAD--CPF-AAIENTErrIYGIQFHPEVRHSvYGNDILKNF 191
Cdd:PRK13146 157 qPANPA--DVVA-WTDygGPFtAAVARDN--LFATQFHPEKSQD-AGLALLRNF 204
|
|
| COG1606 |
COG1606 |
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only]; |
208-424 |
6.57e-05 |
|
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
Pssm-ID: 441214 [Multi-domain] Cd Length: 265 Bit Score: 44.72 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 208 IETEIEKIRQTVGD-KKVLLGLSGGVDSSVVGVLLQRAIGDQLTCIFVDHGLLRKNEgdqvmemlggkfglniirVDAAK 286
Cdd:COG1606 1 LEEKLERLKAILKElGSVLVAFSGGVDSTLLAKVAHDVLGDRVLAVTADSPSLPERE------------------LEEAK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 287 RFLDLLaGVsdpekKRKIIGNEFvyvFDDEA-----------------SKLTDvefLAQGTLYTDIIEsGT---DTAET- 345
Cdd:COG1606 63 ELAKEI-GI-----RHEVIETDE---LEDPEfvanppdrcyhckkelfSKLKE---LAKELGYAVVAD-GTnadDLGDYr 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 346 ----------IKShhnvgglPedmqfkLIEplNTLFKDEVRALGTALGMPdevVWRQPfPGPGLAIRVM-GE-ITEEKLQ 413
Cdd:COG1606 130 pglraakelgVRS-------P------LAE--AGLTKAEIRELARELGLP---TWDKP-SSACLASRIPyGEeITPEKLR 190
|
250
....*....|.
gi 636941923 414 TVRESDAILRE 424
Cdd:COG1606 191 RVERAEAFLRS 201
|
|
| TilS |
COG0037 |
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ... |
214-258 |
6.68e-05 |
|
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439807 [Multi-domain] Cd Length: 235 Bit Score: 44.44 E-value: 6.68e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 636941923 214 KIRQTVGD-------KKVLLGLSGGVDSSVVGVLL---QRAIGDQLTCIFVDHGL 258
Cdd:COG0037 1 KVRKAIRDyrllepgDRILVAVSGGKDSLALLHLLaklRRRLGFELVAVHVDHGL 55
|
|
| MnmA |
COG0482 |
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ... |
222-244 |
2.13e-04 |
|
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: 43.50 E-value: 2.13e-04
10 20
....*....|....*....|...
gi 636941923 222 KKVLLGLSGGVDSSVVGVLLQRA 244
Cdd:COG0482 1 KRVVVGMSGGVDSSVAAALLKEQ 23
|
|
| tRNA_Me_trans |
pfam03054 |
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ... |
222-253 |
2.34e-04 |
|
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: 42.24 E-value: 2.34e-04
10 20 30
....*....|....*....|....*....|..
gi 636941923 222 KKVLLGLSGGVDSSVVGVLLQRAiGDQLTCIF 253
Cdd:pfam03054 1 MKVVVAMSGGVDSSVAAYLLKEQ-GHNVIGVF 31
|
|
| mnmA |
PRK00143 |
tRNA-specific 2-thiouridylase MnmA; Reviewed |
222-244 |
2.55e-04 |
|
tRNA-specific 2-thiouridylase MnmA; Reviewed
Pssm-ID: 234664 [Multi-domain] Cd Length: 346 Bit Score: 43.14 E-value: 2.55e-04
|
| hisH |
PRK13152 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
73-192 |
2.57e-04 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 171876 [Multi-domain] Cd Length: 201 Bit Score: 42.13 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 73 EIFELGIPILGICYGMQLIThKLG-------------GKVVPAGEAGNREY---GQSNLQLKTESALFAGTPEEqlvlms 136
Cdd:PRK13152 68 QVLVQKKPILGICLGMQLFL-ERGyeggvceglgfieGEVVKFEEDLNLKIphmGWNELEILKQSPLYQGIPEK------ 140
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 636941923 137 hgdavteipADFHLV----------GLSADCPF-----AAIEntERRIYGIQFHPEVRHSVyGNDILKNFA 192
Cdd:PRK13152 141 ---------SDFYFVhsfyvkckdeFVSAKAQYghkfvASLQ--KDNIFATQFHPEKSQNL-GLKLLENFA 199
|
|
| LarE-like |
cd01990 |
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ... |
223-415 |
6.75e-04 |
|
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: 41.09 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 223 KVLLGLSGGVDSSVVGVLLQRAIGDQLTCIFVDHGLLRKNEGDQVmEMLGGKFGLNIIRVDaakrfLDLLagvSDPE--- 299
Cdd:cd01990 1 KVVVAFSGGVDSSLLAKLAKEVLGDNVVAVTADSPLVPREELEEA-KRIAEEIGIRHEIIK-----TDEL---DDEEyva 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 300 ---------KKRkiignefVYVFDDEASKLTDVEFLAQGTLYTDIIEsgtdtaetikshHNVGGLP-EDMQFKLIEPLNT 369
Cdd:cd01990 72 ndpdrcyhcKKA-------LYSTLKEIAKERGYDVVLDGTNADDLKD------------YRPGLLAaAELGIRSPLPELG 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 636941923 370 LFKDEVRALGTALGMPdevVWRQPfPGPGLAIRV-MGE-ITEEKLQTV 415
Cdd:cd01990 133 LTKSEIRELARELGLP---NWDKP-ASACLASRIpYGEeITPERLKRI 176
|
|
| GATase1_Glutamyl_Hydrolase |
cd01747 |
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ... |
46-177 |
1.53e-03 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153218 [Multi-domain] Cd Length: 273 Bit Score: 40.38 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 46 RAINpiGIVLSGGPNSVYAENAFDIDPEIFELGI---------PILGICYGMQLITHKLGGKVVPAGEAGNREYGQSnLQ 116
Cdd:cd01747 53 KSIN--GILFPGGAVDIDTSGYARTAKIIYNLALerndagdyfPVWGTCLGFELLTYLTSGETLLLEATEATNSALP-LN 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 117 LKT---ESALFAGTP--------EEQLVLMSHGDAVT-------EIPADFH-LVGLSAD---CPF-AAIENTERRIYGIQ 173
Cdd:cd01747 130 FTEdalQSRLFKRFPpdllkslaTEPLTMNNHRYGISpenftenGLLSDFFnVLTTNDDwngVEFiSTVEAYKYPIYGVQ 209
|
....
gi 636941923 174 FHPE 177
Cdd:cd01747 210 WHPE 213
|
|
| nadE |
PRK00876 |
NAD(+) synthase; |
208-248 |
1.68e-03 |
|
NAD(+) synthase;
Pssm-ID: 179150 [Multi-domain] Cd Length: 326 Bit Score: 40.71 E-value: 1.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 636941923 208 IETEIEKIRQ--------TVGDKKVLLGLSGGVDSSVVGVLLQRAIGDQ 248
Cdd:PRK00876 12 AAAEAERIRAaireqvrgTLRRRGVVLGLSGGIDSSVTAALCVRALGKE 60
|
|
| MnmA_TRMU-like |
cd01998 |
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
223-253 |
2.25e-03 |
|
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.
Pssm-ID: 467502 [Multi-domain] Cd Length: 349 Bit Score: 40.18 E-value: 2.25e-03
10 20 30
....*....|....*....|....*....|.
gi 636941923 223 KVLLGLSGGVDSSVVGVLLQRAiGDQLTCIF 253
Cdd:cd01998 1 KVAVAMSGGVDSSVAAALLKEQ-GYDVIGVF 30
|
|
| tilS |
PRK10660 |
tRNA(Ile)-lysidine synthetase; Provisional |
216-258 |
3.82e-03 |
|
tRNA(Ile)-lysidine synthetase; Provisional
Pssm-ID: 182626 [Multi-domain] Cd Length: 436 Bit Score: 39.61 E-value: 3.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 636941923 216 RQTVGDKKVLLGLSGGVDSSVVGVLL----QRAIGDQLTCIFVDHGL 258
Cdd:PRK10660 10 RQLLTSRQILVAFSGGLDSTVLLHLLvqwrTENPGVTLRAIHVHHGL 56
|
|
| TilS_N |
cd01992 |
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ... |
223-258 |
3.88e-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: 38.34 E-value: 3.88e-03
10 20 30
....*....|....*....|....*....|....*....
gi 636941923 223 KVLLGLSGGVDSSVVGVLLQRAI---GDQLTCIFVDHGL 258
Cdd:cd01992 1 KILVAVSGGPDSMALLHLLKELRpklGLKLVAVHVDHGL 39
|
|
| trmU |
TIGR00420 |
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ... |
222-253 |
7.86e-03 |
|
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase (trmU, asuE, or mnmA) is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine (mnm5s2U34) present in the wobble position of some tRNAs. This enzyme appears not to occur in the Archaea. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 273069 [Multi-domain] Cd Length: 352 Bit Score: 38.52 E-value: 7.86e-03
10 20 30
....*....|....*....|....*....|..
gi 636941923 222 KKVLLGLSGGVDSSVVGVLLQRAiGDQLTCIF 253
Cdd:TIGR00420 1 KKVIVGLSGGVDSSVSAYLLKQQ-GYEVVGVF 31
|
|
| PRK13794 |
PRK13794 |
hypothetical protein; Provisional |
204-286 |
8.95e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237509 [Multi-domain] Cd Length: 479 Bit Score: 38.50 E-value: 8.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636941923 204 MENFIETEIEKIRQTVG--DKKVLLGLSGGVDSSVVGVLLQRAIGDQLTCIFVDHGlLRKNEGDQVMEMLGGKFGLNIIR 281
Cdd:PRK13794 228 LDKYERNSIGFIRNTAEkiNKPVTVAYSGGKDSLATLLLALKALGINFPVLFNDTG-LEFPETLENVEDVEKHYGLEIIR 306
|
....*
gi 636941923 282 VDAAK 286
Cdd:PRK13794 307 TKSEE 311
|
|
| |
