|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02327 |
PLN02327 |
CTP synthase |
1-555 |
0e+00 |
|
CTP synthase
Pssm-ID: 215186 [Multi-domain] Cd Length: 557 Bit Score: 1233.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 1 MKYVLVTGGVVSGLGKGVTASSIGLLLQACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDS 80
Cdd:PLN02327 1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 81 TLTRDNNITTGKIYQSVIDKERKGDYLGRTVQVVPHVTDAIQEWIERVANVPVDGKEGPPDVCVIELGGTIGDIESMPFI 160
Cdd:PLN02327 81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPVDGKEGPADVCVIELGGTVGDIESMPFI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 161 EALGQFSYKVGPGNFCLVHVSLVPVLSVVGEQKTKPTQHSVRGLRSLGLTPNILACRSTKALEENVKTKLSQFCHVPEVN 240
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 241 IVTLYDVPNIWHVPLLLRDQKAHEAILRELNL-SNAIKPDLTEWTARTKIYDTLQDPVRIAMVGKYTGLTDSYLSVLKAL 319
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLlSVAREPDLEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 320 LHASVACHKKLVIEWVAASDLEEITAQETPDVHKAAWDLLKGADGILVPGGFGDRGVQGKILATKYARENQVPFLGICLG 399
Cdd:PLN02327 321 LHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 400 MQLAVVEFARSILGFHDANSTEFEPETSSPCIIFMPEGSTTHMGGTMRLGSRKTYFQVADCKSAKLYGNAKFVDERHRHR 479
Cdd:PLN02327 401 MQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDERHRHR 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15230562 480 YEVNPDMISEIEKAGLSFVGKDETGRRMEIVELPSHPYFVGAQFHPEFKSRPGKPSALFLGLIAAASGCLESVLQT 555
Cdd:PLN02327 481 YEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLNS 556
|
|
| PyrG |
COG0504 |
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ... |
1-545 |
0e+00 |
|
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440270 [Multi-domain] Cd Length: 535 Bit Score: 853.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 1 MKYVLVTGGVVSGLGKGVTASSIGLLLQACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDS 80
Cdd:COG0504 1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 81 TLTRDNNITTGKIYQSVIDKERKGDYLGRTVQVVPHVTDAIQEWIERVAnvpvdgKEGPPDVCVIELGGTIGDIESMPFI 160
Cdd:COG0504 81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAA------EESGADVVIVEIGGTVGDIESLPFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 161 EALGQFSYKVGPGNFCLVHVSLVPVLSVVGEQKTKPTQHSVRGLRSLGLTPNILACRSTKALEENVKTKLSQFCHVPEVN 240
Cdd:COG0504 155 EAIRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 241 IVTLYDVPNIWHVPLLLRDQKAHEAILRELNLsNAIKPDLTEWTARTKIYDTLQDPVRIAMVGKYTGLTDSYLSVLKALL 320
Cdd:COG0504 235 VISAPDVDSIYEVPLMLHEQGLDEIVLKKLGL-EAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 321 HASVACHKKLVIEWVAASDLEEitaqetpdvhKAAWDLLKGADGILVPGGFGDRGVQGKILATKYARENQVPFLGICLGM 400
Cdd:COG0504 314 HAGIANGVKVNIKWIDSEDLEE----------ENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGM 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 401 QLAVVEFARSILGFHDANSTEFEPETSSPCIIFMPE-GSTTHMGGTMRLGSRKTYFqVADCKSAKLYGNAKfVDERHRHR 479
Cdd:COG0504 384 QLAVIEFARNVLGLEDANSTEFDPNTPHPVIDLMPEqKDVSDLGGTMRLGAYPCKL-KPGTLAAEAYGKEE-ISERHRHR 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15230562 480 YEVNPDMISEIEKAGLSFVGKDETGRRMEIVELPSHPYFVGAQFHPEFKSRPGKPSALFLGLIAAA 545
Cdd:COG0504 462 YEFNNEYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAA 527
|
|
| PyrG |
TIGR00337 |
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ... |
1-544 |
0e+00 |
|
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. The enzyme catalyzes the reaction L-glutamine + H2O + UTP + ATP = CTP + phosphate + ADP + L-glutamate. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. This gene has been found circa 500 bp 5' upstream of enolase in both beta (Nitrosomonas europaea) and gamma (E.coli) subdivisions of proteobacterium (FEMS Microbiol Lett 1998 Aug 1;165(1):153-7). [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273021 [Multi-domain] Cd Length: 525 Bit Score: 804.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 1 MKYVLVTGGVVSGLGKGVTASSIGLLLQACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDS 80
Cdd:TIGR00337 1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 81 TLTRDNNITTGKIYQSVIDKERKGDYLGRTVQVVPHVTDAIQEWIERVAnvpvdgKEGPPDVCVIELGGTIGDIESMPFI 160
Cdd:TIGR00337 81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVA------KISGPDVVIVEIGGTVGDIESLPFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 161 EALGQFSYKVGPGNFCLVHVSLVPVLSVVGEQKTKPTQHSVRGLRSLGLTPNILACRSTKALEENVKTKLSQFCHVPEVN 240
Cdd:TIGR00337 155 EAIRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 241 IVTLYDVPNIWHVPLLLRDQKAHEAILRELNLsNAIKPDLTEWTARTKIYDTLQDPVRIAMVGKYTGLTDSYLSVLKALL 320
Cdd:TIGR00337 235 VISAKDVSSIYEVPLLLLKQGLDDYLCRRLNL-NCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 321 HASVACHKKLVIEWVAASDLEEITAQetpdvhkaawdLLKGADGILVPGGFGDRGVQGKILATKYARENQVPFLGICLGM 400
Cdd:TIGR00337 314 HAGAKLDTKVNIKWIDSEDLEEEGVE-----------FLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGM 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 401 QLAVVEFARSILGFHDANSTEFEPETSSPCIIFMPE-GSTTHMGGTMRLGSRKTYFQvADCKSAKLYGNAKfVDERHRHR 479
Cdd:TIGR00337 383 QLAVIEFARNVAGLEGANSTEFDPDTKYPVVDLLPEqKDISDLGGTMRLGLYPCILK-PGTLAFKLYGKEE-VYERHRHR 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15230562 480 YEVNPDMISEIEKAGLSFVGKDETGRRMEIVELPSHPYFVGAQFHPEFKSRPGKPSALFLGLIAA 544
Cdd:TIGR00337 461 YEVNNEYREQIENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
|
|
| CTP_synth_N |
pfam06418 |
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ... |
2-272 |
0e+00 |
|
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase protein (EC:6.3.4.2). This family is found in conjunction with pfam00117 located in the C-terminal region of the protein. CTP synthase catalyzes the synthesis of CTP from UTP by amination of the pyrimidine ring at the 4-position.
Pssm-ID: 461903 Cd Length: 265 Bit Score: 515.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 2 KYVLVTGGVVSGLGKGVTASSIGLLLQACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDST 81
Cdd:pfam06418 1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 82 LTRDNNITTGKIYQSVIDKERKGDYLGRTVQVVPHVTDAIQEWIERVAnvpvdgKEGPPDVCVIELGGTIGDIESMPFIE 161
Cdd:pfam06418 81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVA------KEVGPDVVIVEIGGTVGDIESLPFLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 162 ALGQFSYKVGPGNFCLVHVSLVPVLSVVGEQKTKPTQHSVRGLRSLGLTPNILACRSTKALEENVKTKLSQFCHVPEVNI 241
Cdd:pfam06418 155 AIRQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAV 234
|
250 260 270
....*....|....*....|....*....|.
gi 15230562 242 VTLYDVPNIWHVPLLLRDQKAHEAILRELNL 272
Cdd:pfam06418 235 ISAPDVSSIYEVPLLLEEQGLDDIILKRLNL 265
|
|
| CTPS_N |
cd03113 |
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ... |
2-268 |
1.14e-178 |
|
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase (CTPS) is a two-domain protein, which consists of an N-terminal synthetase domain and C-terminal glutaminase domain. The enzymes hydrolyze the amide bond of glutamine to ammonia and glutamate at the glutaminase domains and transfer nascent ammonia to the acceptor substrate at the synthetase domain to form an aminated product.
Pssm-ID: 349767 Cd Length: 261 Bit Score: 505.10 E-value: 1.14e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 2 KYVLVTGGVVSGLGKGVTASSIGLLLQACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDST 81
Cdd:cd03113 1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 82 LTRDNNITTGKIYQSVIDKERKGDYLGRTVQVVPHVTDAIQEWIERVANVPvdgkegPPDVCVIELGGTIGDIESMPFIE 161
Cdd:cd03113 81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIP------EPDVCIVEIGGTVGDIESLPFLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 162 ALGQFSYKVGPGNFCLVHVSLVPVLSVVGEQKTKPTQHSVRGLRSLGLTPNILACRSTKALEENVKTKLSQFCHVPEVNI 241
Cdd:cd03113 155 ALRQFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAV 234
|
250 260
....*....|....*....|....*..
gi 15230562 242 VTLYDVPNIWHVPLLLRDQKAHEAILR 268
Cdd:cd03113 235 ISVHDVSSIYEVPLLLEKQGLDDYILR 261
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02327 |
PLN02327 |
CTP synthase |
1-555 |
0e+00 |
|
CTP synthase
Pssm-ID: 215186 [Multi-domain] Cd Length: 557 Bit Score: 1233.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 1 MKYVLVTGGVVSGLGKGVTASSIGLLLQACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDS 80
Cdd:PLN02327 1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 81 TLTRDNNITTGKIYQSVIDKERKGDYLGRTVQVVPHVTDAIQEWIERVANVPVDGKEGPPDVCVIELGGTIGDIESMPFI 160
Cdd:PLN02327 81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPVDGKEGPADVCVIELGGTVGDIESMPFI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 161 EALGQFSYKVGPGNFCLVHVSLVPVLSVVGEQKTKPTQHSVRGLRSLGLTPNILACRSTKALEENVKTKLSQFCHVPEVN 240
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 241 IVTLYDVPNIWHVPLLLRDQKAHEAILRELNL-SNAIKPDLTEWTARTKIYDTLQDPVRIAMVGKYTGLTDSYLSVLKAL 319
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLlSVAREPDLEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 320 LHASVACHKKLVIEWVAASDLEEITAQETPDVHKAAWDLLKGADGILVPGGFGDRGVQGKILATKYARENQVPFLGICLG 399
Cdd:PLN02327 321 LHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 400 MQLAVVEFARSILGFHDANSTEFEPETSSPCIIFMPEGSTTHMGGTMRLGSRKTYFQVADCKSAKLYGNAKFVDERHRHR 479
Cdd:PLN02327 401 MQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDERHRHR 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15230562 480 YEVNPDMISEIEKAGLSFVGKDETGRRMEIVELPSHPYFVGAQFHPEFKSRPGKPSALFLGLIAAASGCLESVLQT 555
Cdd:PLN02327 481 YEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLNS 556
|
|
| PyrG |
COG0504 |
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ... |
1-545 |
0e+00 |
|
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440270 [Multi-domain] Cd Length: 535 Bit Score: 853.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 1 MKYVLVTGGVVSGLGKGVTASSIGLLLQACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDS 80
Cdd:COG0504 1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 81 TLTRDNNITTGKIYQSVIDKERKGDYLGRTVQVVPHVTDAIQEWIERVAnvpvdgKEGPPDVCVIELGGTIGDIESMPFI 160
Cdd:COG0504 81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAA------EESGADVVIVEIGGTVGDIESLPFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 161 EALGQFSYKVGPGNFCLVHVSLVPVLSVVGEQKTKPTQHSVRGLRSLGLTPNILACRSTKALEENVKTKLSQFCHVPEVN 240
Cdd:COG0504 155 EAIRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 241 IVTLYDVPNIWHVPLLLRDQKAHEAILRELNLsNAIKPDLTEWTARTKIYDTLQDPVRIAMVGKYTGLTDSYLSVLKALL 320
Cdd:COG0504 235 VISAPDVDSIYEVPLMLHEQGLDEIVLKKLGL-EAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 321 HASVACHKKLVIEWVAASDLEEitaqetpdvhKAAWDLLKGADGILVPGGFGDRGVQGKILATKYARENQVPFLGICLGM 400
Cdd:COG0504 314 HAGIANGVKVNIKWIDSEDLEE----------ENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGM 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 401 QLAVVEFARSILGFHDANSTEFEPETSSPCIIFMPE-GSTTHMGGTMRLGSRKTYFqVADCKSAKLYGNAKfVDERHRHR 479
Cdd:COG0504 384 QLAVIEFARNVLGLEDANSTEFDPNTPHPVIDLMPEqKDVSDLGGTMRLGAYPCKL-KPGTLAAEAYGKEE-ISERHRHR 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15230562 480 YEVNPDMISEIEKAGLSFVGKDETGRRMEIVELPSHPYFVGAQFHPEFKSRPGKPSALFLGLIAAA 545
Cdd:COG0504 462 YEFNNEYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAA 527
|
|
| pyrG |
PRK05380 |
CTP synthetase; Validated |
1-545 |
0e+00 |
|
CTP synthetase; Validated
Pssm-ID: 235437 [Multi-domain] Cd Length: 533 Bit Score: 851.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 1 MKYVLVTGGVVSGLGKGVTASSIGLLLQACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDS 80
Cdd:PRK05380 2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 81 TLTRDNNITTGKIYQSVIDKERKGDYLGRTVQVVPHVTDAIQEWIERVANvpvdgkegPPDVCVIELGGTIGDIESMPFI 160
Cdd:PRK05380 82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAGT--------DADVVIVEIGGTVGDIESLPFL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 161 EALGQFSYKVGPGNFCLVHVSLVPVLSVVGEQKTKPTQHSVRGLRSLGLTPNILACRSTKALEENVKTKLSQFCHVPEVN 240
Cdd:PRK05380 154 EAIRQLRLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 241 IVTLYDVPNIWHVPLLLRDQKAHEAILRELNLsNAIKPDLTEWtarTKIYDTLQDP---VRIAMVGKYTGLTDSYLSVLK 317
Cdd:PRK05380 234 VISAPDVDSIYEVPLLLHEQGLDDIVLERLGL-EAPEPDLSEW---EELVERLKNPkgeVTIALVGKYVELPDAYKSVIE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 318 ALLHASVACHKKLVIEWVAASDLEEITAQEtpdvhkaawdLLKGADGILVPGGFGDRGVQGKILATKYARENQVPFLGIC 397
Cdd:PRK05380 310 ALKHAGIANDVKVNIKWIDSEDLEEENVAE----------LLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGIC 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 398 LGMQLAVVEFARSILGFHDANSTEFEPETSSPCIIFMPE-GSTTHMGGTMRLGSRKTYFqVADCKSAKLYGNAKfVDERH 476
Cdd:PRK05380 380 LGMQLAVIEFARNVLGLEDANSTEFDPDTPHPVIDLMPEqKDVSDLGGTMRLGAYPCKL-KPGTLAAEIYGKEE-IYERH 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15230562 477 RHRYEVNPDMISEIEKAGLSFVGKDETGRRMEIVELPSHPYFVGAQFHPEFKSRPGKPSALFLGLIAAA 545
Cdd:PRK05380 458 RHRYEVNNKYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAA 526
|
|
| PyrG |
TIGR00337 |
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ... |
1-544 |
0e+00 |
|
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. The enzyme catalyzes the reaction L-glutamine + H2O + UTP + ATP = CTP + phosphate + ADP + L-glutamate. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. This gene has been found circa 500 bp 5' upstream of enolase in both beta (Nitrosomonas europaea) and gamma (E.coli) subdivisions of proteobacterium (FEMS Microbiol Lett 1998 Aug 1;165(1):153-7). [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273021 [Multi-domain] Cd Length: 525 Bit Score: 804.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 1 MKYVLVTGGVVSGLGKGVTASSIGLLLQACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDS 80
Cdd:TIGR00337 1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 81 TLTRDNNITTGKIYQSVIDKERKGDYLGRTVQVVPHVTDAIQEWIERVAnvpvdgKEGPPDVCVIELGGTIGDIESMPFI 160
Cdd:TIGR00337 81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVA------KISGPDVVIVEIGGTVGDIESLPFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 161 EALGQFSYKVGPGNFCLVHVSLVPVLSVVGEQKTKPTQHSVRGLRSLGLTPNILACRSTKALEENVKTKLSQFCHVPEVN 240
Cdd:TIGR00337 155 EAIRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 241 IVTLYDVPNIWHVPLLLRDQKAHEAILRELNLsNAIKPDLTEWTARTKIYDTLQDPVRIAMVGKYTGLTDSYLSVLKALL 320
Cdd:TIGR00337 235 VISAKDVSSIYEVPLLLLKQGLDDYLCRRLNL-NCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 321 HASVACHKKLVIEWVAASDLEEITAQetpdvhkaawdLLKGADGILVPGGFGDRGVQGKILATKYARENQVPFLGICLGM 400
Cdd:TIGR00337 314 HAGAKLDTKVNIKWIDSEDLEEEGVE-----------FLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGM 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 401 QLAVVEFARSILGFHDANSTEFEPETSSPCIIFMPE-GSTTHMGGTMRLGSRKTYFQvADCKSAKLYGNAKfVDERHRHR 479
Cdd:TIGR00337 383 QLAVIEFARNVAGLEGANSTEFDPDTKYPVVDLLPEqKDISDLGGTMRLGLYPCILK-PGTLAFKLYGKEE-VYERHRHR 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15230562 480 YEVNPDMISEIEKAGLSFVGKDETGRRMEIVELPSHPYFVGAQFHPEFKSRPGKPSALFLGLIAA 544
Cdd:TIGR00337 461 YEVNNEYREQIENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
|
|
| CTP_synth_N |
pfam06418 |
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ... |
2-272 |
0e+00 |
|
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase protein (EC:6.3.4.2). This family is found in conjunction with pfam00117 located in the C-terminal region of the protein. CTP synthase catalyzes the synthesis of CTP from UTP by amination of the pyrimidine ring at the 4-position.
Pssm-ID: 461903 Cd Length: 265 Bit Score: 515.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 2 KYVLVTGGVVSGLGKGVTASSIGLLLQACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDST 81
Cdd:pfam06418 1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 82 LTRDNNITTGKIYQSVIDKERKGDYLGRTVQVVPHVTDAIQEWIERVAnvpvdgKEGPPDVCVIELGGTIGDIESMPFIE 161
Cdd:pfam06418 81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVA------KEVGPDVVIVEIGGTVGDIESLPFLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 162 ALGQFSYKVGPGNFCLVHVSLVPVLSVVGEQKTKPTQHSVRGLRSLGLTPNILACRSTKALEENVKTKLSQFCHVPEVNI 241
Cdd:pfam06418 155 AIRQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAV 234
|
250 260 270
....*....|....*....|....*....|.
gi 15230562 242 VTLYDVPNIWHVPLLLRDQKAHEAILRELNL 272
Cdd:pfam06418 235 ISAPDVSSIYEVPLLLEEQGLDDIILKRLNL 265
|
|
| CTPS_N |
cd03113 |
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ... |
2-268 |
1.14e-178 |
|
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase (CTPS) is a two-domain protein, which consists of an N-terminal synthetase domain and C-terminal glutaminase domain. The enzymes hydrolyze the amide bond of glutamine to ammonia and glutamate at the glutaminase domains and transfer nascent ammonia to the acceptor substrate at the synthetase domain to form an aminated product.
Pssm-ID: 349767 Cd Length: 261 Bit Score: 505.10 E-value: 1.14e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 2 KYVLVTGGVVSGLGKGVTASSIGLLLQACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDST 81
Cdd:cd03113 1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 82 LTRDNNITTGKIYQSVIDKERKGDYLGRTVQVVPHVTDAIQEWIERVANVPvdgkegPPDVCVIELGGTIGDIESMPFIE 161
Cdd:cd03113 81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIP------EPDVCIVEIGGTVGDIESLPFLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 162 ALGQFSYKVGPGNFCLVHVSLVPVLSVVGEQKTKPTQHSVRGLRSLGLTPNILACRSTKALEENVKTKLSQFCHVPEVNI 241
Cdd:cd03113 155 ALRQFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAV 234
|
250 260
....*....|....*....|....*..
gi 15230562 242 VTLYDVPNIWHVPLLLRDQKAHEAILR 268
Cdd:cd03113 235 ISVHDVSSIYEVPLLLEKQGLDDYILR 261
|
|
| GATase1_CTP_Synthase |
cd01746 |
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ... |
297-542 |
2.90e-139 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153217 [Multi-domain] Cd Length: 235 Bit Score: 403.86 E-value: 2.90e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 297 VRIAMVGKYTGLTDSYLSVLKALLHASVACHKKLVIEWVAASDLEEITAqetpdvhkaaWDLLKGADGILVPGGFGDRGV 376
Cdd:cd01746 1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEENA----------EEALKGADGILVPGGFGIRGV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 377 QGKILATKYARENQVPFLGICLGMQLAVVEFARSILGFHDANSTEFEPETSSPCIIFMPEG-STTHMGGTMRLGSRKTYF 455
Cdd:cd01746 71 EGKILAIKYARENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEQkGVKDLGGTMRLGAYPVIL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 456 QvaDCKSAKLYGNAKFVDERHRHRYEVNPDMISEIEKAGLSFVGKDETGRRMEIVELPSHPYFVGAQFHPEFKSRPGKPS 535
Cdd:cd01746 151 K--PGTLAHKYYGKDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPEFKSRPLKPH 228
|
....*..
gi 15230562 536 ALFLGLI 542
Cdd:cd01746 229 PLFVGFV 235
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
308-544 |
7.39e-43 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 152.01 E-value: 7.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 308 LTDSYLSVLKALLHASVACHKKLVIEWVAASDLEEITAqetpdvhkaawdllkGADGILVPGGFGDRG-VQGKILATKYA 386
Cdd:pfam00117 2 LIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEE---------------NPDGIILSGGPGSPGaAGGAIEAIREA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 387 RENQVPFLGICLGMQLAVVEFARSILgfhdanstefepetsspciifmPEGSTTHMGGTMRLGsrktyfqvaDCKSAKLY 466
Cdd:pfam00117 67 RELKIPILGICLGHQLLALAFGGKVV----------------------KAKKFGHHGKNSPVG---------DDGCGLFY 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15230562 467 GNAKFVDERHRHRYEVNPDmiseIEKAGLSFVGKDETG-RRMEIVELPSHpyFVGAQFHPEFKSRPGKPSALFLGLIAA 544
Cdd:pfam00117 116 GLPNVFIVRRYHSYAVDPD----TLPDGLEVTATSENDgTIMGIRHKKLP--IFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| PRK06186 |
PRK06186 |
hypothetical protein; Validated |
296-548 |
2.87e-36 |
|
hypothetical protein; Validated
Pssm-ID: 180452 [Multi-domain] Cd Length: 229 Bit Score: 135.48 E-value: 2.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 296 PVRIAMVGKYTGLTDSYLSVLKALLHASVACHKKLVIEWVAasdleeitaqeTPDVHKAawDLLKGADGI-LVPGGfGDR 374
Cdd:PRK06186 1 TLRIALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLP-----------TPEITDP--EDLAGFDGIwCVPGS-PYR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 375 GVQGKILATKYARENQVPFLGICLGMQLAVVEFARSILGFHDANSTEFEPETSSPCIIFMPEGSTTHMGG-TMRLGSRkt 453
Cdd:PRK06186 67 NDDGALTAIRFARENGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDRPVIAPLSCSLVEKTGDiRLRPGSL-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 454 yfqvadckSAKLYGnAKFVDERHRHRYEVNPDMISEIEKAGLSFVGKDETGrrmEI--VELPSHPYFVGAQFHPEFKSRP 531
Cdd:PRK06186 145 --------IARAYG-TLEIEEGYHCRYGVNPEFVAALESGDLRVTGWDEDG---DVraVELPGHPFFVATLFQPERAALA 212
|
250
....*....|....*..
gi 15230562 532 GKPSALFLGLIAAASGC 548
Cdd:PRK06186 213 GRPPPLVRAFLRAARAA 229
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
299-405 |
7.64e-10 |
|
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: 56.84 E-value: 7.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 299 IAMVGKYTGLTDSYLSVLKALLHASVAchkklvIEWVAASDLEEITAqetpdvhkaawDLLKGADGILVPGGFGDRGV-- 376
Cdd:cd01653 1 VAVLLFPGFEELELASPLDALREAGAE------VDVVSPDGGPVESD-----------VDLDDYDGLILPGGPGTPDDla 63
|
90 100 110
....*....|....*....|....*....|.
gi 15230562 377 --QGKILATKYARENQVPFLGICLGMQLAVV 405
Cdd:cd01653 64 rdEALLALLREAAAAGKPILGICLGAQLLVL 94
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
299-402 |
3.09e-08 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 51.43 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 299 IAMVGKYTGLTDSYLSVLKALLHASVAchkklvIEWVAASDLEEITAqetpdvhkaawDLLKGADGILVPGGFGDRGV-- 376
Cdd:cd03128 1 VAVLLFGGSEELELASPLDALREAGAE------VDVVSPDGGPVESD-----------VDLDDYDGLILPGGPGTPDDla 63
|
90 100
....*....|....*....|....*...
gi 15230562 377 --QGKILATKYARENQVPFLGICLGMQL 402
Cdd:cd03128 64 wdEALLALLREAAAAGKPVLGICLGAQL 91
|
|
| PuuD |
COG2071 |
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
354-545 |
2.04e-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: 52.09 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 354 AAWDLLKGADGILVPGG-------FGDRGVQGK-----------ILATKYARENQVPFLGICLGMQLAVVefarsilgfh 415
Cdd:COG2071 42 DLDELLDRLDGLVLTGGadvdpalYGEEPHPELgpidperdafeLALIRAALERGKPVLGICRGMQLLNV---------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 416 danstefepetsspciifmpegsttHMGGTMrlgsrktYFQVADCKSAKLYGNAKFVDERHRHRYEVNPD-MISEIekag 494
Cdd:COG2071 112 -------------------------ALGGTL-------YQDLPDQVPGALDHRQPAPRYAPRHTVEIEPGsRLARI---- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15230562 495 lsfVGKDET-------------GRRMEI-----------VELPSHPYFVGAQFHPEFKSRPGKPS-ALFLGLIAAA 545
Cdd:COG2071 156 ---LGEEEIrvnslhhqavkrlGPGLRVsarapdgvieaIESPGAPFVLGVQWHPEWLAASDPLSrRLFEAFVEAA 228
|
|
| hisH |
PRK13146 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
314-443 |
2.34e-06 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237290 [Multi-domain] Cd Length: 209 Bit Score: 48.63 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 314 SVLKALLHAsvACHKKLVIewvaASDLEEITAqetpdvhkaawdllkgADGILVPG---------GFGDRGVQGKILATk 384
Cdd:PRK13146 16 SAAKALERA--GAGADVVV----TADPDAVAA----------------ADRVVLPGvgafadcmrGLRAVGLGEAVIEA- 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15230562 385 yARENQVPFLGICLGMQLAvveFARSI-------LGFHDANSTEFEPETSSPCIifmPegsttHMG 443
Cdd:PRK13146 73 -VLAAGRPFLGICVGMQLL---FERGLehgdtpgLGLIPGEVVRFQPDGPALKV---P-----HMG 126
|
|
| hisH |
PRK13143 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
314-402 |
1.27e-05 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 46.40 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 314 SVLKALLHASvachKKLVIewvaASDLEEITAqetpdvhkaawdllkgADGILVPG--GFGD-----RGVQGKILAtkyA 386
Cdd:PRK13143 15 SVSKALERAG----AEVVI----TSDPEEILD----------------ADGIVLPGvgAFGAamenlSPLRDVILE---A 67
|
90
....*....|....*.
gi 15230562 387 RENQVPFLGICLGMQL 402
Cdd:PRK13143 68 ARSGKPFLGICLGMQL 83
|
|
| IMP_synth_hisH |
TIGR01855 |
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ... |
359-533 |
2.07e-05 |
|
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: 45.78 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 359 LKGADGILVPG--GFGD--RGV--QGKILATKYARENQVPFLGICLGMQLAvveFARSI-------LGFHDANSTEFEPE 425
Cdd:TIGR01855 34 AELADKLILPGvgAFGAamARLreNGLDLFVELVVRLGKPVLGICLGMQLL---FERSEegggvpgLGLIKGNVVKLEAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 426 TsspciifMPegsttHMGGTmRLGSRKtyfqvadcKSAKLYGNAK-----FVderHRHRYEVNPDMISEIEKAGLSFVGK 500
Cdd:TIGR01855 111 K-------VP-----HMGWN-EVHPVK--------ESPLLNGIDEgayfyFV---HSYYAVCEEEAVLAYADYGEKFPAA 166
|
170 180 190
....*....|....*....|....*....|...
gi 15230562 501 DETGRrmeivelpshpyFVGAQFHPEFKSRPGK 533
Cdd:TIGR01855 167 VQKGN------------IFGTQFHPEKSGKTGL 187
|
|
| HisH |
COG0118 |
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
357-402 |
2.11e-05 |
|
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: 45.41 E-value: 2.11e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 15230562 357 DLLKGADGILVPG-G-FGD--RGVQGKIL--ATKYARENQVPFLGICLGMQL 402
Cdd:COG0118 34 DEIRAADRLVLPGvGaFGDamENLRERGLdeAIREAVAGGKPVLGICLGMQL 85
|
|
| hisH |
PRK13141 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
314-402 |
2.32e-05 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 45.51 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 314 SVLKALLHASVAChkklVIEwvaaSDLEEItaqetpdvhkaawdllKGADGILVPG--GFGD-------RGVqgkILATK 384
Cdd:PRK13141 14 SVEKALERLGAEA----VIT----SDPEEI----------------LAADGVILPGvgAFPDamanlreRGL---DEVIK 66
|
90
....*....|....*...
gi 15230562 385 YARENQVPFLGICLGMQL 402
Cdd:PRK13141 67 EAVASGKPLLGICLGMQL 84
|
|
| hisH |
PRK13181 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
314-529 |
3.65e-05 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 44.86 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 314 SVLKALlhasvachKKLVIEWVAASDLEEItaqetpdvhkaawdllKGADGILVPG-GFGDRGVQ-----GKILATKYAR 387
Cdd:PRK13181 14 SVANAL--------KRLGVEAVVSSDPEEI----------------AGADKVILPGvGAFGQAMRslresGLDEALKEHV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 388 ENQVPFLGICLGMQLavveFARSI-------LGFHDANSTEFEPETSSpciifMPegsttHMGgtmrlgsrktYFQVADC 460
Cdd:PRK13181 70 EKKQPVLGICLGMQL----LFESSeegnvkgLGLIPGDVKRFRSEPLK-----VP-----QMG----------WNSVKPL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 461 KSAKLYGNAK------FVderhrHRYEVNP-DMISEIEKA--GLSF---VGKDEtgrrmeivelpshpyFVGAQFHPEfK 528
Cdd:PRK13181 126 KESPLFKGIEegsyfyFV-----HSYYVPCeDPEDVLATTeyGVPFcsaVAKDN---------------IYAVQFHPE-K 184
|
.
gi 15230562 529 S 529
Cdd:PRK13181 185 S 185
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
314-529 |
1.73e-04 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153219 [Multi-domain] Cd Length: 198 Bit Score: 42.87 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 314 SVLKALlhasvachKKLVIEWVAASDLEEItaqetpdvhkaawdllKGADGILVPG-G-FGD-------RGVQGKIlatK 384
Cdd:cd01748 13 SVANAL--------ERLGAEVIITSDPEEI----------------LSADKLILPGvGaFGDamanlreRGLIEAL---K 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230562 385 YARENQVPFLGICLGMQLAvveFARSI-------LGFHDANSTEFEPEtsspciifmPEGSTTHMGGtmrlgsRKTYFQV 457
Cdd:cd01748 66 EAIASGKPFLGICLGMQLL---FESSEegggtkgLGLIPGKVVRFPAS---------EGLKVPHMGW------NQLEITK 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230562 458 ADCKSAKLYGNAK--FVderhrHRYEVNPDmiSEIEKAGLSFVGKDETGrrmeIVElpsHPYFVGAQFHPEfKS 529
Cdd:cd01748 128 ESPLFKGIPDGSYfyFV-----HSYYAPPD--DPDYILATTDYGGKFPA----AVE---KDNIFGTQFHPE-KS 186
|
|
| |
