|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02327 |
PLN02327 |
CTP synthase |
1-560 |
0e+00 |
|
CTP synthase
Pssm-ID: 215186 [Multi-domain] Cd Length: 557 Bit Score: 1269.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 1 MKYVLVTGGVVSGLGKGVTASSIGVVLKDCGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDI 80
Cdd:PLN02327 1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 81 KLTRDNNITTGKIYQAVIDKERRGDYLGKTVQVVPHITDEIQEWIERVAMNPVDGTDEPADVCVIELGGTIGDIESMPFI 160
Cdd:PLN02327 81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPVDGKEGPADVCVIELGGTVGDIESMPFI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 161 EALGQFSYRVGAGNFCLVHVSLVPVLNVVGEQKTKPTQHSVRGLRGLGLIPDILACRSTQPLEENVKVKLAQFCHVPISN 240
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 241 IVNLHDVTNIWHIPLLLRDQKAHESILKVLDLQcvgKVPRAPKLTEWTERASKFDKLKTPVRIAMVGKYTGLSDSYLSVL 320
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLL---SVAREPDLEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 321 KALLHASVALDRKLVVDWVPSCDLEDSAATETPDAYEKAWDLLKGAHGVLVPGGFGDRGVQGKILAAKYARENNVPYLGI 400
Cdd:PLN02327 318 KALLHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 401 CLGMQIAVIEFARSVMKLRGANSTEFDPATTTPCVIFMPEGSKTHMGATMRLGSRRTFFQANTCKSAKLYGNASYVDERH 480
Cdd:PLN02327 398 CLGMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDERH 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 481 RHRYEVNPEMVPEFEKAGLSFVGRDESGTRMEIIELPTHRFFVGAQFHPEFKSRPGKPSPLFMGLIAASSGQLDHLLQQS 560
Cdd:PLN02327 478 RHRYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLNSS 557
|
|
| pyrG |
PRK05380 |
CTP synthetase; Validated |
1-549 |
0e+00 |
|
CTP synthetase; Validated
Pssm-ID: 235437 [Multi-domain] Cd Length: 533 Bit Score: 883.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 1 MKYVLVTGGVVSGLGKGVTASSIGVVLKDCGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDI 80
Cdd:PRK05380 2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 81 KLTRDNNITTGKIYQAVIDKERRGDYLGKTVQVVPHITDEIQEWIERVAMNPvdgtdepaDVCVIELGGTIGDIESMPFI 160
Cdd:PRK05380 82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAGTDA--------DVVIVEIGGTVGDIESLPFL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 161 EALGQFSYRVGAGNFCLVHVSLVPVLNVVGEQKTKPTQHSVRGLRGLGLIPDILACRSTQPLEENVKVKLAQFCHVPISN 240
Cdd:PRK05380 154 EAIRQLRLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 241 IVNLHDVTNIWHIPLLLRDQKAHESILKVLDLQCvgkvpRAPKLTEWTERASKFDKLKTPVRIAMVGKYTGLSDSYLSVL 320
Cdd:PRK05380 234 VISAPDVDSIYEVPLLLHEQGLDDIVLERLGLEA-----PEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 321 KALLHASVALDRKLVVDWVPSCDLEDSAATEtpdayekawdLLKGAHGVLVPGGFGDRGVQGKILAAKYARENNVPYLGI 400
Cdd:PRK05380 309 EALKHAGIANDVKVNIKWIDSEDLEEENVAE----------LLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 401 CLGMQIAVIEFARSVMKLRGANSTEFDPATTTPCVIFMPE-GSKTHMGATMRLGSRRTFFQANTcKSAKLYGNASyVDER 479
Cdd:PRK05380 379 CLGMQLAVIEFARNVLGLEDANSTEFDPDTPHPVIDLMPEqKDVSDLGGTMRLGAYPCKLKPGT-LAAEIYGKEE-IYER 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 480 HRHRYEVNPEMVPEFEKAGLSFVGRDESGTRMEIIELPTHRFFVGAQFHPEFKSRPGKPSPLFMGLIAAS 549
Cdd:PRK05380 457 HRHRYEVNNKYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAA 526
|
|
| PyrG |
COG0504 |
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ... |
1-549 |
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: 880.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 1 MKYVLVTGGVVSGLGKGVTASSIGVVLKDCGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDI 80
Cdd:COG0504 1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 81 KLTRDNNITTGKIYQAVIDKERRGDYLGKTVQVVPHITDEIQEWIERVAmnpvdgTDEPADVCVIELGGTIGDIESMPFI 160
Cdd:COG0504 81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAA------EESGADVVIVEIGGTVGDIESLPFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 161 EALGQFSYRVGAGNFCLVHVSLVPVLNVVGEQKTKPTQHSVRGLRGLGLIPDILACRSTQPLEENVKVKLAQFCHVPISN 240
Cdd:COG0504 155 EAIRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 241 IVNLHDVTNIWHIPLLLRDQKAHESILKVLDLQCvgkvpRAPKLTEWTERASKFDKLKTPVRIAMVGKYTGLSDSYLSVL 320
Cdd:COG0504 235 VISAPDVDSIYEVPLMLHEQGLDEIVLKKLGLEA-----REPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 321 KALLHASVALDRKLVVDWVPSCDLEDsaatetpdayEKAWDLLKGAHGVLVPGGFGDRGVQGKILAAKYARENNVPYLGI 400
Cdd:COG0504 310 EALKHAGIANGVKVNIKWIDSEDLEE----------ENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 401 CLGMQIAVIEFARSVMKLRGANSTEFDPATTTPCVIFMPE-GSKTHMGATMRLGSRRTFFQANTcKSAKLYGnASYVDER 479
Cdd:COG0504 380 CLGMQLAVIEFARNVLGLEDANSTEFDPNTPHPVIDLMPEqKDVSDLGGTMRLGAYPCKLKPGT-LAAEAYG-KEEISER 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 480 HRHRYEVNPEMVPEFEKAGLSFVGRDESGTRMEIIELPTHRFFVGAQFHPEFKSRPGKPSPLFMGLIAAS 549
Cdd:COG0504 458 HRHRYEFNNEYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAA 527
|
|
| PyrG |
TIGR00337 |
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ... |
1-548 |
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: 820.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 1 MKYVLVTGGVVSGLGKGVTASSIGVVLKDCGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDI 80
Cdd:TIGR00337 1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 81 KLTRDNNITTGKIYQAVIDKERRGDYLGKTVQVVPHITDEIQEWIERVAMNpvdgtdEPADVCVIELGGTIGDIESMPFI 160
Cdd:TIGR00337 81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAKI------SGPDVVIVEIGGTVGDIESLPFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 161 EALGQFSYRVGAGNFCLVHVSLVPVLNVVGEQKTKPTQHSVRGLRGLGLIPDILACRSTQPLEENVKVKLAQFCHVPISN 240
Cdd:TIGR00337 155 EAIRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 241 IVNLHDVTNIWHIPLLLRDQKAHESILKVLDLQCvgkvpRAPKLTEWTERASKFDKLKTPVRIAMVGKYTGLSDSYLSVL 320
Cdd:TIGR00337 235 VISAKDVSSIYEVPLLLLKQGLDDYLCRRLNLNC-----DEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 321 KALLHASVALDRKLVVDWVPSCDLEdsaatetpdayEKAWDLLKGAHGVLVPGGFGDRGVQGKILAAKYARENNVPYLGI 400
Cdd:TIGR00337 310 EALKHAGAKLDTKVNIKWIDSEDLE-----------EEGVEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 401 CLGMQIAVIEFARSVMKLRGANSTEFDPATTTPCVIFMPE-GSKTHMGATMRLGSRRTFFQANTcKSAKLYGNASyVDER 479
Cdd:TIGR00337 379 CLGMQLAVIEFARNVAGLEGANSTEFDPDTKYPVVDLLPEqKDISDLGGTMRLGLYPCILKPGT-LAFKLYGKEE-VYER 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002271798 480 HRHRYEVNPEMVPEFEKAGLSFVGRDESGTRMEIIELPTHRFFVGAQFHPEFKSRPGKPSPLFMGLIAA 548
Cdd:TIGR00337 457 HRHRYEVNNEYREQIENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 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: 541.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 2 KYVLVTGGVVSGLGKGVTASSIGVVLKDCGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDIK 81
Cdd:pfam06418 1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 82 LTRDNNITTGKIYQAVIDKERRGDYLGKTVQVVPHITDEIQEWIERVAmnpvdgTDEPADVCVIELGGTIGDIESMPFIE 161
Cdd:pfam06418 81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVA------KEVGPDVVIVEIGGTVGDIESLPFLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 162 ALGQFSYRVGAGNFCLVHVSLVPVLNVVGEQKTKPTQHSVRGLRGLGLIPDILACRSTQPLEENVKVKLAQFCHVPISNI 241
Cdd:pfam06418 155 AIRQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAV 234
|
250 260 270
....*....|....*....|....*....|.
gi 1002271798 242 VNLHDVTNIWHIPLLLRDQKAHESILKVLDL 272
Cdd:pfam06418 235 ISAPDVSSIYEVPLLLEEQGLDDIILKRLNL 265
|
|
| CTPS_N |
cd03113 |
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ... |
2-268 |
0e+00 |
|
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: 531.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 2 KYVLVTGGVVSGLGKGVTASSIGVVLKDCGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDIK 81
Cdd:cd03113 1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 82 LTRDNNITTGKIYQAVIDKERRGDYLGKTVQVVPHITDEIQEWIERVAMNPvdgtdePADVCVIELGGTIGDIESMPFIE 161
Cdd:cd03113 81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIP------EPDVCIVEIGGTVGDIESLPFLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 162 ALGQFSYRVGAGNFCLVHVSLVPVLNVVGEQKTKPTQHSVRGLRGLGLIPDILACRSTQPLEENVKVKLAQFCHVPISNI 241
Cdd:cd03113 155 ALRQFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAV 234
|
250 260
....*....|....*....|....*..
gi 1002271798 242 VNLHDVTNIWHIPLLLRDQKAHESILK 268
Cdd:cd03113 235 ISVHDVSSIYEVPLLLEKQGLDDYILR 261
|
|
| GATase1_CTP_Synthase |
cd01746 |
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ... |
301-546 |
3.32e-142 |
|
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: 411.95 E-value: 3.32e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 301 VRIAMVGKYTGLSDSYLSVLKALLHASVALDRKLVVDWVPSCDLEDsaatetpdayEKAWDLLKGAHGVLVPGGFGDRGV 380
Cdd:cd01746 1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEE----------ENAEEALKGADGILVPGGFGIRGV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 381 QGKILAAKYARENNVPYLGICLGMQIAVIEFARSVMKLRGANSTEFDPATTTPCVIFMPEG-SKTHMGATMRLGSRRTFF 459
Cdd:cd01746 71 EGKILAIKYARENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEQkGVKDLGGTMRLGAYPVIL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 460 QANTckSAKLYGNASYVDERHRHRYEVNPEMVPEFEKAGLSFVGRDESGTRMEIIELPTHRFFVGAQFHPEFKSRPGKPS 539
Cdd:cd01746 151 KPGT--LAHKYYGKDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPEFKSRPLKPH 228
|
....*..
gi 1002271798 540 PLFMGLI 546
Cdd:cd01746 229 PLFVGFV 235
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
314-548 |
1.06e-45 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 159.71 E-value: 1.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 314 DSYLSVLKALLHASVALDRKLVVDWVPSCDLEDsaATETPDayekawdllkgahGVLVPGGFGDRG-VQGKILAAKYARE 392
Cdd:pfam00117 4 DNGDSFTYNLARALRELGVEVTVVPNDTPAEEI--LEENPD-------------GIILSGGPGSPGaAGGAIEAIREARE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 393 NNVPYLGICLGMQIAVIEFARSVMKLRganstefdpatttpcvifmpegSKTHMGATMRLGSRRTffqantcksAKLYGN 472
Cdd:pfam00117 69 LKIPILGICLGHQLLALAFGGKVVKAK----------------------KFGHHGKNSPVGDDGC---------GLFYGL 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002271798 473 ASYVDERHRHRYEVNPEMVPEfekaGLSFVG-RDESGTRMEIIELPthRFFVGAQFHPEFKSRPGKPSPLFMGLIAA 548
Cdd:pfam00117 118 PNVFIVRRYHSYAVDPDTLPD----GLEVTAtSENDGTIMGIRHKK--LPIFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| PRK06186 |
PRK06186 |
hypothetical protein; Validated |
300-552 |
2.95e-37 |
|
hypothetical protein; Validated
Pssm-ID: 180452 [Multi-domain] Cd Length: 229 Bit Score: 138.17 E-value: 2.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 300 PVRIAMVGKYTGLSDSYLSVLKALLHASVALDRKLVVDWVPSCDLEDSAAtetpdayekawdlLKGAHGV-LVPGGfGDR 378
Cdd:PRK06186 1 TLRIALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTPEITDPED-------------LAGFDGIwCVPGS-PYR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 379 GVQGKILAAKYARENNVPYLGICLGMQIAVIEFARSVMKLRGANSTEFDPATTTPcVIfmpegskTHMGATMRLGSRRTF 458
Cdd:PRK06186 67 NDDGALTAIRFARENGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDRP-VI-------APLSCSLVEKTGDIR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 459 FQANTcKSAKLYGnASYVDERHRHRYEVNPEMVPEFEKAGLSFVGRDESGtrmEI--IELPTHRFFVGAQFHPEFKSRPG 536
Cdd:PRK06186 139 LRPGS-LIARAYG-TLEIEEGYHCRYGVNPEFVAALESGDLRVTGWDEDG---DVraVELPGHPFFVATLFQPERAALAG 213
|
250
....*....|....*.
gi 1002271798 537 KPSPLFMGLIAASSGQ 552
Cdd:PRK06186 214 RPPPLVRAFLRAARAA 229
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
303-409 |
2.50e-09 |
|
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: 55.30 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 303 IAMVGKYTGLSDSYLSVLKALLHASVAldrklvVDWVPScdledsaatetPDAYEKAWDLLKGAHGVLVPGGFGDRGV-- 380
Cdd:cd01653 1 VAVLLFPGFEELELASPLDALREAGAE------VDVVSP-----------DGGPVESDVDLDDYDGLILPGGPGTPDDla 63
|
90 100 110
....*....|....*....|....*....|.
gi 1002271798 381 --QGKILAAKYARENNVPYLGICLGMQIAVI 409
Cdd:cd01653 64 rdEALLALLREAAAAGKPILGICLGAQLLVL 94
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
303-406 |
6.56e-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: 50.66 E-value: 6.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 303 IAMVGKYTGLSDSYLSVLKALLHASVAldrklvVDWVPscdledsaateTPDAYEKAWDLLKGAHGVLVPGGFGDRGV-- 380
Cdd:cd03128 1 VAVLLFGGSEELELASPLDALREAGAE------VDVVS-----------PDGGPVESDVDLDDYDGLILPGGPGTPDDla 63
|
90 100
....*....|....*....|....*...
gi 1002271798 381 --QGKILAAKYARENNVPYLGICLGMQI 406
Cdd:cd03128 64 wdEALLALLREAAAAGKPVLGICLGAQL 91
|
|
| PuuD |
COG2071 |
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
354-548 |
1.93e-05 |
|
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: 46.32 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 354 DAYEKAWDLLKGAHGVLVPGG-------FGDRGVQGK-----------ILAAKYARENNVPYLGICLGMQI--------- 406
Cdd:COG2071 38 GDEEDLDELLDRLDGLVLTGGadvdpalYGEEPHPELgpidperdafeLALIRAALERGKPVLGICRGMQLlnvalggtl 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 407 --AVIEFARSVMKLRGANSTEFdPATTtpcVIFMPEGskthmgatmRLgsrrtffqantcksAKLYGnasyvderhRHRY 484
Cdd:COG2071 118 yqDLPDQVPGALDHRQPAPRYA-PRHT---VEIEPGS---------RL--------------ARILG---------EEEI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002271798 485 EVN-----------PEMVPEfekaglsfvGRDESGTrMEIIELPTHRFFVGAQFHPEFKSRPGKPS-PLFMGLIAA 548
Cdd:COG2071 162 RVNslhhqavkrlgPGLRVS---------ARAPDGV-IEAIESPGAPFVLGVQWHPEWLAASDPLSrRLFEAFVEA 227
|
|
| hisH |
PRK13146 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
318-415 |
1.61e-04 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237290 [Multi-domain] Cd Length: 209 Bit Score: 43.23 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 318 SVLKALLHAsvALDRKLVVdwvpSCDLEDSAAtetpdayekawdllkgAHGVLVPG---------GFGDRGVQGKILAAk 388
Cdd:PRK13146 16 SAAKALERA--GAGADVVV----TADPDAVAA----------------ADRVVLPGvgafadcmrGLRAVGLGEAVIEA- 72
|
90 100
....*....|....*....|....*..
gi 1002271798 389 yARENNVPYLGICLGMQIAvieFARSV 415
Cdd:PRK13146 73 -VLAAGRPFLGICVGMQLL---FERGL 95
|
|
| hisH |
PRK13141 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
361-406 |
2.87e-03 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 39.34 E-value: 2.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1002271798 361 DLLKGAHGVLVPG--GFGD-------RGVQGKIlaaKYARENNVPYLGICLGMQI 406
Cdd:PRK13141 33 EEILAADGVILPGvgAFPDamanlreRGLDEVI---KEAVASGKPLLGICLGMQL 84
|
|
| IMP_synth_hisH |
TIGR01855 |
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ... |
363-537 |
4.54e-03 |
|
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: 38.85 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 363 LKGAHGVLVPG--GFGD--RGV--QGKILAAKYARENNVPYLGICLGMQiaviefarsvmkLRGANSTEFDpatTTPC-- 434
Cdd:TIGR01855 34 AELADKLILPGvgAFGAamARLreNGLDLFVELVVRLGKPVLGICLGMQ------------LLFERSEEGG---GVPGlg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 435 -----VIFMPEGSKTHMGAtmrlgsRRTFFQAntcKSAKLYG--NASYVDERHRHRYEVNPEMVPEFEKAGLSFVGRDES 507
Cdd:TIGR01855 99 likgnVVKLEARKVPHMGW------NEVHPVK---ESPLLNGidEGAYFYFVHSYYAVCEEEAVLAYADYGEKFPAAVQK 169
|
170 180 190
....*....|....*....|....*....|
gi 1002271798 508 GTrmeiielpthrfFVGAQFHPEFKSRPGK 537
Cdd:TIGR01855 170 GN------------IFGTQFHPEKSGKTGL 187
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
384-531 |
5.52e-03 |
|
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: 38.33 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271798 384 ILAAKYARENNVPYLGICLGMQ-IAViefarsvmklrganstefdpatttpcvifmpegsktHMGATMrlgsrrtfFQAN 462
Cdd:cd01745 90 LALLRAALERGKPILGICRGMQlLNV------------------------------------ALGGTL--------YQDI 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002271798 463 TCKSaklygnasyvderhRHRYEVNPemVPEfekaGLSFVGRDESGTrMEIIELPTHRFFVGAQFHPEF 531
Cdd:cd01745 126 RVNS--------------LHHQAIKR--LAD----GLRVEARAPDGV-IEAIESPDRPFVLGVQWHPEW 173
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
386-415 |
7.85e-03 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 37.91 E-value: 7.85e-03
10 20 30
....*....|....*....|....*....|
gi 1002271798 386 AAKYARENNVPYLGICLGMQIAVIEFARSV 415
Cdd:PRK00758 59 CPEYLKELDVPILGICLGHQLIAKAFGGEV 88
|
|
| hisH |
PRK13143 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
363-406 |
8.11e-03 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 37.93 E-value: 8.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1002271798 363 LKGAHGVLVPG--GFGD-----RGVQGKILAAkyaRENNVPYLGICLGMQI 406
Cdd:PRK13143 36 ILDADGIVLPGvgAFGAamenlSPLRDVILEA---ARSGKPFLGICLGMQL 83
|
|
| HisH |
COG0118 |
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
361-406 |
9.61e-03 |
|
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: 37.71 E-value: 9.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1002271798 361 DLLKGAHGVLVPG-G-FGD--RGVQGKILAA--KYARENNVPYLGICLGMQI 406
Cdd:COG0118 34 DEIRAADRLVLPGvGaFGDamENLRERGLDEaiREAVAGGKPVLGICLGMQL 85
|
|
| |
