|
Name |
Accession |
Description |
Interval |
E-value |
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
5-528 |
0e+00 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 999.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 5 RPIRRALLSVSDKTGIVEFARALEAQGVEILSTGGTCKLLADNAIKVTEVSDHTGHPEIMDGRVKTLHPKIHGGILARRG 84
Cdd:PRK00881 2 RMIKRALISVSDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVTGFPEILDGRVKTLHPKIHGGILARRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 85 QDEDV--MADNNISAIDIVVVNLYPFANTVAQENCSLEDAIENIDIGGPTMVRAAAKNHKDVTIVVNASDYDRVISEMqN 162
Cdd:PRK00881 82 NPEHVaaLEEHGIEPIDLVVVNLYPFEETVAKPGVTLEEAIENIDIGGPTMVRAAAKNHKDVAVVVDPADYDAVLEEL-K 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 163 NNGSTTYKTRFDLAIAAYEHTAQYDGMIANYFGKMVPdyteeaaidTKFPRTINMQFTKKQDMRYGENSHQDAAFYVEND 242
Cdd:PRK00881 161 ANGSTTLETRFRLAAKAFAHTAAYDAAIANYLTEQVG---------EEFPETLNLSFEKKQDLRYGENPHQKAAFYRDPN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 243 ITeASVATATQLQGKALSFNNIADTDAALECVKEFDVPACVIVKHANPCGVSIGDNILEAYERAFKTDPTSAFGGIIAFN 322
Cdd:PRK00881 232 AE-GGVATAEQLQGKELSYNNIADADAALELVKEFDEPACVIVKHANPCGVAVGDTILEAYDKAYACDPVSAFGGIIAFN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 323 QELDAKTAQAIVErQFVEVIIAPSVSAEAAQIVSAKQNVRLLECGEfsAKGTGHDIKRVNGGVLIQDRDLGMVTQGDLTV 402
Cdd:PRK00881 311 REVDAETAEAIHK-IFLEVIIAPSFSEEALEILAKKKNLRLLECPF--PGGWEGDFKSVSGGLLVQDRDLGMVDPADLKV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 403 VSKRQPSEQELKDLLFCWKVAKFVKSNAIVYARDGMTIGVGAGQMSRVYSAKIAGIKAADESLEVKGSVMASDAFFPFRD 482
Cdd:PRK00881 388 VTKRQPTEQELKDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEKAGDAGLDLKGAVLASDAFFPFRD 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 655452172 483 GIDAAAEAGITAVIQPGGSMRDEEVIAAADEAGMAMVFTGMRHFRH 528
Cdd:PRK00881 468 GVEAAAKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGVRHFRH 513
|
|
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
5-528 |
0e+00 |
|
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR transformylase/IMP cyclohydrolase PurH is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439908 Cd Length: 512 Bit Score: 992.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 5 RPIRRALLSVSDKTGIVEFARALEAQGVEILSTGGTCKLLADNAIKVTEVSDHTGHPEIMDGRVKTLHPKIHGGILARRG 84
Cdd:COG0138 1 VPIKRALISVSDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVTGFPEILDGRVKTLHPKIHGGILARRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 85 QDEDV--MADNNISAIDIVVVNLYPFANTVAQENCSLEDAIENIDIGGPTMVRAAAKNHKDVTIVVNASDYDRVISEMQN 162
Cdd:COG0138 81 NPEHVaqLEEHGIEPIDLVVVNLYPFEETVAKPGATLEEAIENIDIGGPAMLRAAAKNHADVAVVVDPADYDAVLEELKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 163 NnGSTTYKTRFDLAIAAYEHTAQYDGMIANYFGKMVPDyteeaaidTKFPRTINMQFTKKQDMRYGENSHQDAAFYVEND 242
Cdd:COG0138 161 N-GGTSLETRRRLAAKAFAHTAAYDAAIANYLAEQLGE--------EEFPETLTLSFEKVQDLRYGENPHQKAAFYRDPG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 243 iTEASVATATQLQGKALSFNNIADTDAALECVKEFDVPACVIVKHANPCGVSIGDNILEAYERAFKTDPTSAFGGIIAFN 322
Cdd:COG0138 232 -AEGGLATAEQLQGKELSYNNILDADAALELVKEFDEPAVVIVKHANPCGVAVGDTLAEAYEKAYACDPVSAFGGIIAFN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 323 QELDAKTAQAIVErQFVEVIIAPSVSAEAAQIVSAKQNVRLLECGEFSAKGTGHDIKRVNGGVLIQDRDLGMVTQGDLTV 402
Cdd:COG0138 311 RPVDAATAEAIAK-IFLEVIIAPDFSPEALEILAKKKNLRLLELGGLDPPAPGLDVKSVSGGLLVQDRDLGLIDPADLKV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 403 VSKRQPSEQELKDLLFCWKVAKFVKSNAIVYARDGMTIGVGAGQMSRVYSAKIAGIKAADeslEVKGSVMASDAFFPFRD 482
Cdd:COG0138 390 VTKRAPTEEELADLLFAWKVVKHVKSNAIVLAKDGATVGIGAGQMSRVDSARIALEKAGE---RAKGSVLASDAFFPFRD 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 655452172 483 GIDAAAEAGITAVIQPGGSMRDEEVIAAADEAGMAMVFTGMRHFRH 528
Cdd:COG0138 467 GVEAAAKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGMRHFRH 512
|
|
| purH |
TIGR00355 |
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is ... |
8-528 |
0e+00 |
|
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is bifunctional: IMP cyclohydrolase (EC 3.5.4.10); phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) Involved in purine ribonucleotide biosynthesis. The IMP cyclohydrolase activity is in the N-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273032 Cd Length: 511 Bit Score: 820.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 8 RRALLSVSDKTGIVEFARALEAQGVEILSTGGTCKLLADNAIKVTEVSDHTGHPEIMDGRVKTLHPKIHGGILARRGQDE 87
Cdd:TIGR00355 1 RRALLSVSDKTGIVEFAQGLVERGVELLSTGGTAKLLAEAGVPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILARRGDDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 88 D-VMADNNISAIDIVVVNLYPFANTVAQENCSLEDAIENIDIGGPTMVRAAAKNHKDVTIVVNASDYDRVISEMQNNnGS 166
Cdd:TIGR00355 81 DaDLEEHGIEPIDLVVVNLYPFKETVAKPGVTLAEAVENIDIGGPTMLRAAAKNHADVTILVDPKDYSAILSELDEQ-GS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 167 TTYKTRFDLAIAAYEHTAQYDGMIANYFGKMVPDyteeaaidtKFPRTINMQFTKKQDMRYGENSHQDAAFYVENDITEA 246
Cdd:TIGR00355 160 ISLALRFDLAIKAFEHTAAYDAAIANYFGKLVGE---------KEPRQFNLNFTKKQTLRYGENPHQKAAFYVTQNVKEG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 247 SVATATQLQGKALSFNNIADTDAALECVKEFDVPACVIVKHANPCGVSIGDNILEAYERAFKTDPTSAFGGIIAFNQELD 326
Cdd:TIGR00355 231 SVATAEQLQGKELSYNNIADADAALEIVKEFDEPAAVIVKHANPCGVALGKTILDAYDRAFGADPTSAFGGIIALNRELD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 327 AKTAQAIVeRQFVEVIIAPSVSAEAAQIVSAKQNVRLLECGEFSAKGTGHDIKRVNGGVLIQDRDLGMVTQGDLTVVSKR 406
Cdd:TIGR00355 311 VPTAKAIV-RQFLEVIIAPGYSAEALEILAKKKNLRVLILGIWANRVPELDFKRVNGGLLVQDRDDGMVDQSTLKVVTKR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 407 QPSEQELKDLLFCWKVAKFVKSNAIVYARDGMTIGVGAGQMSRVYSAKIAGIKAADESLEVKGSVMASDAFFPFRDGIDA 486
Cdd:TIGR00355 390 QPTEQELIDLLFAWKVAKHVKSNAIVYAKNNMTVGVGAGQMSRVGSAKIAGIKADDEGLEAKGSSLASDAFFPFRDGVEE 469
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 655452172 487 AAEAGITAVIQPGGSMRDEEVIAAADEAGMAMVFTGMRHFRH 528
Cdd:TIGR00355 470 AAAAGITCIIQPGGSMRDEDSIWAADEHGIVMVFTGMRHFRH 511
|
|
| AICARFT_IMPCHas |
smart00798 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
137-460 |
0e+00 |
|
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two steps in de novo purine biosynthesis. The bifunctional enzyme is found in both prokaryotes and eukaryotes. The second last step is catalysed by 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase (AICARFT), this enzyme catalyses the formylation of AICAR with 10-formyl-tetrahydrofolate to yield FAICAR and tetrahydrofolate. The last step is catalysed by IMP (Inosine monophosphate) cyclohydrolase (IMPCHase), cyclizing FAICAR (5-formylaminoimidazole-4-carboxamide ribonucleotide) to IMP.
Pssm-ID: 214822 Cd Length: 311 Bit Score: 539.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 137 AAKNHKDVTIVVNASDYDRVISEMqNNNGSTTYKTRFDLAIAAYEHTAQYDGMIANYFGKMVPDyteeaaidtKFPRTIN 216
Cdd:smart00798 1 AAKNHKDVTVVVDPADYAEVLEEL-KANGGLSLETRKRLAAKAFAHTAAYDAAISNYLAKQLAS---------EFPETLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 217 MQFTKKQDMRYGENSHQDAAFYVENDiTEASVATATQLQGKALSFNNIADTDAALECVKEFDVPACVIVKHANPCGVSIG 296
Cdd:smart00798 71 LSFEKKQDLRYGENPHQKAAFYTDPD-ALGGIATAKQLQGKELSYNNILDADAALELVKEFDEPACVIVKHANPCGVAVG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 297 DNILEAYERAFKTDPTSAFGGIIAFNQELDAKTAQAIVeRQFVEVIIAPSVSAEAAQIVSAKQNVRLLECGEFsAKGTGH 376
Cdd:smart00798 150 DTLAEAYRKAYAADPVSAFGGIIAFNRPVDEETAEAIN-KIFLEVIIAPDFDEEALEILSKKKNLRLLECGPL-PDPDGL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 377 DIKRVNGGVLIQDRDLGMVTQGDLTVVSKRQPSEQELKDLLFCWKVAKFVKSNAIVYARDGMTIGVGAGQMSRVYSAKIA 456
Cdd:smart00798 228 EFKSVSGGLLVQDRDNGGIDPEDLKVVTKRQPTEEELADLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIA 307
|
....
gi 655452172 457 GIKA 460
Cdd:smart00798 308 AEKA 311
|
|
| AICARFT_IMPCHas |
pfam01808 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
137-459 |
0e+00 |
|
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two steps in de novo purine biosynthesis. The bifunctional enzyme is found in both prokaryotes and eukaryotes. The second last step is catalyzed by 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase EC:2.1.2.3 (AICARFT), this enzyme catalyzes the formylation of AICAR with 10-formyl-tetrahydrofolate to yield FAICAR and tetrahydrofolate. This is catalyzed by a pair of C-terminal deaminase fold domains in the protein, where the active site is formed by the dimeric interface of two monomeric units. The last step is catalyzed by the N-terminal IMP (Inosine monophosphate) cyclohydrolase domain EC:3.5.4.10 (IMPCHase), cyclizing FAICAR (5-formylaminoimidazole-4-carboxamide ribonucleotide) to IMP.
Pssm-ID: 460341 Cd Length: 308 Bit Score: 532.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 137 AAKNHKDVTIVVNASDYDRVISEMQNNnGSTTYKTRFDLAIAAYEHTAQYDGMIANYFGKmvpdyteeaaidTKFPRTIN 216
Cdd:pfam01808 1 AAKNHKDVTVVVDPADYAEVLEELKAN-GGTSLETRRRLAAKAFAHTAAYDAAIANYLAG------------KEFPETLT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 217 MQFTKKQDMRYGENSHQDAAFYVENDiTEASVATATQLQGKALSFNNIADTDAALECVKEFDVPACVIVKHANPCGVSIG 296
Cdd:pfam01808 68 LSFEKVQDLRYGENPHQKAAFYRDPG-PAGGLATAEQLQGKELSYNNILDADAALELVKEFDEPAAVIVKHANPCGVAVG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 297 DNILEAYERAFKTDPTSAFGGIIAFNQELDAKTAQAIVErQFVEVIIAPSVSAEAAQIVSAKQNVRLLECGEFSAKGTGH 376
Cdd:pfam01808 147 DTLAEAYRRALAADPVSAFGGIIALNRPVDAATAEEISK-IFLEVIIAPGFTPEALEILKKKKNLRLLEIDPLYPPPPGL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 377 DIKRVNGGVLIQDRDLGMVTQGDLTVVSKRQPSEQELKDLLFCWKVAKFVKSNAIVYARDGMTIGVGAGQMSRVYSAKIA 456
Cdd:pfam01808 226 EFRSVSGGLLVQDRDDALIDPDDLKVVTKRAPTEEELRDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIA 305
|
...
gi 655452172 457 GIK 459
Cdd:pfam01808 306 IEK 308
|
|
| IMPCH |
cd01421 |
Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine ... |
8-194 |
4.11e-106 |
|
Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine biosynthesis pathway protein ATIC (purH). The bifunctional ATIC protein contains a C-terminal ATIC formylase domain that formylates 5-aminoimidazole-4-carboxamide-ribonucleotide. The IMPCH domain then converts the formyl-5-aminoimidazole-4-carboxamide-ribonucleotide to inosine monophosphate. This is the final step in de novo purine production.
Pssm-ID: 238709 [Multi-domain] Cd Length: 187 Bit Score: 314.92 E-value: 4.11e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 8 RRALLSVSDKTGIVEFARALEAQGVEILSTGGTCKLLADNAIKVTEVSDHTGHPEIMDGRVKTLHPKIHGGILARRGQDE 87
Cdd:cd01421 1 KRALISVSDKTGLVEFAKELVELGVEILSTGGTAKFLKEAGIPVTDVSDITGFPEILGGRVKTLHPKIHGGILARRDNEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 88 DV-MADNNISAIDIVVVNLYPFANTVAQENCSLEDAIENIDIGGPTMVRAAAKNHKDVTIVVNASDYDRVISEMqNNNGS 166
Cdd:cd01421 81 HKdLEEHGIEPIDLVVVNLYPFEETVAKGNVTLEEAIENIDIGGPSLLRAAAKNYKDVTVLVDPADYQKVLEEL-KSNGS 159
|
170 180
....*....|....*....|....*...
gi 655452172 167 TTYKTRFDLAIAAYEHTAQYDGMIANYF 194
Cdd:cd01421 160 ISEETRRRLALKAFAHTAEYDAAISNYL 187
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
5-528 |
0e+00 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 999.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 5 RPIRRALLSVSDKTGIVEFARALEAQGVEILSTGGTCKLLADNAIKVTEVSDHTGHPEIMDGRVKTLHPKIHGGILARRG 84
Cdd:PRK00881 2 RMIKRALISVSDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVTGFPEILDGRVKTLHPKIHGGILARRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 85 QDEDV--MADNNISAIDIVVVNLYPFANTVAQENCSLEDAIENIDIGGPTMVRAAAKNHKDVTIVVNASDYDRVISEMqN 162
Cdd:PRK00881 82 NPEHVaaLEEHGIEPIDLVVVNLYPFEETVAKPGVTLEEAIENIDIGGPTMVRAAAKNHKDVAVVVDPADYDAVLEEL-K 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 163 NNGSTTYKTRFDLAIAAYEHTAQYDGMIANYFGKMVPdyteeaaidTKFPRTINMQFTKKQDMRYGENSHQDAAFYVEND 242
Cdd:PRK00881 161 ANGSTTLETRFRLAAKAFAHTAAYDAAIANYLTEQVG---------EEFPETLNLSFEKKQDLRYGENPHQKAAFYRDPN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 243 ITeASVATATQLQGKALSFNNIADTDAALECVKEFDVPACVIVKHANPCGVSIGDNILEAYERAFKTDPTSAFGGIIAFN 322
Cdd:PRK00881 232 AE-GGVATAEQLQGKELSYNNIADADAALELVKEFDEPACVIVKHANPCGVAVGDTILEAYDKAYACDPVSAFGGIIAFN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 323 QELDAKTAQAIVErQFVEVIIAPSVSAEAAQIVSAKQNVRLLECGEfsAKGTGHDIKRVNGGVLIQDRDLGMVTQGDLTV 402
Cdd:PRK00881 311 REVDAETAEAIHK-IFLEVIIAPSFSEEALEILAKKKNLRLLECPF--PGGWEGDFKSVSGGLLVQDRDLGMVDPADLKV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 403 VSKRQPSEQELKDLLFCWKVAKFVKSNAIVYARDGMTIGVGAGQMSRVYSAKIAGIKAADESLEVKGSVMASDAFFPFRD 482
Cdd:PRK00881 388 VTKRQPTEQELKDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEKAGDAGLDLKGAVLASDAFFPFRD 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 655452172 483 GIDAAAEAGITAVIQPGGSMRDEEVIAAADEAGMAMVFTGMRHFRH 528
Cdd:PRK00881 468 GVEAAAKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGVRHFRH 513
|
|
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
5-528 |
0e+00 |
|
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR transformylase/IMP cyclohydrolase PurH is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439908 Cd Length: 512 Bit Score: 992.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 5 RPIRRALLSVSDKTGIVEFARALEAQGVEILSTGGTCKLLADNAIKVTEVSDHTGHPEIMDGRVKTLHPKIHGGILARRG 84
Cdd:COG0138 1 VPIKRALISVSDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVTGFPEILDGRVKTLHPKIHGGILARRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 85 QDEDV--MADNNISAIDIVVVNLYPFANTVAQENCSLEDAIENIDIGGPTMVRAAAKNHKDVTIVVNASDYDRVISEMQN 162
Cdd:COG0138 81 NPEHVaqLEEHGIEPIDLVVVNLYPFEETVAKPGATLEEAIENIDIGGPAMLRAAAKNHADVAVVVDPADYDAVLEELKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 163 NnGSTTYKTRFDLAIAAYEHTAQYDGMIANYFGKMVPDyteeaaidTKFPRTINMQFTKKQDMRYGENSHQDAAFYVEND 242
Cdd:COG0138 161 N-GGTSLETRRRLAAKAFAHTAAYDAAIANYLAEQLGE--------EEFPETLTLSFEKVQDLRYGENPHQKAAFYRDPG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 243 iTEASVATATQLQGKALSFNNIADTDAALECVKEFDVPACVIVKHANPCGVSIGDNILEAYERAFKTDPTSAFGGIIAFN 322
Cdd:COG0138 232 -AEGGLATAEQLQGKELSYNNILDADAALELVKEFDEPAVVIVKHANPCGVAVGDTLAEAYEKAYACDPVSAFGGIIAFN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 323 QELDAKTAQAIVErQFVEVIIAPSVSAEAAQIVSAKQNVRLLECGEFSAKGTGHDIKRVNGGVLIQDRDLGMVTQGDLTV 402
Cdd:COG0138 311 RPVDAATAEAIAK-IFLEVIIAPDFSPEALEILAKKKNLRLLELGGLDPPAPGLDVKSVSGGLLVQDRDLGLIDPADLKV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 403 VSKRQPSEQELKDLLFCWKVAKFVKSNAIVYARDGMTIGVGAGQMSRVYSAKIAGIKAADeslEVKGSVMASDAFFPFRD 482
Cdd:COG0138 390 VTKRAPTEEELADLLFAWKVVKHVKSNAIVLAKDGATVGIGAGQMSRVDSARIALEKAGE---RAKGSVLASDAFFPFRD 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 655452172 483 GIDAAAEAGITAVIQPGGSMRDEEVIAAADEAGMAMVFTGMRHFRH 528
Cdd:COG0138 467 GVEAAAKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGMRHFRH 512
|
|
| purH |
TIGR00355 |
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is ... |
8-528 |
0e+00 |
|
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is bifunctional: IMP cyclohydrolase (EC 3.5.4.10); phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) Involved in purine ribonucleotide biosynthesis. The IMP cyclohydrolase activity is in the N-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273032 Cd Length: 511 Bit Score: 820.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 8 RRALLSVSDKTGIVEFARALEAQGVEILSTGGTCKLLADNAIKVTEVSDHTGHPEIMDGRVKTLHPKIHGGILARRGQDE 87
Cdd:TIGR00355 1 RRALLSVSDKTGIVEFAQGLVERGVELLSTGGTAKLLAEAGVPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILARRGDDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 88 D-VMADNNISAIDIVVVNLYPFANTVAQENCSLEDAIENIDIGGPTMVRAAAKNHKDVTIVVNASDYDRVISEMQNNnGS 166
Cdd:TIGR00355 81 DaDLEEHGIEPIDLVVVNLYPFKETVAKPGVTLAEAVENIDIGGPTMLRAAAKNHADVTILVDPKDYSAILSELDEQ-GS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 167 TTYKTRFDLAIAAYEHTAQYDGMIANYFGKMVPDyteeaaidtKFPRTINMQFTKKQDMRYGENSHQDAAFYVENDITEA 246
Cdd:TIGR00355 160 ISLALRFDLAIKAFEHTAAYDAAIANYFGKLVGE---------KEPRQFNLNFTKKQTLRYGENPHQKAAFYVTQNVKEG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 247 SVATATQLQGKALSFNNIADTDAALECVKEFDVPACVIVKHANPCGVSIGDNILEAYERAFKTDPTSAFGGIIAFNQELD 326
Cdd:TIGR00355 231 SVATAEQLQGKELSYNNIADADAALEIVKEFDEPAAVIVKHANPCGVALGKTILDAYDRAFGADPTSAFGGIIALNRELD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 327 AKTAQAIVeRQFVEVIIAPSVSAEAAQIVSAKQNVRLLECGEFSAKGTGHDIKRVNGGVLIQDRDLGMVTQGDLTVVSKR 406
Cdd:TIGR00355 311 VPTAKAIV-RQFLEVIIAPGYSAEALEILAKKKNLRVLILGIWANRVPELDFKRVNGGLLVQDRDDGMVDQSTLKVVTKR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 407 QPSEQELKDLLFCWKVAKFVKSNAIVYARDGMTIGVGAGQMSRVYSAKIAGIKAADESLEVKGSVMASDAFFPFRDGIDA 486
Cdd:TIGR00355 390 QPTEQELIDLLFAWKVAKHVKSNAIVYAKNNMTVGVGAGQMSRVGSAKIAGIKADDEGLEAKGSSLASDAFFPFRDGVEE 469
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 655452172 487 AAEAGITAVIQPGGSMRDEEVIAAADEAGMAMVFTGMRHFRH 528
Cdd:TIGR00355 470 AAAAGITCIIQPGGSMRDEDSIWAADEHGIVMVFTGMRHFRH 511
|
|
| PLN02891 |
PLN02891 |
IMP cyclohydrolase |
8-528 |
0e+00 |
|
IMP cyclohydrolase
Pssm-ID: 178479 [Multi-domain] Cd Length: 547 Bit Score: 540.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 8 RRALLSVSDKTGIVEFARALEAQGVEILSTGGTCKLLADNAIKVTEVSDHTGHPEIMDGRVKTLHPKIHGGILARRGQDE 87
Cdd:PLN02891 23 KQALISLSDKTDLALLANGLQELGYTIVSTGGTASALEAAGVSVTKVEELTNFPEMLDGRVKTLHPAVHGGILARRDQEH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 88 --DVMADNNISAIDIVVVNLYPFANTVAQENCSLEDAIENIDIGGPTMVRAAAKNHKDVTIVVNASDYDRVISEMQNNNg 165
Cdd:PLN02891 103 hmEALNEHGIGTIDVVVVNLYPFYDTVTSGGISFEDGVENIDIGGPAMIRAAAKNHKDVLVVVDPADYPALLEYLKGKQ- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 166 STTYKTRFDLAIAAYEHTAQYDGMIANYFGKmvpdyteEAAIDTKFPRTINMQFTKKQDMRYGENSHQDAAFYVENDITE 245
Cdd:PLN02891 182 DDQQDFRRKLAWKAFQHVASYDSAVSEWLWK-------QINGGGKFPPSLTVPLTLKSSLRYGENPHQKAAFYVDKSLSE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 246 AS---VATATQLQGKALSFNNIADTDAALECVKEFDVPACVIVKHANPCGVSIGDNILEAYERAFKTDPTSAFGGIIAFN 322
Cdd:PLN02891 255 VNaggIATAIQHHGKEMSYNNYLDADAAWNCVSEFSNPTCVVVKHTNPCGVASRGDILEAYRLAVRADPVSAFGGIVAFN 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 323 QELDAKTAQAIVE---------RQFVEVIIAPSVSAEAAQIVSAK-QNVRLLEcGEFSAKGTgHDIKRVNGGVLIQDRDl 392
Cdd:PLN02891 335 CEVDEDLAREIREfrsptdgetRMFYEIVVAPKYTEKGLEVLKGKsKTLRILE-AKPRKKGR-LSLRQVGGGWLAQDSD- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 393 gMVTQGDLT--VVSKRQPSEQELKDLLFCWKVAKFVKSNAIVYARDGMTIGVGAGQMSRVYSAKIAGIKAADeslEVKGS 470
Cdd:PLN02891 412 -DLTPEDITftVVSEKVPTESELEDAKFAWLCVKHVKSNAIVVAKNNRMLGMGSGQPNRVESLRIALEKAGE---EAKGA 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 471 VMASDAFFPF--RDGIDAAAEAGITAVIQPGGSMRDEEVIAAADEAGMAMVFTGMRHFRH 528
Cdd:PLN02891 488 ALASDAFFPFawNDAVEEACQAGVKVIAEPGGSMRDQDAIDCCNKYGVALLFTGVRHFRH 547
|
|
| AICARFT_IMPCHas |
smart00798 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
137-460 |
0e+00 |
|
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two steps in de novo purine biosynthesis. The bifunctional enzyme is found in both prokaryotes and eukaryotes. The second last step is catalysed by 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase (AICARFT), this enzyme catalyses the formylation of AICAR with 10-formyl-tetrahydrofolate to yield FAICAR and tetrahydrofolate. The last step is catalysed by IMP (Inosine monophosphate) cyclohydrolase (IMPCHase), cyclizing FAICAR (5-formylaminoimidazole-4-carboxamide ribonucleotide) to IMP.
Pssm-ID: 214822 Cd Length: 311 Bit Score: 539.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 137 AAKNHKDVTIVVNASDYDRVISEMqNNNGSTTYKTRFDLAIAAYEHTAQYDGMIANYFGKMVPDyteeaaidtKFPRTIN 216
Cdd:smart00798 1 AAKNHKDVTVVVDPADYAEVLEEL-KANGGLSLETRKRLAAKAFAHTAAYDAAISNYLAKQLAS---------EFPETLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 217 MQFTKKQDMRYGENSHQDAAFYVENDiTEASVATATQLQGKALSFNNIADTDAALECVKEFDVPACVIVKHANPCGVSIG 296
Cdd:smart00798 71 LSFEKKQDLRYGENPHQKAAFYTDPD-ALGGIATAKQLQGKELSYNNILDADAALELVKEFDEPACVIVKHANPCGVAVG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 297 DNILEAYERAFKTDPTSAFGGIIAFNQELDAKTAQAIVeRQFVEVIIAPSVSAEAAQIVSAKQNVRLLECGEFsAKGTGH 376
Cdd:smart00798 150 DTLAEAYRKAYAADPVSAFGGIIAFNRPVDEETAEAIN-KIFLEVIIAPDFDEEALEILSKKKNLRLLECGPL-PDPDGL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 377 DIKRVNGGVLIQDRDLGMVTQGDLTVVSKRQPSEQELKDLLFCWKVAKFVKSNAIVYARDGMTIGVGAGQMSRVYSAKIA 456
Cdd:smart00798 228 EFKSVSGGLLVQDRDNGGIDPEDLKVVTKRQPTEEELADLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIA 307
|
....
gi 655452172 457 GIKA 460
Cdd:smart00798 308 AEKA 311
|
|
| AICARFT_IMPCHas |
pfam01808 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
137-459 |
0e+00 |
|
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two steps in de novo purine biosynthesis. The bifunctional enzyme is found in both prokaryotes and eukaryotes. The second last step is catalyzed by 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase EC:2.1.2.3 (AICARFT), this enzyme catalyzes the formylation of AICAR with 10-formyl-tetrahydrofolate to yield FAICAR and tetrahydrofolate. This is catalyzed by a pair of C-terminal deaminase fold domains in the protein, where the active site is formed by the dimeric interface of two monomeric units. The last step is catalyzed by the N-terminal IMP (Inosine monophosphate) cyclohydrolase domain EC:3.5.4.10 (IMPCHase), cyclizing FAICAR (5-formylaminoimidazole-4-carboxamide ribonucleotide) to IMP.
Pssm-ID: 460341 Cd Length: 308 Bit Score: 532.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 137 AAKNHKDVTIVVNASDYDRVISEMQNNnGSTTYKTRFDLAIAAYEHTAQYDGMIANYFGKmvpdyteeaaidTKFPRTIN 216
Cdd:pfam01808 1 AAKNHKDVTVVVDPADYAEVLEELKAN-GGTSLETRRRLAAKAFAHTAAYDAAIANYLAG------------KEFPETLT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 217 MQFTKKQDMRYGENSHQDAAFYVENDiTEASVATATQLQGKALSFNNIADTDAALECVKEFDVPACVIVKHANPCGVSIG 296
Cdd:pfam01808 68 LSFEKVQDLRYGENPHQKAAFYRDPG-PAGGLATAEQLQGKELSYNNILDADAALELVKEFDEPAAVIVKHANPCGVAVG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 297 DNILEAYERAFKTDPTSAFGGIIAFNQELDAKTAQAIVErQFVEVIIAPSVSAEAAQIVSAKQNVRLLECGEFSAKGTGH 376
Cdd:pfam01808 147 DTLAEAYRRALAADPVSAFGGIIALNRPVDAATAEEISK-IFLEVIIAPGFTPEALEILKKKKNLRLLEIDPLYPPPPGL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 377 DIKRVNGGVLIQDRDLGMVTQGDLTVVSKRQPSEQELKDLLFCWKVAKFVKSNAIVYARDGMTIGVGAGQMSRVYSAKIA 456
Cdd:pfam01808 226 EFRSVSGGLLVQDRDDALIDPDDLKVVTKRAPTEEELRDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIA 305
|
...
gi 655452172 457 GIK 459
Cdd:pfam01808 306 IEK 308
|
|
| IMPCH |
cd01421 |
Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine ... |
8-194 |
4.11e-106 |
|
Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine biosynthesis pathway protein ATIC (purH). The bifunctional ATIC protein contains a C-terminal ATIC formylase domain that formylates 5-aminoimidazole-4-carboxamide-ribonucleotide. The IMPCH domain then converts the formyl-5-aminoimidazole-4-carboxamide-ribonucleotide to inosine monophosphate. This is the final step in de novo purine production.
Pssm-ID: 238709 [Multi-domain] Cd Length: 187 Bit Score: 314.92 E-value: 4.11e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 8 RRALLSVSDKTGIVEFARALEAQGVEILSTGGTCKLLADNAIKVTEVSDHTGHPEIMDGRVKTLHPKIHGGILARRGQDE 87
Cdd:cd01421 1 KRALISVSDKTGLVEFAKELVELGVEILSTGGTAKFLKEAGIPVTDVSDITGFPEILGGRVKTLHPKIHGGILARRDNEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 88 DV-MADNNISAIDIVVVNLYPFANTVAQENCSLEDAIENIDIGGPTMVRAAAKNHKDVTIVVNASDYDRVISEMqNNNGS 166
Cdd:cd01421 81 HKdLEEHGIEPIDLVVVNLYPFEETVAKGNVTLEEAIENIDIGGPSLLRAAAKNYKDVTVLVDPADYQKVLEEL-KSNGS 159
|
170 180
....*....|....*....|....*...
gi 655452172 167 TTYKTRFDLAIAAYEHTAQYDGMIANYF 194
Cdd:cd01421 160 ISEETRRRLALKAFAHTAEYDAAISNYL 187
|
|
| PRK07106 |
PRK07106 |
phosphoribosylaminoimidazolecarboxamide formyltransferase; |
225-528 |
7.17e-49 |
|
phosphoribosylaminoimidazolecarboxamide formyltransferase;
Pssm-ID: 180841 Cd Length: 390 Bit Score: 173.31 E-value: 7.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 225 MRYGENSHQDAA-FYVENDITEASVatatqLQGKAlSFNNIADTDAALECVKE----FDVPACVIVKHANPCGVSIG--- 296
Cdd:PRK07106 6 LKYGCNPNQKPArIFMKEGELPIEV-----LNGRP-GYINFLDALNSWQLVKElkeaTGLPAAASFKHVSPAGAAVGlpl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 297 DNILE---------------AYERAFKTDPTSAFGGIIAFNQELDAKTAQaIVERQFVEVIIAPSVSAEAAQIVSAKQNV 361
Cdd:PRK07106 80 SDTLKkiyfvddmelsplacAYARARGADRMSSYGDFAALSDVCDVETAK-LLKREVSDGIIAPGYTPEALEILKAKKKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 362 RLL--------ECGEFsakgtghDIKRVNGGVLIQDRDLGMVTQGDLT--VVSKRQPSEQELKDLLFCWKVAKFVKSNAI 431
Cdd:PRK07106 159 NYNiikidpnyEPAPI-------ETKDVFGITFEQGRNELKIDEDLLKniVTENKELPDEAKRDLIIALITLKYTQSNSV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 432 VYARDGMTIGVGAGQMSRVYSAKIAGIKA---------------------------------ADESLEV----------- 467
Cdd:PRK07106 232 CYAKDGQAIGIGAGQQSRIHCTRLAGNKAdiwylrqhpkvlnlpfkegirrpdrdnaidvylSDDYMDVladgvwqqfft 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655452172 468 ------------------KGSVMASDAFFPFRDGIDAAAEAGITAVIQPGGSMRDEEVIAAADEAGMAMVFTGMRHFRH 528
Cdd:PRK07106 312 ekpepltreekrawlatlTGVALGSDAFFPFGDNIERAAKSGVKYIAQPGGSIRDDNVIETCNKYGMTMAFTGVRLFHH 390
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
19-132 |
1.05e-26 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 214855 [Multi-domain] Cd Length: 91 Bit Score: 103.32 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 19 GIVEFARALEAQGVEILSTGGTCKLLADNAIKVtevsdhtghpeimdgrVKTLHPKIHGGILArrgqdedVMADNNISAI 98
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPV----------------VKTLHPKVHGGIPQ-------ILDLIKNGEI 57
|
90 100 110
....*....|....*....|....*....|....
gi 655452172 99 DIVVVNLYPFANTVAQENCSLEDAIENIDIGGPT 132
Cdd:smart00851 58 DLVINTLYPFEAQAHEDGYSIRRAAENIDIPGPT 91
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
19-132 |
1.04e-25 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 460462 [Multi-domain] Cd Length: 93 Bit Score: 100.64 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 19 GIVEFARALEAQGVEILSTGGTCKLLADNAIKVTEVSDHTGHPeIMDGRVktlhpkihggilarrgQDEDVMADNNisaI 98
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGEG-RPGGRV----------------QIGDLIKNGE---I 60
|
90 100 110
....*....|....*....|....*....|....
gi 655452172 99 DIVVVNLYPFANTVAqENCSLEDAIENIDIGGPT 132
Cdd:pfam02142 61 DLVINTLYPFKATVH-DGYAIRRAAENIDIPGPT 93
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
9-156 |
1.61e-09 |
|
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to produce methylglyoxal. The family also includes the C-terminal domain in carbamoyl phosphate synthetase (CPS) where it catalyzes the last phosphorylation of a coaboxyphosphate intermediate to form the product carbamoyl phosphate and may also play a regulatory role. This family also includes inosine monophosphate cyclohydrolase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 238297 [Multi-domain] Cd Length: 112 Bit Score: 55.60 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 9 RALLSVSD--KTGIVEFARALEAQGVEILSTGGTCKLLADNAIKVTEVSDHTGhpeimdgrvkTLHPKIHGGILARrgqd 86
Cdd:cd00532 1 GVFLSVSDhvKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHE----------DGEPTVDAAIAEK---- 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 87 edvmadnniSAIDIVVVNLYPFANtvaqencsledaiENIDIGGPTMVRAAAKNHkdVTIVVNASDYDRV 156
Cdd:cd00532 67 ---------GKFDVVINLRDPRRD-------------RCTDEDGTALLRLARLYK--IPVTTPNATAMFV 112
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
9-66 |
1.74e-08 |
|
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate synthetase (CSP). CSP, a CarA and CarB heterodimer, catalyzes the production of carbamoyl phosphate which is subsequently employed in the metabolic pathways responsible for the synthesis of pyrimidine nucleotides or arginine. The MGS-like domain is the C-terminal domain of CarB and appears to play a regulatory role in CPS function by binding allosteric effector molecules, including UMP and ornithine.
Pssm-ID: 238712 [Multi-domain] Cd Length: 110 Bit Score: 52.48 E-value: 1.74e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655452172 9 RALLSV--SDKTGIVEFARALEAQGVEILSTGGTCKLLADNAIKVTEVS-DHTGHPEIMDG 66
Cdd:cd01424 2 TVFISVadRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNkVSEGRPNIVDL 62
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
9-65 |
1.84e-07 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 53.95 E-value: 1.84e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 655452172 9 RALLSV--SDKTGIVEFARALEAQGVEILSTGGTCKLLADNAIKVTEVSD-HTGHPEIMD 65
Cdd:PRK05294 939 TVFLSVrdRDKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELVNKvHEGRPHIVD 998
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
9-65 |
9.10e-04 |
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carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 42.29 E-value: 9.10e-04
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gi 655452172 9 RALLSV--SDKTGIVEFARALEAQGVEILSTGGTCKLLADNAIKVTEVSDHT-GHPEIMD 65
Cdd:TIGR01369 939 SVLLSVrdKDKEELLDLARKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSeGRPNILD 998
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