|
Name |
Accession |
Description |
Interval |
E-value |
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
7-535 |
0e+00 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 948.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 7 RLPIRRALISVSDKTGVVDFARELVALGVEILSTGGTYKLLRDNGISAVEVADYTGFPEMMDGRVKTLHPKVHGGILGRR 86
Cdd:PRK00881 1 RRMIKRALISVSDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVTGFPEILDGRVKTLHPKIHGGILARR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 87 DLDG--AVMEQHGIKPIDLVAVNLYPFEATVARPDCDLPTAIENIDIGGPTMVRSAAKNHKDVAIVVNAGDYAAVIESLK 164
Cdd:PRK00881 81 DNPEhvAALEEHGIEPIDLVVVNLYPFEETVAKPGVTLEEAIENIDIGGPTMVRAAAKNHKDVAVVVDPADYDAVLEELK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 165 AGG-LTYAQRFDLALKAFEHTSAYDGMIANYLGTIDQTrdtlgtadrgAFPRTFNSQFVKAQEMRYGENPHQSAAFYVEA 243
Cdd:PRK00881 161 ANGsTTLETRFRLAAKAFAHTAAYDAAIANYLTEQVGE----------EFPETLNLSFEKKQDLRYGENPHQKAAFYRDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 244 KkGEASVSTAIQLQGKELSFNNVADTDAALECVKSFLKPACVIVKHANPCGVAVVPEdeggIRKAYDLAYATDSESAFGG 323
Cdd:PRK00881 231 N-AEGGVATAEQLQGKELSYNNIADADAALELVKEFDEPACVIVKHANPCGVAVGDT----ILEAYDKAYACDPVSAFGG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 324 IIAFNRELDGETAKAIVErQFVEVIIAPKISAAAREVVAAKANVRLLECGEWPAeraPGWDFKRVNGGLLVQSRDIGMIK 403
Cdd:PRK00881 306 IIAFNREVDAETAEAIHK-IFLEVIIAPSFSEEALEILAKKKNLRLLECPFPGG---WEGDFKSVSGGLLVQDRDLGMVD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 404 AEDLKIVTRRAPTEQEIHDLIFAWKVAKFVKSNAIVYARNRQTVGVGAGQMSRVNSARIAAIKAEHAGLEVKGAVMASDA 483
Cdd:PRK00881 382 PADLKVVTKRQPTEQELKDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEKAGDAGLDLKGAVLASDA 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 15600047 484 FFPFRDGIDNAAKAGITAVIQPGGSMRDNEVIAAADEADIAMVFTGMRHFRH 535
Cdd:PRK00881 462 FFPFRDGVEAAAKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGVRHFRH 513
|
|
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
9-535 |
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: 938.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 9 PIRRALISVSDKTGVVDFARELVALGVEILSTGGTYKLLRDNGISAVEVADYTGFPEMMDGRVKTLHPKVHGGILGRRDL 88
Cdd:COG0138 2 PIKRALISVSDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVTGFPEILDGRVKTLHPKIHGGILARRDN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 89 DGAV--MEQHGIKPIDLVAVNLYPFEATVARPDCDLPTAIENIDIGGPTMVRSAAKNHKDVAIVVNAGDYAAVIESLKA- 165
Cdd:COG0138 82 PEHVaqLEEHGIEPIDLVVVNLYPFEETVAKPGATLEEAIENIDIGGPAMLRAAAKNHADVAVVVDPADYDAVLEELKAn 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 166 GGLTYAQRFDLALKAFEHTSAYDGMIANYLGtidqtrdtlGTADRGAFPRTFNSQFVKAQEMRYGENPHQSAAFYVEAKK 245
Cdd:COG0138 162 GGTSLETRRRLAAKAFAHTAAYDAAIANYLA---------EQLGEEEFPETLTLSFEKVQDLRYGENPHQKAAFYRDPGA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 246 gEASVSTAIQLQGKELSFNNVADTDAALECVKSFLKPACVIVKHANPCGVAVVPEdeggIRKAYDLAYATDSESAFGGII 325
Cdd:COG0138 233 -EGGLATAEQLQGKELSYNNILDADAALELVKEFDEPAVVIVKHANPCGVAVGDT----LAEAYEKAYACDPVSAFGGII 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 326 AFNRELDGETAKAIVErQFVEVIIAPKISAAAREVVAAKANVRLLECGEWPAeRAPGWDFKRVNGGLLVQSRDIGMIKAE 405
Cdd:COG0138 308 AFNRPVDAATAEAIAK-IFLEVIIAPDFSPEALEILAKKKNLRLLELGGLDP-PAPGLDVKSVSGGLLVQDRDLGLIDPA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 406 DLKIVTRRAPTEQEIHDLIFAWKVAKFVKSNAIVYARNRQTVGVGAGQMSRVNSARIAAIKAEHaglEVKGAVMASDAFF 485
Cdd:COG0138 386 DLKVVTKRAPTEEELADLLFAWKVVKHVKSNAIVLAKDGATVGIGAGQMSRVDSARIALEKAGE---RAKGSVLASDAFF 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15600047 486 PFRDGIDNAAKAGITAVIQPGGSMRDNEVIAAADEADIAMVFTGMRHFRH 535
Cdd:COG0138 463 PFRDGVEAAAKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGMRHFRH 512
|
|
| purH |
TIGR00355 |
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is ... |
11-535 |
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: 760.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 11 RRALISVSDKTGVVDFARELVALGVEILSTGGTYKLLRDNGISAVEVADYTGFPEMMDGRVKTLHPKVHGGILGRRDLDG 90
Cdd:TIGR00355 1 RRALLSVSDKTGIVEFAQGLVERGVELLSTGGTAKLLAEAGVPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILARRGDDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 91 -AVMEQHGIKPIDLVAVNLYPFEATVARPDCDLPTAIENIDIGGPTMVRSAAKNHKDVAIVVNAGDYAAVIESLKA-GGL 168
Cdd:TIGR00355 81 dADLEEHGIEPIDLVVVNLYPFKETVAKPGVTLAEAVENIDIGGPTMLRAAAKNHADVTILVDPKDYSAILSELDEqGSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 169 TYAQRFDLALKAFEHTSAYDGMIANYLGTIDQTRDtlgtadrgafPRTFNSQFVKAQEMRYGENPHQSAAFYVEAKKGEA 248
Cdd:TIGR00355 161 SLALRFDLAIKAFEHTAAYDAAIANYFGKLVGEKE----------PRQFNLNFTKKQTLRYGENPHQKAAFYVTQNVKEG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 249 SVSTAIQLQGKELSFNNVADTDAALECVKSFLKPACVIVKHANPCGVAVVPEdeggIRKAYDLAYATDSESAFGGIIAFN 328
Cdd:TIGR00355 231 SVATAEQLQGKELSYNNIADADAALEIVKEFDEPAAVIVKHANPCGVALGKT----ILDAYDRAFGADPTSAFGGIIALN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 329 RELDGETAKAIVeRQFVEVIIAPKISAAAREVVAAKANVRLLECGEWPaERAPGWDFKRVNGGLLVQSRDIGMIKAEDLK 408
Cdd:TIGR00355 307 RELDVPTAKAIV-RQFLEVIIAPGYSAEALEILAKKKNLRVLILGIWA-NRVPELDFKRVNGGLLVQDRDDGMVDQSTLK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 409 IVTRRAPTEQEIHDLIFAWKVAKFVKSNAIVYARNRQTVGVGAGQMSRVNSARIAAIKAEHAGLEVKGAVMASDAFFPFR 488
Cdd:TIGR00355 385 VVTKRQPTEQELIDLLFAWKVAKHVKSNAIVYAKNNMTVGVGAGQMSRVGSAKIAGIKADDEGLEAKGSSLASDAFFPFR 464
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15600047 489 DGIDNAAKAGITAVIQPGGSMRDNEVIAAADEADIAMVFTGMRHFRH 535
Cdd:TIGR00355 465 DGVEEAAAAGITCIIQPGGSMRDEDSIWAADEHGIVMVFTGMRHFRH 511
|
|
| AICARFT_IMPCHas |
smart00798 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
140-467 |
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: 519.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 140 AAKNHKDVAIVVNAGDYAAVIESLKA-GGLTYAQRFDLALKAFEHTSAYDGMIANYLGTIDQTrdtlgtadrgAFPRTFN 218
Cdd:smart00798 1 AAKNHKDVTVVVDPADYAEVLEELKAnGGLSLETRKRLAAKAFAHTAAYDAAISNYLAKQLAS----------EFPETLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 219 SQFVKAQEMRYGENPHQSAAFYVEAKKGEaSVSTAIQLQGKELSFNNVADTDAALECVKSFLKPACVIVKHANPCGVAVV 298
Cdd:smart00798 71 LSFEKKQDLRYGENPHQKAAFYTDPDALG-GIATAKQLQGKELSYNNILDADAALELVKEFDEPACVIVKHANPCGVAVG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 299 PEdeggIRKAYDLAYATDSESAFGGIIAFNRELDGETAKAIVeRQFVEVIIAPKISAAAREVVAAKANVRLLECGEWPae 378
Cdd:smart00798 150 DT----LAEAYRKAYAADPVSAFGGIIAFNRPVDEETAEAIN-KIFLEVIIAPDFDEEALEILSKKKNLRLLECGPLP-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 379 RAPGWDFKRVNGGLLVQSRDIGMIKAEDLKIVTRRAPTEQEIHDLIFAWKVAKFVKSNAIVYARNRQTVGVGAGQMSRVN 458
Cdd:smart00798 223 DPDGLEFKSVSGGLLVQDRDNGGIDPEDLKVVTKRQPTEEELADLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVD 302
|
....*....
gi 15600047 459 SARIAAIKA 467
Cdd:smart00798 303 SARIAAEKA 311
|
|
| AICARFT_IMPCHas |
pfam01808 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
140-466 |
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: 511.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 140 AAKNHKDVAIVVNAGDYAAVIESLKA-GGLTYAQRFDLALKAFEHTSAYDGMIANYLGtidqtrdtlgtadRGAFPRTFN 218
Cdd:pfam01808 1 AAKNHKDVTVVVDPADYAEVLEELKAnGGTSLETRRRLAAKAFAHTAAYDAAIANYLA-------------GKEFPETLT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 219 SQFVKAQEMRYGENPHQSAAFYVEAKkGEASVSTAIQLQGKELSFNNVADTDAALECVKSFLKPACVIVKHANPCGVAVV 298
Cdd:pfam01808 68 LSFEKVQDLRYGENPHQKAAFYRDPG-PAGGLATAEQLQGKELSYNNILDADAALELVKEFDEPAAVIVKHANPCGVAVG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 299 PEdeggIRKAYDLAYATDSESAFGGIIAFNRELDGETAKAIVErQFVEVIIAPKISAAAREVVAAKANVRLLECGEWPAE 378
Cdd:pfam01808 147 DT----LAEAYRRALAADPVSAFGGIIALNRPVDAATAEEISK-IFLEVIIAPGFTPEALEILKKKKNLRLLEIDPLYPP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 379 RaPGWDFKRVNGGLLVQSRDIGMIKAEDLKIVTRRAPTEQEIHDLIFAWKVAKFVKSNAIVYARNRQTVGVGAGQMSRVN 458
Cdd:pfam01808 222 P-PGLEFRSVSGGLLVQDRDDALIDPDDLKVVTKRAPTEEELRDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVD 300
|
....*...
gi 15600047 459 SARIAAIK 466
Cdd:pfam01808 301 SARIAIEK 308
|
|
| IMPCH |
cd01421 |
Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine ... |
11-195 |
1.70e-109 |
|
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: 323.78 E-value: 1.70e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 11 RRALISVSDKTGVVDFARELVALGVEILSTGGTYKLLRDNGISAVEVADYTGFPEMMDGRVKTLHPKVHGGILGRRDLDG 90
Cdd:cd01421 1 KRALISVSDKTGLVEFAKELVELGVEILSTGGTAKFLKEAGIPVTDVSDITGFPEILGGRVKTLHPKIHGGILARRDNEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 91 -AVMEQHGIKPIDLVAVNLYPFEATVARPDCDLPTAIENIDIGGPTMVRSAAKNHKDVAIVVNAGDYAAVIESLKAGG-L 168
Cdd:cd01421 81 hKDLEEHGIEPIDLVVVNLYPFEETVAKGNVTLEEAIENIDIGGPSLLRAAAKNYKDVTVLVDPADYQKVLEELKSNGsI 160
|
170 180
....*....|....*....|....*..
gi 15600047 169 TYAQRFDLALKAFEHTSAYDGMIANYL 195
Cdd:cd01421 161 SEETRRRLALKAFAHTAEYDAAISNYL 187
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
7-535 |
0e+00 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 948.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 7 RLPIRRALISVSDKTGVVDFARELVALGVEILSTGGTYKLLRDNGISAVEVADYTGFPEMMDGRVKTLHPKVHGGILGRR 86
Cdd:PRK00881 1 RRMIKRALISVSDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVTGFPEILDGRVKTLHPKIHGGILARR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 87 DLDG--AVMEQHGIKPIDLVAVNLYPFEATVARPDCDLPTAIENIDIGGPTMVRSAAKNHKDVAIVVNAGDYAAVIESLK 164
Cdd:PRK00881 81 DNPEhvAALEEHGIEPIDLVVVNLYPFEETVAKPGVTLEEAIENIDIGGPTMVRAAAKNHKDVAVVVDPADYDAVLEELK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 165 AGG-LTYAQRFDLALKAFEHTSAYDGMIANYLGTIDQTrdtlgtadrgAFPRTFNSQFVKAQEMRYGENPHQSAAFYVEA 243
Cdd:PRK00881 161 ANGsTTLETRFRLAAKAFAHTAAYDAAIANYLTEQVGE----------EFPETLNLSFEKKQDLRYGENPHQKAAFYRDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 244 KkGEASVSTAIQLQGKELSFNNVADTDAALECVKSFLKPACVIVKHANPCGVAVVPEdeggIRKAYDLAYATDSESAFGG 323
Cdd:PRK00881 231 N-AEGGVATAEQLQGKELSYNNIADADAALELVKEFDEPACVIVKHANPCGVAVGDT----ILEAYDKAYACDPVSAFGG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 324 IIAFNRELDGETAKAIVErQFVEVIIAPKISAAAREVVAAKANVRLLECGEWPAeraPGWDFKRVNGGLLVQSRDIGMIK 403
Cdd:PRK00881 306 IIAFNREVDAETAEAIHK-IFLEVIIAPSFSEEALEILAKKKNLRLLECPFPGG---WEGDFKSVSGGLLVQDRDLGMVD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 404 AEDLKIVTRRAPTEQEIHDLIFAWKVAKFVKSNAIVYARNRQTVGVGAGQMSRVNSARIAAIKAEHAGLEVKGAVMASDA 483
Cdd:PRK00881 382 PADLKVVTKRQPTEQELKDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEKAGDAGLDLKGAVLASDA 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 15600047 484 FFPFRDGIDNAAKAGITAVIQPGGSMRDNEVIAAADEADIAMVFTGMRHFRH 535
Cdd:PRK00881 462 FFPFRDGVEAAAKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGVRHFRH 513
|
|
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
9-535 |
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: 938.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 9 PIRRALISVSDKTGVVDFARELVALGVEILSTGGTYKLLRDNGISAVEVADYTGFPEMMDGRVKTLHPKVHGGILGRRDL 88
Cdd:COG0138 2 PIKRALISVSDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVTGFPEILDGRVKTLHPKIHGGILARRDN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 89 DGAV--MEQHGIKPIDLVAVNLYPFEATVARPDCDLPTAIENIDIGGPTMVRSAAKNHKDVAIVVNAGDYAAVIESLKA- 165
Cdd:COG0138 82 PEHVaqLEEHGIEPIDLVVVNLYPFEETVAKPGATLEEAIENIDIGGPAMLRAAAKNHADVAVVVDPADYDAVLEELKAn 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 166 GGLTYAQRFDLALKAFEHTSAYDGMIANYLGtidqtrdtlGTADRGAFPRTFNSQFVKAQEMRYGENPHQSAAFYVEAKK 245
Cdd:COG0138 162 GGTSLETRRRLAAKAFAHTAAYDAAIANYLA---------EQLGEEEFPETLTLSFEKVQDLRYGENPHQKAAFYRDPGA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 246 gEASVSTAIQLQGKELSFNNVADTDAALECVKSFLKPACVIVKHANPCGVAVVPEdeggIRKAYDLAYATDSESAFGGII 325
Cdd:COG0138 233 -EGGLATAEQLQGKELSYNNILDADAALELVKEFDEPAVVIVKHANPCGVAVGDT----LAEAYEKAYACDPVSAFGGII 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 326 AFNRELDGETAKAIVErQFVEVIIAPKISAAAREVVAAKANVRLLECGEWPAeRAPGWDFKRVNGGLLVQSRDIGMIKAE 405
Cdd:COG0138 308 AFNRPVDAATAEAIAK-IFLEVIIAPDFSPEALEILAKKKNLRLLELGGLDP-PAPGLDVKSVSGGLLVQDRDLGLIDPA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 406 DLKIVTRRAPTEQEIHDLIFAWKVAKFVKSNAIVYARNRQTVGVGAGQMSRVNSARIAAIKAEHaglEVKGAVMASDAFF 485
Cdd:COG0138 386 DLKVVTKRAPTEEELADLLFAWKVVKHVKSNAIVLAKDGATVGIGAGQMSRVDSARIALEKAGE---RAKGSVLASDAFF 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15600047 486 PFRDGIDNAAKAGITAVIQPGGSMRDNEVIAAADEADIAMVFTGMRHFRH 535
Cdd:COG0138 463 PFRDGVEAAAKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGMRHFRH 512
|
|
| purH |
TIGR00355 |
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is ... |
11-535 |
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: 760.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 11 RRALISVSDKTGVVDFARELVALGVEILSTGGTYKLLRDNGISAVEVADYTGFPEMMDGRVKTLHPKVHGGILGRRDLDG 90
Cdd:TIGR00355 1 RRALLSVSDKTGIVEFAQGLVERGVELLSTGGTAKLLAEAGVPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILARRGDDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 91 -AVMEQHGIKPIDLVAVNLYPFEATVARPDCDLPTAIENIDIGGPTMVRSAAKNHKDVAIVVNAGDYAAVIESLKA-GGL 168
Cdd:TIGR00355 81 dADLEEHGIEPIDLVVVNLYPFKETVAKPGVTLAEAVENIDIGGPTMLRAAAKNHADVTILVDPKDYSAILSELDEqGSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 169 TYAQRFDLALKAFEHTSAYDGMIANYLGTIDQTRDtlgtadrgafPRTFNSQFVKAQEMRYGENPHQSAAFYVEAKKGEA 248
Cdd:TIGR00355 161 SLALRFDLAIKAFEHTAAYDAAIANYFGKLVGEKE----------PRQFNLNFTKKQTLRYGENPHQKAAFYVTQNVKEG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 249 SVSTAIQLQGKELSFNNVADTDAALECVKSFLKPACVIVKHANPCGVAVVPEdeggIRKAYDLAYATDSESAFGGIIAFN 328
Cdd:TIGR00355 231 SVATAEQLQGKELSYNNIADADAALEIVKEFDEPAAVIVKHANPCGVALGKT----ILDAYDRAFGADPTSAFGGIIALN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 329 RELDGETAKAIVeRQFVEVIIAPKISAAAREVVAAKANVRLLECGEWPaERAPGWDFKRVNGGLLVQSRDIGMIKAEDLK 408
Cdd:TIGR00355 307 RELDVPTAKAIV-RQFLEVIIAPGYSAEALEILAKKKNLRVLILGIWA-NRVPELDFKRVNGGLLVQDRDDGMVDQSTLK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 409 IVTRRAPTEQEIHDLIFAWKVAKFVKSNAIVYARNRQTVGVGAGQMSRVNSARIAAIKAEHAGLEVKGAVMASDAFFPFR 488
Cdd:TIGR00355 385 VVTKRQPTEQELIDLLFAWKVAKHVKSNAIVYAKNNMTVGVGAGQMSRVGSAKIAGIKADDEGLEAKGSSLASDAFFPFR 464
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15600047 489 DGIDNAAKAGITAVIQPGGSMRDNEVIAAADEADIAMVFTGMRHFRH 535
Cdd:TIGR00355 465 DGVEEAAAAGITCIIQPGGSMRDEDSIWAADEHGIVMVFTGMRHFRH 511
|
|
| PLN02891 |
PLN02891 |
IMP cyclohydrolase |
11-535 |
0e+00 |
|
IMP cyclohydrolase
Pssm-ID: 178479 [Multi-domain] Cd Length: 547 Bit Score: 537.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 11 RRALISVSDKTGVVDFARELVALGVEILSTGGTYKLLRDNGISAVEVADYTGFPEMMDGRVKTLHPKVHGGILGRRDLDG 90
Cdd:PLN02891 23 KQALISLSDKTDLALLANGLQELGYTIVSTGGTASALEAAGVSVTKVEELTNFPEMLDGRVKTLHPAVHGGILARRDQEH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 91 AV--MEQHGIKPIDLVAVNLYPFEATVARPDCDLPTAIENIDIGGPTMVRSAAKNHKDVAIVVNAGDYAAVIESLKaGGL 168
Cdd:PLN02891 103 HMeaLNEHGIGTIDVVVVNLYPFYDTVTSGGISFEDGVENIDIGGPAMIRAAAKNHKDVLVVVDPADYPALLEYLK-GKQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 169 TYAQRF--DLALKAFEHTSAYDGMIANYLGTidQTRDTlgtadrGAFPRTFNSQFVKAQEMRYGENPHQSAAFYVEAKKG 246
Cdd:PLN02891 182 DDQQDFrrKLAWKAFQHVASYDSAVSEWLWK--QINGG------GKFPPSLTVPLTLKSSLRYGENPHQKAAFYVDKSLS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 247 EAS---VSTAIQLQGKELSFNNVADTDAALECVKSFLKPACVIVKHANPCGVAvvpeDEGGIRKAYDLAYATDSESAFGG 323
Cdd:PLN02891 254 EVNaggIATAIQHHGKEMSYNNYLDADAAWNCVSEFSNPTCVVVKHTNPCGVA----SRGDILEAYRLAVRADPVSAFGG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 324 IIAFNRELDGETAKAIVE---------RQFVEVIIAPKISAAAREVVAAKA-NVRLLECgewpAERAPG-WDFKRVNGGL 392
Cdd:PLN02891 330 IVAFNCEVDEDLAREIREfrsptdgetRMFYEIVVAPKYTEKGLEVLKGKSkTLRILEA----KPRKKGrLSLRQVGGGW 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 393 LVQSRDigMIKAEDL--KIVTRRAPTEQEIHDLIFAWKVAKFVKSNAIVYARNRQTVGVGAGQMSRVNSARIAaikAEHA 470
Cdd:PLN02891 406 LAQDSD--DLTPEDItfTVVSEKVPTESELEDAKFAWLCVKHVKSNAIVVAKNNRMLGMGSGQPNRVESLRIA---LEKA 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600047 471 GLEVKGAVMASDAFFPF--RDGIDNAAKAGITAVIQPGGSMRDNEVIAAADEADIAMVFTGMRHFRH 535
Cdd:PLN02891 481 GEEAKGAALASDAFFPFawNDAVEEACQAGVKVIAEPGGSMRDQDAIDCCNKYGVALLFTGVRHFRH 547
|
|
| AICARFT_IMPCHas |
smart00798 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
140-467 |
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: 519.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 140 AAKNHKDVAIVVNAGDYAAVIESLKA-GGLTYAQRFDLALKAFEHTSAYDGMIANYLGTIDQTrdtlgtadrgAFPRTFN 218
Cdd:smart00798 1 AAKNHKDVTVVVDPADYAEVLEELKAnGGLSLETRKRLAAKAFAHTAAYDAAISNYLAKQLAS----------EFPETLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 219 SQFVKAQEMRYGENPHQSAAFYVEAKKGEaSVSTAIQLQGKELSFNNVADTDAALECVKSFLKPACVIVKHANPCGVAVV 298
Cdd:smart00798 71 LSFEKKQDLRYGENPHQKAAFYTDPDALG-GIATAKQLQGKELSYNNILDADAALELVKEFDEPACVIVKHANPCGVAVG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 299 PEdeggIRKAYDLAYATDSESAFGGIIAFNRELDGETAKAIVeRQFVEVIIAPKISAAAREVVAAKANVRLLECGEWPae 378
Cdd:smart00798 150 DT----LAEAYRKAYAADPVSAFGGIIAFNRPVDEETAEAIN-KIFLEVIIAPDFDEEALEILSKKKNLRLLECGPLP-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 379 RAPGWDFKRVNGGLLVQSRDIGMIKAEDLKIVTRRAPTEQEIHDLIFAWKVAKFVKSNAIVYARNRQTVGVGAGQMSRVN 458
Cdd:smart00798 223 DPDGLEFKSVSGGLLVQDRDNGGIDPEDLKVVTKRQPTEEELADLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVD 302
|
....*....
gi 15600047 459 SARIAAIKA 467
Cdd:smart00798 303 SARIAAEKA 311
|
|
| AICARFT_IMPCHas |
pfam01808 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
140-466 |
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: 511.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 140 AAKNHKDVAIVVNAGDYAAVIESLKA-GGLTYAQRFDLALKAFEHTSAYDGMIANYLGtidqtrdtlgtadRGAFPRTFN 218
Cdd:pfam01808 1 AAKNHKDVTVVVDPADYAEVLEELKAnGGTSLETRRRLAAKAFAHTAAYDAAIANYLA-------------GKEFPETLT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 219 SQFVKAQEMRYGENPHQSAAFYVEAKkGEASVSTAIQLQGKELSFNNVADTDAALECVKSFLKPACVIVKHANPCGVAVV 298
Cdd:pfam01808 68 LSFEKVQDLRYGENPHQKAAFYRDPG-PAGGLATAEQLQGKELSYNNILDADAALELVKEFDEPAAVIVKHANPCGVAVG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 299 PEdeggIRKAYDLAYATDSESAFGGIIAFNRELDGETAKAIVErQFVEVIIAPKISAAAREVVAAKANVRLLECGEWPAE 378
Cdd:pfam01808 147 DT----LAEAYRRALAADPVSAFGGIIALNRPVDAATAEEISK-IFLEVIIAPGFTPEALEILKKKKNLRLLEIDPLYPP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 379 RaPGWDFKRVNGGLLVQSRDIGMIKAEDLKIVTRRAPTEQEIHDLIFAWKVAKFVKSNAIVYARNRQTVGVGAGQMSRVN 458
Cdd:pfam01808 222 P-PGLEFRSVSGGLLVQDRDDALIDPDDLKVVTKRAPTEEELRDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVD 300
|
....*...
gi 15600047 459 SARIAAIK 466
Cdd:pfam01808 301 SARIAIEK 308
|
|
| IMPCH |
cd01421 |
Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine ... |
11-195 |
1.70e-109 |
|
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: 323.78 E-value: 1.70e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 11 RRALISVSDKTGVVDFARELVALGVEILSTGGTYKLLRDNGISAVEVADYTGFPEMMDGRVKTLHPKVHGGILGRRDLDG 90
Cdd:cd01421 1 KRALISVSDKTGLVEFAKELVELGVEILSTGGTAKFLKEAGIPVTDVSDITGFPEILGGRVKTLHPKIHGGILARRDNEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 91 -AVMEQHGIKPIDLVAVNLYPFEATVARPDCDLPTAIENIDIGGPTMVRSAAKNHKDVAIVVNAGDYAAVIESLKAGG-L 168
Cdd:cd01421 81 hKDLEEHGIEPIDLVVVNLYPFEETVAKGNVTLEEAIENIDIGGPSLLRAAAKNYKDVTVLVDPADYQKVLEELKSNGsI 160
|
170 180
....*....|....*....|....*..
gi 15600047 169 TYAQRFDLALKAFEHTSAYDGMIANYL 195
Cdd:cd01421 161 SEETRRRLALKAFAHTAEYDAAISNYL 187
|
|
| PRK07106 |
PRK07106 |
phosphoribosylaminoimidazolecarboxamide formyltransferase; |
226-535 |
2.39e-42 |
|
phosphoribosylaminoimidazolecarboxamide formyltransferase;
Pssm-ID: 180841 Cd Length: 390 Bit Score: 155.98 E-value: 2.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 226 EMRYGENPHQSAAfYVEAKKGEASVSTaiqLQGKElSFNNVADTDAALECVK----SFLKPACVIVKHANPCGVAV-VP- 299
Cdd:PRK07106 5 ELKYGCNPNQKPA-RIFMKEGELPIEV---LNGRP-GYINFLDALNSWQLVKelkeATGLPAAASFKHVSPAGAAVgLPl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 300 ------------EDEGGIRKAYDLAYATDSESAFGGIIAFNRELDGETAKaIVERQFVEVIIAPKISAAAREVVAAKANV 367
Cdd:PRK07106 80 sdtlkkiyfvddMELSPLACAYARARGADRMSSYGDFAALSDVCDVETAK-LLKREVSDGIIAPGYTPEALEILKAKKKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 368 RLLECGEWPAERAPGWDFKRVNGGLLVQSRDIGMIKAEDLK-IVTR-RAPTEQEIHDLIFAWKVAKFVKSNAIVYARNRQ 445
Cdd:PRK07106 159 NYNIIKIDPNYEPAPIETKDVFGITFEQGRNELKIDEDLLKnIVTEnKELPDEAKRDLIIALITLKYTQSNSVCYAKDGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 446 TVGVGAGQMSRVNSARIAAIKAE---------------------------------------------HAGLEVK----- 475
Cdd:PRK07106 239 AIGIGAGQQSRIHCTRLAGNKADiwylrqhpkvlnlpfkegirrpdrdnaidvylsddymdvladgvwQQFFTEKpeplt 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600047 476 ------------GAVMASDAFFPFRDGIDNAAKAGITAVIQPGGSMRDNEVIAAADEADIAMVFTGMRHFRH 535
Cdd:PRK07106 319 reekrawlatltGVALGSDAFFPFGDNIERAAKSGVKYIAQPGGSIRDDNVIETCNKYGMTMAFTGVRLFHH 390
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
22-135 |
5.20e-30 |
|
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: 112.57 E-value: 5.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 22 GVVDFARELVALGVEILSTGGTYKLLRDNGISAVevadytgfpemmdgrvKTLHPKVHGGILgrrdldgAVMEQHGIKPI 101
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPVV----------------KTLHPKVHGGIP-------QILDLIKNGEI 57
|
90 100 110
....*....|....*....|....*....|....
gi 15600047 102 DLVAVNLYPFEATVARPDCDLPTAIENIDIGGPT 135
Cdd:smart00851 58 DLVINTLYPFEAQAHEDGYSIRRAAENIDIPGPT 91
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
22-135 |
5.84e-27 |
|
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: 104.11 E-value: 5.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 22 GVVDFARELVALGVEILSTGGTYKLLRDNGISAVEVADYTGFPeMMDGRVKtlhpkvhggilgrrdlDGAVMEQHGikpI 101
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGEG-RPGGRVQ----------------IGDLIKNGE---I 60
|
90 100 110
....*....|....*....|....*....|....
gi 15600047 102 DLVAVNLYPFEATVaRPDCDLPTAIENIDIGGPT 135
Cdd:pfam02142 61 DLVINTLYPFKATV-HDGYAIRRAAENIDIPGPT 93
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
12-69 |
7.35e-09 |
|
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: 53.64 E-value: 7.35e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600047 12 RALISV--SDKTGVVDFARELVALGVEILSTGGTYKLLRDNGISAVEVA-DYTGFPEMMDG 69
Cdd:cd01424 2 TVFISVadRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNkVSEGRPNIVDL 62
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
12-156 |
2.81e-08 |
|
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: 52.13 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600047 12 RALISVSD--KTGVVDFARELVALGVEILSTGGTYKLLRDNGISAVEVADYTGFpemmdgrvktLHPKVHGGILGRRDld 89
Cdd:cd00532 1 GVFLSVSDhvKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHED----------GEPTVDAAIAEKGK-- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600047 90 gavmeqhgikpIDLVAVNLYPFEAtvarpdcdlptaiENIDIGGPTMVRSAAKNHKDVAIVVNAGDY 156
Cdd:cd00532 69 -----------FDVVINLRDPRRD-------------RCTDEDGTALLRLARLYKIPVTTPNATAMF 111
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
6-57 |
1.80e-07 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 53.95 E-value: 1.80e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 15600047 6 TRLPIR-RALISV--SDKTGVVDFARELVALGVEILSTGGTYKLLRDNGISAVEV 57
Cdd:PRK05294 932 NRLPTSgTVFLSVrdRDKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELV 986
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
12-68 |
1.66e-03 |
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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: 41.14 E-value: 1.66e-03
10 20 30 40 50 60
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gi 15600047 12 RALISV--SDKTGVVDFARELVALGVEILSTGGTYKLLRDNGISAVEVADYT-GFPEMMD 68
Cdd:TIGR01369 939 SVLLSVrdKDKEELLDLARKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSeGRPNILD 998
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| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
7-70 |
2.86e-03 |
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carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 40.53 E-value: 2.86e-03
10 20 30 40 50 60
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gi 15600047 7 RLPIR-RALISVSDKT--GVVDFARELVALGVEILSTGGTYKLLRDNGISaVEVAdytgfPEMMDGR 70
Cdd:PLN02735 968 RLPLSgTVFISLNDLTkpHLVPIARGFLELGFRIVSTSGTAHFLELAGIP-VERV-----LKLHEGR 1028
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