|
Name |
Accession |
Description |
Interval |
E-value |
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
8-525 |
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: 874.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 8 IKRALISVYDKTGLEDLARALNDAGVEIVSTGSTAAKIADLGVPVIPVEQLTGFPECLEGRVKTLHPMVHAGILADTRKE 87
Cdd:COG0138 3 IKRALISVSDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVTGFPEILDGRVKTLHPKIHGGILARRDNP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 88 DHLKQLDELNVAPFQLVVVNLYPFTQTVAS-GADFDACVEQIDIGGPSMVRAAAKNHPSIAVVVSPSRYSEIIAAV-GNG 165
Cdd:COG0138 83 EHVAQLEEHGIEPIDLVVVNLYPFEETVAKpGATLEEAIENIDIGGPAMLRAAAKNHADVAVVVDPADYDAVLEELkANG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 166 GFTRAERTALAVDAFRHTASYDVAVATWMGEQIadADEPFAEWIGASYELANILRYGENPHQAAALYTDPAAPAGLAQAT 245
Cdd:COG0138 163 GTSLETRRRLAAKAFAHTAAYDAAIANYLAEQL--GEEEFPETLTLSFEKVQDLRYGENPHQKAAFYRDPGAEGGLATAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 246 QLHGKEMSYNNYTDSDAAWRAAWDHERPCVAIIKHANPCGIAVSDvSIAEAHRTAHACDPVSAFGGVIASNREVSVDMAK 325
Cdd:COG0138 241 QLQGKELSYNNILDADAALELVKEFDEPAVVIVKHANPCGVAVGD-TLAEAYEKAYACDPVSAFGGIIAFNRPVDAATAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 326 QVSEIFTEVIIAPSYEDGAVDILSQKKNIRILVAP--QPQRDELEQRQISGGVLVQRRDLVDAEgdnPANWILAAGEAAS 403
Cdd:COG0138 320 AIAKIFLEVIIAPDFSPEALEILAKKKNLRLLELGglDPPAPGLDVKSVSGGLLVQDRDLGLID---PADLKVVTKRAPT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 404 EELLAELEFAWRAVRAVKSNAILLAQGGATVGVGMGQVNRVDAAKLAVERAnslagdEQRAKGSVAASDAFFPFADGLEV 483
Cdd:COG0138 397 EEELADLLFAWKVVKHVKSNAIVLAKDGATVGIGAGQMSRVDSARIALEKA------GERAKGSVLASDAFFPFRDGVEA 470
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 504075279 484 LAEAGVRAVVQPGGSIRDAEVIEAANKAGVTMYLTGARHFAH 525
Cdd:COG0138 471 AAKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGMRHFRH 512
|
|
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
5-525 |
0e+00 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 873.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 5 RKQIKRALISVYDKTGLEDLARALNDAGVEIVSTGSTAAKIADLGVPVIPVEQLTGFPECLEGRVKTLHPMVHAGILADT 84
Cdd:PRK00881 1 RRMIKRALISVSDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVTGFPEILDGRVKTLHPKIHGGILARR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 85 RKEDHLKQLDELNVAPFQLVVVNLYPFTQTVAS-GADFDACVEQIDIGGPSMVRAAAKNHPSIAVVVSPSRYSEIIAAV- 162
Cdd:PRK00881 81 DNPEHVAALEEHGIEPIDLVVVNLYPFEETVAKpGVTLEEAIENIDIGGPTMVRAAAKNHKDVAVVVDPADYDAVLEELk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 163 GNGGFTRAERTALAVDAFRHTASYDVAVATWMGEQiadADEPFAEWIGASYELANILRYGENPHQAAALYTDPAAPAGLA 242
Cdd:PRK00881 161 ANGSTTLETRFRLAAKAFAHTAAYDAAIANYLTEQ---VGEEFPETLNLSFEKKQDLRYGENPHQKAAFYRDPNAEGGVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 243 QATQLHGKEMSYNNYTDSDAAWRAAWDHERPCVAIIKHANPCGIAVSDvSIAEAHRTAHACDPVSAFGGVIASNREVSVD 322
Cdd:PRK00881 238 TAEQLQGKELSYNNIADADAALELVKEFDEPACVIVKHANPCGVAVGD-TILEAYDKAYACDPVSAFGGIIAFNREVDAE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 323 MAKQVSEIFTEVIIAPSYEDGAVDILSQKKNIRILVAPQPQRDELEQRQISGGVLVQRRDLVDAEgdnPANWILAAGEAA 402
Cdd:PRK00881 317 TAEAIHKIFLEVIIAPSFSEEALEILAKKKNLRLLECPFPGGWEGDFKSVSGGLLVQDRDLGMVD---PADLKVVTKRQP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 403 SEELLAELEFAWRAVRAVKSNAILLAQGGATVGVGMGQVNRVDAAKLAVERANSLAGDeqrAKGSVAASDAFFPFADGLE 482
Cdd:PRK00881 394 TEQELKDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEKAGDAGLD---LKGAVLASDAFFPFRDGVE 470
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 504075279 483 VLAEAGVRAVVQPGGSIRDAEVIEAANKAGVTMYLTGARHFAH 525
Cdd:PRK00881 471 AAAKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGVRHFRH 513
|
|
| purH |
TIGR00355 |
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is ... |
9-525 |
1.90e-179 |
|
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: 514.37 E-value: 1.90e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 9 KRALISVYDKTGLEDLARALNDAGVEIVSTGSTAAKIADLGVPVIPVEQLTGFPECLEGRVKTLHPMVHAGILAdTRKED 88
Cdd:TIGR00355 1 RRALLSVSDKTGIVEFAQGLVERGVELLSTGGTAKLLAEAGVPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILA-RRGDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 89 HLKQLDELNVAPFQLVVVNLYPFTQTVAS-GADFDACVEQIDIGGPSMVRAAAKNHPSIAVVVSPSRYSEIIAAVG-NGG 166
Cdd:TIGR00355 80 DDADLEEHGIEPIDLVVVNLYPFKETVAKpGVTLAEAVENIDIGGPTMLRAAAKNHADVTILVDPKDYSAILSELDeQGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 167 FTRAERTALAVDAFRHTASYDVAVATWMGEQIADADepfAEWIGASYELANILRYGENPHQAAALY-TDPAAPAGLAQAT 245
Cdd:TIGR00355 160 ISLALRFDLAIKAFEHTAAYDAAIANYFGKLVGEKE---PRQFNLNFTKKQTLRYGENPHQKAAFYvTQNVKEGSVATAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 246 QLHGKEMSYNNYTDSDAAWRAAWDHERPCVAIIKHANPCGIAVSdVSIAEAHRTAHACDPVSAFGGVIASNREVSVDMAK 325
Cdd:TIGR00355 237 QLQGKELSYNNIADADAALEIVKEFDEPAAVIVKHANPCGVALG-KTILDAYDRAFGADPTSAFGGIIALNRELDVPTAK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 326 QVSEIFTEVIIAPSYEDGAVDILSQKKNIRILVAPQ-PQR-DELEQRQISGGVLVQRRDLvdaEGDNPANWILAAGEAAS 403
Cdd:TIGR00355 316 AIVRQFLEVIIAPGYSAEALEILAKKKNLRVLILGIwANRvPELDFKRVNGGLLVQDRDD---GMVDQSTLKVVTKRQPT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 404 EELLAELEFAWRAVRAVKSNAILLAQGGATVGVGMGQVNRVDAAKLAVERANSlAGDEqrAKGSVAASDAFFPFADGLEV 483
Cdd:TIGR00355 393 EQELIDLLFAWKVAKHVKSNAIVYAKNNMTVGVGAGQMSRVGSAKIAGIKADD-EGLE--AKGSSLASDAFFPFRDGVEE 469
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 504075279 484 LAEAGVRAVVQPGGSIRDAEVIEAANKAGVTMYLTGARHFAH 525
Cdd:TIGR00355 470 AAAAGITCIIQPGGSMRDEDSIWAADEHGIVMVFTGMRHFRH 511
|
|
| AICARFT_IMPCHas |
smart00798 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
139-454 |
1.04e-165 |
|
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: 471.59 E-value: 1.04e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 139 AAKNHPSIAVVVSPSRYSEIIAAV-GNGGFTRAERTALAVDAFRHTASYDVAVATWMGEQIADAdepFAEWIGASYELAN 217
Cdd:smart00798 1 AAKNHKDVTVVVDPADYAEVLEELkANGGLSLETRKRLAAKAFAHTAAYDAAISNYLAKQLASE---FPETLTLSFEKKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 218 ILRYGENPHQAAALYTDPAAPAGLAQATQLHGKEMSYNNYTDSDAAWRAAWDHERPCVAIIKHANPCGIAVSDvSIAEAH 297
Cdd:smart00798 78 DLRYGENPHQKAAFYTDPDALGGIATAKQLQGKELSYNNILDADAALELVKEFDEPACVIVKHANPCGVAVGD-TLAEAY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 298 RTAHACDPVSAFGGVIASNREVSVDMAKQVSEIFTEVIIAPSYEDGAVDILSQKKNIRILVAPQ-PQRDELEQRQISGGV 376
Cdd:smart00798 157 RKAYAADPVSAFGGIIAFNRPVDEETAEAINKIFLEVIIAPDFDEEALEILSKKKNLRLLECGPlPDPDGLEFKSVSGGL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504075279 377 LVQRRDLVdaeGDNPANWILAAGEAASEELLAELEFAWRAVRAVKSNAILLAQGGATVGVGMGQVNRVDAAKLAVERA 454
Cdd:smart00798 237 LVQDRDNG---GIDPEDLKVVTKRQPTEEELADLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAAEKA 311
|
|
| AICARFT_IMPCHas |
pfam01808 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
139-453 |
6.86e-161 |
|
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: 459.18 E-value: 6.86e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 139 AAKNHPSIAVVVSPSRYSEIIAAV-GNGGFTRAERTALAVDAFRHTASYDVAVATWMgeqiadADEPFAEWIGASYELAN 217
Cdd:pfam01808 1 AAKNHKDVTVVVDPADYAEVLEELkANGGTSLETRRRLAAKAFAHTAAYDAAIANYL------AGKEFPETLTLSFEKVQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 218 ILRYGENPHQAAALYTDPAAPAGLAQATQLHGKEMSYNNYTDSDAAWRAAWDHERPCVAIIKHANPCGIAVSDvSIAEAH 297
Cdd:pfam01808 75 DLRYGENPHQKAAFYRDPGPAGGLATAEQLQGKELSYNNILDADAALELVKEFDEPAAVIVKHANPCGVAVGD-TLAEAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 298 RTAHACDPVSAFGGVIASNREVSVDMAKQVSEIFTEVIIAPSYEDGAVDILSQKKNIRILVAPQ--PQRDELEQRQISGG 375
Cdd:pfam01808 154 RRALAADPVSAFGGIIALNRPVDAATAEEISKIFLEVIIAPGFTPEALEILKKKKNLRLLEIDPlyPPPPGLEFRSVSGG 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504075279 376 VLVQRRDLVDaegDNPANWILAAGEAASEELLAELEFAWRAVRAVKSNAILLAQGGATVGVGMGQVNRVDAAKLAVER 453
Cdd:pfam01808 234 LLVQDRDDAL---IDPDDLKVVTKRAPTEEELRDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEK 308
|
|
| IMPCH |
cd01421 |
Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine ... |
9-194 |
4.20e-88 |
|
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: 268.70 E-value: 4.20e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 9 KRALISVYDKTGLEDLARALNDAGVEIVSTGSTAAKIADLGVPVIPVEQLTGFPECLEGRVKTLHPMVHAGILADTRKED 88
Cdd:cd01421 1 KRALISVSDKTGLVEFAKELVELGVEILSTGGTAKFLKEAGIPVTDVSDITGFPEILGGRVKTLHPKIHGGILARRDNEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 89 HlKQLDELNVAPFQLVVVNLYPFTQTVASGA-DFDACVEQIDIGGPSMVRAAAKNHPSIAVVVSPSRYSEIIAAV-GNGG 166
Cdd:cd01421 81 H-KDLEEHGIEPIDLVVVNLYPFEETVAKGNvTLEEAIENIDIGGPSLLRAAAKNYKDVTVLVDPADYQKVLEELkSNGS 159
|
170 180
....*....|....*....|....*...
gi 504075279 167 FTRAERTALAVDAFRHTASYDVAVATWM 194
Cdd:cd01421 160 ISEETRRRLALKAFAHTAEYDAAISNYL 187
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
8-525 |
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: 874.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 8 IKRALISVYDKTGLEDLARALNDAGVEIVSTGSTAAKIADLGVPVIPVEQLTGFPECLEGRVKTLHPMVHAGILADTRKE 87
Cdd:COG0138 3 IKRALISVSDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVTGFPEILDGRVKTLHPKIHGGILARRDNP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 88 DHLKQLDELNVAPFQLVVVNLYPFTQTVAS-GADFDACVEQIDIGGPSMVRAAAKNHPSIAVVVSPSRYSEIIAAV-GNG 165
Cdd:COG0138 83 EHVAQLEEHGIEPIDLVVVNLYPFEETVAKpGATLEEAIENIDIGGPAMLRAAAKNHADVAVVVDPADYDAVLEELkANG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 166 GFTRAERTALAVDAFRHTASYDVAVATWMGEQIadADEPFAEWIGASYELANILRYGENPHQAAALYTDPAAPAGLAQAT 245
Cdd:COG0138 163 GTSLETRRRLAAKAFAHTAAYDAAIANYLAEQL--GEEEFPETLTLSFEKVQDLRYGENPHQKAAFYRDPGAEGGLATAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 246 QLHGKEMSYNNYTDSDAAWRAAWDHERPCVAIIKHANPCGIAVSDvSIAEAHRTAHACDPVSAFGGVIASNREVSVDMAK 325
Cdd:COG0138 241 QLQGKELSYNNILDADAALELVKEFDEPAVVIVKHANPCGVAVGD-TLAEAYEKAYACDPVSAFGGIIAFNRPVDAATAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 326 QVSEIFTEVIIAPSYEDGAVDILSQKKNIRILVAP--QPQRDELEQRQISGGVLVQRRDLVDAEgdnPANWILAAGEAAS 403
Cdd:COG0138 320 AIAKIFLEVIIAPDFSPEALEILAKKKNLRLLELGglDPPAPGLDVKSVSGGLLVQDRDLGLID---PADLKVVTKRAPT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 404 EELLAELEFAWRAVRAVKSNAILLAQGGATVGVGMGQVNRVDAAKLAVERAnslagdEQRAKGSVAASDAFFPFADGLEV 483
Cdd:COG0138 397 EEELADLLFAWKVVKHVKSNAIVLAKDGATVGIGAGQMSRVDSARIALEKA------GERAKGSVLASDAFFPFRDGVEA 470
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 504075279 484 LAEAGVRAVVQPGGSIRDAEVIEAANKAGVTMYLTGARHFAH 525
Cdd:COG0138 471 AAKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGMRHFRH 512
|
|
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
5-525 |
0e+00 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 873.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 5 RKQIKRALISVYDKTGLEDLARALNDAGVEIVSTGSTAAKIADLGVPVIPVEQLTGFPECLEGRVKTLHPMVHAGILADT 84
Cdd:PRK00881 1 RRMIKRALISVSDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVTGFPEILDGRVKTLHPKIHGGILARR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 85 RKEDHLKQLDELNVAPFQLVVVNLYPFTQTVAS-GADFDACVEQIDIGGPSMVRAAAKNHPSIAVVVSPSRYSEIIAAV- 162
Cdd:PRK00881 81 DNPEHVAALEEHGIEPIDLVVVNLYPFEETVAKpGVTLEEAIENIDIGGPTMVRAAAKNHKDVAVVVDPADYDAVLEELk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 163 GNGGFTRAERTALAVDAFRHTASYDVAVATWMGEQiadADEPFAEWIGASYELANILRYGENPHQAAALYTDPAAPAGLA 242
Cdd:PRK00881 161 ANGSTTLETRFRLAAKAFAHTAAYDAAIANYLTEQ---VGEEFPETLNLSFEKKQDLRYGENPHQKAAFYRDPNAEGGVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 243 QATQLHGKEMSYNNYTDSDAAWRAAWDHERPCVAIIKHANPCGIAVSDvSIAEAHRTAHACDPVSAFGGVIASNREVSVD 322
Cdd:PRK00881 238 TAEQLQGKELSYNNIADADAALELVKEFDEPACVIVKHANPCGVAVGD-TILEAYDKAYACDPVSAFGGIIAFNREVDAE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 323 MAKQVSEIFTEVIIAPSYEDGAVDILSQKKNIRILVAPQPQRDELEQRQISGGVLVQRRDLVDAEgdnPANWILAAGEAA 402
Cdd:PRK00881 317 TAEAIHKIFLEVIIAPSFSEEALEILAKKKNLRLLECPFPGGWEGDFKSVSGGLLVQDRDLGMVD---PADLKVVTKRQP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 403 SEELLAELEFAWRAVRAVKSNAILLAQGGATVGVGMGQVNRVDAAKLAVERANSLAGDeqrAKGSVAASDAFFPFADGLE 482
Cdd:PRK00881 394 TEQELKDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEKAGDAGLD---LKGAVLASDAFFPFRDGVE 470
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 504075279 483 VLAEAGVRAVVQPGGSIRDAEVIEAANKAGVTMYLTGARHFAH 525
Cdd:PRK00881 471 AAAKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGVRHFRH 513
|
|
| PLN02891 |
PLN02891 |
IMP cyclohydrolase |
9-525 |
0e+00 |
|
IMP cyclohydrolase
Pssm-ID: 178479 [Multi-domain] Cd Length: 547 Bit Score: 525.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 9 KRALISVYDKTGLEDLARALNDAGVEIVSTGSTAAKIADLGVPVIPVEQLTGFPECLEGRVKTLHPMVHAGILADTRKED 88
Cdd:PLN02891 23 KQALISLSDKTDLALLANGLQELGYTIVSTGGTASALEAAGVSVTKVEELTNFPEMLDGRVKTLHPAVHGGILARRDQEH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 89 HLKQLDELNVAPFQLVVVNLYPFTQTVASGA-DFDACVEQIDIGGPSMVRAAAKNHPSIAVVVSPSRYSEIIAAV-GNGG 166
Cdd:PLN02891 103 HMEALNEHGIGTIDVVVVNLYPFYDTVTSGGiSFEDGVENIDIGGPAMIRAAAKNHKDVLVVVDPADYPALLEYLkGKQD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 167 FTRAERTALAVDAFRHTASYDVAVATWMGEQIaDADEPFAEWIGASYELANILRYGENPHQAAALYTDP----AAPAGLA 242
Cdd:PLN02891 183 DQQDFRRKLAWKAFQHVASYDSAVSEWLWKQI-NGGGKFPPSLTVPLTLKSSLRYGENPHQKAAFYVDKslseVNAGGIA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 243 QATQLHGKEMSYNNYTDSDAAWRAAWDHERPCVAIIKHANPCGIAvSDVSIAEAHRTAHACDPVSAFGGVIASNREVSVD 322
Cdd:PLN02891 262 TAIQHHGKEMSYNNYLDADAAWNCVSEFSNPTCVVVKHTNPCGVA-SRGDILEAYRLAVRADPVSAFGGIVAFNCEVDED 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 323 MAKQVSE----------IFTEVIIAPSYEDGAVDILSQK-KNIRILVAPQPQRDELEQRQISGGVLVQRRDLVDAEGdnp 391
Cdd:PLN02891 341 LAREIREfrsptdgetrMFYEIVVAPKYTEKGLEVLKGKsKTLRILEAKPRKKGRLSLRQVGGGWLAQDSDDLTPED--- 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 392 ANWILAAGEAASEELLAELEFAWRAVRAVKSNAILLAQGGATVGVGMGQVNRVDAAKLAVERanslAGDEqrAKGSVAAS 471
Cdd:PLN02891 418 ITFTVVSEKVPTESELEDAKFAWLCVKHVKSNAIVVAKNNRMLGMGSGQPNRVESLRIALEK----AGEE--AKGAALAS 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 504075279 472 DAFFPFA--DGLEVLAEAGVRAVVQPGGSIRDAEVIEAANKAGVTMYLTGARHFAH 525
Cdd:PLN02891 492 DAFFPFAwnDAVEEACQAGVKVIAEPGGSMRDQDAIDCCNKYGVALLFTGVRHFRH 547
|
|
| purH |
TIGR00355 |
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is ... |
9-525 |
1.90e-179 |
|
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: 514.37 E-value: 1.90e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 9 KRALISVYDKTGLEDLARALNDAGVEIVSTGSTAAKIADLGVPVIPVEQLTGFPECLEGRVKTLHPMVHAGILAdTRKED 88
Cdd:TIGR00355 1 RRALLSVSDKTGIVEFAQGLVERGVELLSTGGTAKLLAEAGVPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILA-RRGDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 89 HLKQLDELNVAPFQLVVVNLYPFTQTVAS-GADFDACVEQIDIGGPSMVRAAAKNHPSIAVVVSPSRYSEIIAAVG-NGG 166
Cdd:TIGR00355 80 DDADLEEHGIEPIDLVVVNLYPFKETVAKpGVTLAEAVENIDIGGPTMLRAAAKNHADVTILVDPKDYSAILSELDeQGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 167 FTRAERTALAVDAFRHTASYDVAVATWMGEQIADADepfAEWIGASYELANILRYGENPHQAAALY-TDPAAPAGLAQAT 245
Cdd:TIGR00355 160 ISLALRFDLAIKAFEHTAAYDAAIANYFGKLVGEKE---PRQFNLNFTKKQTLRYGENPHQKAAFYvTQNVKEGSVATAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 246 QLHGKEMSYNNYTDSDAAWRAAWDHERPCVAIIKHANPCGIAVSdVSIAEAHRTAHACDPVSAFGGVIASNREVSVDMAK 325
Cdd:TIGR00355 237 QLQGKELSYNNIADADAALEIVKEFDEPAAVIVKHANPCGVALG-KTILDAYDRAFGADPTSAFGGIIALNRELDVPTAK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 326 QVSEIFTEVIIAPSYEDGAVDILSQKKNIRILVAPQ-PQR-DELEQRQISGGVLVQRRDLvdaEGDNPANWILAAGEAAS 403
Cdd:TIGR00355 316 AIVRQFLEVIIAPGYSAEALEILAKKKNLRVLILGIwANRvPELDFKRVNGGLLVQDRDD---GMVDQSTLKVVTKRQPT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 404 EELLAELEFAWRAVRAVKSNAILLAQGGATVGVGMGQVNRVDAAKLAVERANSlAGDEqrAKGSVAASDAFFPFADGLEV 483
Cdd:TIGR00355 393 EQELIDLLFAWKVAKHVKSNAIVYAKNNMTVGVGAGQMSRVGSAKIAGIKADD-EGLE--AKGSSLASDAFFPFRDGVEE 469
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 504075279 484 LAEAGVRAVVQPGGSIRDAEVIEAANKAGVTMYLTGARHFAH 525
Cdd:TIGR00355 470 AAAAGITCIIQPGGSMRDEDSIWAADEHGIVMVFTGMRHFRH 511
|
|
| AICARFT_IMPCHas |
smart00798 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
139-454 |
1.04e-165 |
|
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: 471.59 E-value: 1.04e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 139 AAKNHPSIAVVVSPSRYSEIIAAV-GNGGFTRAERTALAVDAFRHTASYDVAVATWMGEQIADAdepFAEWIGASYELAN 217
Cdd:smart00798 1 AAKNHKDVTVVVDPADYAEVLEELkANGGLSLETRKRLAAKAFAHTAAYDAAISNYLAKQLASE---FPETLTLSFEKKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 218 ILRYGENPHQAAALYTDPAAPAGLAQATQLHGKEMSYNNYTDSDAAWRAAWDHERPCVAIIKHANPCGIAVSDvSIAEAH 297
Cdd:smart00798 78 DLRYGENPHQKAAFYTDPDALGGIATAKQLQGKELSYNNILDADAALELVKEFDEPACVIVKHANPCGVAVGD-TLAEAY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 298 RTAHACDPVSAFGGVIASNREVSVDMAKQVSEIFTEVIIAPSYEDGAVDILSQKKNIRILVAPQ-PQRDELEQRQISGGV 376
Cdd:smart00798 157 RKAYAADPVSAFGGIIAFNRPVDEETAEAINKIFLEVIIAPDFDEEALEILSKKKNLRLLECGPlPDPDGLEFKSVSGGL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504075279 377 LVQRRDLVdaeGDNPANWILAAGEAASEELLAELEFAWRAVRAVKSNAILLAQGGATVGVGMGQVNRVDAAKLAVERA 454
Cdd:smart00798 237 LVQDRDNG---GIDPEDLKVVTKRQPTEEELADLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAAEKA 311
|
|
| AICARFT_IMPCHas |
pfam01808 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
139-453 |
6.86e-161 |
|
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: 459.18 E-value: 6.86e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 139 AAKNHPSIAVVVSPSRYSEIIAAV-GNGGFTRAERTALAVDAFRHTASYDVAVATWMgeqiadADEPFAEWIGASYELAN 217
Cdd:pfam01808 1 AAKNHKDVTVVVDPADYAEVLEELkANGGTSLETRRRLAAKAFAHTAAYDAAIANYL------AGKEFPETLTLSFEKVQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 218 ILRYGENPHQAAALYTDPAAPAGLAQATQLHGKEMSYNNYTDSDAAWRAAWDHERPCVAIIKHANPCGIAVSDvSIAEAH 297
Cdd:pfam01808 75 DLRYGENPHQKAAFYRDPGPAGGLATAEQLQGKELSYNNILDADAALELVKEFDEPAAVIVKHANPCGVAVGD-TLAEAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 298 RTAHACDPVSAFGGVIASNREVSVDMAKQVSEIFTEVIIAPSYEDGAVDILSQKKNIRILVAPQ--PQRDELEQRQISGG 375
Cdd:pfam01808 154 RRALAADPVSAFGGIIALNRPVDAATAEEISKIFLEVIIAPGFTPEALEILKKKKNLRLLEIDPlyPPPPGLEFRSVSGG 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504075279 376 VLVQRRDLVDaegDNPANWILAAGEAASEELLAELEFAWRAVRAVKSNAILLAQGGATVGVGMGQVNRVDAAKLAVER 453
Cdd:pfam01808 234 LLVQDRDDAL---IDPDDLKVVTKRAPTEEELRDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEK 308
|
|
| IMPCH |
cd01421 |
Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine ... |
9-194 |
4.20e-88 |
|
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: 268.70 E-value: 4.20e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 9 KRALISVYDKTGLEDLARALNDAGVEIVSTGSTAAKIADLGVPVIPVEQLTGFPECLEGRVKTLHPMVHAGILADTRKED 88
Cdd:cd01421 1 KRALISVSDKTGLVEFAKELVELGVEILSTGGTAKFLKEAGIPVTDVSDITGFPEILGGRVKTLHPKIHGGILARRDNEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 89 HlKQLDELNVAPFQLVVVNLYPFTQTVASGA-DFDACVEQIDIGGPSMVRAAAKNHPSIAVVVSPSRYSEIIAAV-GNGG 166
Cdd:cd01421 81 H-KDLEEHGIEPIDLVVVNLYPFEETVAKGNvTLEEAIENIDIGGPSLLRAAAKNYKDVTVLVDPADYQKVLEELkSNGS 159
|
170 180
....*....|....*....|....*...
gi 504075279 167 FTRAERTALAVDAFRHTASYDVAVATWM 194
Cdd:cd01421 160 ISEETRRRLALKAFAHTAEYDAAISNYL 187
|
|
| PRK07106 |
PRK07106 |
phosphoribosylaminoimidazolecarboxamide formyltransferase; |
219-525 |
6.12e-45 |
|
phosphoribosylaminoimidazolecarboxamide formyltransferase;
Pssm-ID: 180841 Cd Length: 390 Bit Score: 162.53 E-value: 6.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 219 LRYGENPHQAAALYTdpaAPAGLAQATQLHGKEmSYNNYTDSDAAW------RAAWDheRPCVAIIKHANPCGIAV---- 288
Cdd:PRK07106 6 LKYGCNPNQKPARIF---MKEGELPIEVLNGRP-GYINFLDALNSWqlvkelKEATG--LPAAASFKHVSPAGAAVglpl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 289 SDV-------------SIAEAHRTAHACDPVSAFGGVIASNREVSVDMAKQVSEIFTEVIIAPSYEDGAVDILSQKKN-- 353
Cdd:PRK07106 80 SDTlkkiyfvddmelsPLACAYARARGADRMSSYGDFAALSDVCDVETAKLLKREVSDGIIAPGYTPEALEILKAKKKgn 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 354 ---IRILVAPQPqrDELEQRQISGGVLVQRRDLVDAEGDNPANwILAAGEAASEELLAELEFAWRAVRAVKSNAILLAQG 430
Cdd:PRK07106 160 yniIKIDPNYEP--APIETKDVFGITFEQGRNELKIDEDLLKN-IVTENKELPDEAKRDLIIALITLKYTQSNSVCYAKD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 431 GATVGVGMGQVNRVDAAKLA--------------------------VERANS---------------------------- 456
Cdd:PRK07106 237 GQAIGIGAGQQSRIHCTRLAgnkadiwylrqhpkvlnlpfkegirrPDRDNAidvylsddymdvladgvwqqfftekpep 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504075279 457 LAGDEQRA-----KGSVAASDAFFPFADGLEVLAEAGVRAVVQPGGSIRDAEVIEAANKAGVTMYLTGARHFAH 525
Cdd:PRK07106 317 LTREEKRAwlatlTGVALGSDAFFPFGDNIERAAKSGVKYIAQPGGSIRDDNVIETCNKYGMTMAFTGVRLFHH 390
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
20-134 |
5.44e-21 |
|
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: 87.54 E-value: 5.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 20 GLEDLARALNDAGVEIVSTGSTAAKIADLGVPVIPVEQLTGFPeCLEGRVktlhpmvhagiladtrkeDHLKQLDELNVa 99
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGEG-RPGGRV------------------QIGDLIKNGEI- 60
|
90 100 110
....*....|....*....|....*....|....*
gi 504075279 100 pfQLVVVNLYPFTQTVASGADFDACVEQIDIGGPS 134
Cdd:pfam02142 61 --DLVINTLYPFKATVHDGYAIRRAAENIDIPGPT 93
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
20-134 |
2.73e-19 |
|
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: 82.52 E-value: 2.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075279 20 GLEDLARALNDAGVEIVSTGSTAAKIADLGVPVipveqltgfpeclegrVKTLHPMVHAGILAdtrkedhlkQLDELNVA 99
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPV----------------VKTLHPKVHGGIPQ---------ILDLIKNG 55
|
90 100 110
....*....|....*....|....*....|....*.
gi 504075279 100 PFQLVVVNLYPFTQTVAS-GADFDACVEQIDIGGPS 134
Cdd:smart00851 56 EIDLVINTLYPFEAQAHEdGYSIRRAAENIDIPGPT 91
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
10-55 |
4.12e-04 |
|
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: 39.77 E-value: 4.12e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 504075279 10 RALISV--YDKTGLEDLARALNDAGVEIVSTGSTAAKIADLGVPVIPV 55
Cdd:cd01424 2 TVFISVadRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVV 49
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
10-55 |
1.30e-03 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 41.62 E-value: 1.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 504075279 10 RALISVY--DKTGLEDLARALNDAGVEIVSTGSTAAKIADLGVPVIPV 55
Cdd:PRK05294 939 TVFLSVRdrDKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELV 986
|
|
| |
