|
Name |
Accession |
Description |
Interval |
E-value |
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
5-529 |
0e+00 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 1014.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 5 RPIRRALLSVSDKTGITEFAQALSARGVELLSTGGTARLLADAGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRG 84
Cdd:PRK00881 2 RMIKRALISVSDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVTGFPEILDGRVKTLHPKIHGGILARRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 85 TDDEI--MAKHQISAIDMVVVNLYPFAETVAKPGCTLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYSNIIAEMDA 162
Cdd:PRK00881 82 NPEHVaaLEEHGIEPIDLVVVNLYPFEETVAKPGVTLEEAIENIDIGGPTMVRAAAKNHKDVAVVVDPADYDAVLEELKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 163 GqNSLSFDTRFDLAIKAFEHTAAYDSMIANYFgqkvkpyfgdTTQPSGQFPRTLNLNFIKKQDMRYGENSHQNAAFYIEE 242
Cdd:PRK00881 162 N-GSTTLETRFRLAAKAFAHTAAYDAAIANYL----------TEQVGEEFPETLNLSFEKKQDLRYGENPHQKAAFYRDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 243 NiQEASISTAVQLQGKALSYNNIADTDAALECVKQFDKPACVIVKHANPCGVAIADTLLTAYDNAFKTDPTSAFGGIIAF 322
Cdd:PRK00881 231 N-AEGGVATAEQLQGKELSYNNIADADAALELVKEFDEPACVIVKHANPCGVAVGDTILEAYDKAYACDPVSAFGGIIAF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 323 NRELDAQTAAEITErQFVEVIIAPSVAEDALPVLAAKQNVRVLTCGQWQHPvaALDFKRVNGGLLVQDRDLGMVGDTDLK 402
Cdd:PRK00881 310 NREVDAETAEAIHK-IFLEVIIAPSFSEEALEILAKKKNLRLLECPFPGGW--EGDFKSVSGGLLVQDRDLGMVDPADLK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 403 VVSKRQPTEQELKDALFCWKVAKFVKSNAIVYSKNNMTIGVGAGQMSRVYSAKIAGIKAGDEGLEVAGCAMASDAFFPFR 482
Cdd:PRK00881 387 VVTKRQPTEQELKDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEKAGDAGLDLKGAVLASDAFFPFR 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1081357639 483 DGIDAAAAVGITCVIQPGGSIRDDEVIAAADEHNIAMIFTGMRHFRH 529
Cdd:PRK00881 467 DGVEAAAKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGVRHFRH 513
|
|
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
5-529 |
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: 1003.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 5 RPIRRALLSVSDKTGITEFAQALSARGVELLSTGGTARLLADAGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRG 84
Cdd:COG0138 1 VPIKRALISVSDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVTGFPEILDGRVKTLHPKIHGGILARRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 85 TDDEI--MAKHQISAIDMVVVNLYPFAETVAKPGCTLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYSNIIAEMDA 162
Cdd:COG0138 81 NPEHVaqLEEHGIEPIDLVVVNLYPFEETVAKPGATLEEAIENIDIGGPAMLRAAAKNHADVAVVVDPADYDAVLEELKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 163 gQNSLSFDTRFDLAIKAFEHTAAYDSMIANYFGQKVkpyfgdttqPSGQFPRTLNLNFIKKQDMRYGENSHQNAAFYIEE 242
Cdd:COG0138 161 -NGGTSLETRRRLAAKAFAHTAAYDAAIANYLAEQL---------GEEEFPETLTLSFEKVQDLRYGENPHQKAAFYRDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 243 NiQEASISTAVQLQGKALSYNNIADTDAALECVKQFDKPACVIVKHANPCGVAIADTLLTAYDNAFKTDPTSAFGGIIAF 322
Cdd:COG0138 231 G-AEGGLATAEQLQGKELSYNNILDADAALELVKEFDEPAVVIVKHANPCGVAVGDTLAEAYEKAYACDPVSAFGGIIAF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 323 NRELDAQTAAEITErQFVEVIIAPSVAEDALPVLAAKQNVRVLTCGQWQHPVAALDFKRVNGGLLVQDRDLGMVGDTDLK 402
Cdd:COG0138 310 NRPVDAATAEAIAK-IFLEVIIAPDFSPEALEILAKKKNLRLLELGGLDPPAPGLDVKSVSGGLLVQDRDLGLIDPADLK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 403 VVSKRQPTEQELKDALFCWKVAKFVKSNAIVYSKNNMTIGVGAGQMSRVYSAKIAGIKAGDeglEVAGCAMASDAFFPFR 482
Cdd:COG0138 389 VVTKRAPTEEELADLLFAWKVVKHVKSNAIVLAKDGATVGIGAGQMSRVDSARIALEKAGE---RAKGSVLASDAFFPFR 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1081357639 483 DGIDAAAAVGITCVIQPGGSIRDDEVIAAADEHNIAMIFTGMRHFRH 529
Cdd:COG0138 466 DGVEAAAKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGMRHFRH 512
|
|
| purH |
TIGR00355 |
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is ... |
8-529 |
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: 879.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 8 RRALLSVSDKTGITEFAQALSARGVELLSTGGTARLLADAGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRGTDD 87
Cdd:TIGR00355 1 RRALLSVSDKTGIVEFAQGLVERGVELLSTGGTAKLLAEAGVPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILARRGDDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 88 E-IMAKHQISAIDMVVVNLYPFAETVAKPGCTLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYSNIIAEMDAgQNS 166
Cdd:TIGR00355 81 DaDLEEHGIEPIDLVVVNLYPFKETVAKPGVTLAEAVENIDIGGPTMLRAAAKNHADVTILVDPKDYSAILSELDE-QGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 167 LSFDTRFDLAIKAFEHTAAYDSMIANYFGQKVkpyfgdttqpSGQFPRTLNLNFIKKQDMRYGENSHQNAAFYIEENIQE 246
Cdd:TIGR00355 160 ISLALRFDLAIKAFEHTAAYDAAIANYFGKLV----------GEKEPRQFNLNFTKKQTLRYGENPHQKAAFYVTQNVKE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 247 ASISTAVQLQGKALSYNNIADTDAALECVKQFDKPACVIVKHANPCGVAIADTLLTAYDNAFKTDPTSAFGGIIAFNREL 326
Cdd:TIGR00355 230 GSVATAEQLQGKELSYNNIADADAALEIVKEFDEPAAVIVKHANPCGVALGKTILDAYDRAFGADPTSAFGGIIALNREL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 327 DAQTAAEITeRQFVEVIIAPSVAEDALPVLAAKQNVRVLTCGQWQHPVAALDFKRVNGGLLVQDRDLGMVGDTDLKVVSK 406
Cdd:TIGR00355 310 DVPTAKAIV-RQFLEVIIAPGYSAEALEILAKKKNLRVLILGIWANRVPELDFKRVNGGLLVQDRDDGMVDQSTLKVVTK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 407 RQPTEQELKDALFCWKVAKFVKSNAIVYSKNNMTIGVGAGQMSRVYSAKIAGIKAGDEGLEVAGCAMASDAFFPFRDGID 486
Cdd:TIGR00355 389 RQPTEQELIDLLFAWKVAKHVKSNAIVYAKNNMTVGVGAGQMSRVGSAKIAGIKADDEGLEAKGSSLASDAFFPFRDGVE 468
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1081357639 487 AAAAVGITCVIQPGGSIRDDEVIAAADEHNIAMIFTGMRHFRH 529
Cdd:TIGR00355 469 EAAAAGITCIIQPGGSMRDEDSIWAADEHGIVMVFTGMRHFRH 511
|
|
| AICARFT_IMPCHas |
smart00798 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
137-461 |
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: 545.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 137 AAKNHKDVAIVVKSSDYSNIIAEMDAGqNSLSFDTRFDLAIKAFEHTAAYDSMIANYFGQKVKpyfgdttqpsGQFPRTL 216
Cdd:smart00798 1 AAKNHKDVTVVVDPADYAEVLEELKAN-GGLSLETRKRLAAKAFAHTAAYDAAISNYLAKQLA----------SEFPETL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 217 NLNFIKKQDMRYGENSHQNAAFYIEENIQEaSISTAVQLQGKALSYNNIADTDAALECVKQFDKPACVIVKHANPCGVAI 296
Cdd:smart00798 70 TLSFEKKQDLRYGENPHQKAAFYTDPDALG-GIATAKQLQGKELSYNNILDADAALELVKEFDEPACVIVKHANPCGVAV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 297 ADTLLTAYDNAFKTDPTSAFGGIIAFNRELDAQTAAEITeRQFVEVIIAPSVAEDALPVLAAKQNVRVLTCGQWQHPvAA 376
Cdd:smart00798 149 GDTLAEAYRKAYAADPVSAFGGIIAFNRPVDEETAEAIN-KIFLEVIIAPDFDEEALEILSKKKNLRLLECGPLPDP-DG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 377 LDFKRVNGGLLVQDRDLGMVGDTDLKVVSKRQPTEQELKDALFCWKVAKFVKSNAIVYSKNNMTIGVGAGQMSRVYSAKI 456
Cdd:smart00798 227 LEFKSVSGGLLVQDRDNGGIDPEDLKVVTKRQPTEEELADLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARI 306
|
....*
gi 1081357639 457 AGIKA 461
Cdd:smart00798 307 AAEKA 311
|
|
| AICARFT_IMPCHas |
pfam01808 |
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 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: 533.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 137 AAKNHKDVAIVVKSSDYSNIIAEMDAGqNSLSFDTRFDLAIKAFEHTAAYDSMIANYFGQKvkpyfgdttqpsgQFPRTL 216
Cdd:pfam01808 1 AAKNHKDVTVVVDPADYAEVLEELKAN-GGTSLETRRRLAAKAFAHTAAYDAAIANYLAGK-------------EFPETL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 217 NLNFIKKQDMRYGENSHQNAAFYIEENiQEASISTAVQLQGKALSYNNIADTDAALECVKQFDKPACVIVKHANPCGVAI 296
Cdd:pfam01808 67 TLSFEKVQDLRYGENPHQKAAFYRDPG-PAGGLATAEQLQGKELSYNNILDADAALELVKEFDEPAAVIVKHANPCGVAV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 297 ADTLLTAYDNAFKTDPTSAFGGIIAFNRELDAQTAAEITErQFVEVIIAPSVAEDALPVLAAKQNVRVLTCGQWQHPVAA 376
Cdd:pfam01808 146 GDTLAEAYRRALAADPVSAFGGIIALNRPVDAATAEEISK-IFLEVIIAPGFTPEALEILKKKKNLRLLEIDPLYPPPPG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 377 LDFKRVNGGLLVQDRDLGMVGDTDLKVVSKRQPTEQELKDALFCWKVAKFVKSNAIVYSKNNMTIGVGAGQMSRVYSAKI 456
Cdd:pfam01808 225 LEFRSVSGGLLVQDRDDALIDPDDLKVVTKRAPTEEELRDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARI 304
|
....
gi 1081357639 457 AGIK 460
Cdd:pfam01808 305 AIEK 308
|
|
| IMPCH |
cd01421 |
Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine ... |
8-194 |
2.89e-114 |
|
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: 336.11 E-value: 2.89e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 8 RRALLSVSDKTGITEFAQALSARGVELLSTGGTARLLADAGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRGTDD 87
Cdd:cd01421 1 KRALISVSDKTGLVEFAKELVELGVEILSTGGTAKFLKEAGIPVTDVSDITGFPEILGGRVKTLHPKIHGGILARRDNEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 88 E-IMAKHQISAIDMVVVNLYPFAETVAKPGCTLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYSNIIAEMDAGqNS 166
Cdd:cd01421 81 HkDLEEHGIEPIDLVVVNLYPFEETVAKGNVTLEEAIENIDIGGPSLLRAAAKNYKDVTVLVDPADYQKVLEELKSN-GS 159
|
170 180
....*....|....*....|....*...
gi 1081357639 167 LSFDTRFDLAIKAFEHTAAYDSMIANYF 194
Cdd:cd01421 160 ISEETRRRLALKAFAHTAEYDAAISNYL 187
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
5-529 |
0e+00 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 1014.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 5 RPIRRALLSVSDKTGITEFAQALSARGVELLSTGGTARLLADAGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRG 84
Cdd:PRK00881 2 RMIKRALISVSDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVTGFPEILDGRVKTLHPKIHGGILARRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 85 TDDEI--MAKHQISAIDMVVVNLYPFAETVAKPGCTLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYSNIIAEMDA 162
Cdd:PRK00881 82 NPEHVaaLEEHGIEPIDLVVVNLYPFEETVAKPGVTLEEAIENIDIGGPTMVRAAAKNHKDVAVVVDPADYDAVLEELKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 163 GqNSLSFDTRFDLAIKAFEHTAAYDSMIANYFgqkvkpyfgdTTQPSGQFPRTLNLNFIKKQDMRYGENSHQNAAFYIEE 242
Cdd:PRK00881 162 N-GSTTLETRFRLAAKAFAHTAAYDAAIANYL----------TEQVGEEFPETLNLSFEKKQDLRYGENPHQKAAFYRDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 243 NiQEASISTAVQLQGKALSYNNIADTDAALECVKQFDKPACVIVKHANPCGVAIADTLLTAYDNAFKTDPTSAFGGIIAF 322
Cdd:PRK00881 231 N-AEGGVATAEQLQGKELSYNNIADADAALELVKEFDEPACVIVKHANPCGVAVGDTILEAYDKAYACDPVSAFGGIIAF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 323 NRELDAQTAAEITErQFVEVIIAPSVAEDALPVLAAKQNVRVLTCGQWQHPvaALDFKRVNGGLLVQDRDLGMVGDTDLK 402
Cdd:PRK00881 310 NREVDAETAEAIHK-IFLEVIIAPSFSEEALEILAKKKNLRLLECPFPGGW--EGDFKSVSGGLLVQDRDLGMVDPADLK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 403 VVSKRQPTEQELKDALFCWKVAKFVKSNAIVYSKNNMTIGVGAGQMSRVYSAKIAGIKAGDEGLEVAGCAMASDAFFPFR 482
Cdd:PRK00881 387 VVTKRQPTEQELKDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEKAGDAGLDLKGAVLASDAFFPFR 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1081357639 483 DGIDAAAAVGITCVIQPGGSIRDDEVIAAADEHNIAMIFTGMRHFRH 529
Cdd:PRK00881 467 DGVEAAAKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGVRHFRH 513
|
|
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
5-529 |
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: 1003.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 5 RPIRRALLSVSDKTGITEFAQALSARGVELLSTGGTARLLADAGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRG 84
Cdd:COG0138 1 VPIKRALISVSDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVTGFPEILDGRVKTLHPKIHGGILARRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 85 TDDEI--MAKHQISAIDMVVVNLYPFAETVAKPGCTLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYSNIIAEMDA 162
Cdd:COG0138 81 NPEHVaqLEEHGIEPIDLVVVNLYPFEETVAKPGATLEEAIENIDIGGPAMLRAAAKNHADVAVVVDPADYDAVLEELKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 163 gQNSLSFDTRFDLAIKAFEHTAAYDSMIANYFGQKVkpyfgdttqPSGQFPRTLNLNFIKKQDMRYGENSHQNAAFYIEE 242
Cdd:COG0138 161 -NGGTSLETRRRLAAKAFAHTAAYDAAIANYLAEQL---------GEEEFPETLTLSFEKVQDLRYGENPHQKAAFYRDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 243 NiQEASISTAVQLQGKALSYNNIADTDAALECVKQFDKPACVIVKHANPCGVAIADTLLTAYDNAFKTDPTSAFGGIIAF 322
Cdd:COG0138 231 G-AEGGLATAEQLQGKELSYNNILDADAALELVKEFDEPAVVIVKHANPCGVAVGDTLAEAYEKAYACDPVSAFGGIIAF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 323 NRELDAQTAAEITErQFVEVIIAPSVAEDALPVLAAKQNVRVLTCGQWQHPVAALDFKRVNGGLLVQDRDLGMVGDTDLK 402
Cdd:COG0138 310 NRPVDAATAEAIAK-IFLEVIIAPDFSPEALEILAKKKNLRLLELGGLDPPAPGLDVKSVSGGLLVQDRDLGLIDPADLK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 403 VVSKRQPTEQELKDALFCWKVAKFVKSNAIVYSKNNMTIGVGAGQMSRVYSAKIAGIKAGDeglEVAGCAMASDAFFPFR 482
Cdd:COG0138 389 VVTKRAPTEEELADLLFAWKVVKHVKSNAIVLAKDGATVGIGAGQMSRVDSARIALEKAGE---RAKGSVLASDAFFPFR 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1081357639 483 DGIDAAAAVGITCVIQPGGSIRDDEVIAAADEHNIAMIFTGMRHFRH 529
Cdd:COG0138 466 DGVEAAAKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGMRHFRH 512
|
|
| purH |
TIGR00355 |
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is ... |
8-529 |
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: 879.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 8 RRALLSVSDKTGITEFAQALSARGVELLSTGGTARLLADAGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRGTDD 87
Cdd:TIGR00355 1 RRALLSVSDKTGIVEFAQGLVERGVELLSTGGTAKLLAEAGVPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILARRGDDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 88 E-IMAKHQISAIDMVVVNLYPFAETVAKPGCTLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYSNIIAEMDAgQNS 166
Cdd:TIGR00355 81 DaDLEEHGIEPIDLVVVNLYPFKETVAKPGVTLAEAVENIDIGGPTMLRAAAKNHADVTILVDPKDYSAILSELDE-QGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 167 LSFDTRFDLAIKAFEHTAAYDSMIANYFGQKVkpyfgdttqpSGQFPRTLNLNFIKKQDMRYGENSHQNAAFYIEENIQE 246
Cdd:TIGR00355 160 ISLALRFDLAIKAFEHTAAYDAAIANYFGKLV----------GEKEPRQFNLNFTKKQTLRYGENPHQKAAFYVTQNVKE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 247 ASISTAVQLQGKALSYNNIADTDAALECVKQFDKPACVIVKHANPCGVAIADTLLTAYDNAFKTDPTSAFGGIIAFNREL 326
Cdd:TIGR00355 230 GSVATAEQLQGKELSYNNIADADAALEIVKEFDEPAAVIVKHANPCGVALGKTILDAYDRAFGADPTSAFGGIIALNREL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 327 DAQTAAEITeRQFVEVIIAPSVAEDALPVLAAKQNVRVLTCGQWQHPVAALDFKRVNGGLLVQDRDLGMVGDTDLKVVSK 406
Cdd:TIGR00355 310 DVPTAKAIV-RQFLEVIIAPGYSAEALEILAKKKNLRVLILGIWANRVPELDFKRVNGGLLVQDRDDGMVDQSTLKVVTK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 407 RQPTEQELKDALFCWKVAKFVKSNAIVYSKNNMTIGVGAGQMSRVYSAKIAGIKAGDEGLEVAGCAMASDAFFPFRDGID 486
Cdd:TIGR00355 389 RQPTEQELIDLLFAWKVAKHVKSNAIVYAKNNMTVGVGAGQMSRVGSAKIAGIKADDEGLEAKGSSLASDAFFPFRDGVE 468
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1081357639 487 AAAAVGITCVIQPGGSIRDDEVIAAADEHNIAMIFTGMRHFRH 529
Cdd:TIGR00355 469 EAAAAGITCIIQPGGSMRDEDSIWAADEHGIVMVFTGMRHFRH 511
|
|
| PLN02891 |
PLN02891 |
IMP cyclohydrolase |
8-529 |
0e+00 |
|
IMP cyclohydrolase
Pssm-ID: 178479 [Multi-domain] Cd Length: 547 Bit Score: 555.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 8 RRALLSVSDKTGITEFAQALSARGVELLSTGGTARLLADAGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRGTDD 87
Cdd:PLN02891 23 KQALISLSDKTDLALLANGLQELGYTIVSTGGTASALEAAGVSVTKVEELTNFPEMLDGRVKTLHPAVHGGILARRDQEH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 88 --EIMAKHQISAIDMVVVNLYPFAETVAKPGCTLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYSNIIAEMDAGQN 165
Cdd:PLN02891 103 hmEALNEHGIGTIDVVVVNLYPFYDTVTSGGISFEDGVENIDIGGPAMIRAAAKNHKDVLVVVDPADYPALLEYLKGKQD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 166 SLSfDTRFDLAIKAFEHTAAYDSMIANYFGQKvkpyfgdtTQPSGQFPRTLNLNFIKKQDMRYGENSHQNAAFYIEENIQ 245
Cdd:PLN02891 183 DQQ-DFRRKLAWKAFQHVASYDSAVSEWLWKQ--------INGGGKFPPSLTVPLTLKSSLRYGENPHQKAAFYVDKSLS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 246 EAS---ISTAVQLQGKALSYNNIADTDAALECVKQFDKPACVIVKHANPCGVAIADTLLTAYDNAFKTDPTSAFGGIIAF 322
Cdd:PLN02891 254 EVNaggIATAIQHHGKEMSYNNYLDADAAWNCVSEFSNPTCVVVKHTNPCGVASRGDILEAYRLAVRADPVSAFGGIVAF 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 323 NRELDAQTAAEITE---------RQFVEVIIAPSVAEDALPVLAAK-QNVRVLTCGQWQHpvAALDFKRVNGGLLVQDRD 392
Cdd:PLN02891 334 NCEVDEDLAREIREfrsptdgetRMFYEIVVAPKYTEKGLEVLKGKsKTLRILEAKPRKK--GRLSLRQVGGGWLAQDSD 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 393 LGMVGDTDLKVVSKRQPTEQELKDALFCWKVAKFVKSNAIVYSKNNMTIGVGAGQMSRVYSAKIAGIKAGDeglEVAGCA 472
Cdd:PLN02891 412 DLTPEDITFTVVSEKVPTESELEDAKFAWLCVKHVKSNAIVVAKNNRMLGMGSGQPNRVESLRIALEKAGE---EAKGAA 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1081357639 473 MASDAFFPF--RDGIDAAAAVGITCVIQPGGSIRDDEVIAAADEHNIAMIFTGMRHFRH 529
Cdd:PLN02891 489 LASDAFFPFawNDAVEEACQAGVKVIAEPGGSMRDQDAIDCCNKYGVALLFTGVRHFRH 547
|
|
| AICARFT_IMPCHas |
smart00798 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
137-461 |
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: 545.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 137 AAKNHKDVAIVVKSSDYSNIIAEMDAGqNSLSFDTRFDLAIKAFEHTAAYDSMIANYFGQKVKpyfgdttqpsGQFPRTL 216
Cdd:smart00798 1 AAKNHKDVTVVVDPADYAEVLEELKAN-GGLSLETRKRLAAKAFAHTAAYDAAISNYLAKQLA----------SEFPETL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 217 NLNFIKKQDMRYGENSHQNAAFYIEENIQEaSISTAVQLQGKALSYNNIADTDAALECVKQFDKPACVIVKHANPCGVAI 296
Cdd:smart00798 70 TLSFEKKQDLRYGENPHQKAAFYTDPDALG-GIATAKQLQGKELSYNNILDADAALELVKEFDEPACVIVKHANPCGVAV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 297 ADTLLTAYDNAFKTDPTSAFGGIIAFNRELDAQTAAEITeRQFVEVIIAPSVAEDALPVLAAKQNVRVLTCGQWQHPvAA 376
Cdd:smart00798 149 GDTLAEAYRKAYAADPVSAFGGIIAFNRPVDEETAEAIN-KIFLEVIIAPDFDEEALEILSKKKNLRLLECGPLPDP-DG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 377 LDFKRVNGGLLVQDRDLGMVGDTDLKVVSKRQPTEQELKDALFCWKVAKFVKSNAIVYSKNNMTIGVGAGQMSRVYSAKI 456
Cdd:smart00798 227 LEFKSVSGGLLVQDRDNGGIDPEDLKVVTKRQPTEEELADLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARI 306
|
....*
gi 1081357639 457 AGIKA 461
Cdd:smart00798 307 AAEKA 311
|
|
| AICARFT_IMPCHas |
pfam01808 |
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 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: 533.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 137 AAKNHKDVAIVVKSSDYSNIIAEMDAGqNSLSFDTRFDLAIKAFEHTAAYDSMIANYFGQKvkpyfgdttqpsgQFPRTL 216
Cdd:pfam01808 1 AAKNHKDVTVVVDPADYAEVLEELKAN-GGTSLETRRRLAAKAFAHTAAYDAAIANYLAGK-------------EFPETL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 217 NLNFIKKQDMRYGENSHQNAAFYIEENiQEASISTAVQLQGKALSYNNIADTDAALECVKQFDKPACVIVKHANPCGVAI 296
Cdd:pfam01808 67 TLSFEKVQDLRYGENPHQKAAFYRDPG-PAGGLATAEQLQGKELSYNNILDADAALELVKEFDEPAAVIVKHANPCGVAV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 297 ADTLLTAYDNAFKTDPTSAFGGIIAFNRELDAQTAAEITErQFVEVIIAPSVAEDALPVLAAKQNVRVLTCGQWQHPVAA 376
Cdd:pfam01808 146 GDTLAEAYRRALAADPVSAFGGIIALNRPVDAATAEEISK-IFLEVIIAPGFTPEALEILKKKKNLRLLEIDPLYPPPPG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 377 LDFKRVNGGLLVQDRDLGMVGDTDLKVVSKRQPTEQELKDALFCWKVAKFVKSNAIVYSKNNMTIGVGAGQMSRVYSAKI 456
Cdd:pfam01808 225 LEFRSVSGGLLVQDRDDALIDPDDLKVVTKRAPTEEELRDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARI 304
|
....
gi 1081357639 457 AGIK 460
Cdd:pfam01808 305 AIEK 308
|
|
| IMPCH |
cd01421 |
Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine ... |
8-194 |
2.89e-114 |
|
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: 336.11 E-value: 2.89e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 8 RRALLSVSDKTGITEFAQALSARGVELLSTGGTARLLADAGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRGTDD 87
Cdd:cd01421 1 KRALISVSDKTGLVEFAKELVELGVEILSTGGTAKFLKEAGIPVTDVSDITGFPEILGGRVKTLHPKIHGGILARRDNEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 88 E-IMAKHQISAIDMVVVNLYPFAETVAKPGCTLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYSNIIAEMDAGqNS 166
Cdd:cd01421 81 HkDLEEHGIEPIDLVVVNLYPFEETVAKGNVTLEEAIENIDIGGPSLLRAAAKNYKDVTVLVDPADYQKVLEELKSN-GS 159
|
170 180
....*....|....*....|....*...
gi 1081357639 167 LSFDTRFDLAIKAFEHTAAYDSMIANYF 194
Cdd:cd01421 160 ISEETRRRLALKAFAHTAEYDAAISNYL 187
|
|
| PRK07106 |
PRK07106 |
phosphoribosylaminoimidazolecarboxamide formyltransferase; |
226-529 |
9.19e-50 |
|
phosphoribosylaminoimidazolecarboxamide formyltransferase;
Pssm-ID: 180841 Cd Length: 390 Bit Score: 175.62 E-value: 9.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 226 MRYGENSHQNAA-FYIEENiqEASISTavqLQGKAlSYNNIADTDAALECVKQ----FDKPACVIVKHANPCGVAIA--- 297
Cdd:PRK07106 6 LKYGCNPNQKPArIFMKEG--ELPIEV---LNGRP-GYINFLDALNSWQLVKElkeaTGLPAAASFKHVSPAGAAVGlpl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 298 -DTL--------------LTAYDNAFKTDPTSAFGGIIAFNRELDAQTAaEITERQFVEVIIAPSVAEDALPVLAAKQ-- 360
Cdd:PRK07106 80 sDTLkkiyfvddmelsplACAYARARGADRMSSYGDFAALSDVCDVETA-KLLKREVSDGIIAPGYTPEALEILKAKKkg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 361 NVRVLTCGQWQHPvAALDFKRVNGGLLVQDRDLGMVGDTDLK--VVSKRQPTEQELKDALFCWKVAKFVKSNAIVYSKNN 438
Cdd:PRK07106 159 NYNIIKIDPNYEP-APIETKDVFGITFEQGRNELKIDEDLLKniVTENKELPDEAKRDLIIALITLKYTQSNSVCYAKDG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 439 MTIGVGAGQMSRVYSAKIAGIKA---------------------------------GDEGLEVA---------------- 469
Cdd:PRK07106 238 QAIGIGAGQQSRIHCTRLAGNKAdiwylrqhpkvlnlpfkegirrpdrdnaidvylSDDYMDVLadgvwqqfftekpepl 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081357639 470 -------------GCAMASDAFFPFRDGIDAAAAVGITCVIQPGGSIRDDEVIAAADEHNIAMIFTGMRHFRH 529
Cdd:PRK07106 318 treekrawlatltGVALGSDAFFPFGDNIERAAKSGVKYIAQPGGSIRDDNVIETCNKYGMTMAFTGVRLFHH 390
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
19-132 |
1.16e-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: 114.49 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 19 GITEFAQALSARGVELLSTGGTARLLADAGLPVtevsdytgfpemmdgrVKTLHPKVHGGILgrrgtddEIMAKHQISAI 98
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPV----------------VKTLHPKVHGGIP-------QILDLIKNGEI 57
|
90 100 110
....*....|....*....|....*....|....
gi 1081357639 99 DMVVVNLYPFAETVAKPGCTLEDAVENIDIGGPT 132
Cdd:smart00851 58 DLVINTLYPFEAQAHEDGYSIRRAAENIDIPGPT 91
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
19-132 |
3.09e-29 |
|
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: 110.66 E-value: 3.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 19 GITEFAQALSARGVELLSTGGTARLLADAGLPVTEVSDYTGFPeMMDGRVKTLhpkvhggilgrrgtddEIMAKHQisaI 98
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGEG-RPGGRVQIG----------------DLIKNGE---I 60
|
90 100 110
....*....|....*....|....*....|....
gi 1081357639 99 DMVVVNLYPFAETVAkPGCTLEDAVENIDIGGPT 132
Cdd:pfam02142 61 DLVINTLYPFKATVH-DGYAIRRAAENIDIPGPT 93
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
9-141 |
4.83e-12 |
|
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: 62.53 E-value: 4.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 9 RALLSVSD--KTGITEFAQALSARGVELLSTGGTARLLADAGLPVTEVSDYTGFpemmdgrvktLHPKVHGGILgrrgtd 86
Cdd:cd00532 1 GVFLSVSDhvKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHED----------GEPTVDAAIA------ 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1081357639 87 deimAKHQisaIDMVVVNLYPFAEtvakpgctledavENIDIGGPTMVRSAAKNH 141
Cdd:cd00532 65 ----EKGK---FDVVINLRDPRRD-------------RCTDEDGTALLRLARLYK 99
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
9-66 |
1.33e-06 |
|
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: 47.09 E-value: 1.33e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081357639 9 RALLSV--SDKTGITEFAQALSARGVELLSTGGTARLLADAGLPVTEVS-DYTGFPEMMDG 66
Cdd:cd01424 2 TVFISVadRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNkVSEGRPNIVDL 62
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
9-54 |
1.16e-05 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 48.17 E-value: 1.16e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1081357639 9 RALLSV--SDKTGITEFAQALSARGVELLSTGGTARLLADAGLPVTEV 54
Cdd:PRK05294 939 TVFLSVrdRDKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELV 986
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
10-67 |
5.30e-03 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 39.76 E-value: 5.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357639 10 ALLSVSDKT--GITEFAQALSARGVELLSTGGTARLLADAGLPVTEVsdytgfPEMMDGR 67
Cdd:PLN02735 975 VFISLNDLTkpHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERV------LKLHEGR 1028
|
|
| |
