|
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: 849.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 8 IRRALISVSDKTGVAELAAALHQMDVEILSTGGTARTLREAGVPVTEVSEHTGAPEIMDGRVKTLHPKIHGGLLGRRDVD 87
Cdd:COG0138 3 IKRALISVSDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVTGFPEILDGRVKTLHPKIHGGILARRDNP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 88 GPV--MAEHGIAPIDLLVVNLYPFRETVARPGCTPADAIENIDIGGPAMLRAAAKNHAFVTVLVDAADYDGVLAEIRAEG 165
Cdd:COG0138 83 EHVaqLEEHGIEPIDLVVVNLYPFEETVAKPGATLEEAIENIDIGGPAMLRAAAKNHADVAVVVDPADYDAVLEELKANG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 166 NVAATTRAHLAAKGFAHTAAYDGAVADYLGSLEADGsrrPFADTLDLQYRKCLDLRYGENPHQAAAFYAEDDAGPGtLAG 245
Cdd:COG0138 163 GTSLETRRRLAAKAFAHTAAYDAAIANYLAEQLGEE---EFPETLTLSFEKVQDLRYGENPHQKAAFYRDPGAEGG-LAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 246 ARQLQGKALSYNNLADADAALACVRAFDTPACVIVKHANPCGVAVAETPLAAYRAAFATDPTSAFGGILAFNRELDADTA 325
Cdd:COG0138 239 AEQLQGKELSYNNILDADAALELVKEFDEPAVVIVKHANPCGVAVGDTLAEAYEKAYACDPVSAFGGIIAFNRPVDAATA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 326 AEIvATQFAEVILAPSVATDAAAALARKKNLRVLATGPLEAAdsAPRRELKQLAGGVLVQDADLALLDEAGLRTVTRREP 405
Cdd:COG0138 319 EAI-AKIFLEVIIAPDFSPEALEILAKKKNLRLLELGGLDPP--APGLDVKSVSGGLLVQDRDLGLIDPADLKVVTKRAP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 406 TAEERADLLFAWRVAKYVKSNAIVYARDGQTVGVGAGQMSRVDSARIASLKAEDaglAVAGAVMASDAFFPFRDGIDAAA 485
Cdd:COG0138 396 TEEELADLLFAWKVVKHVKSNAIVLAKDGATVGIGAGQMSRVDSARIALEKAGE---RAKGSVLASDAFFPFRDGVEAAA 472
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2751193822 486 KAGIRAVIQPGGSIRDEEVVAAADEADMAMLFTGMRHFRH 525
Cdd:COG0138 473 KAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGMRHFRH 512
|
|
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
7-525 |
0e+00 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 847.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 7 RIRRALISVSDKTGVAELAAALHQMDVEILSTGGTARTLREAGVPVTEVSEHTGAPEIMDGRVKTLHPKIHGGLLGRRDV 86
Cdd:PRK00881 3 MIKRALISVSDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVTGFPEILDGRVKTLHPKIHGGILARRDN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 87 DGPV--MAEHGIAPIDLLVVNLYPFRETVARPGCTPADAIENIDIGGPAMLRAAAKNHAFVTVLVDAADYDGVLAEIRAE 164
Cdd:PRK00881 83 PEHVaaLEEHGIEPIDLVVVNLYPFEETVAKPGVTLEEAIENIDIGGPTMVRAAAKNHKDVAVVVDPADYDAVLEELKAN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 165 GNVAATTRAHLAAKGFAHTAAYDGAVADYLGSLEADGsrrpFADTLDLQYRKCLDLRYGENPHQAAAFYAEDDAGPGtLA 244
Cdd:PRK00881 163 GSTTLETRFRLAAKAFAHTAAYDAAIANYLTEQVGEE----FPETLNLSFEKKQDLRYGENPHQKAAFYRDPNAEGG-VA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 245 GARQLQGKALSYNNLADADAALACVRAFDTPACVIVKHANPCGVAVAETPLAAYRAAFATDPTSAFGGILAFNRELDADT 324
Cdd:PRK00881 238 TAEQLQGKELSYNNIADADAALELVKEFDEPACVIVKHANPCGVAVGDTILEAYDKAYACDPVSAFGGIIAFNREVDAET 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 325 AAEIVAtQFAEVILAPSVATDAAAALARKKNLRVLATgpleAADSAPRRELKQLAGGVLVQDADLALLDEAGLRTVTRRE 404
Cdd:PRK00881 318 AEAIHK-IFLEVIIAPSFSEEALEILAKKKNLRLLEC----PFPGGWEGDFKSVSGGLLVQDRDLGMVDPADLKVVTKRQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 405 PTAEERADLLFAWRVAKYVKSNAIVYARDGQTVGVGAGQMSRVDSARIASLKAEDAGLAVAGAVMASDAFFPFRDGIDAA 484
Cdd:PRK00881 393 PTEQELKDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEKAGDAGLDLKGAVLASDAFFPFRDGVEAA 472
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2751193822 485 AKAGIRAVIQPGGSIRDEEVVAAADEADMAMLFTGMRHFRH 525
Cdd:PRK00881 473 AKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGVRHFRH 513
|
|
| purH |
TIGR00355 |
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is ... |
9-525 |
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: 665.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 9 RRALISVSDKTGVAELAAALHQMDVEILSTGGTARTLREAGVPVTEVSEHTGAPEIMDGRVKTLHPKIHGGLLGRRDVDG 88
Cdd:TIGR00355 1 RRALLSVSDKTGIVEFAQGLVERGVELLSTGGTAKLLAEAGVPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILARRGDDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 89 -PVMAEHGIAPIDLLVVNLYPFRETVARPGCTPADAIENIDIGGPAMLRAAAKNHAFVTVLVDAADYDGVLAEIRAEGNV 167
Cdd:TIGR00355 81 dADLEEHGIEPIDLVVVNLYPFKETVAKPGVTLAEAVENIDIGGPTMLRAAAKNHADVTILVDPKDYSAILSELDEQGSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 168 AATTRAHLAAKGFAHTAAYDGAVADYLGSLEADGSRRpfadTLDLQYRKCLDLRYGENPHQAAAFYAEDDAGPGTLAGAR 247
Cdd:TIGR00355 161 SLALRFDLAIKAFEHTAAYDAAIANYFGKLVGEKEPR----QFNLNFTKKQTLRYGENPHQKAAFYVTQNVKEGSVATAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 248 QLQGKALSYNNLADADAALACVRAFDTPACVIVKHANPCGVAVAETPLAAYRAAFATDPTSAFGGILAFNRELDADTAAE 327
Cdd:TIGR00355 237 QLQGKELSYNNIADADAALEIVKEFDEPAAVIVKHANPCGVALGKTILDAYDRAFGADPTSAFGGIIALNRELDVPTAKA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 328 IVaTQFAEVILAPSVATDAAAALARKKNLRVLATGplEAADSAPRRELKQLAGGVLVQDADLALLDEAGLRTVTRREPTA 407
Cdd:TIGR00355 317 IV-RQFLEVIIAPGYSAEALEILAKKKNLRVLILG--IWANRVPELDFKRVNGGLLVQDRDDGMVDQSTLKVVTKRQPTE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 408 EERADLLFAWRVAKYVKSNAIVYARDGQTVGVGAGQMSRVDSARIASLKAEDAGLAVAGAVMASDAFFPFRDGIDAAAKA 487
Cdd:TIGR00355 394 QELIDLLFAWKVAKHVKSNAIVYAKNNMTVGVGAGQMSRVGSAKIAGIKADDEGLEAKGSSLASDAFFPFRDGVEEAAAA 473
|
490 500 510
....*....|....*....|....*....|....*...
gi 2751193822 488 GIRAVIQPGGSIRDEEVVAAADEADMAMLFTGMRHFRH 525
Cdd:TIGR00355 474 GITCIIQPGGSMRDEDSIWAADEHGIVMVFTGMRHFRH 511
|
|
| AICARFT_IMPCHas |
pfam01808 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
138-456 |
1.13e-156 |
|
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: 448.39 E-value: 1.13e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 138 AAKNHAFVTVLVDAADYDGVLAEIRAEGNVAATTRAHLAAKGFAHTAAYDGAVADYLGSLEadgsrrpFADTLDLQYRKC 217
Cdd:pfam01808 1 AAKNHKDVTVVVDPADYAEVLEELKANGGTSLETRRRLAAKAFAHTAAYDAAIANYLAGKE-------FPETLTLSFEKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 218 LDLRYGENPHQAAAFYAEDDAGPGtLAGARQLQGKALSYNNLADADAALACVRAFDTPACVIVKHANPCGVAVAETPLAA 297
Cdd:pfam01808 74 QDLRYGENPHQKAAFYRDPGPAGG-LATAEQLQGKELSYNNILDADAALELVKEFDEPAAVIVKHANPCGVAVGDTLAEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 298 YRAAFATDPTSAFGGILAFNRELDADTAAEIvATQFAEVILAPSVATDAAAALARKKNLRVLATGPLeaADSAPRRELKQ 377
Cdd:pfam01808 153 YRRALAADPVSAFGGIIALNRPVDAATAEEI-SKIFLEVIIAPGFTPEALEILKKKKNLRLLEIDPL--YPPPPGLEFRS 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2751193822 378 LAGGVLVQDADLALLDEAGLRTVTRREPTAEERADLLFAWRVAKYVKSNAIVYARDGQTVGVGAGQMSRVDSARIASLK 456
Cdd:pfam01808 230 VSGGLLVQDRDDALIDPDDLKVVTKRAPTEEELRDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEK 308
|
|
| AICARFT_IMPCHas |
smart00798 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
138-457 |
2.27e-156 |
|
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: 447.71 E-value: 2.27e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 138 AAKNHAFVTVLVDAADYDGVLAEIRAEGNVAATTRAHLAAKGFAHTAAYDGAVADYLGSLEADGsrrpFADTLDLQYRKC 217
Cdd:smart00798 1 AAKNHKDVTVVVDPADYAEVLEELKANGGLSLETRKRLAAKAFAHTAAYDAAISNYLAKQLASE----FPETLTLSFEKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 218 LDLRYGENPHQAAAFYAEDDAGPGtLAGARQLQGKALSYNNLADADAALACVRAFDTPACVIVKHANPCGVAVAETPLAA 297
Cdd:smart00798 77 QDLRYGENPHQKAAFYTDPDALGG-IATAKQLQGKELSYNNILDADAALELVKEFDEPACVIVKHANPCGVAVGDTLAEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 298 YRAAFATDPTSAFGGILAFNRELDADTAAEIVAtQFAEVILAPSVATDAAAALARKKNLRVLATGPLeaaDSAPRRELKQ 377
Cdd:smart00798 156 YRKAYAADPVSAFGGIIAFNRPVDEETAEAINK-IFLEVIIAPDFDEEALEILSKKKNLRLLECGPL---PDPDGLEFKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 378 LAGGVLVQDADLALLDEAGLRTVTRREPTAEERADLLFAWRVAKYVKSNAIVYARDGQTVGVGAGQMSRVDSARIASLKA 457
Cdd:smart00798 232 VSGGLLVQDRDNGGIDPEDLKVVTKRQPTEEELADLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAAEKA 311
|
|
| IMPCH |
cd01421 |
Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine ... |
9-194 |
6.27e-107 |
|
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: 317.23 E-value: 6.27e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 9 RRALISVSDKTGVAELAAALHQMDVEILSTGGTARTLREAGVPVTEVSEHTGAPEIMDGRVKTLHPKIHGGLLGRRDVDG 88
Cdd:cd01421 1 KRALISVSDKTGLVEFAKELVELGVEILSTGGTAKFLKEAGIPVTDVSDITGFPEILGGRVKTLHPKIHGGILARRDNEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 89 PV-MAEHGIAPIDLLVVNLYPFRETVARPGCTPADAIENIDIGGPAMLRAAAKNHAFVTVLVDAADYDGVLAEIRAEGNV 167
Cdd:cd01421 81 HKdLEEHGIEPIDLVVVNLYPFEETVAKGNVTLEEAIENIDIGGPSLLRAAAKNYKDVTVLVDPADYQKVLEELKSNGSI 160
|
170 180
....*....|....*....|....*..
gi 2751193822 168 AATTRAHLAAKGFAHTAAYDGAVADYL 194
Cdd:cd01421 161 SEETRRRLALKAFAHTAEYDAAISNYL 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: 849.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 8 IRRALISVSDKTGVAELAAALHQMDVEILSTGGTARTLREAGVPVTEVSEHTGAPEIMDGRVKTLHPKIHGGLLGRRDVD 87
Cdd:COG0138 3 IKRALISVSDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVTGFPEILDGRVKTLHPKIHGGILARRDNP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 88 GPV--MAEHGIAPIDLLVVNLYPFRETVARPGCTPADAIENIDIGGPAMLRAAAKNHAFVTVLVDAADYDGVLAEIRAEG 165
Cdd:COG0138 83 EHVaqLEEHGIEPIDLVVVNLYPFEETVAKPGATLEEAIENIDIGGPAMLRAAAKNHADVAVVVDPADYDAVLEELKANG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 166 NVAATTRAHLAAKGFAHTAAYDGAVADYLGSLEADGsrrPFADTLDLQYRKCLDLRYGENPHQAAAFYAEDDAGPGtLAG 245
Cdd:COG0138 163 GTSLETRRRLAAKAFAHTAAYDAAIANYLAEQLGEE---EFPETLTLSFEKVQDLRYGENPHQKAAFYRDPGAEGG-LAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 246 ARQLQGKALSYNNLADADAALACVRAFDTPACVIVKHANPCGVAVAETPLAAYRAAFATDPTSAFGGILAFNRELDADTA 325
Cdd:COG0138 239 AEQLQGKELSYNNILDADAALELVKEFDEPAVVIVKHANPCGVAVGDTLAEAYEKAYACDPVSAFGGIIAFNRPVDAATA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 326 AEIvATQFAEVILAPSVATDAAAALARKKNLRVLATGPLEAAdsAPRRELKQLAGGVLVQDADLALLDEAGLRTVTRREP 405
Cdd:COG0138 319 EAI-AKIFLEVIIAPDFSPEALEILAKKKNLRLLELGGLDPP--APGLDVKSVSGGLLVQDRDLGLIDPADLKVVTKRAP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 406 TAEERADLLFAWRVAKYVKSNAIVYARDGQTVGVGAGQMSRVDSARIASLKAEDaglAVAGAVMASDAFFPFRDGIDAAA 485
Cdd:COG0138 396 TEEELADLLFAWKVVKHVKSNAIVLAKDGATVGIGAGQMSRVDSARIALEKAGE---RAKGSVLASDAFFPFRDGVEAAA 472
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2751193822 486 KAGIRAVIQPGGSIRDEEVVAAADEADMAMLFTGMRHFRH 525
Cdd:COG0138 473 KAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGMRHFRH 512
|
|
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
7-525 |
0e+00 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 847.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 7 RIRRALISVSDKTGVAELAAALHQMDVEILSTGGTARTLREAGVPVTEVSEHTGAPEIMDGRVKTLHPKIHGGLLGRRDV 86
Cdd:PRK00881 3 MIKRALISVSDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVTGFPEILDGRVKTLHPKIHGGILARRDN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 87 DGPV--MAEHGIAPIDLLVVNLYPFRETVARPGCTPADAIENIDIGGPAMLRAAAKNHAFVTVLVDAADYDGVLAEIRAE 164
Cdd:PRK00881 83 PEHVaaLEEHGIEPIDLVVVNLYPFEETVAKPGVTLEEAIENIDIGGPTMVRAAAKNHKDVAVVVDPADYDAVLEELKAN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 165 GNVAATTRAHLAAKGFAHTAAYDGAVADYLGSLEADGsrrpFADTLDLQYRKCLDLRYGENPHQAAAFYAEDDAGPGtLA 244
Cdd:PRK00881 163 GSTTLETRFRLAAKAFAHTAAYDAAIANYLTEQVGEE----FPETLNLSFEKKQDLRYGENPHQKAAFYRDPNAEGG-VA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 245 GARQLQGKALSYNNLADADAALACVRAFDTPACVIVKHANPCGVAVAETPLAAYRAAFATDPTSAFGGILAFNRELDADT 324
Cdd:PRK00881 238 TAEQLQGKELSYNNIADADAALELVKEFDEPACVIVKHANPCGVAVGDTILEAYDKAYACDPVSAFGGIIAFNREVDAET 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 325 AAEIVAtQFAEVILAPSVATDAAAALARKKNLRVLATgpleAADSAPRRELKQLAGGVLVQDADLALLDEAGLRTVTRRE 404
Cdd:PRK00881 318 AEAIHK-IFLEVIIAPSFSEEALEILAKKKNLRLLEC----PFPGGWEGDFKSVSGGLLVQDRDLGMVDPADLKVVTKRQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 405 PTAEERADLLFAWRVAKYVKSNAIVYARDGQTVGVGAGQMSRVDSARIASLKAEDAGLAVAGAVMASDAFFPFRDGIDAA 484
Cdd:PRK00881 393 PTEQELKDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEKAGDAGLDLKGAVLASDAFFPFRDGVEAA 472
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2751193822 485 AKAGIRAVIQPGGSIRDEEVVAAADEADMAMLFTGMRHFRH 525
Cdd:PRK00881 473 AKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGVRHFRH 513
|
|
| purH |
TIGR00355 |
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is ... |
9-525 |
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: 665.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 9 RRALISVSDKTGVAELAAALHQMDVEILSTGGTARTLREAGVPVTEVSEHTGAPEIMDGRVKTLHPKIHGGLLGRRDVDG 88
Cdd:TIGR00355 1 RRALLSVSDKTGIVEFAQGLVERGVELLSTGGTAKLLAEAGVPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILARRGDDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 89 -PVMAEHGIAPIDLLVVNLYPFRETVARPGCTPADAIENIDIGGPAMLRAAAKNHAFVTVLVDAADYDGVLAEIRAEGNV 167
Cdd:TIGR00355 81 dADLEEHGIEPIDLVVVNLYPFKETVAKPGVTLAEAVENIDIGGPTMLRAAAKNHADVTILVDPKDYSAILSELDEQGSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 168 AATTRAHLAAKGFAHTAAYDGAVADYLGSLEADGSRRpfadTLDLQYRKCLDLRYGENPHQAAAFYAEDDAGPGTLAGAR 247
Cdd:TIGR00355 161 SLALRFDLAIKAFEHTAAYDAAIANYFGKLVGEKEPR----QFNLNFTKKQTLRYGENPHQKAAFYVTQNVKEGSVATAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 248 QLQGKALSYNNLADADAALACVRAFDTPACVIVKHANPCGVAVAETPLAAYRAAFATDPTSAFGGILAFNRELDADTAAE 327
Cdd:TIGR00355 237 QLQGKELSYNNIADADAALEIVKEFDEPAAVIVKHANPCGVALGKTILDAYDRAFGADPTSAFGGIIALNRELDVPTAKA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 328 IVaTQFAEVILAPSVATDAAAALARKKNLRVLATGplEAADSAPRRELKQLAGGVLVQDADLALLDEAGLRTVTRREPTA 407
Cdd:TIGR00355 317 IV-RQFLEVIIAPGYSAEALEILAKKKNLRVLILG--IWANRVPELDFKRVNGGLLVQDRDDGMVDQSTLKVVTKRQPTE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 408 EERADLLFAWRVAKYVKSNAIVYARDGQTVGVGAGQMSRVDSARIASLKAEDAGLAVAGAVMASDAFFPFRDGIDAAAKA 487
Cdd:TIGR00355 394 QELIDLLFAWKVAKHVKSNAIVYAKNNMTVGVGAGQMSRVGSAKIAGIKADDEGLEAKGSSLASDAFFPFRDGVEEAAAA 473
|
490 500 510
....*....|....*....|....*....|....*...
gi 2751193822 488 GIRAVIQPGGSIRDEEVVAAADEADMAMLFTGMRHFRH 525
Cdd:TIGR00355 474 GITCIIQPGGSMRDEDSIWAADEHGIVMVFTGMRHFRH 511
|
|
| PLN02891 |
PLN02891 |
IMP cyclohydrolase |
9-525 |
1.15e-179 |
|
IMP cyclohydrolase
Pssm-ID: 178479 [Multi-domain] Cd Length: 547 Bit Score: 516.26 E-value: 1.15e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 9 RRALISVSDKTGVAELAAALHQMDVEILSTGGTARTLREAGVPVTEVSEHTGAPEIMDGRVKTLHPKIHGGLLGRRDVDG 88
Cdd:PLN02891 23 KQALISLSDKTDLALLANGLQELGYTIVSTGGTASALEAAGVSVTKVEELTNFPEMLDGRVKTLHPAVHGGILARRDQEH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 89 PVMA--EHGIAPIDLLVVNLYPFRETVARPGCTPADAIENIDIGGPAMLRAAAKNHAFVTVLVDAADYDGVLAEIRAEGN 166
Cdd:PLN02891 103 HMEAlnEHGIGTIDVVVVNLYPFYDTVTSGGISFEDGVENIDIGGPAMIRAAAKNHKDVLVVVDPADYPALLEYLKGKQD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 167 VAATTRAHLAAKGFAHTAAYDGAVADYLGSLEADGSRRPFADTLDLQYRKclDLRYGENPHQAAAFYAED---DAGPGTL 243
Cdd:PLN02891 183 DQQDFRRKLAWKAFQHVASYDSAVSEWLWKQINGGGKFPPSLTVPLTLKS--SLRYGENPHQKAAFYVDKslsEVNAGGI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 244 AGARQLQGKALSYNNLADADAALACVRAFDTPACVIVKHANPCGVAVAETPLAAYRAAFATDPTSAFGGILAFNRELDAD 323
Cdd:PLN02891 261 ATAIQHHGKEMSYNNYLDADAAWNCVSEFSNPTCVVVKHTNPCGVASRGDILEAYRLAVRADPVSAFGGIVAFNCEVDED 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 324 TAAEI---------VATQFAEVILAPSVATDAAAALARK-KNLRVlatgpLEAADSAP-RRELKQLAGGVLVQDADLALL 392
Cdd:PLN02891 341 LAREIrefrsptdgETRMFYEIVVAPKYTEKGLEVLKGKsKTLRI-----LEAKPRKKgRLSLRQVGGGWLAQDSDDLTP 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 393 DEAGLRTVTRREPTAEERADLLFAWRVAKYVKSNAIVYARDGQTVGVGAGQMSRVDSARIAslkAEDAGLAVAGAVMASD 472
Cdd:PLN02891 416 EDITFTVVSEKVPTESELEDAKFAWLCVKHVKSNAIVVAKNNRMLGMGSGQPNRVESLRIA---LEKAGEEAKGAALASD 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2751193822 473 AFFPF--RDGIDAAAKAGIRAVIQPGGSIRDEEVVAAADEADMAMLFTGMRHFRH 525
Cdd:PLN02891 493 AFFPFawNDAVEEACQAGVKVIAEPGGSMRDQDAIDCCNKYGVALLFTGVRHFRH 547
|
|
| AICARFT_IMPCHas |
pfam01808 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
138-456 |
1.13e-156 |
|
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: 448.39 E-value: 1.13e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 138 AAKNHAFVTVLVDAADYDGVLAEIRAEGNVAATTRAHLAAKGFAHTAAYDGAVADYLGSLEadgsrrpFADTLDLQYRKC 217
Cdd:pfam01808 1 AAKNHKDVTVVVDPADYAEVLEELKANGGTSLETRRRLAAKAFAHTAAYDAAIANYLAGKE-------FPETLTLSFEKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 218 LDLRYGENPHQAAAFYAEDDAGPGtLAGARQLQGKALSYNNLADADAALACVRAFDTPACVIVKHANPCGVAVAETPLAA 297
Cdd:pfam01808 74 QDLRYGENPHQKAAFYRDPGPAGG-LATAEQLQGKELSYNNILDADAALELVKEFDEPAAVIVKHANPCGVAVGDTLAEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 298 YRAAFATDPTSAFGGILAFNRELDADTAAEIvATQFAEVILAPSVATDAAAALARKKNLRVLATGPLeaADSAPRRELKQ 377
Cdd:pfam01808 153 YRRALAADPVSAFGGIIALNRPVDAATAEEI-SKIFLEVIIAPGFTPEALEILKKKKNLRLLEIDPL--YPPPPGLEFRS 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2751193822 378 LAGGVLVQDADLALLDEAGLRTVTRREPTAEERADLLFAWRVAKYVKSNAIVYARDGQTVGVGAGQMSRVDSARIASLK 456
Cdd:pfam01808 230 VSGGLLVQDRDDALIDPDDLKVVTKRAPTEEELRDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEK 308
|
|
| AICARFT_IMPCHas |
smart00798 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
138-457 |
2.27e-156 |
|
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: 447.71 E-value: 2.27e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 138 AAKNHAFVTVLVDAADYDGVLAEIRAEGNVAATTRAHLAAKGFAHTAAYDGAVADYLGSLEADGsrrpFADTLDLQYRKC 217
Cdd:smart00798 1 AAKNHKDVTVVVDPADYAEVLEELKANGGLSLETRKRLAAKAFAHTAAYDAAISNYLAKQLASE----FPETLTLSFEKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 218 LDLRYGENPHQAAAFYAEDDAGPGtLAGARQLQGKALSYNNLADADAALACVRAFDTPACVIVKHANPCGVAVAETPLAA 297
Cdd:smart00798 77 QDLRYGENPHQKAAFYTDPDALGG-IATAKQLQGKELSYNNILDADAALELVKEFDEPACVIVKHANPCGVAVGDTLAEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 298 YRAAFATDPTSAFGGILAFNRELDADTAAEIVAtQFAEVILAPSVATDAAAALARKKNLRVLATGPLeaaDSAPRRELKQ 377
Cdd:smart00798 156 YRKAYAADPVSAFGGIIAFNRPVDEETAEAINK-IFLEVIIAPDFDEEALEILSKKKNLRLLECGPL---PDPDGLEFKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 378 LAGGVLVQDADLALLDEAGLRTVTRREPTAEERADLLFAWRVAKYVKSNAIVYARDGQTVGVGAGQMSRVDSARIASLKA 457
Cdd:smart00798 232 VSGGLLVQDRDNGGIDPEDLKVVTKRQPTEEELADLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAAEKA 311
|
|
| IMPCH |
cd01421 |
Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine ... |
9-194 |
6.27e-107 |
|
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: 317.23 E-value: 6.27e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 9 RRALISVSDKTGVAELAAALHQMDVEILSTGGTARTLREAGVPVTEVSEHTGAPEIMDGRVKTLHPKIHGGLLGRRDVDG 88
Cdd:cd01421 1 KRALISVSDKTGLVEFAKELVELGVEILSTGGTAKFLKEAGIPVTDVSDITGFPEILGGRVKTLHPKIHGGILARRDNEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 89 PV-MAEHGIAPIDLLVVNLYPFRETVARPGCTPADAIENIDIGGPAMLRAAAKNHAFVTVLVDAADYDGVLAEIRAEGNV 167
Cdd:cd01421 81 HKdLEEHGIEPIDLVVVNLYPFEETVAKGNVTLEEAIENIDIGGPSLLRAAAKNYKDVTVLVDPADYQKVLEELKSNGSI 160
|
170 180
....*....|....*....|....*..
gi 2751193822 168 AATTRAHLAAKGFAHTAAYDGAVADYL 194
Cdd:cd01421 161 SEETRRRLALKAFAHTAEYDAAISNYL 187
|
|
| PRK07106 |
PRK07106 |
phosphoribosylaminoimidazolecarboxamide formyltransferase; |
218-525 |
1.55e-40 |
|
phosphoribosylaminoimidazolecarboxamide formyltransferase;
Pssm-ID: 180841 Cd Length: 390 Bit Score: 150.58 E-value: 1.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 218 LDLRYGENPHQAAA-FYAEDDAGPGTLagarqLQGKAlSYNNLADADAALACVR----AFDTPACVIVKHANPCGVAVA- 291
Cdd:PRK07106 4 LELKYGCNPNQKPArIFMKEGELPIEV-----LNGRP-GYINFLDALNSWQLVKelkeATGLPAAASFKHVSPAGAAVGl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 292 ----------------ETPLA-AYRAAFATDPTSAFGGILAFNRELDADTAaEIVATQFAEVILAPSVATDAAAALARKK 354
Cdd:PRK07106 78 plsdtlkkiyfvddmeLSPLAcAYARARGADRMSSYGDFAALSDVCDVETA-KLLKREVSDGIIAPGYTPEALEILKAKK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 355 --NLRVLATGPleaADSAPRRELKQLAGGVLVQDADLALLDEAGLRTV--TRREPTAEERADLLFAWRVAKYVKSNAIVY 430
Cdd:PRK07106 157 kgNYNIIKIDP---NYEPAPIETKDVFGITFEQGRNELKIDEDLLKNIvtENKELPDEAKRDLIIALITLKYTQSNSVCY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 431 ARDGQTVGVGAGQMSRVDSARIASLKAE----------------------DAGLAV------------------------ 464
Cdd:PRK07106 234 AKDGQAIGIGAGQQSRIHCTRLAGNKADiwylrqhpkvlnlpfkegirrpDRDNAIdvylsddymdvladgvwqqfftek 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2751193822 465 ----------------AGAVMASDAFFPFRDGIDAAAKAGIRAVIQPGGSIRDEEVVAAADEADMAMLFTGMRHFRH 525
Cdd:PRK07106 314 pepltreekrawlatlTGVALGSDAFFPFGDNIERAAKSGVKYIAQPGGSIRDDNVIETCNKYGMTMAFTGVRLFHH 390
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
20-133 |
7.20e-26 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 214855 [Multi-domain] Cd Length: 91 Bit Score: 101.01 E-value: 7.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 20 GVAELAAALHQMDVEILSTGGTARTLREAGVPVtevsehtgapeimdgrVKTLHPKIHGGLLGrrdvdgpVMAEHGIAPI 99
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPV----------------VKTLHPKVHGGIPQ-------ILDLIKNGEI 57
|
90 100 110
....*....|....*....|....*....|....
gi 2751193822 100 DLLVVNLYPFRETVARPGCTPADAIENIDIGGPA 133
Cdd:smart00851 58 DLVINTLYPFEAQAHEDGYSIRRAAENIDIPGPT 91
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
20-133 |
1.53e-24 |
|
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: 97.56 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 20 GVAELAAALHQMDVEILSTGGTARTLREAGVPVTEVSEHTGAPeIMDGRVKtlhpkihggllgrrDVDgpVMAEHGiapI 99
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGEG-RPGGRVQ--------------IGD--LIKNGE---I 60
|
90 100 110
....*....|....*....|....*....|....
gi 2751193822 100 DLLVVNLYPFRETVaRPGCTPADAIENIDIGGPA 133
Cdd:pfam02142 61 DLVINTLYPFKATV-HDGYAIRRAAENIDIPGPT 93
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
10-67 |
1.14e-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: 55.95 E-value: 1.14e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2751193822 10 RALISV--SDKTGVAELAAALHQMDVEILSTGGTARTLREAGVPVTEVSE-HTGAPEIMDG 67
Cdd:cd01424 2 TVFISVadRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKvSEGRPNIVDL 62
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
10-157 |
1.68e-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: 52.51 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 10 RALISVSD--KTGVAELAAALHQMDVEILSTGGTARTLREAGVPVTEVSEHTGApeimdgrvktLHPKIHGGLLGRRDvd 87
Cdd:cd00532 1 GVFLSVSDhvKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHED----------GEPTVDAAIAEKGK-- 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 88 gpvmaehgiapIDLLVVNLYPFREtvarpgctpadaiENIDIGGPAMLRAAAKNHafVTVLVDAADYDGV 157
Cdd:cd00532 69 -----------FDVVINLRDPRRD-------------RCTDEDGTALLRLARLYK--IPVTTPNATAMFV 112
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
10-66 |
5.31e-08 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 55.87 E-value: 5.31e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751193822 10 RALISV--SDKTGVAELAAALHQMDVEILSTGGTARTLREAGVPVTEVSE-HTGAPEIMD 66
Cdd:PRK05294 939 TVFLSVrdRDKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELVNKvHEGRPHIVD 998
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
11-66 |
1.30e-05 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 48.24 E-value: 1.30e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2751193822 11 ALISVSDKT--GVAELAAALHQMDVEILSTGGTARTLREAGVPVTEVSE-HTGAPEIMD 66
Cdd:PLN02735 975 VFISLNDLTkpHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVLKlHEGRPHAGD 1033
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
9-68 |
8.70e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 42.26 E-value: 8.70e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2751193822 9 RRALISVSD--KTGVAELAAALHQMDVEILSTGGTARTLREAGVPVTEVSE-HTGAPEIMDGR 68
Cdd:PRK12815 938 GTIFISVRDedKPEVTKLARRFAQLGFKLLATEGTANWLAEEGITTGVVEKvQEGSPSLLERI 1000
|
|
| |
