|
Name |
Accession |
Description |
Interval |
E-value |
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
4-529 |
0e+00 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 1007.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 4 RRPVRRALLSVSDKAGIVEFAQALSARGVELLSTGGTARLLAEKGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRR 83
Cdd:PRK00881 1 RRMIKRALISVSDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVTGFPEILDGRVKTLHPKIHGGILARR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 84 GQDD--AIMEEHQIQPIDIVVVNLYPFAQTVAREGCSLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYDAIIKEMD 161
Cdd:PRK00881 81 DNPEhvAALEEHGIEPIDLVVVNLYPFEETVAKPGVTLEEAIENIDIGGPTMVRAAAKNHKDVAVVVDPADYDAVLEELK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 162 DNeGSLTLATRFDLAIKAFEHTAAYDSMIANYFGSMVPayhgeskeaaGRFPRTLNLNFIKKQDMRYGENSHQQAAFYIE 241
Cdd:PRK00881 161 AN-GSTTLETRFRLAAKAFAHTAAYDAAIANYLTEQVG----------EEFPETLNLSFEKKQDLRYGENPHQKAAFYRD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 242 ENVKeASVATATQVQGKALSYNNIADTDAALECVKEFAEPACVIVKHANPCGVAIGNSILDAYDRAYKTDPTSAFGGIIA 321
Cdd:PRK00881 230 PNAE-GGVATAEQLQGKELSYNNIADADAALELVKEFDEPACVIVKHANPCGVAVGDTILEAYDKAYACDPVSAFGGIIA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 322 FNRELDAETAQAIiSRQFVEVIIAPSASEEALKITAAKQNVRVLTCGQWGErvPGLDFKRVNGGLLVQDRDLGMVGAEEL 401
Cdd:PRK00881 309 FNREVDAETAEAI-HKIFLEVIIAPSFSEEALEILAKKKNLRLLECPFPGG--WEGDFKSVSGGLLVQDRDLGMVDPADL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 402 RVVTQRQPTEQELRDALFCWKVAKFVKSNAIVYAKNNMTIGIGAGQMSRVYSAKIAGIKAADEGLEVKGSSMASDAFFPF 481
Cdd:PRK00881 386 KVVTKRQPTEQELKDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEKAGDAGLDLKGAVLASDAFFPF 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 487499382 482 RDGIDAAAAAGVTCVIQPGGSIRDDEVIAAADEHGIAMLFTDMRPFRH 529
Cdd:PRK00881 466 RDGVEAAAKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGVRHFRH 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: 993.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 5 RPVRRALLSVSDKAGIVEFAQALSARGVELLSTGGTARLLAEKGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRG 84
Cdd:COG0138 1 VPIKRALISVSDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVTGFPEILDGRVKTLHPKIHGGILARRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 85 QDD--AIMEEHQIQPIDIVVVNLYPFAQTVAREGCSLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYDAIIKEMDD 162
Cdd:COG0138 81 NPEhvAQLEEHGIEPIDLVVVNLYPFEETVAKPGATLEEAIENIDIGGPAMLRAAAKNHADVAVVVDPADYDAVLEELKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 163 NeGSLTLATRFDLAIKAFEHTAAYDSMIANYFGSMVpayhgeskeAAGRFPRTLNLNFIKKQDMRYGENSHQQAAFYIEE 242
Cdd:COG0138 161 N-GGTSLETRRRLAAKAFAHTAAYDAAIANYLAEQL---------GEEEFPETLTLSFEKVQDLRYGENPHQKAAFYRDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 243 NvKEASVATATQVQGKALSYNNIADTDAALECVKEFAEPACVIVKHANPCGVAIGNSILDAYDRAYKTDPTSAFGGIIAF 322
Cdd:COG0138 231 G-AEGGLATAEQLQGKELSYNNILDADAALELVKEFDEPAVVIVKHANPCGVAVGDTLAEAYEKAYACDPVSAFGGIIAF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 323 NRELDAETAQAIiSRQFVEVIIAPSASEEALKITAAKQNVRVLTCGQWGERVPGLDFKRVNGGLLVQDRDLGMVGAEELR 402
Cdd:COG0138 310 NRPVDAATAEAI-AKIFLEVIIAPDFSPEALEILAKKKNLRLLELGGLDPPAPGLDVKSVSGGLLVQDRDLGLIDPADLK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 403 VVTQRQPTEQELRDALFCWKVAKFVKSNAIVYAKNNMTIGIGAGQMSRVYSAKIAGIKAADeglEVKGSSMASDAFFPFR 482
Cdd:COG0138 389 VVTKRAPTEEELADLLFAWKVVKHVKSNAIVLAKDGATVGIGAGQMSRVDSARIALEKAGE---RAKGSVLASDAFFPFR 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 487499382 483 DGIDAAAAAGVTCVIQPGGSIRDDEVIAAADEHGIAMLFTDMRPFRH 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: 919.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 8 RRALLSVSDKAGIVEFAQALSARGVELLSTGGTARLLAEKGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRGQD- 86
Cdd:TIGR00355 1 RRALLSVSDKTGIVEFAQGLVERGVELLSTGGTAKLLAEAGVPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILARRGDDd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 87 DAIMEEHQIQPIDIVVVNLYPFAQTVAREGCSLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYDAIIKEMDDnEGS 166
Cdd:TIGR00355 81 DADLEEHGIEPIDLVVVNLYPFKETVAKPGVTLAEAVENIDIGGPTMLRAAAKNHADVTILVDPKDYSAILSELDE-QGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 167 LTLATRFDLAIKAFEHTAAYDSMIANYFGSMVPayhgeSKEaagrfPRTLNLNFIKKQDMRYGENSHQQAAFYIEENVKE 246
Cdd:TIGR00355 160 ISLALRFDLAIKAFEHTAAYDAAIANYFGKLVG-----EKE-----PRQFNLNFTKKQTLRYGENPHQKAAFYVTQNVKE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 247 ASVATATQVQGKALSYNNIADTDAALECVKEFAEPACVIVKHANPCGVAIGNSILDAYDRAYKTDPTSAFGGIIAFNREL 326
Cdd:TIGR00355 230 GSVATAEQLQGKELSYNNIADADAALEIVKEFDEPAAVIVKHANPCGVALGKTILDAYDRAFGADPTSAFGGIIALNREL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 327 DAETAQAIIsRQFVEVIIAPSASEEALKITAAKQNVRVLTCGQWGERVPGLDFKRVNGGLLVQDRDLGMVGAEELRVVTQ 406
Cdd:TIGR00355 310 DVPTAKAIV-RQFLEVIIAPGYSAEALEILAKKKNLRVLILGIWANRVPELDFKRVNGGLLVQDRDDGMVDQSTLKVVTK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 407 RQPTEQELRDALFCWKVAKFVKSNAIVYAKNNMTIGIGAGQMSRVYSAKIAGIKAADEGLEVKGSSMASDAFFPFRDGID 486
Cdd:TIGR00355 389 RQPTEQELIDLLFAWKVAKHVKSNAIVYAKNNMTVGVGAGQMSRVGSAKIAGIKADDEGLEAKGSSLASDAFFPFRDGVE 468
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 487499382 487 AAAAAGVTCVIQPGGSIRDDEVIAAADEHGIAMLFTDMRPFRH 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: 560.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 137 AAKNHKDVAIVVKSSDYDAIIKEMDDNeGSLTLATRFDLAIKAFEHTAAYDSMIANYFgsmvpayhgeSKEAAGRFPRTL 216
Cdd:smart00798 1 AAKNHKDVTVVVDPADYAEVLEELKAN-GGLSLETRKRLAAKAFAHTAAYDAAISNYL----------AKQLASEFPETL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 217 NLNFIKKQDMRYGENSHQQAAFYIEENvKEASVATATQVQGKALSYNNIADTDAALECVKEFAEPACVIVKHANPCGVAI 296
Cdd:smart00798 70 TLSFEKKQDLRYGENPHQKAAFYTDPD-ALGGIATAKQLQGKELSYNNILDADAALELVKEFDEPACVIVKHANPCGVAV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 297 GNSILDAYDRAYKTDPTSAFGGIIAFNRELDAETAQAiISRQFVEVIIAPSASEEALKITAAKQNVRVLTCGQWGERvPG 376
Cdd:smart00798 149 GDTLAEAYRKAYAADPVSAFGGIIAFNRPVDEETAEA-INKIFLEVIIAPDFDEEALEILSKKKNLRLLECGPLPDP-DG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 377 LDFKRVNGGLLVQDRDLGMVGAEELRVVTQRQPTEQELRDALFCWKVAKFVKSNAIVYAKNNMTIGIGAGQMSRVYSAKI 456
Cdd:smart00798 227 LEFKSVSGGLLVQDRDNGGIDPEDLKVVTKRQPTEEELADLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARI 306
|
....*
gi 487499382 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: 549.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 137 AAKNHKDVAIVVKSSDYDAIIKEMDDNeGSLTLATRFDLAIKAFEHTAAYDSMIANYFgsmvpayhgeskeAAGRFPRTL 216
Cdd:pfam01808 1 AAKNHKDVTVVVDPADYAEVLEELKAN-GGTSLETRRRLAAKAFAHTAAYDAAIANYL-------------AGKEFPETL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 217 NLNFIKKQDMRYGENSHQQAAFYIEENVKeASVATATQVQGKALSYNNIADTDAALECVKEFAEPACVIVKHANPCGVAI 296
Cdd:pfam01808 67 TLSFEKVQDLRYGENPHQKAAFYRDPGPA-GGLATAEQLQGKELSYNNILDADAALELVKEFDEPAAVIVKHANPCGVAV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 297 GNSILDAYDRAYKTDPTSAFGGIIAFNRELDAETAQAIiSRQFVEVIIAPSASEEALKITAAKQNVRVLTCGQWGERVPG 376
Cdd:pfam01808 146 GDTLAEAYRRALAADPVSAFGGIIALNRPVDAATAEEI-SKIFLEVIIAPGFTPEALEILKKKKNLRLLEIDPLYPPPPG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 377 LDFKRVNGGLLVQDRDLGMVGAEELRVVTQRQPTEQELRDALFCWKVAKFVKSNAIVYAKNNMTIGIGAGQMSRVYSAKI 456
Cdd:pfam01808 225 LEFRSVSGGLLVQDRDDALIDPDDLKVVTKRAPTEEELRDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARI 304
|
....
gi 487499382 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 |
5.85e-115 |
|
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: 337.65 E-value: 5.85e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 8 RRALLSVSDKAGIVEFAQALSARGVELLSTGGTARLLAEKGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRG-QD 86
Cdd:cd01421 1 KRALISVSDKTGLVEFAKELVELGVEILSTGGTAKFLKEAGIPVTDVSDITGFPEILGGRVKTLHPKIHGGILARRDnEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 87 DAIMEEHQIQPIDIVVVNLYPFAQTVAREGCSLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYDAIIKEMDDNeGS 166
Cdd:cd01421 81 HKDLEEHGIEPIDLVVVNLYPFEETVAKGNVTLEEAIENIDIGGPSLLRAAAKNYKDVTVLVDPADYQKVLEELKSN-GS 159
|
170 180
....*....|....*....|....*...
gi 487499382 167 LTLATRFDLAIKAFEHTAAYDSMIANYF 194
Cdd:cd01421 160 ISEETRRRLALKAFAHTAEYDAAISNYL 187
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
4-529 |
0e+00 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 1007.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 4 RRPVRRALLSVSDKAGIVEFAQALSARGVELLSTGGTARLLAEKGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRR 83
Cdd:PRK00881 1 RRMIKRALISVSDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVTGFPEILDGRVKTLHPKIHGGILARR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 84 GQDD--AIMEEHQIQPIDIVVVNLYPFAQTVAREGCSLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYDAIIKEMD 161
Cdd:PRK00881 81 DNPEhvAALEEHGIEPIDLVVVNLYPFEETVAKPGVTLEEAIENIDIGGPTMVRAAAKNHKDVAVVVDPADYDAVLEELK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 162 DNeGSLTLATRFDLAIKAFEHTAAYDSMIANYFGSMVPayhgeskeaaGRFPRTLNLNFIKKQDMRYGENSHQQAAFYIE 241
Cdd:PRK00881 161 AN-GSTTLETRFRLAAKAFAHTAAYDAAIANYLTEQVG----------EEFPETLNLSFEKKQDLRYGENPHQKAAFYRD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 242 ENVKeASVATATQVQGKALSYNNIADTDAALECVKEFAEPACVIVKHANPCGVAIGNSILDAYDRAYKTDPTSAFGGIIA 321
Cdd:PRK00881 230 PNAE-GGVATAEQLQGKELSYNNIADADAALELVKEFDEPACVIVKHANPCGVAVGDTILEAYDKAYACDPVSAFGGIIA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 322 FNRELDAETAQAIiSRQFVEVIIAPSASEEALKITAAKQNVRVLTCGQWGErvPGLDFKRVNGGLLVQDRDLGMVGAEEL 401
Cdd:PRK00881 309 FNREVDAETAEAI-HKIFLEVIIAPSFSEEALEILAKKKNLRLLECPFPGG--WEGDFKSVSGGLLVQDRDLGMVDPADL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 402 RVVTQRQPTEQELRDALFCWKVAKFVKSNAIVYAKNNMTIGIGAGQMSRVYSAKIAGIKAADEGLEVKGSSMASDAFFPF 481
Cdd:PRK00881 386 KVVTKRQPTEQELKDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEKAGDAGLDLKGAVLASDAFFPF 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 487499382 482 RDGIDAAAAAGVTCVIQPGGSIRDDEVIAAADEHGIAMLFTDMRPFRH 529
Cdd:PRK00881 466 RDGVEAAAKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGVRHFRH 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: 993.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 5 RPVRRALLSVSDKAGIVEFAQALSARGVELLSTGGTARLLAEKGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRG 84
Cdd:COG0138 1 VPIKRALISVSDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVTGFPEILDGRVKTLHPKIHGGILARRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 85 QDD--AIMEEHQIQPIDIVVVNLYPFAQTVAREGCSLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYDAIIKEMDD 162
Cdd:COG0138 81 NPEhvAQLEEHGIEPIDLVVVNLYPFEETVAKPGATLEEAIENIDIGGPAMLRAAAKNHADVAVVVDPADYDAVLEELKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 163 NeGSLTLATRFDLAIKAFEHTAAYDSMIANYFGSMVpayhgeskeAAGRFPRTLNLNFIKKQDMRYGENSHQQAAFYIEE 242
Cdd:COG0138 161 N-GGTSLETRRRLAAKAFAHTAAYDAAIANYLAEQL---------GEEEFPETLTLSFEKVQDLRYGENPHQKAAFYRDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 243 NvKEASVATATQVQGKALSYNNIADTDAALECVKEFAEPACVIVKHANPCGVAIGNSILDAYDRAYKTDPTSAFGGIIAF 322
Cdd:COG0138 231 G-AEGGLATAEQLQGKELSYNNILDADAALELVKEFDEPAVVIVKHANPCGVAVGDTLAEAYEKAYACDPVSAFGGIIAF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 323 NRELDAETAQAIiSRQFVEVIIAPSASEEALKITAAKQNVRVLTCGQWGERVPGLDFKRVNGGLLVQDRDLGMVGAEELR 402
Cdd:COG0138 310 NRPVDAATAEAI-AKIFLEVIIAPDFSPEALEILAKKKNLRLLELGGLDPPAPGLDVKSVSGGLLVQDRDLGLIDPADLK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 403 VVTQRQPTEQELRDALFCWKVAKFVKSNAIVYAKNNMTIGIGAGQMSRVYSAKIAGIKAADeglEVKGSSMASDAFFPFR 482
Cdd:COG0138 389 VVTKRAPTEEELADLLFAWKVVKHVKSNAIVLAKDGATVGIGAGQMSRVDSARIALEKAGE---RAKGSVLASDAFFPFR 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 487499382 483 DGIDAAAAAGVTCVIQPGGSIRDDEVIAAADEHGIAMLFTDMRPFRH 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: 919.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 8 RRALLSVSDKAGIVEFAQALSARGVELLSTGGTARLLAEKGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRGQD- 86
Cdd:TIGR00355 1 RRALLSVSDKTGIVEFAQGLVERGVELLSTGGTAKLLAEAGVPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILARRGDDd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 87 DAIMEEHQIQPIDIVVVNLYPFAQTVAREGCSLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYDAIIKEMDDnEGS 166
Cdd:TIGR00355 81 DADLEEHGIEPIDLVVVNLYPFKETVAKPGVTLAEAVENIDIGGPTMLRAAAKNHADVTILVDPKDYSAILSELDE-QGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 167 LTLATRFDLAIKAFEHTAAYDSMIANYFGSMVPayhgeSKEaagrfPRTLNLNFIKKQDMRYGENSHQQAAFYIEENVKE 246
Cdd:TIGR00355 160 ISLALRFDLAIKAFEHTAAYDAAIANYFGKLVG-----EKE-----PRQFNLNFTKKQTLRYGENPHQKAAFYVTQNVKE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 247 ASVATATQVQGKALSYNNIADTDAALECVKEFAEPACVIVKHANPCGVAIGNSILDAYDRAYKTDPTSAFGGIIAFNREL 326
Cdd:TIGR00355 230 GSVATAEQLQGKELSYNNIADADAALEIVKEFDEPAAVIVKHANPCGVALGKTILDAYDRAFGADPTSAFGGIIALNREL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 327 DAETAQAIIsRQFVEVIIAPSASEEALKITAAKQNVRVLTCGQWGERVPGLDFKRVNGGLLVQDRDLGMVGAEELRVVTQ 406
Cdd:TIGR00355 310 DVPTAKAIV-RQFLEVIIAPGYSAEALEILAKKKNLRVLILGIWANRVPELDFKRVNGGLLVQDRDDGMVDQSTLKVVTK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 407 RQPTEQELRDALFCWKVAKFVKSNAIVYAKNNMTIGIGAGQMSRVYSAKIAGIKAADEGLEVKGSSMASDAFFPFRDGID 486
Cdd:TIGR00355 389 RQPTEQELIDLLFAWKVAKHVKSNAIVYAKNNMTVGVGAGQMSRVGSAKIAGIKADDEGLEAKGSSLASDAFFPFRDGVE 468
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 487499382 487 AAAAAGVTCVIQPGGSIRDDEVIAAADEHGIAMLFTDMRPFRH 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: 560.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 137 AAKNHKDVAIVVKSSDYDAIIKEMDDNeGSLTLATRFDLAIKAFEHTAAYDSMIANYFgsmvpayhgeSKEAAGRFPRTL 216
Cdd:smart00798 1 AAKNHKDVTVVVDPADYAEVLEELKAN-GGLSLETRKRLAAKAFAHTAAYDAAISNYL----------AKQLASEFPETL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 217 NLNFIKKQDMRYGENSHQQAAFYIEENvKEASVATATQVQGKALSYNNIADTDAALECVKEFAEPACVIVKHANPCGVAI 296
Cdd:smart00798 70 TLSFEKKQDLRYGENPHQKAAFYTDPD-ALGGIATAKQLQGKELSYNNILDADAALELVKEFDEPACVIVKHANPCGVAV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 297 GNSILDAYDRAYKTDPTSAFGGIIAFNRELDAETAQAiISRQFVEVIIAPSASEEALKITAAKQNVRVLTCGQWGERvPG 376
Cdd:smart00798 149 GDTLAEAYRKAYAADPVSAFGGIIAFNRPVDEETAEA-INKIFLEVIIAPDFDEEALEILSKKKNLRLLECGPLPDP-DG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 377 LDFKRVNGGLLVQDRDLGMVGAEELRVVTQRQPTEQELRDALFCWKVAKFVKSNAIVYAKNNMTIGIGAGQMSRVYSAKI 456
Cdd:smart00798 227 LEFKSVSGGLLVQDRDNGGIDPEDLKVVTKRQPTEEELADLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARI 306
|
....*
gi 487499382 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: 549.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 137 AAKNHKDVAIVVKSSDYDAIIKEMDDNeGSLTLATRFDLAIKAFEHTAAYDSMIANYFgsmvpayhgeskeAAGRFPRTL 216
Cdd:pfam01808 1 AAKNHKDVTVVVDPADYAEVLEELKAN-GGTSLETRRRLAAKAFAHTAAYDAAIANYL-------------AGKEFPETL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 217 NLNFIKKQDMRYGENSHQQAAFYIEENVKeASVATATQVQGKALSYNNIADTDAALECVKEFAEPACVIVKHANPCGVAI 296
Cdd:pfam01808 67 TLSFEKVQDLRYGENPHQKAAFYRDPGPA-GGLATAEQLQGKELSYNNILDADAALELVKEFDEPAAVIVKHANPCGVAV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 297 GNSILDAYDRAYKTDPTSAFGGIIAFNRELDAETAQAIiSRQFVEVIIAPSASEEALKITAAKQNVRVLTCGQWGERVPG 376
Cdd:pfam01808 146 GDTLAEAYRRALAADPVSAFGGIIALNRPVDAATAEEI-SKIFLEVIIAPGFTPEALEILKKKKNLRLLEIDPLYPPPPG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 377 LDFKRVNGGLLVQDRDLGMVGAEELRVVTQRQPTEQELRDALFCWKVAKFVKSNAIVYAKNNMTIGIGAGQMSRVYSAKI 456
Cdd:pfam01808 225 LEFRSVSGGLLVQDRDDALIDPDDLKVVTKRAPTEEELRDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARI 304
|
....
gi 487499382 457 AGIK 460
Cdd:pfam01808 305 AIEK 308
|
|
| PLN02891 |
PLN02891 |
IMP cyclohydrolase |
7-529 |
0e+00 |
|
IMP cyclohydrolase
Pssm-ID: 178479 [Multi-domain] Cd Length: 547 Bit Score: 535.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 7 VRRALLSVSDKAGIVEFAQALSARGVELLSTGGTARLLAEKGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRGQD 86
Cdd:PLN02891 22 KKQALISLSDKTDLALLANGLQELGYTIVSTGGTASALEAAGVSVTKVEELTNFPEMLDGRVKTLHPAVHGGILARRDQE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 87 ---DAImEEHQIQPIDIVVVNLYPFAQTVAREGCSLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYDAII---KEM 160
Cdd:PLN02891 102 hhmEAL-NEHGIGTIDVVVVNLYPFYDTVTSGGISFEDGVENIDIGGPAMIRAAAKNHKDVLVVVDPADYPALLeylKGK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 161 DDNEGSLtlatRFDLAIKAFEHTAAYDSMIANYFGSMVpayhgeskEAAGRFPRTLNLNFIKKQDMRYGENSHQQAAFYI 240
Cdd:PLN02891 181 QDDQQDF----RRKLAWKAFQHVASYDSAVSEWLWKQI--------NGGGKFPPSLTVPLTLKSSLRYGENPHQKAAFYV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 241 EENVKEAS---VATATQVQGKALSYNNIADTDAALECVKEFAEPACVIVKHANPCGVAIGNSILDAYDRAYKTDPTSAFG 317
Cdd:PLN02891 249 DKSLSEVNaggIATAIQHHGKEMSYNNYLDADAAWNCVSEFSNPTCVVVKHTNPCGVASRGDILEAYRLAVRADPVSAFG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 318 GIIAFNRELDAETAQAII---------SRQFVEVIIAPSASEEALKITAAK-QNVRVLtcgQWGERVPG-LDFKRVNGGL 386
Cdd:PLN02891 329 GIVAFNCEVDEDLAREIRefrsptdgeTRMFYEIVVAPKYTEKGLEVLKGKsKTLRIL---EAKPRKKGrLSLRQVGGGW 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 387 LVQDRDLGMVGAEELRVVTQRQPTEQELRDALFCWKVAKFVKSNAIVYAKNNMTIGIGAGQMSRVYSAKIAGIKAADegl 466
Cdd:PLN02891 406 LAQDSDDLTPEDITFTVVSEKVPTESELEDAKFAWLCVKHVKSNAIVVAKNNRMLGMGSGQPNRVESLRIALEKAGE--- 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487499382 467 EVKGSSMASDAFFPF--RDGIDAAAAAGVTCVIQPGGSIRDDEVIAAADEHGIAMLFTDMRPFRH 529
Cdd:PLN02891 483 EAKGAALASDAFFPFawNDAVEEACQAGVKVIAEPGGSMRDQDAIDCCNKYGVALLFTGVRHFRH 547
|
|
| IMPCH |
cd01421 |
Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine ... |
8-194 |
5.85e-115 |
|
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: 337.65 E-value: 5.85e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 8 RRALLSVSDKAGIVEFAQALSARGVELLSTGGTARLLAEKGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRG-QD 86
Cdd:cd01421 1 KRALISVSDKTGLVEFAKELVELGVEILSTGGTAKFLKEAGIPVTDVSDITGFPEILGGRVKTLHPKIHGGILARRDnEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 87 DAIMEEHQIQPIDIVVVNLYPFAQTVAREGCSLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYDAIIKEMDDNeGS 166
Cdd:cd01421 81 HKDLEEHGIEPIDLVVVNLYPFEETVAKGNVTLEEAIENIDIGGPSLLRAAAKNYKDVTVLVDPADYQKVLEELKSN-GS 159
|
170 180
....*....|....*....|....*...
gi 487499382 167 LTLATRFDLAIKAFEHTAAYDSMIANYF 194
Cdd:cd01421 160 ISEETRRRLALKAFAHTAEYDAAISNYL 187
|
|
| PRK07106 |
PRK07106 |
phosphoribosylaminoimidazolecarboxamide formyltransferase; |
226-529 |
1.24e-53 |
|
phosphoribosylaminoimidazolecarboxamide formyltransferase;
Pssm-ID: 180841 Cd Length: 390 Bit Score: 186.02 E-value: 1.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 226 MRYGENSHQQAA-FYIEENVKEASVatatqVQGKAlSYNNIADTDAALECVKE----FAEPACVIVKHANPCGVAIGNSI 300
Cdd:PRK07106 6 LKYGCNPNQKPArIFMKEGELPIEV-----LNGRP-GYINFLDALNSWQLVKElkeaTGLPAAASFKHVSPAGAAVGLPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 301 LD------------------AYDRAYKTDPTSAFGGIIAFNRELDAETAQaIISRQFVEVIIAPSASEEALKITAAKQNV 362
Cdd:PRK07106 80 SDtlkkiyfvddmelsplacAYARARGADRMSSYGDFAALSDVCDVETAK-LLKREVSDGIIAPGYTPEALEILKAKKKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 363 RVLTCGQWGERVP-GLDFKRVNGGLLVQDRDLGMVGAEELR--VVTQRQPTEQELRDALFCWKVAKFVKSNAIVYAKNNM 439
Cdd:PRK07106 159 NYNIIKIDPNYEPaPIETKDVFGITFEQGRNELKIDEDLLKniVTENKELPDEAKRDLIIALITLKYTQSNSVCYAKDGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 440 TIGIGAGQMSRVYSAKIAGIKA---------------------------------ADEGLEV------------------ 468
Cdd:PRK07106 239 AIGIGAGQQSRIHCTRLAGNKAdiwylrqhpkvlnlpfkegirrpdrdnaidvylSDDYMDVladgvwqqfftekpeplt 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487499382 469 -----------KGSSMASDAFFPFRDGIDAAAAAGVTCVIQPGGSIRDDEVIAAADEHGIAMLFTDMRPFRH 529
Cdd:PRK07106 319 reekrawlatlTGVALGSDAFFPFGDNIERAAKSGVKYIAQPGGSIRDDNVIETCNKYGMTMAFTGVRLFHH 390
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
19-132 |
7.79e-32 |
|
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: 117.57 E-value: 7.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 19 GIVEFAQALSARGVELLSTGGTARLLAEKGLPVtevsdytgfpemmdgrVKTLHPKVHGGILgrrgqddAIMEEHQIQPI 98
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPV----------------VKTLHPKVHGGIP-------QILDLIKNGEI 57
|
90 100 110
....*....|....*....|....*....|....
gi 487499382 99 DIVVVNLYPFAQTVAREGCSLEDAVENIDIGGPT 132
Cdd:smart00851 58 DLVINTLYPFEAQAHEDGYSIRRAAENIDIPGPT 91
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
19-132 |
5.84e-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: 460462 [Multi-domain] Cd Length: 93 Bit Score: 112.58 E-value: 5.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 19 GIVEFAQALSARGVELLSTGGTARLLAEKGLPVTEVSDYTGFPeMMDGRVktlhpkvhggilgrrgQDDAIMEEHQiqpI 98
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGEG-RPGGRV----------------QIGDLIKNGE---I 60
|
90 100 110
....*....|....*....|....*....|....
gi 487499382 99 DIVVVNLYPFAQTVaREGCSLEDAVENIDIGGPT 132
Cdd:pfam02142 61 DLVINTLYPFKATV-HDGYAIRRAAENIDIPGPT 93
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
9-141 |
4.02e-13 |
|
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: 65.61 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 9 RALLSVSD--KAGIVEFAQALSARGVELLSTGGTARLLAEKGLPVTEVSDYTGFpemmdgrvktLHPKVHGGILgrrgqd 86
Cdd:cd00532 1 GVFLSVSDhvKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHED----------GEPTVDAAIA------ 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 487499382 87 daimEEHQiqpIDIVVVNLYPFAQtvaregcsledavENIDIGGPTMVRSAAKNH 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 |
9.00e-08 |
|
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate synthetase (CSP). CSP, a CarA and CarB heterodimer, catalyzes the production of carbamoyl phosphate which is subsequently employed in the metabolic pathways responsible for the synthesis of pyrimidine nucleotides or arginine. The MGS-like domain is the C-terminal domain of CarB and appears to play a regulatory role in CPS function by binding allosteric effector molecules, including UMP and ornithine.
Pssm-ID: 238712 [Multi-domain] Cd Length: 110 Bit Score: 50.56 E-value: 9.00e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487499382 9 RALLSV--SDKAGIVEFAQALSARGVELLSTGGTARLLAEKGLPVTEVS-DYTGFPEMMDG 66
Cdd:cd01424 2 TVFISVadRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNkVSEGRPNIVDL 62
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
9-54 |
2.06e-06 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 50.87 E-value: 2.06e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 487499382 9 RALLSV--SDKAGIVEFAQALSARGVELLSTGGTARLLAEKGLPVTEV 54
Cdd:PRK05294 939 TVFLSVrdRDKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELV 986
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
3-67 |
7.03e-04 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 42.46 E-value: 7.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487499382 3 QRRPVR-RALLSVSD--KAGIVEFAQALSARGVELLSTGGTARLLAEKGLPVTEVsdytgfPEMMDGR 67
Cdd:PLN02735 967 QRLPLSgTVFISLNDltKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERV------LKLHEGR 1028
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
8-90 |
3.18e-03 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 40.34 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487499382 8 RRALLSVSD--KAGIVEFAQALSARGVELLSTGGTARLLAEKGLPVTEVSD-YTGFPEMMDGRVKTLHPKVHGGILGRRG 84
Cdd:PRK12815 938 GTIFISVRDedKPEVTKLARRFAQLGFKLLATEGTANWLAEEGITTGVVEKvQEGSPSLLERIKQHRIVLVVNTSLSDSA 1017
|
....*.
gi 487499382 85 QDDAIM 90
Cdd:PRK12815 1018 SEDAIK 1023
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
11-62 |
5.48e-03 |
|
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases (CPS), including ammonia-dependent CPS Type I, and glutamine-dependent CPS Type III. These are multidomain proteins, in which MGS is the C-terminal domain.
Pssm-ID: 238711 [Multi-domain] Cd Length: 116 Bit Score: 36.89 E-value: 5.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 487499382 11 LLS--VSDKAGIVEFAQALSARGVELLSTGGTARLLAEKGLPVTEVSDYTGFPE 62
Cdd:cd01423 4 LISigSYSKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQ 57
|
|
| |
