|
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: 1020.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 4 RRPVRRALLSVSDKAGIVEFAQALSARGVELLSTGGTARLLADKGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRR 83
Cdd:PRK00881 1 RRMIKRALISVSDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVTGFPEILDGRVKTLHPKIHGGILARR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 84 GQDDGI--MQQHGIAPIDMVVVNLYPFAQTVAREGCSLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYDAIINEMD 161
Cdd:PRK00881 81 DNPEHVaaLEEHGIEPIDLVVVNLYPFEETVAKPGVTLEEAIENIDIGGPTMVRAAAKNHKDVAVVVDPADYDAVLEELK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 162 ANeGSLTLATRFDLAIKAFEHTAAYDSMIANYFGSMVPayhgeskeaaGRFPRTLNLNFIKKQDMRYGENSHQQAAFYIE 241
Cdd:PRK00881 161 AN-GSTTLETRFRLAAKAFAHTAAYDAAIANYLTEQVG----------EEFPETLNLSFEKKQDLRYGENPHQKAAFYRD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 242 ENVKeASVATATQLQGKALSYNNIADTDAALECVKEFNEPACVIVKHANPCGVAVSNSILDAYDRAYKTDPTSAFGGIIA 321
Cdd:PRK00881 230 PNAE-GGVATAEQLQGKELSYNNIADADAALELVKEFDEPACVIVKHANPCGVAVGDTILEAYDKAYACDPVSAFGGIIA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 322 FNRELDAETAQAIiSRQFVEVIIAPSASEEALKITAAKQNVRVLTCGqwDTRVAGLDFKRVNGGLLVQDHDLGMVTAGEL 401
Cdd:PRK00881 309 FNREVDAETAEAI-HKIFLEVIIAPSFSEEALEILAKKKNLRLLECP--FPGGWEGDFKSVSGGLLVQDRDLGMVDPADL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 402 RVVSKRQPTEQELRDALFCWKVAKFVKSNAIVYAKDNMTIGIGAGQMSRVYSAKIAGIKAGDEGLEVKGSAMASDAFFPF 481
Cdd:PRK00881 386 KVVTKRQPTEQELKDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEKAGDAGLDLKGAVLASDAFFPF 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 694089016 482 RDGIDAAAAVGITCVIQPGGSIRDDEVIAAADEHGIAMIFTDMRHFRH 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: 1009.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 5 RPVRRALLSVSDKAGIVEFAQALSARGVELLSTGGTARLLADKGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRG 84
Cdd:COG0138 1 VPIKRALISVSDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVTGFPEILDGRVKTLHPKIHGGILARRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 85 QDDGI--MQQHGIAPIDMVVVNLYPFAQTVAREGCSLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYDAIINEMDA 162
Cdd:COG0138 81 NPEHVaqLEEHGIEPIDLVVVNLYPFEETVAKPGATLEEAIENIDIGGPAMLRAAAKNHADVAVVVDPADYDAVLEELKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 163 NeGSLTLATRFDLAIKAFEHTAAYDSMIANYFGSMVpayhgeskeAAGRFPRTLNLNFIKKQDMRYGENSHQQAAFYIEE 242
Cdd:COG0138 161 N-GGTSLETRRRLAAKAFAHTAAYDAAIANYLAEQL---------GEEEFPETLTLSFEKVQDLRYGENPHQKAAFYRDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 243 NvKEASVATATQLQGKALSYNNIADTDAALECVKEFNEPACVIVKHANPCGVAVSNSILDAYDRAYKTDPTSAFGGIIAF 322
Cdd:COG0138 231 G-AEGGLATAEQLQGKELSYNNILDADAALELVKEFDEPAVVIVKHANPCGVAVGDTLAEAYEKAYACDPVSAFGGIIAF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 323 NRELDAETAQAIiSRQFVEVIIAPSASEEALKITAAKQNVRVLTCGQWDTRVAGLDFKRVNGGLLVQDHDLGMVTAGELR 402
Cdd:COG0138 310 NRPVDAATAEAI-AKIFLEVIIAPDFSPEALEILAKKKNLRLLELGGLDPPAPGLDVKSVSGGLLVQDRDLGLIDPADLK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 403 VVSKRQPTEQELRDALFCWKVAKFVKSNAIVYAKDNMTIGIGAGQMSRVYSAKIAGIKAGDeglEVKGSAMASDAFFPFR 482
Cdd:COG0138 389 VVTKRAPTEEELADLLFAWKVVKHVKSNAIVLAKDGATVGIGAGQMSRVDSARIALEKAGE---RAKGSVLASDAFFPFR 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 694089016 483 DGIDAAAAVGITCVIQPGGSIRDDEVIAAADEHGIAMIFTDMRHFRH 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: 908.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 8 RRALLSVSDKAGIVEFAQALSARGVELLSTGGTARLLADKGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRGQD- 86
Cdd:TIGR00355 1 RRALLSVSDKTGIVEFAQGLVERGVELLSTGGTAKLLAEAGVPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILARRGDDd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 87 DGIMQQHGIAPIDMVVVNLYPFAQTVAREGCSLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYDAIINEMDaNEGS 166
Cdd:TIGR00355 81 DADLEEHGIEPIDLVVVNLYPFKETVAKPGVTLAEAVENIDIGGPTMLRAAAKNHADVTILVDPKDYSAILSELD-EQGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 167 LTLATRFDLAIKAFEHTAAYDSMIANYFGSMVPayhgeSKEaagrfPRTLNLNFIKKQDMRYGENSHQQAAFYIEENVKE 246
Cdd:TIGR00355 160 ISLALRFDLAIKAFEHTAAYDAAIANYFGKLVG-----EKE-----PRQFNLNFTKKQTLRYGENPHQKAAFYVTQNVKE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 247 ASVATATQLQGKALSYNNIADTDAALECVKEFNEPACVIVKHANPCGVAVSNSILDAYDRAYKTDPTSAFGGIIAFNREL 326
Cdd:TIGR00355 230 GSVATAEQLQGKELSYNNIADADAALEIVKEFDEPAAVIVKHANPCGVALGKTILDAYDRAFGADPTSAFGGIIALNREL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 327 DAETAQAIIsRQFVEVIIAPSASEEALKITAAKQNVRVLTCGQWDTRVAGLDFKRVNGGLLVQDHDLGMVTAGELRVVSK 406
Cdd:TIGR00355 310 DVPTAKAIV-RQFLEVIIAPGYSAEALEILAKKKNLRVLILGIWANRVPELDFKRVNGGLLVQDRDDGMVDQSTLKVVTK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 407 RQPTEQELRDALFCWKVAKFVKSNAIVYAKDNMTIGIGAGQMSRVYSAKIAGIKAGDEGLEVKGSAMASDAFFPFRDGID 486
Cdd:TIGR00355 389 RQPTEQELIDLLFAWKVAKHVKSNAIVYAKNNMTVGVGAGQMSRVGSAKIAGIKADDEGLEAKGSSLASDAFFPFRDGVE 468
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 694089016 487 AAAAVGITCVIQPGGSIRDDEVIAAADEHGIAMIFTDMRHFRH 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: 554.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 137 AAKNHKDVAIVVKSSDYDAIINEMDANeGSLTLATRFDLAIKAFEHTAAYDSMIANYFgsmvpayhgeSKEAAGRFPRTL 216
Cdd:smart00798 1 AAKNHKDVTVVVDPADYAEVLEELKAN-GGLSLETRKRLAAKAFAHTAAYDAAISNYL----------AKQLASEFPETL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 217 NLNFIKKQDMRYGENSHQQAAFYIEENvKEASVATATQLQGKALSYNNIADTDAALECVKEFNEPACVIVKHANPCGVAV 296
Cdd:smart00798 70 TLSFEKKQDLRYGENPHQKAAFYTDPD-ALGGIATAKQLQGKELSYNNILDADAALELVKEFDEPACVIVKHANPCGVAV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 297 SNSILDAYDRAYKTDPTSAFGGIIAFNRELDAETAQAiISRQFVEVIIAPSASEEALKITAAKQNVRVLTCGQWDTRvAG 376
Cdd:smart00798 149 GDTLAEAYRKAYAADPVSAFGGIIAFNRPVDEETAEA-INKIFLEVIIAPDFDEEALEILSKKKNLRLLECGPLPDP-DG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 377 LDFKRVNGGLLVQDHDLGMVTAGELRVVSKRQPTEQELRDALFCWKVAKFVKSNAIVYAKDNMTIGIGAGQMSRVYSAKI 456
Cdd:smart00798 227 LEFKSVSGGLLVQDRDNGGIDPEDLKVVTKRQPTEEELADLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARI 306
|
....*
gi 694089016 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: 543.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 137 AAKNHKDVAIVVKSSDYDAIINEMDANeGSLTLATRFDLAIKAFEHTAAYDSMIANYFgsmvpayhgeskeAAGRFPRTL 216
Cdd:pfam01808 1 AAKNHKDVTVVVDPADYAEVLEELKAN-GGTSLETRRRLAAKAFAHTAAYDAAIANYL-------------AGKEFPETL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 217 NLNFIKKQDMRYGENSHQQAAFYIEENVKeASVATATQLQGKALSYNNIADTDAALECVKEFNEPACVIVKHANPCGVAV 296
Cdd:pfam01808 67 TLSFEKVQDLRYGENPHQKAAFYRDPGPA-GGLATAEQLQGKELSYNNILDADAALELVKEFDEPAAVIVKHANPCGVAV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 297 SNSILDAYDRAYKTDPTSAFGGIIAFNRELDAETAQAIiSRQFVEVIIAPSASEEALKITAAKQNVRVLTCGQWDTRVAG 376
Cdd:pfam01808 146 GDTLAEAYRRALAADPVSAFGGIIALNRPVDAATAEEI-SKIFLEVIIAPGFTPEALEILKKKKNLRLLEIDPLYPPPPG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 377 LDFKRVNGGLLVQDHDLGMVTAGELRVVSKRQPTEQELRDALFCWKVAKFVKSNAIVYAKDNMTIGIGAGQMSRVYSAKI 456
Cdd:pfam01808 225 LEFRSVSGGLLVQDRDDALIDPDDLKVVTKRAPTEEELRDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARI 304
|
....
gi 694089016 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 |
2.80e-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: 2.80e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 8 RRALLSVSDKAGIVEFAQALSARGVELLSTGGTARLLADKGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRG-QD 86
Cdd:cd01421 1 KRALISVSDKTGLVEFAKELVELGVEILSTGGTAKFLKEAGIPVTDVSDITGFPEILGGRVKTLHPKIHGGILARRDnEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 87 DGIMQQHGIAPIDMVVVNLYPFAQTVAREGCSLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYDAIINEMDANeGS 166
Cdd:cd01421 81 HKDLEEHGIEPIDLVVVNLYPFEETVAKGNVTLEEAIENIDIGGPSLLRAAAKNYKDVTVLVDPADYQKVLEELKSN-GS 159
|
170 180
....*....|....*....|....*...
gi 694089016 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: 1020.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 4 RRPVRRALLSVSDKAGIVEFAQALSARGVELLSTGGTARLLADKGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRR 83
Cdd:PRK00881 1 RRMIKRALISVSDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVTGFPEILDGRVKTLHPKIHGGILARR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 84 GQDDGI--MQQHGIAPIDMVVVNLYPFAQTVAREGCSLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYDAIINEMD 161
Cdd:PRK00881 81 DNPEHVaaLEEHGIEPIDLVVVNLYPFEETVAKPGVTLEEAIENIDIGGPTMVRAAAKNHKDVAVVVDPADYDAVLEELK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 162 ANeGSLTLATRFDLAIKAFEHTAAYDSMIANYFGSMVPayhgeskeaaGRFPRTLNLNFIKKQDMRYGENSHQQAAFYIE 241
Cdd:PRK00881 161 AN-GSTTLETRFRLAAKAFAHTAAYDAAIANYLTEQVG----------EEFPETLNLSFEKKQDLRYGENPHQKAAFYRD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 242 ENVKeASVATATQLQGKALSYNNIADTDAALECVKEFNEPACVIVKHANPCGVAVSNSILDAYDRAYKTDPTSAFGGIIA 321
Cdd:PRK00881 230 PNAE-GGVATAEQLQGKELSYNNIADADAALELVKEFDEPACVIVKHANPCGVAVGDTILEAYDKAYACDPVSAFGGIIA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 322 FNRELDAETAQAIiSRQFVEVIIAPSASEEALKITAAKQNVRVLTCGqwDTRVAGLDFKRVNGGLLVQDHDLGMVTAGEL 401
Cdd:PRK00881 309 FNREVDAETAEAI-HKIFLEVIIAPSFSEEALEILAKKKNLRLLECP--FPGGWEGDFKSVSGGLLVQDRDLGMVDPADL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 402 RVVSKRQPTEQELRDALFCWKVAKFVKSNAIVYAKDNMTIGIGAGQMSRVYSAKIAGIKAGDEGLEVKGSAMASDAFFPF 481
Cdd:PRK00881 386 KVVTKRQPTEQELKDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEKAGDAGLDLKGAVLASDAFFPF 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 694089016 482 RDGIDAAAAVGITCVIQPGGSIRDDEVIAAADEHGIAMIFTDMRHFRH 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: 1009.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 5 RPVRRALLSVSDKAGIVEFAQALSARGVELLSTGGTARLLADKGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRG 84
Cdd:COG0138 1 VPIKRALISVSDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVTGFPEILDGRVKTLHPKIHGGILARRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 85 QDDGI--MQQHGIAPIDMVVVNLYPFAQTVAREGCSLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYDAIINEMDA 162
Cdd:COG0138 81 NPEHVaqLEEHGIEPIDLVVVNLYPFEETVAKPGATLEEAIENIDIGGPAMLRAAAKNHADVAVVVDPADYDAVLEELKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 163 NeGSLTLATRFDLAIKAFEHTAAYDSMIANYFGSMVpayhgeskeAAGRFPRTLNLNFIKKQDMRYGENSHQQAAFYIEE 242
Cdd:COG0138 161 N-GGTSLETRRRLAAKAFAHTAAYDAAIANYLAEQL---------GEEEFPETLTLSFEKVQDLRYGENPHQKAAFYRDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 243 NvKEASVATATQLQGKALSYNNIADTDAALECVKEFNEPACVIVKHANPCGVAVSNSILDAYDRAYKTDPTSAFGGIIAF 322
Cdd:COG0138 231 G-AEGGLATAEQLQGKELSYNNILDADAALELVKEFDEPAVVIVKHANPCGVAVGDTLAEAYEKAYACDPVSAFGGIIAF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 323 NRELDAETAQAIiSRQFVEVIIAPSASEEALKITAAKQNVRVLTCGQWDTRVAGLDFKRVNGGLLVQDHDLGMVTAGELR 402
Cdd:COG0138 310 NRPVDAATAEAI-AKIFLEVIIAPDFSPEALEILAKKKNLRLLELGGLDPPAPGLDVKSVSGGLLVQDRDLGLIDPADLK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 403 VVSKRQPTEQELRDALFCWKVAKFVKSNAIVYAKDNMTIGIGAGQMSRVYSAKIAGIKAGDeglEVKGSAMASDAFFPFR 482
Cdd:COG0138 389 VVTKRAPTEEELADLLFAWKVVKHVKSNAIVLAKDGATVGIGAGQMSRVDSARIALEKAGE---RAKGSVLASDAFFPFR 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 694089016 483 DGIDAAAAVGITCVIQPGGSIRDDEVIAAADEHGIAMIFTDMRHFRH 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: 908.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 8 RRALLSVSDKAGIVEFAQALSARGVELLSTGGTARLLADKGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRGQD- 86
Cdd:TIGR00355 1 RRALLSVSDKTGIVEFAQGLVERGVELLSTGGTAKLLAEAGVPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILARRGDDd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 87 DGIMQQHGIAPIDMVVVNLYPFAQTVAREGCSLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYDAIINEMDaNEGS 166
Cdd:TIGR00355 81 DADLEEHGIEPIDLVVVNLYPFKETVAKPGVTLAEAVENIDIGGPTMLRAAAKNHADVTILVDPKDYSAILSELD-EQGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 167 LTLATRFDLAIKAFEHTAAYDSMIANYFGSMVPayhgeSKEaagrfPRTLNLNFIKKQDMRYGENSHQQAAFYIEENVKE 246
Cdd:TIGR00355 160 ISLALRFDLAIKAFEHTAAYDAAIANYFGKLVG-----EKE-----PRQFNLNFTKKQTLRYGENPHQKAAFYVTQNVKE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 247 ASVATATQLQGKALSYNNIADTDAALECVKEFNEPACVIVKHANPCGVAVSNSILDAYDRAYKTDPTSAFGGIIAFNREL 326
Cdd:TIGR00355 230 GSVATAEQLQGKELSYNNIADADAALEIVKEFDEPAAVIVKHANPCGVALGKTILDAYDRAFGADPTSAFGGIIALNREL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 327 DAETAQAIIsRQFVEVIIAPSASEEALKITAAKQNVRVLTCGQWDTRVAGLDFKRVNGGLLVQDHDLGMVTAGELRVVSK 406
Cdd:TIGR00355 310 DVPTAKAIV-RQFLEVIIAPGYSAEALEILAKKKNLRVLILGIWANRVPELDFKRVNGGLLVQDRDDGMVDQSTLKVVTK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 407 RQPTEQELRDALFCWKVAKFVKSNAIVYAKDNMTIGIGAGQMSRVYSAKIAGIKAGDEGLEVKGSAMASDAFFPFRDGID 486
Cdd:TIGR00355 389 RQPTEQELIDLLFAWKVAKHVKSNAIVYAKNNMTVGVGAGQMSRVGSAKIAGIKADDEGLEAKGSSLASDAFFPFRDGVE 468
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 694089016 487 AAAAVGITCVIQPGGSIRDDEVIAAADEHGIAMIFTDMRHFRH 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: 554.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 137 AAKNHKDVAIVVKSSDYDAIINEMDANeGSLTLATRFDLAIKAFEHTAAYDSMIANYFgsmvpayhgeSKEAAGRFPRTL 216
Cdd:smart00798 1 AAKNHKDVTVVVDPADYAEVLEELKAN-GGLSLETRKRLAAKAFAHTAAYDAAISNYL----------AKQLASEFPETL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 217 NLNFIKKQDMRYGENSHQQAAFYIEENvKEASVATATQLQGKALSYNNIADTDAALECVKEFNEPACVIVKHANPCGVAV 296
Cdd:smart00798 70 TLSFEKKQDLRYGENPHQKAAFYTDPD-ALGGIATAKQLQGKELSYNNILDADAALELVKEFDEPACVIVKHANPCGVAV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 297 SNSILDAYDRAYKTDPTSAFGGIIAFNRELDAETAQAiISRQFVEVIIAPSASEEALKITAAKQNVRVLTCGQWDTRvAG 376
Cdd:smart00798 149 GDTLAEAYRKAYAADPVSAFGGIIAFNRPVDEETAEA-INKIFLEVIIAPDFDEEALEILSKKKNLRLLECGPLPDP-DG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 377 LDFKRVNGGLLVQDHDLGMVTAGELRVVSKRQPTEQELRDALFCWKVAKFVKSNAIVYAKDNMTIGIGAGQMSRVYSAKI 456
Cdd:smart00798 227 LEFKSVSGGLLVQDRDNGGIDPEDLKVVTKRQPTEEELADLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARI 306
|
....*
gi 694089016 457 AGIKA 461
Cdd:smart00798 307 AAEKA 311
|
|
| PLN02891 |
PLN02891 |
IMP cyclohydrolase |
7-529 |
0e+00 |
|
IMP cyclohydrolase
Pssm-ID: 178479 [Multi-domain] Cd Length: 547 Bit Score: 549.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 7 VRRALLSVSDKAGIVEFAQALSARGVELLSTGGTARLLADKGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRGQD 86
Cdd:PLN02891 22 KKQALISLSDKTDLALLANGLQELGYTIVSTGGTASALEAAGVSVTKVEELTNFPEMLDGRVKTLHPAVHGGILARRDQE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 87 DGI--MQQHGIAPIDMVVVNLYPFAQTVAREGCSLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYDAIINEMDANE 164
Cdd:PLN02891 102 HHMeaLNEHGIGTIDVVVVNLYPFYDTVTSGGISFEDGVENIDIGGPAMIRAAAKNHKDVLVVVDPADYPALLEYLKGKQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 165 GSlTLATRFDLAIKAFEHTAAYDSMIANYFGSMVpayhgeskEAAGRFPRTLNLNFIKKQDMRYGENSHQQAAFYIEENV 244
Cdd:PLN02891 182 DD-QQDFRRKLAWKAFQHVASYDSAVSEWLWKQI--------NGGGKFPPSLTVPLTLKSSLRYGENPHQKAAFYVDKSL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 245 KEAS---VATATQLQGKALSYNNIADTDAALECVKEFNEPACVIVKHANPCGVAVSNSILDAYDRAYKTDPTSAFGGIIA 321
Cdd:PLN02891 253 SEVNaggIATAIQHHGKEMSYNNYLDADAAWNCVSEFSNPTCVVVKHTNPCGVASRGDILEAYRLAVRADPVSAFGGIVA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 322 FNRELDAETAQAII---------SRQFVEVIIAPSASEEALKITAAK-QNVRVLTCGQwdTRVAGLDFKRVNGGLLVQDH 391
Cdd:PLN02891 333 FNCEVDEDLAREIRefrsptdgeTRMFYEIVVAPKYTEKGLEVLKGKsKTLRILEAKP--RKKGRLSLRQVGGGWLAQDS 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 392 DLGMVTAGELRVVSKRQPTEQELRDALFCWKVAKFVKSNAIVYAKDNMTIGIGAGQMSRVYSAKIAGIKAGDeglEVKGS 471
Cdd:PLN02891 411 DDLTPEDITFTVVSEKVPTESELEDAKFAWLCVKHVKSNAIVVAKNNRMLGMGSGQPNRVESLRIALEKAGE---EAKGA 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 472 AMASDAFFPF--RDGIDAAAAVGITCVIQPGGSIRDDEVIAAADEHGIAMIFTDMRHFRH 529
Cdd:PLN02891 488 ALASDAFFPFawNDAVEEACQAGVKVIAEPGGSMRDQDAIDCCNKYGVALLFTGVRHFRH 547
|
|
| 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: 543.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 137 AAKNHKDVAIVVKSSDYDAIINEMDANeGSLTLATRFDLAIKAFEHTAAYDSMIANYFgsmvpayhgeskeAAGRFPRTL 216
Cdd:pfam01808 1 AAKNHKDVTVVVDPADYAEVLEELKAN-GGTSLETRRRLAAKAFAHTAAYDAAIANYL-------------AGKEFPETL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 217 NLNFIKKQDMRYGENSHQQAAFYIEENVKeASVATATQLQGKALSYNNIADTDAALECVKEFNEPACVIVKHANPCGVAV 296
Cdd:pfam01808 67 TLSFEKVQDLRYGENPHQKAAFYRDPGPA-GGLATAEQLQGKELSYNNILDADAALELVKEFDEPAAVIVKHANPCGVAV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 297 SNSILDAYDRAYKTDPTSAFGGIIAFNRELDAETAQAIiSRQFVEVIIAPSASEEALKITAAKQNVRVLTCGQWDTRVAG 376
Cdd:pfam01808 146 GDTLAEAYRRALAADPVSAFGGIIALNRPVDAATAEEI-SKIFLEVIIAPGFTPEALEILKKKKNLRLLEIDPLYPPPPG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 377 LDFKRVNGGLLVQDHDLGMVTAGELRVVSKRQPTEQELRDALFCWKVAKFVKSNAIVYAKDNMTIGIGAGQMSRVYSAKI 456
Cdd:pfam01808 225 LEFRSVSGGLLVQDRDDALIDPDDLKVVTKRAPTEEELRDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARI 304
|
....
gi 694089016 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 |
2.80e-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: 2.80e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 8 RRALLSVSDKAGIVEFAQALSARGVELLSTGGTARLLADKGLPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILGRRG-QD 86
Cdd:cd01421 1 KRALISVSDKTGLVEFAKELVELGVEILSTGGTAKFLKEAGIPVTDVSDITGFPEILGGRVKTLHPKIHGGILARRDnEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 87 DGIMQQHGIAPIDMVVVNLYPFAQTVAREGCSLEDAVENIDIGGPTMVRSAAKNHKDVAIVVKSSDYDAIINEMDANeGS 166
Cdd:cd01421 81 HKDLEEHGIEPIDLVVVNLYPFEETVAKGNVTLEEAIENIDIGGPSLLRAAAKNYKDVTVLVDPADYQKVLEELKSN-GS 159
|
170 180
....*....|....*....|....*...
gi 694089016 167 LTLATRFDLAIKAFEHTAAYDSMIANYF 194
Cdd:cd01421 160 ISEETRRRLALKAFAHTAEYDAAISNYL 187
|
|
| PRK07106 |
PRK07106 |
phosphoribosylaminoimidazolecarboxamide formyltransferase; |
226-529 |
4.99e-55 |
|
phosphoribosylaminoimidazolecarboxamide formyltransferase;
Pssm-ID: 180841 Cd Length: 390 Bit Score: 189.87 E-value: 4.99e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 226 MRYGENSHQQAA-FYIEENVKEASVatatqLQGKAlSYNNIADTDAALECVKEFNE----PACVIVKHANPCGVAVSNSI 300
Cdd:PRK07106 6 LKYGCNPNQKPArIFMKEGELPIEV-----LNGRP-GYINFLDALNSWQLVKELKEatglPAAASFKHVSPAGAAVGLPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 301 LD------------------AYDRAYKTDPTSAFGGIIAFNRELDAETAQaIISRQFVEVIIAPSASEEALKITAAKQNV 362
Cdd:PRK07106 80 SDtlkkiyfvddmelsplacAYARARGADRMSSYGDFAALSDVCDVETAK-LLKREVSDGIIAPGYTPEALEILKAKKKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 363 RVLTCgQWDT--RVAGLDFKRVNGGLLVQDHDLGMVTAGELR--VVSKRQPTEQELRDALFCWKVAKFVKSNAIVYAKDN 438
Cdd:PRK07106 159 NYNII-KIDPnyEPAPIETKDVFGITFEQGRNELKIDEDLLKniVTENKELPDEAKRDLIIALITLKYTQSNSVCYAKDG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 439 MTIGIGAGQMSRVYSAKIAGIKA---------------------------------GDEGLEV----------------- 468
Cdd:PRK07106 238 QAIGIGAGQQSRIHCTRLAGNKAdiwylrqhpkvlnlpfkegirrpdrdnaidvylSDDYMDVladgvwqqfftekpepl 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694089016 469 ------------KGSAMASDAFFPFRDGIDAAAAVGITCVIQPGGSIRDDEVIAAADEHGIAMIFTDMRHFRH 529
Cdd:PRK07106 318 treekrawlatlTGVALGSDAFFPFGDNIERAAKSGVKYIAQPGGSIRDDNVIETCNKYGMTMAFTGVRLFHH 390
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
19-132 |
6.16e-31 |
|
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: 115.26 E-value: 6.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 19 GIVEFAQALSARGVELLSTGGTARLLADKGLPVtevsdytgfpemmdgrVKTLHPKVHGGILGrrgqddgIMQQHGIAPI 98
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPV----------------VKTLHPKVHGGIPQ-------ILDLIKNGEI 57
|
90 100 110
....*....|....*....|....*....|....
gi 694089016 99 DMVVVNLYPFAQTVAREGCSLEDAVENIDIGGPT 132
Cdd:smart00851 58 DLVINTLYPFEAQAHEDGYSIRRAAENIDIPGPT 91
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
19-132 |
3.20e-28 |
|
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: 107.57 E-value: 3.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 19 GIVEFAQALSARGVELLSTGGTARLLADKGLPVTEVSDYTGFPeMMDGRVktlhpkvhggilgrrgQDDGIMQQHGiapI 98
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGEG-RPGGRV----------------QIGDLIKNGE---I 60
|
90 100 110
....*....|....*....|....*....|....
gi 694089016 99 DMVVVNLYPFAQTVaREGCSLEDAVENIDIGGPT 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 |
1.64e-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: 64.07 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694089016 9 RALLSVSD--KAGIVEFAQALSARGVELLSTGGTARLLADKGLPVTEVSDYTGFpemmdgrvktLHPKVHGGILgRRGQd 86
Cdd:cd00532 1 GVFLSVSDhvKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHED----------GEPTVDAAIA-EKGK- 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 694089016 87 dgimqqhgiapIDMVVVNLYPFAQtvaregcsledavENIDIGGPTMVRSAAKNH 141
Cdd:cd00532 69 -----------FDVVINLRDPRRD-------------RCTDEDGTALLRLARLYK 99
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
9-66 |
1.81e-07 |
|
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: 49.40 E-value: 1.81e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694089016 9 RALLSV--SDKAGIVEFAQALSARGVELLSTGGTARLLADKGLPVTEVS-DYTGFPEMMDG 66
Cdd:cd01424 2 TVFISVadRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNkVSEGRPNIVDL 62
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
9-54 |
3.99e-06 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 49.71 E-value: 3.99e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 694089016 9 RALLSV--SDKAGIVEFAQALSARGVELLSTGGTARLLADKGLPVTEV 54
Cdd:PRK05294 939 TVFLSVrdRDKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELV 986
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
3-67 |
5.83e-04 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 42.84 E-value: 5.83e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694089016 3 QRRPVR-RALLSVSD--KAGIVEFAQALSARGVELLSTGGTARLLADKGLPVTEVsdytgfPEMMDGR 67
Cdd:PLN02735 967 QRLPLSgTVFISLNDltKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERV------LKLHEGR 1028
|
|
| |
