|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
1-435 |
0e+00 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 753.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 1 MKILVIGGGGREHALAWRLVQSPKTHKIYLAPGNGGTAQDARFENVPMTDVNELCAWALAQKIVLTVVGPEVPLAAGVVD 80
Cdd:COG0151 1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 81 IFRKHGLRIFGPTQAAAQLESSKAFSKAFMKRHAIPTAEFETFTDPVAAHAYINQKGAPIVVKADGLAAGKGVVVASTLA 160
Cdd:COG0151 81 AFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAETLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 161 EAHEAVDFMLLDNALGvvhNAGAdgaavpRVVIEEFLQGEEASFIVMVDGKNVLPLATSQDHKRLLDGDQGPNTGGMGAY 240
Cdd:COG0151 161 EALAAVDDMLADGKFG---DAGA------RVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 241 SPAPVVTPDVHARAMRDIILPTVRGMEKDGIAFTGFLYAGLMIDAQGqPKTLEFNCRMGDPETQPIMMRLKSDLVDVMMA 320
Cdd:COG0151 232 SPAPVVTEELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADG-PKVLEFNVRFGDPETQVVLPRLESDLLELLLA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 321 ATEpgphGKLDQVELEWDRRTALGVVLAAHGYPMSPRKGDVISGVP-AEAEDACVFHAGTALQDGQLTTSGGRVLCVTVL 399
Cdd:COG0151 311 AAE----GRLDEVELEWDDRAAVCVVLASGGYPGSYEKGDVITGLEeAEAEGVKVFHAGTALEDGKLVTNGGRVLGVTAL 386
|
410 420 430
....*....|....*....|....*....|....*.
gi 1278638884 400 ADNARLAQQRAYEVVMGIRFDGMQYRHDIGHRAIKG 435
Cdd:COG0151 387 GDTLEEARERAYEAVEKIRFEGMFYRRDIGWRALKR 422
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
1-434 |
0e+00 |
|
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase (GARS). This enzyme appears as a monofunctional protein in prokaryotes but as part of a larger, multidomain protein in eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273315 [Multi-domain] Cd Length: 422 Bit Score: 577.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 1 MKILVIGGGGREHALAWRLVQSPKTHKIYLAPGNGGTAQDARFENV--PMTDVNELCAWALAQKIVLTVVGPEVPLAAGV 78
Cdd:TIGR00877 1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVaiEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 79 VDIFRKHGLRIFGPTQAAAQLESSKAFSKAFMKRHAIPTAEFETFTDPVAAHAYINQKGAPIVVKADGLAAGKGVVVAST 158
Cdd:TIGR00877 81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 159 LAEAHEAVDFMLLDNAlgvvhnagadGAAVPRVVIEEFLQGEEASFIVMVDGKNVLPLATSQDHKRLLDGDQGPNTGGMG 238
Cdd:TIGR00877 161 NEEAIKAVEDILEQKF----------GDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 239 AYSPAPVVTPDVHARAMRDIILPTVRGMEKDGIAFTGFLYAGLMIDAQGqPKTLEFNCRMGDPETQPIMMRLKSDLVDVM 318
Cdd:TIGR00877 231 AYSPAPVFTEEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEG-PKVLEFNCRFGDPETQAVLPLLKSDLLEVC 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 319 MAATEpgphGKLDQVELEWDRRTALGVVLAAHGYPMSPRKGDVISGVP-AEAEDACVFHAGTALQDGQLTTSGGRVLCVT 397
Cdd:TIGR00877 310 LAAVE----GKLDEVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPlAEAEGVKVFHAGTKADNGKLVTNGGRVLAVT 385
|
410 420 430
....*....|....*....|....*....|....*..
gi 1278638884 398 VLADNARLAQQRAYEVVMGIRFDGMQYRHDIGHRAIK 434
Cdd:TIGR00877 386 ALGKTLEEARERAYEAVEYIKFEGMFYRKDIGFRALE 422
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
4-434 |
1.08e-177 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 503.50 E-value: 1.08e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 4 LVIGGGGREHALAWRLVQSPKTHKIYLAPGNGGTAQDARFENVPMTDVNELCA---WALAQKIVLTVVGPEVPLAAGVVD 80
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCVPDLDISDSAAvisFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 81 IFRKHGLRIFGPTQAAAQLESSKAFSKAFMKRHAIPTAEFETFTDPVAAHAYINQKGAPIVVKADGLAAGKGVVVASTLA 160
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 161 EAHEAVDFMLLDNALGvvhNAGAdgaavpRVVIEEFLQGEEASFIVMVDGKNVLPLATSQDHKRLLDGDQGPNTGGMGAY 240
Cdd:PLN02257 161 EAYEAVDSMLVKGAFG---SAGS------EVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 241 SPAPVVTPDVHARAMRDIILPTVRGMEKDGIAFTGFLYAGLMIDAQ-GQPKTLEFNCRMGDPETQPIMMRLKSDLVDVMM 319
Cdd:PLN02257 232 SPAPVLTPELESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKsGLPKLLEYNVRFGDPECQVLMMRLESDLAQVLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 320 AATEpgphGKLDQVELEWDRRTALGVVLAAHGYPMSPRKGDVISGVPaEAEDAC----VFHAGTALQ-DGQLTTSGGRVL 394
Cdd:PLN02257 312 AACK----GELSGVSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLD-EAEAVApgvkVFHAGTALDsDGNVVAAGGRVL 386
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1278638884 395 CVTVLADNARLAQQRAYEVVMGIRFDGMQYRHDIGHRAIK 434
Cdd:PLN02257 387 GVTAKGKDIAEARARAYDAVDQIDWPGGFFRRDIGWRAVA 426
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
101-303 |
7.86e-97 |
|
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).
Pssm-ID: 395851 [Multi-domain] Cd Length: 194 Bit Score: 288.41 E-value: 7.86e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 101 SSKAFSKAFMKRHAIPTAEFETFTDPVAAHAYINQKGAPI-VVKADGLAAGKGVVVASTLAEAHEAVDFMLLDnalgvvh 179
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEQ------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 180 naGADGAAVPRVVIEEFLQGEEASFIVMVDGKNVLPLATSQDHKRLLDGDQGPNTGGMGAYSPAPVVTPDVHARAMRDII 259
Cdd:pfam01071 74 --KKFGEAGETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1278638884 260 LPTVRGMEKDGIAFTGFLYAGLMIDAQGqPKTLEFNCRMGDPET 303
Cdd:pfam01071 152 EPTVDGLRKEGIPFKGVLYAGLMLTKDG-PKVLEFNCRFGDPET 194
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
1-435 |
0e+00 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 753.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 1 MKILVIGGGGREHALAWRLVQSPKTHKIYLAPGNGGTAQDARFENVPMTDVNELCAWALAQKIVLTVVGPEVPLAAGVVD 80
Cdd:COG0151 1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 81 IFRKHGLRIFGPTQAAAQLESSKAFSKAFMKRHAIPTAEFETFTDPVAAHAYINQKGAPIVVKADGLAAGKGVVVASTLA 160
Cdd:COG0151 81 AFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAETLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 161 EAHEAVDFMLLDNALGvvhNAGAdgaavpRVVIEEFLQGEEASFIVMVDGKNVLPLATSQDHKRLLDGDQGPNTGGMGAY 240
Cdd:COG0151 161 EALAAVDDMLADGKFG---DAGA------RVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 241 SPAPVVTPDVHARAMRDIILPTVRGMEKDGIAFTGFLYAGLMIDAQGqPKTLEFNCRMGDPETQPIMMRLKSDLVDVMMA 320
Cdd:COG0151 232 SPAPVVTEELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADG-PKVLEFNVRFGDPETQVVLPRLESDLLELLLA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 321 ATEpgphGKLDQVELEWDRRTALGVVLAAHGYPMSPRKGDVISGVP-AEAEDACVFHAGTALQDGQLTTSGGRVLCVTVL 399
Cdd:COG0151 311 AAE----GRLDEVELEWDDRAAVCVVLASGGYPGSYEKGDVITGLEeAEAEGVKVFHAGTALEDGKLVTNGGRVLGVTAL 386
|
410 420 430
....*....|....*....|....*....|....*.
gi 1278638884 400 ADNARLAQQRAYEVVMGIRFDGMQYRHDIGHRAIKG 435
Cdd:COG0151 387 GDTLEEARERAYEAVEKIRFEGMFYRRDIGWRALKR 422
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
1-434 |
0e+00 |
|
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase (GARS). This enzyme appears as a monofunctional protein in prokaryotes but as part of a larger, multidomain protein in eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273315 [Multi-domain] Cd Length: 422 Bit Score: 577.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 1 MKILVIGGGGREHALAWRLVQSPKTHKIYLAPGNGGTAQDARFENV--PMTDVNELCAWALAQKIVLTVVGPEVPLAAGV 78
Cdd:TIGR00877 1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVaiEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 79 VDIFRKHGLRIFGPTQAAAQLESSKAFSKAFMKRHAIPTAEFETFTDPVAAHAYINQKGAPIVVKADGLAAGKGVVVAST 158
Cdd:TIGR00877 81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 159 LAEAHEAVDFMLLDNAlgvvhnagadGAAVPRVVIEEFLQGEEASFIVMVDGKNVLPLATSQDHKRLLDGDQGPNTGGMG 238
Cdd:TIGR00877 161 NEEAIKAVEDILEQKF----------GDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 239 AYSPAPVVTPDVHARAMRDIILPTVRGMEKDGIAFTGFLYAGLMIDAQGqPKTLEFNCRMGDPETQPIMMRLKSDLVDVM 318
Cdd:TIGR00877 231 AYSPAPVFTEEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEG-PKVLEFNCRFGDPETQAVLPLLKSDLLEVC 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 319 MAATEpgphGKLDQVELEWDRRTALGVVLAAHGYPMSPRKGDVISGVP-AEAEDACVFHAGTALQDGQLTTSGGRVLCVT 397
Cdd:TIGR00877 310 LAAVE----GKLDEVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPlAEAEGVKVFHAGTKADNGKLVTNGGRVLAVT 385
|
410 420 430
....*....|....*....|....*....|....*..
gi 1278638884 398 VLADNARLAQQRAYEVVMGIRFDGMQYRHDIGHRAIK 434
Cdd:TIGR00877 386 ALGKTLEEARERAYEAVEYIKFEGMFYRKDIGFRALE 422
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
4-434 |
1.08e-177 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 503.50 E-value: 1.08e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 4 LVIGGGGREHALAWRLVQSPKTHKIYLAPGNGGTAQDARFENVPMTDVNELCA---WALAQKIVLTVVGPEVPLAAGVVD 80
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCVPDLDISDSAAvisFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 81 IFRKHGLRIFGPTQAAAQLESSKAFSKAFMKRHAIPTAEFETFTDPVAAHAYINQKGAPIVVKADGLAAGKGVVVASTLA 160
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 161 EAHEAVDFMLLDNALGvvhNAGAdgaavpRVVIEEFLQGEEASFIVMVDGKNVLPLATSQDHKRLLDGDQGPNTGGMGAY 240
Cdd:PLN02257 161 EAYEAVDSMLVKGAFG---SAGS------EVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 241 SPAPVVTPDVHARAMRDIILPTVRGMEKDGIAFTGFLYAGLMIDAQ-GQPKTLEFNCRMGDPETQPIMMRLKSDLVDVMM 319
Cdd:PLN02257 232 SPAPVLTPELESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKsGLPKLLEYNVRFGDPECQVLMMRLESDLAQVLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 320 AATEpgphGKLDQVELEWDRRTALGVVLAAHGYPMSPRKGDVISGVPaEAEDAC----VFHAGTALQ-DGQLTTSGGRVL 394
Cdd:PLN02257 312 AACK----GELSGVSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLD-EAEAVApgvkVFHAGTALDsDGNVVAAGGRVL 386
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1278638884 395 CVTVLADNARLAQQRAYEVVMGIRFDGMQYRHDIGHRAIK 434
Cdd:PLN02257 387 GVTAKGKDIAEARARAYDAVDQIDWPGGFFRRDIGWRAVA 426
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
101-303 |
7.86e-97 |
|
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).
Pssm-ID: 395851 [Multi-domain] Cd Length: 194 Bit Score: 288.41 E-value: 7.86e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 101 SSKAFSKAFMKRHAIPTAEFETFTDPVAAHAYINQKGAPI-VVKADGLAAGKGVVVASTLAEAHEAVDFMLLDnalgvvh 179
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEQ------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 180 naGADGAAVPRVVIEEFLQGEEASFIVMVDGKNVLPLATSQDHKRLLDGDQGPNTGGMGAYSPAPVVTPDVHARAMRDII 259
Cdd:pfam01071 74 --KKFGEAGETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1278638884 260 LPTVRGMEKDGIAFTGFLYAGLMIDAQGqPKTLEFNCRMGDPET 303
Cdd:pfam01071 152 EPTVDGLRKEGIPFKGVLYAGLMLTKDG-PKVLEFNCRFGDPET 194
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
1-100 |
5.01e-50 |
|
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the N-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam00289). This domain is structurally related to the PreATP-grasp domain.
Pssm-ID: 460723 [Multi-domain] Cd Length: 102 Bit Score: 164.84 E-value: 5.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 1 MKILVIGGGGREHALAWRLVQSPKTHKIYLAPGNGGTAQDARFENVPMTDVNELCAWALAQKIVLTVVGPEVPLAAGVVD 80
Cdd:pfam02844 1 MKVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLAECVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGIVD 80
|
90 100
....*....|....*....|..
gi 1278638884 81 IF--RKHGLRIFGPTQAAAQLE 100
Cdd:pfam02844 81 ALreRAAGIPVFGPSKAAAQLE 102
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
342-431 |
1.61e-39 |
|
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the C-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02787).
Pssm-ID: 460722 [Multi-domain] Cd Length: 88 Bit Score: 136.81 E-value: 1.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 342 ALGVVLAAHGYPMSPRKGDVISGVpaEAEDACVFHAGTALQDGQLTTSGGRVLCVTVLADNARLAQQRAYEVVMGIRFDG 421
Cdd:pfam02843 1 AVCVVLASGGYPGSYEKGDVITGL--DEAGVKVFHAGTKLKDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDFEG 78
|
90
....*....|
gi 1278638884 422 MQYRHDIGHR 431
Cdd:pfam02843 79 MFYRKDIGTR 88
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
64-299 |
2.08e-19 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 87.24 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 64 VLTVVGPEVPLAAGVVDifrKHGLRifGPTQAAAQLESSKAFSKAFMKRHAIPTAEFETFTDPVAAHAYINQKGAPIVVK 143
Cdd:COG0439 21 VLSESEFAVETAAELAE---ELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 144 ADGLAAGKGVVVASTLAEAHEAVDFmlldnALGVVHNAGADGaavpRVVIEEFLQGEEASFIVMVDGKNVLPLATSQDHK 223
Cdd:COG0439 96 PADGAGSRGVRVVRDEEELEAALAE-----ARAEAKAGSPNG----EVLVEEFLEGREYSVEGLVRDGEVVVCSITRKHQ 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278638884 224 RlldgdqGPNTGGMGAYSPAPvVTPDVHARaMRDIilpTVRGMEKDGIAFtGFLYAGLMIDAQGQPKTLEFNCRMG 299
Cdd:COG0439 167 K------PPYFVELGHEAPSP-LPEELRAE-IGEL---VARALRALGYRR-GAFHTEFLLTPDGEPYLIEINARLG 230
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
75-211 |
9.41e-06 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 47.24 E-value: 9.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 75 AAGVVDIFRKHGLRIFGPTQAAAQLeSSKAFSKAFMKRHAIPTAEFETFTDPVAAHAYINQKGAPIVVK-ADGlAAGKGV 153
Cdd:COG0189 70 GLALLRQLEAAGVPVVNDPEAIRRA-RDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKpLDG-SGGRGV 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 154 VVASTLAEAHEAVDFMLldnalgvvhnagADGAAVprVVIEEFLQGEEASF--IVMVDGK 211
Cdd:COG0189 148 FLVEDEDALESILEALT------------ELGSEP--VLVQEFIPEEDGRDirVLVVGGE 193
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
92-169 |
1.03e-05 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 47.38 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 92 PTQAAAQLESSKAFS---------------KAFMKRHAIPTAEFETFTDPVAAHAYINQKGAPIVVKA-----DglaaGK 151
Cdd:COG0026 64 PAEALEALEAEVPVRpgpealeiaqdrlleKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTrrggyD----GK 139
|
90
....*....|....*...
gi 1278638884 152 GVVVASTLAEAHEAVDFM 169
Cdd:COG0026 140 GQVVIKSAADLEAAWAAL 157
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
106-195 |
4.97e-04 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 41.09 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 106 SKAFMKRHAIPTAEFETFTDPVAAHAYINQKGAP-IVVKADGLAAGK----GVVVASTLAEAHEAVDFMLLDNAlgVVHN 180
Cdd:pfam08442 7 AKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKvYVVKAQVLAGGRgkagGVKLAKSPEEAKEVAKEMLGKNL--VTKQ 84
|
90
....*....|....*
gi 1278638884 181 AGADGAAVPRVVIEE 195
Cdd:pfam08442 85 TGPDGQPVNKVLVEE 99
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
79-155 |
5.35e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 42.04 E-value: 5.35e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278638884 79 VDIFRKHGLRIFGPTQAAAQLESSKAFSKAFMKRHAIPTAEFET--FTDPVAAHAYINQKGAPIVVKADGLAAGKGVVV 155
Cdd:PRK08462 94 VEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDgaLKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRV 172
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
81-162 |
1.85e-03 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 40.02 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 81 IFRKHGLRIFGPTQAAAqLESSKAFSKAFMKRHAIPTAEFETFTDPVAAHAYINQKGAPIVVKADGLAAGKGVVVASTLA 160
Cdd:TIGR00768 68 YLESLGVPVINSSDAIL-NAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQ 146
|
..
gi 1278638884 161 EA 162
Cdd:TIGR00768 147 AA 148
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
1-201 |
3.25e-03 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 39.48 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 1 MKILVIGGGGReHALAWRLVQSPKTHKIY------LAPGnggtAQDA-RFENVPM-TDVN------ELCAwalAQKIVLT 66
Cdd:PRK12767 2 MNILVTSAGRR-VQLVKALKKSLLKGRVIgadiseLAPA----LYFAdKFYVVPKvTDPNyidrllDICK---KEKIDLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 67 VVG--PEVPLAAGVVDIFRKHGLRIFGPTQAAAQLESSKAFSKAFMKRHAIPTAEFETFTD-PVAAHAYINQK-GAPIVV 142
Cdd:PRK12767 74 IPLidPELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESlEDFKAALAKGElQFPLFV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1278638884 143 KADGLAAGKGVVVASTLAEaheavdfmlLDNALgvvhnagadgAAVPRVVIEEFLQGEE 201
Cdd:PRK12767 154 KPRDGSASIGVFKVNDKEE---------LEFLL----------EYVPNLIIQEFIEGQE 193
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
107-167 |
3.68e-03 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 39.37 E-value: 3.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278638884 107 KAFMKRHAIPTAEFETFTDPVAAHAYINQKGAPIVVKA-----DglaaGKGVVVASTLAEAHEAVD 167
Cdd:PRK06019 105 KQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTrrggyD----GKGQWVIRSAEDLEAAWA 166
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
76-212 |
5.48e-03 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 39.21 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278638884 76 AGVVDifrKHGLRIFG-PTQAAAQLESSKAFsKAFMKRHAIPTAEFETFTDPVAAHAYINQKGAPIVVKADGLAAGKGVV 154
Cdd:TIGR01369 104 SGVLE---KYGVEVLGtPVEAIKKAEDRELF-REAMKEIGEPVPESEIAHSVEEALAAAKEIGYPVIVRPAFTLGGTGGG 179
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1278638884 155 VASTLAEAHEavdfmLLDNALgvvhnagaDGAAVPRVVIEEFLQG-EEASFIVMVDGKN 212
Cdd:TIGR01369 180 IAYNREELKE-----IAERAL--------SASPINQVLVEKSLAGwKEIEYEVMRDSND 225
|
|
| |
