|
Name |
Accession |
Description |
Interval |
E-value |
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-469 |
0e+00 |
|
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; Glutamine phosphoribosylpyrophosphate amidotransferase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439804 [Multi-domain] Cd Length: 464 Bit Score: 654.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 1 MICLGLVALQHRGQESAGIVTSLGKsskNFSVHKGMGMINNLFNDEAIRKLKGNLGIGHTRYSTAAASEVVNCQPFVVHT 80
Cdd:COG0034 22 LTYYGLYALQHRGQESAGIATSDGG---RFHLHKGMGLVSDVFDEEDLERLKGNIAIGHVRYSTTGSSSLENAQPFYVNS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 81 AHGALAIAHNGELVNCESLRREVLERGVGLSTHSDSELIAQSLccapedVSEHDGPNWPARIRHFMTLAPLSYSLVVMHK 160
Cdd:COG0034 99 PFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLI------ARELTKEDLEEAIKEALRRVKGAYSLVILTG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 161 DKIYAVRDSYGNRPLCLGKivpvdaghanindqLAEGWVVSSESCGFLSIGARYVREVEPGEIIELSRNGYRTVDIVERP 240
Cdd:COG0034 173 DGLIAARDPNGIRPLVLGK--------------LEDGYVVASESCALDILGAEFVRDVEPGEIVVIDEDGLRSRQFAEKP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 241 dykRMAFCIFEYVYFARSDSMFEGQMVYSARLQCGRQLARESPLDADLVSSVPESGTAAAHGYARESGLPFGEVLCKNRY 320
Cdd:COG0034 239 ---RPAPCIFEYVYFARPDSVIDGRSVYEARKRMGRELAREAPVDADVVIPVPDSGRPAAIGYAEESGIPYEEGLIKNRY 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 321 VGRTFIQPSTRLRQLGVAKKFGALAQNVEGKRIVLVDDSIVRGNTIGPIIKLLRDAGATEVHIRIASPPLQYPCYMGINI 400
Cdd:COG0034 316 VGRTFIQPTQELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKMLREAGAKEVHFRIASPPIRYPCYYGIDT 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24659604 401 PTREELIANKLNADQLADHVGADSLAYLSVEGLVKAVQMNkahvnplKAGYCTACLTGEYPGGLPEELS 469
Cdd:COG0034 396 PTREELIAANRSVEEIREYIGADSLGYLSLEGLIEAVGEP-------IEGFCTACFTGDYPTGIPDEEK 457
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
4-461 |
0e+00 |
|
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273461 [Multi-domain] Cd Length: 442 Bit Score: 535.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 4 LGLVALQHRGQESAGIVTSLGKsskNFSVHKGMGMINNLFNDEAIRKLKGNLGIGHTRYSTAAASEVVNCQPFVVHTAHG 83
Cdd:TIGR01134 19 YGLYALQHRGQESAGISVFDGN---RFRLHKGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAGSSGLENAQPFVVNSPYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 84 ALAIAHNGELVNCESLRREVLERGVGLSTHSDSELIAQSLccAPEDVSEHDGPnwpARIRHFMTLAPLSYSLVVMHKDKI 163
Cdd:TIGR01134 96 GLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLL--AHNDESKDDLF---DAVARVLERVRGAYALVLMTEDGL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 164 YAVRDSYGNRPLCLGkivpvdaghanindQLAEGWVVSSESCGFLSIGARYVREVEPGEIIELSRNGYRTVDIVERPdyk 243
Cdd:TIGR01134 171 VAVRDPHGIRPLVLG--------------RRGDGYVVASESCALDILGAEFVRDVEPGEVVVIFDGGLESRQCARRP--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 244 rMAFCIFEYVYFARSDSMFEGQMVYSARLQCGRQLARESPLDADLVSSVPESGTAAAHGYARESGLPFGEVLCKNRYVGR 323
Cdd:TIGR01134 234 -RAPCVFEYVYFARPDSVIDGISVYYARKRMGKELARESPVEADVVVPVPDSGRSAALGFAQASGIPYREGLIKNRYVGR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 324 TFIQPSTRLRQLGVAKKFGALAQNVEGKRIVLVDDSIVRGNTIGPIIKLLRDAGATEVHIRIASPPLQYPCYMGINIPTR 403
Cdd:TIGR01134 313 TFIMPTQELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEMLRDAGAKEVHVRIASPPIRYPCYYGIDMPTR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 24659604 404 EELIANKLNADQLADhVGADSLAYLSVEGLVKAVQMNKAHvnplkagYCTACLTGEYP 461
Cdd:TIGR01134 393 EELIAARRTVEEIRK-IGADSLAYLSLEGLKEAVGNPESD-------LCLACFTGEYP 442
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
1-469 |
2.59e-180 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 512.66 E-value: 2.59e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 1 MICLGLVALQHRGQESAGIVTSLGKSsknFSVHKGMGMINNLFNDEAIRKLKGNLGIGHTRYSTAAASEVVNCQPFVVHT 80
Cdd:PRK05793 31 LTYYGLYALQHRGQESAGIAVSDGEK---IKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYSTTGASDLDNAQPLVANY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 81 AHGALAIAHNGELVNCESLRREVLERGVGLSTHSDSE----LIAQSLCCAPEDVsehdgpnwparIRHFMTLAPLSYSLV 156
Cdd:PRK05793 108 KLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEvilnLIARSAKKGLEKA-----------LVDAIQAIKGSYALV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 157 VMHKDKIYAVRDSYGNRPLCLGKivpvdaghanindqLAEGWVVSSESCGFLSIGARYVREVEPGEIIELSRNGYRTVDI 236
Cdd:PRK05793 177 ILTEDKLIGVRDPHGIRPLCLGK--------------LGDDYILSSESCALDTIGAEFIRDVEPGEIVIIDEDGIKSIKF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 237 VERPdyKRMAfCIFEYVYFARSDSMFEGQMVYSARLQCGRQLARESPLDADLVSSVPESGTAAAHGYARESGLPFGEVLC 316
Cdd:PRK05793 243 AEKT--KCQT-CAFEYIYFARPDSVIDGISVYESRVRAGRQLYKEYPVDADIVIGVPDSGIPAAIGYAEASGIPYGIGFI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 317 KNRYVGRTFIQPSTRLRQLGVAKKFGALAQNVEGKRIVLVDDSIVRGNTIGPIIKLLRDAGATEVHIRIASPPLQYPCYM 396
Cdd:PRK05793 320 KNKYVGRTFIAPSQELRERAVRVKLNPLKVNVEGKRVVLIDDSIVRGTTSKRLVELLRKAGAKEVHFRVSSPPVKYPCYF 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24659604 397 GINIPTREELIANKLNADQLADHVGADSLAYLSVEGLVKAVQMNKahvnplkaGYCTACLTGEYPGGLPEELS 469
Cdd:PRK05793 400 GIDTPYRKELIGANMSVEEIREMIGADSLGYLSIEGLLESLNGDK--------GFCLGCFNGVYPVSAPKEGP 464
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-461 |
2.89e-155 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 449.51 E-value: 2.89e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 1 MICLGLVALQHRGQESAGIVTSLGKSsknFSVHKGMGMINNLFNDEAIRKLKGNLGIGHTRYSTAAASEVVNCQPFVVHT 80
Cdd:PLN02440 16 LCYLGLHALQHRGQEGAGIVTVDGNR---LQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAGASSLKNVQPFVANY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 81 AHGALAIAHNGELVNCESLRREVLERGVGLSTHSDSE----LIAQSLccapedvsehdGPNWPARIRHFMTLAPLSYSLV 156
Cdd:PLN02440 93 RFGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEvllhLIAISK-----------ARPFFSRIVDACEKLKGAYSMV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 157 VMHKDKIYAVRDSYGNRPLCLGKivpvdaghanindQLAEGWVVSSESCGFLSIGARYVREVEPGEIIELSRN-GYRTVD 235
Cdd:PLN02440 162 FLTEDKLVAVRDPHGFRPLVMGR-------------RSNGAVVFASETCALDLIGATYEREVNPGEVIVVDKDkGVSSQC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 236 IVERPDYKRmafCIFEYVYFARSDSMFEGQMVYSARLQCGRQLARESPLDADLVSSVPESGTAAAHGYARESGLPFGEVL 315
Cdd:PLN02440 229 LMPHPEPKP---CIFEHIYFARPNSIVFGRSVYESRLEFGEILATEIPVDCDVVIPVPDSGRVAALGYAAKLGVPFQQGL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 316 CKNRYVGRTFIQPSTRLRQLGVAKKFGALAQNVEGKRIVLVDDSIVRGNTIGPIIKLLRDAGATEVHIRIASPPLQYPCY 395
Cdd:PLN02440 306 IRSHYVGRTFIEPSQKIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVRMLREAGAKEVHMRIASPPIIASCY 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24659604 396 MGINIPTREELIANKLNADQLADHVGADSLAYLSVEGLVKAVQMNkAHVnplkagYCTACLTGEYP 461
Cdd:PLN02440 386 YGVDTPSREELISNRMSVEEIRKFIGCDSLAFLPLEDLKKSLGEE-SPR------FCYACFSGDYP 444
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-263 |
2.05e-122 |
|
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the N-terminus of glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase) . The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. GPATase crystalizes as a homotetramer, but can also exist as a homdimer.
Pssm-ID: 238367 [Multi-domain] Cd Length: 252 Bit Score: 357.16 E-value: 2.05e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 2 ICLGLVALQHRGQESAGIVTSLGKsskNFSVHKGMGMINNLFNDEAIRKLKGNLGIGHTRYSTAAASEVVNCQPFVVHTA 81
Cdd:cd00715 16 TYLGLYALQHRGQESAGIATSDGK---RFHTHKGMGLVSDVFDEEKLRRLPGNIAIGHVRYSTAGSSSLENAQPFVVNSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 82 HGALAIAHNGELVNCESLRREVLERGVGLSTHSDSELIAQSLCCAPEDvsehdgPNWPARIRHFMTLAPLSYSLVVMHKD 161
Cdd:cd00715 93 LGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAK------DDLFEAIIDALERVKGAYSLVIMTAD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 162 KIYAVRDSYGNRPLCLGKIVPvdaghanindqlaEGWVVSSESCGFLSIGARYVREVEPGEIIELSRNGYRTVDIVERPd 241
Cdd:cd00715 167 GLIAVRDPHGIRPLVLGKLEG-------------DGYVVASESCALDIIGAEFVRDVEPGEIVVIDDDGLESSQRAPKP- 232
|
250 260
....*....|....*....|..
gi 24659604 242 ykRMAFCIFEYVYFARSDSMFE 263
Cdd:cd00715 233 --KPAPCIFEYVYFARPDSVID 252
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
5-224 |
2.99e-50 |
|
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.
Pssm-ID: 238212 [Multi-domain] Cd Length: 220 Bit Score: 170.32 E-value: 2.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 5 GLVALQHRGQESAGIVTSlgkSSKNFSVHKGMGMINNLFNDEAIRKLKGNLGIGHTRYSTAAASEVVNCQPFVVHTahGA 84
Cdd:cd00352 23 GLAALEHRGPDGAGIAVY---DGDGLFVEKRAGPVSDVALDLLDEPLKSGVALGHVRLATNGLPSEANAQPFRSED--GR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 85 LAIAHNGELVNCESLRREVLERGVGLSTHSDSELIAQSLCcapedvSEHDGPNWPARIRHFMTLAPLSYSLVVMHK--DK 162
Cdd:cd00352 98 IALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLE------RLGREGGLFEAVEDALKRLDGPFAFALWDGkpDR 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24659604 163 IYAVRDSYGNRPLCLGKIVPvdaghanindqlaEGWVVSSESCGFLSIGARYVREVEPGEII 224
Cdd:cd00352 172 LFAARDRFGIRPLYYGITKD-------------GGLVFASEPKALLALPFKGVRRLPPGELL 220
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
274-410 |
1.15e-20 |
|
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.
Pssm-ID: 206754 [Multi-domain] Cd Length: 130 Bit Score: 87.45 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 274 CGRQLARE---SPLDADLVSSVPESGTAAAHGYARESGLPFGEVLCKNRYVGRTFIQPSTRLRQLGVakkfgalaqNVEG 350
Cdd:cd06223 1 AGRLLAEEireDLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLELPLGG---------DVKG 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 351 KRIVLVDDSIVRGNTIGPIIKLLRDAGATEVHIrIASPPLQYPCYMGINIPTREELIANK 410
Cdd:cd06223 72 KRVLLVDDVIATGGTLLAAIELLKEAGAKVVGV-AVLLDKPEGGARELASPGDPVYSLFT 130
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
5-240 |
1.21e-16 |
|
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440218 [Multi-domain] Cd Length: 610 Bit Score: 82.37 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 5 GLVALQHRGQESAGIVTslgKSSKNFSVHKGMGMINNLFNDEAIRKLKGNLGIGHTRYSTAAASEVVNCQPfvvHT-AHG 83
Cdd:COG0449 20 GLKRLEYRGYDSAGIAV---LDDGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGAPSDENAHP---HTsCSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 84 ALAIAHNG--ElvNCESLRREVLERGVGLSTHSDSELIAQsLccapedVSEH--DGPNWPARIRHfmTLAPL--SYSLVV 157
Cdd:COG0449 94 RIAVVHNGiiE--NYAELREELEAKGHTFKSETDTEVIAH-L------IEEYlkGGGDLLEAVRK--ALKRLegAYALAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 158 MHK---DKIYAVR-DSygnrPLCLGkivpvdaghanindqLAEG-WVVSSESCGFLSIgARYVREVEPGEIIELSRNGYR 232
Cdd:COG0449 163 ISAdepDRIVAARkGS----PLVIG---------------LGEGeNFLASDVPALLPY-TRRVIYLEDGEIAVLTRDGVE 222
|
250
....*....|..
gi 24659604 233 TVDI----VERP 240
Cdd:COG0449 223 IYDLdgepVERE 234
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
5-179 |
4.63e-16 |
|
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus of glucosamine-6P synthase (GlmS, or GFAT in humans). The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. In humans, GFAT catalyzes the first and rate-limiting step of hexosamine metabolism, the conversion of D-fructose-6P (Fru6P) into D-glucosamine-6P using L-glutamine as a nitrogen source. The end product of this pathway, UDP-N-acetyl glucosamine, is a major building block of the bacterial peptidoglycan and fungal chitin.
Pssm-ID: 238366 [Multi-domain] Cd Length: 215 Bit Score: 76.72 E-value: 4.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 5 GLVALQHRGQESAGIVTSlgkSSKNFSVHKGMGMINNLFNDEAIRKLKGNLGIGHTRYSTAAASEVVNCQPfvvHT-AHG 83
Cdd:cd00714 19 GLKRLEYRGYDSAGIAVI---GDGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEPTDVNAHP---HRsCDG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 84 ALAIAHNGELVNCESLRREVLERGVGLSTHSDSELIAQSLccapedvsEH---DGPNWPARIRhfMTLAPL--SYSLVVM 158
Cdd:cd00714 93 EIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLI--------EYyydGGLDLLEAVK--KALKRLegAYALAVI 162
|
170 180
....*....|....*....|....*
gi 24659604 159 HK---DKIYAVR-DSygnrPLCLGK 179
Cdd:cd00714 163 SKdepDEIVAARnGS----PLVIGI 183
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
5-243 |
1.69e-14 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 75.85 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 5 GLVALQHRGQESAGIVTSlgkSSKNFSVHKGMGMINNLFNDEAIRKLKGNLGIGHTRYSTAAASEVVNCQPfvvHT-AHG 83
Cdd:PRK00331 20 GLKRLEYRGYDSAGIAVL---DDGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGKPTERNAHP---HTdCSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 84 ALAIAHNGELVNCESLRREVLERGVGLSTHSDSELIAQsLccapedVSEH--DGPNWPARIRHfmTLAPL--SYSLVVMH 159
Cdd:PRK00331 94 RIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAH-L------IEEElkEGGDLLEAVRK--ALKRLegAYALAVID 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 160 K---DKIYAVR-DSygnrPLCLGkivpvdaghanindqLAEG-WVVSSESCGFLSigarYVREV---EPGEIIELSRNGY 231
Cdd:PRK00331 165 KdepDTIVAARnGS----PLVIG---------------LGEGeNFLASDALALLP----YTRRViylEDGEIAVLTRDGV 221
|
250
....*....|....*.
gi 24659604 232 RTVDI----VERPDYK 243
Cdd:PRK00331 222 EIFDFdgnpVEREVYT 237
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
1-224 |
7.47e-14 |
|
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238888 [Multi-domain] Cd Length: 249 Bit Score: 71.15 E-value: 7.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 1 MICLGLVALQHRG-QESAGI-------VTSLGkSSKNFSVHKGMG---MINNLFNdeaIRKLKGNLGIGHTRYSTAAASE 69
Cdd:cd01907 18 LLVEMLDAMQERGpGDGAGFalygdpdAFVYS-SGKDMEVFKGVGypeDIARRYD---LEEYKGYHWIAHTRQPTNSAVW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 70 VVNCQPFVVhtahGALAIAHNGELVNCESLRREVLERGVGLSTHSDSELIAQSLccaPEDVSEHDGP--------NWPAR 141
Cdd:cd01907 94 WYGAHPFSI----GDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYL---DLLLRKGGLPleyykhiiRMPEE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 142 IRHF-----MTLAPLS----YSLVVMHKDKIYAVRDSYGNRPLCLGKivpvdaghaniNDQLaegWVVSSESCGFLSIGA 212
Cdd:cd01907 167 ERELllalrLTYRLADldgpFTIIVGTPDGFIVIRDRIKLRPAVVAE-----------TDDY---VAIASEECAIREIPD 232
|
250
....*....|....*
gi 24659604 213 RYVREV---EPGEII 224
Cdd:cd01907 233 RDNAKVwepRPGEYV 247
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
43-229 |
1.12e-13 |
|
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine amidotransferase-like protein of unknown function found in prokaryotes, eukaryotes and archaea. YafJ has a conserved structural fold similar to those of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The YafJ fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238889 [Multi-domain] Cd Length: 257 Bit Score: 70.88 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 43 FNDEA----IRKLKGNLGIGHTRYSTAAASEVVNCQPFVvhtaHGALAIAHNGELVNCESLRREVLE---RGVGLSThsD 115
Cdd:cd01908 66 WSDINleslARPIKSPLVLAHVRAATVGPVSLENCHPFT----RGRWLFAHNGQLDGFRLLRRRLLRllpRLPVGTT--D 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 116 SELIaqsLCCAPEDVSEHDgPNWPARIRHFM---------TLAPLSYSLVVMHKDKIYAVRDS------YGNRPLCLGKI 180
Cdd:cd01908 140 SELA---FALLLSRLLERD-PLDPAELLDAIlqtlrelaaLAPPGRLNLLLSDGEYLIATRYAsapslyYLTRRAPFGCA 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24659604 181 VPVDAGHANINDqlaEGWVVSSESCGFlsigARYVREVEPGEIIELSRN 229
Cdd:cd01908 216 RLLFRSVTTPND---DGVVVASEPLTD----DEGWTEVPPGELVVVSEG 257
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
53-178 |
3.09e-13 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.
Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 66.56 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 53 GNLGIGHTRYSTAAASEVVNcQPFVvhTAHGALAIAHNGELVNCESLRREVLERGVGLSTHSDSELIAQSLCCAPEDVSE 132
Cdd:pfam13522 10 GGVALGHVRLAIVDLPDAGN-QPML--SRDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYEEWGEDCLE 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 24659604 133 hdgpnwpaRIRHFMTLAplsysLVVMHKDKIYAVRDSYGNRPLCLG 178
Cdd:pfam13522 87 --------RLRGMFAFA-----IWDRRRRTLFLARDRLGIKPLYYG 119
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
5-121 |
2.30e-12 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 69.28 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 5 GLVALQHRGQESAGIVT-----SLgKSSKNFSVHKGMGMINNLFNDEAIRKLKGNLGIGHTRYSTAAASEVVNCQPFvvH 79
Cdd:PTZ00295 43 GIEILQNRGYDSCGISTissggEL-KTTKYASDGTTSDSIEILKEKLLDSHKNSTIGIAHTRWATHGGKTDENAHPH--C 119
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 24659604 80 TAHGALAIAHNGELVNCESLRREVLERGVGLSTHSDSELIAQ 121
Cdd:PTZ00295 120 DYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIAN 161
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
74-208 |
3.89e-11 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes such as asparagine synthetase and glutamine-fructose-6-phosphate transaminase.
Pssm-ID: 433289 [Multi-domain] Cd Length: 123 Bit Score: 60.22 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 74 QPFVVHtAHGALAIAHNGELVNCESLRREVLERGVGLSTHSDSELIAQSLccapedvSEHDGPNWPARIRHfmtlaplSY 153
Cdd:pfam13537 14 QPMVSS-EDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLY-------EAEWGEDCVDRLNG-------MF 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 24659604 154 SLVVM--HKDKIYAVRDSYGNRPLCLGKivpvDAGhanindqlaEGWVVSSESCGFL 208
Cdd:pfam13537 79 AFAIWdrRRQRLFLARDRFGIKPLYYGR----DDG---------GRLLFASELKALL 122
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
53-234 |
6.34e-11 |
|
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia.
Pssm-ID: 238364 [Multi-domain] Cd Length: 220 Bit Score: 61.80 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 53 GNLGIGHTRYS---TAAASevvncQPFvvHTAHGALAIAHNGELVNCESLRREVLERGVGLSTHSDSELIAQSLccaped 129
Cdd:cd00712 40 EGVALGHRRLSiidLSGGA-----QPM--VSEDGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHLY------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 130 vsEHDGPNWPARIRHFmtlaplsYSLVV--MHKDKIYAVRDSYGNRPLCLGK-------------IVPVDAGHANIN--- 191
Cdd:cd00712 107 --EEWGEDCLERLNGM-------FAFALwdKRKRRLFLARDRFGIKPLYYGRdggglafaselkaLLALPGVPRELDeaa 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 24659604 192 -DQLAEGWVVSSESCGFlsigaRYVREVEPGEIIELSRNGYRTV 234
Cdd:cd00712 178 lAEYLAFQYVPAPRTIF-----KGIRKLPPGHYLTVDPGGVEIR 216
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
53-230 |
4.59e-10 |
|
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis
Pssm-ID: 440136 [Multi-domain] Cd Length: 558 Bit Score: 61.78 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 53 GNLGIGHTRYS----TAAASevvncQPFvvHTAHGALAIAHNGELVNCESLRREVLERGVGLSTHSDSELIAQSLccape 128
Cdd:COG0367 40 GGVALGHRRLSiidlSEGGH-----QPM--VSEDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHAY----- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 129 dvsEHDGPNWPARIRHfMtlaplsYSLVV--MHKDKIYAVRDSYGNRPLCLGK-------------IVPVDAGHANINDQ 193
Cdd:COG0367 108 ---EEWGEDCLERLNG-M------FAFAIwdRRERRLFLARDRFGIKPLYYAEdggglafaselkaLLAHPGVDRELDPE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24659604 194 -----LAEGWVVSSESCgFlsigaRYVREVEPGEIIELSRNG 230
Cdd:COG0367 178 alaeyLTLGYVPAPRTI-F-----KGIRKLPPGHYLTVDAGG 213
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
45-230 |
1.53e-09 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 58.44 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 45 DEAIRKLKGNLGIGHTRYSTAAASEVVNCQPFVvhtaHGALAIAHNGELVNCESLRREVLER-GVGLSTH----SDSELI 119
Cdd:COG0121 68 RLLARPIKSRLVIAHVRKATVGPVSLENTHPFR----GGRWLFAHNGQLDGFDRLRRRLAEElPDELYFQpvgtTDSELA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 120 AqslCCAPEDVSEHDGPNWPARIRHFMTL-----APLSYSLVVMHKDKIYAVRDSYGNRPLCLGKIVPVDAGHanindql 194
Cdd:COG0121 144 F---ALLLSRLRDGGPDPAEALAEALRELaelarAPGRLNLLLSDGERLYATRYTSDDPYPTLYYLTRTTPDD------- 213
|
170 180 190
....*....|....*....|....*....|....*.
gi 24659604 195 aEGWVVSSEScgfLSIGARYvREVEPGEIIELSRNG 230
Cdd:COG0121 214 -RVVVVASEP---LTDDEGW-TEVPPGELLVVRDGL 244
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
5-119 |
3.94e-07 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 52.45 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 5 GLVALQHRGQESAGIVTSLGKSSKNFS--VHKGMGMINNL---FNDEAIRK-LKGNL------GIGHTRYSTAAASEVVN 72
Cdd:PLN02981 26 GLRRLEYRGYDSAGIAIDNDPSLESSSplVFREEGKIESLvrsVYEEVAETdLNLDLvfenhaGIAHTRWATHGPPAPRN 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 24659604 73 CQPfvvHT--AHGALAIAHNGELVNCESLRREVLERGVGLSTHSDSELI 119
Cdd:PLN02981 106 SHP---QSsgPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVI 151
|
|
| PRK07322 |
PRK07322 |
adenine phosphoribosyltransferase; Provisional |
275-381 |
6.86e-07 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 180928 Cd Length: 178 Bit Score: 49.21 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 275 GRQLARESPLDADLVSSVPESGTAAAHGYARESGLPFgEVLCKNR--YVGRTFIQP----STRLRQLGVAKkfGALAQNV 348
Cdd:PRK07322 42 AEALAKRLPTEVDVLVTPETKGIPLAHALSRRLGKPY-VVARKSRkpYMQDPIIQEvvsiTTGKPQLLVLD--GADAEKL 118
|
90 100 110
....*....|....*....|....*....|...
gi 24659604 349 EGKRIVLVDDSIVRGNTIGPIIKLLRDAGATEV 381
Cdd:PRK07322 119 KGKRVAIVDDVVSTGGTLTALERLVERAGGQVV 151
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
5-120 |
3.05e-06 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 49.88 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 5 GLVALQHRGQESAGIVTSLGKSSKNFS------------VHKGMGMINNL----FNDEAI-------RKLKGNLGIGHTR 61
Cdd:PTZ00394 26 GIQKVEYRGYDSAGLAIDANIGSEKEDgtaasaptprpcVVRSVGNISQLrekvFSEAVAatlppmdATTSHHVGIAHTR 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 24659604 62 YSTAAASEVVNCQPfvVHTAHGALAIAHNGELVNCESLRREVLERGVGLSTHSDSELIA 120
Cdd:PTZ00394 106 WATHGGVCERNCHP--QQSNNGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEVIS 162
|
|
| PRK02277 |
PRK02277 |
orotate phosphoribosyltransferase-like protein; Provisional |
338-381 |
9.71e-06 |
|
orotate phosphoribosyltransferase-like protein; Provisional
Pssm-ID: 235023 [Multi-domain] Cd Length: 200 Bit Score: 46.40 E-value: 9.71e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 24659604 338 AKKFGALAQN---VEGKRIVLVDDSIVRGNTIGPIIKLLRDAGATEV 381
Cdd:PRK02277 125 EKKTGSFSRNfasVEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPV 171
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
9-178 |
6.19e-05 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 45.48 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 9 LQHRGQESAGI-VTSLGKSSKNFSVHKGMGMINnlfndeairklkgnLGIGHtrystaaasevvncQPFVVhtAHGALAI 87
Cdd:PTZ00077 28 LRHRGPDWSGIiVLENSPGTYNILAHERLAIVD--------------LSDGK--------------QPLLD--DDETVAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 88 AHNGELVNCESLRREVLERGVGLSTHSDSELIaqslccaPEDVSEHDGPNWPARIRHFmtlaplsYSLVV--MHKDKIYA 165
Cdd:PTZ00077 78 MQNGEIYNHWEIRPELEKEGYKFSSNSDCEII-------GHLYKEYGPKDFWNHLDGM-------FATVIydMKTNTFFA 143
|
170
....*....|...
gi 24659604 166 VRDSYGNRPLCLG 178
Cdd:PTZ00077 144 ARDHIGIIPLYIG 156
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
308-383 |
1.64e-04 |
|
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.
Pssm-ID: 425489 [Multi-domain] Cd Length: 150 Bit Score: 41.97 E-value: 1.64e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24659604 308 GLPFGEVLCKNRYVGRTFIQPSTRLRQLGVAKKFGALAQNVEGKRIVLVDDSIVRGNTIGPIIKLLRDAGATEVHI 383
Cdd:pfam00156 40 GLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKTSSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKI 115
|
|
| PRK02269 |
PRK02269 |
ribose-phosphate diphosphokinase; |
347-435 |
1.89e-03 |
|
ribose-phosphate diphosphokinase;
Pssm-ID: 167353 [Multi-domain] Cd Length: 320 Bit Score: 40.16 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 347 NVEGKRIVLVDDSIVRGNTIGPIIKLLRDAGATEVHIRIASPPLQYPCYMGINIPTREELIAN---KLNADQLADHVGAD 423
Cdd:PRK02269 214 NVKGKKCILIDDMIDTAGTICHAADALAEAGATEVYASCTHPVLSGPALDNIQKSAIEKLVVLdtiYLPEERLIDKIEQI 293
|
90
....*....|..
gi 24659604 424 SLAYLSVEGLVK 435
Cdd:PRK02269 294 SIADLLGEAIIR 305
|
|
| Hpt1 |
COG2236 |
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ... |
342-383 |
1.90e-03 |
|
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage
Pssm-ID: 441837 [Multi-domain] Cd Length: 153 Bit Score: 38.67 E-value: 1.90e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 24659604 342 GALAQNVEGKRIVLVDDSIVRGNTIGPIIKLLRDAGATEVHI 383
Cdd:COG2236 80 GPLDEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRT 121
|
|
| PyrE |
COG0461 |
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ... |
270-383 |
2.71e-03 |
|
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440229 Cd Length: 201 Bit Score: 38.98 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 270 ARLQCGRQLA---RESPLDADLVSSVPESGTAAAHGYARESGLPFGevlcknrYVGRtfiqpstrlrqlgVAKKFGALAQ 346
Cdd:COG0461 45 ALELLGEALAeliKELGPEFDAVAGPATGGIPLAAAVARALGLPAI-------FVRK-------------EAKDHGTGGQ 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 24659604 347 ----NVEGKRIVLVDDSIVRGNTIGPIIKLLRDAGATEVHI 383
Cdd:COG0461 105 ieggLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGV 145
|
|
| PrsA |
COG0462 |
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ... |
347-383 |
2.86e-03 |
|
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; Phosphoribosylpyrophosphate synthetase is part of the Pathway/BioSystem: Histidine biosynthesis, Purine biosynthesis
Pssm-ID: 440230 [Multi-domain] Cd Length: 311 Bit Score: 39.66 E-value: 2.86e-03
10 20 30
....*....|....*....|....*....|....*..
gi 24659604 347 NVEGKRIVLVDDSIVRGNTIGPIIKLLRDAGATEVHI 383
Cdd:COG0462 208 DVEGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVYA 244
|
|
| PRK09162 |
PRK09162 |
hypoxanthine-guanine phosphoribosyltransferase; Provisional |
345-403 |
3.11e-03 |
|
hypoxanthine-guanine phosphoribosyltransferase; Provisional
Pssm-ID: 181675 Cd Length: 181 Bit Score: 38.69 E-value: 3.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24659604 345 AQNVEGKRIVLVDDSIVRGNTIGPIIKLLRDAGATEVHIRI--------ASPPLQyPCYMGINIPTR 403
Cdd:PRK09162 92 RESLKGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAVlvdkthdrKAKPLK-ADFVGLEVPDR 157
|
|
| PRK03092 |
PRK03092 |
ribose-phosphate diphosphokinase; |
347-383 |
3.55e-03 |
|
ribose-phosphate diphosphokinase;
Pssm-ID: 179535 [Multi-domain] Cd Length: 304 Bit Score: 39.16 E-value: 3.55e-03
10 20 30
....*....|....*....|....*....|....*..
gi 24659604 347 NVEGKRIVLVDDSIVRGNTIGPIIKLLRDAGATEVHI 383
Cdd:PRK03092 198 DVEGRTCVLVDDMIDTGGTIAGAVRALKEAGAKDVII 234
|
|
| Apt |
COG0503 |
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ... |
273-383 |
4.37e-03 |
|
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism]; Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein is part of the Pathway/BioSystem: Purine salvage
Pssm-ID: 440269 Cd Length: 171 Bit Score: 38.13 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659604 273 QCGRQLARE-SPLDADLVSSVPESGTAAAHGYARESGLPFgeVLC-KNRYVGRTFIQPS-----TRLRQLGVAKKfgALA 345
Cdd:COG0503 35 AAGDELAERfADKGIDKVVGIEARGFILAAALAYALGVPF--VPArKPGKLPGETVSEEydleyGTGDTLELHKD--ALK 110
|
90 100 110
....*....|....*....|....*....|....*...
gi 24659604 346 qnvEGKRIVLVDDSIVRGNTIGPIIKLLRDAGATEVHI 383
Cdd:COG0503 111 ---PGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGI 145
|
|
| PLN02238 |
PLN02238 |
hypoxanthine phosphoribosyltransferase |
336-381 |
6.66e-03 |
|
hypoxanthine phosphoribosyltransferase
Pssm-ID: 215132 Cd Length: 189 Bit Score: 37.71 E-value: 6.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 24659604 336 GVAK-KFGALAQNVEGKRIVLVDDSIVRGNTIGPIIKLLRDAGATEV 381
Cdd:PLN02238 82 GVAKvSGADLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASV 128
|
|
| ribP_PPkin |
TIGR01251 |
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ... |
347-381 |
7.55e-03 |
|
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In some systems, close homologs lacking enzymatic activity exist and perform regulatory functions. The model is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273523 [Multi-domain] Cd Length: 308 Bit Score: 38.41 E-value: 7.55e-03
10 20 30
....*....|....*....|....*....|....*
gi 24659604 347 NVEGKRIVLVDDSIVRGNTIGPIIKLLRDAGATEV 381
Cdd:TIGR01251 207 DVEGKDVVIVDDIIDTGGTIAKAAEILKSAGAKRV 241
|
|
| PRK01259 |
PRK01259 |
ribose-phosphate diphosphokinase; |
347-407 |
9.67e-03 |
|
ribose-phosphate diphosphokinase;
Pssm-ID: 234929 [Multi-domain] Cd Length: 309 Bit Score: 37.79 E-value: 9.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24659604 347 NVEGKRIVLVDDSIVRGNTIGPIIKLLRDAGATEVHIRIASPPLQYPCYMGINIPTREELI 407
Cdd:PRK01259 205 DVEGRDCILVDDMIDTAGTLCKAAEALKERGAKSVYAYATHPVLSGGAIERIENSVIDELV 265
|
|
| |
