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Conserved domains on  [gi|253972259|gb|ACT37930|]
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gamma-glutamyl kinase [Escherichia coli B str. REL606]

Protein Classification

glutamate 5-kinase( domain architecture ID 11490098)

glutamate 5-kinase catalyzes glutamate-dependent ATP cleavage, and transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, in the first and controlling step of proline (or ornithine) biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proB TIGR01027
glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ...
 5-366 0e+00

glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ProB-like domain of delta 1-pyrroline-5-carboxylate synthetase does not hit the C-terminal 100 residues of this model. The noise cutoff is set low enough to hit delta 1-pyrroline-5-carboxylate synthetase and other partial matches to this family. [Amino acid biosynthesis, Glutamate family]


:

Pssm-ID: 162163 [Multi-domain]  Cd Length: 363  Bit Score: 577.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259    5 QTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPELPATIASKQLLAAVGQSRLI 84
Cdd:TIGR01027   1 QRIVVKVGSSSLTGSSGSLDRSHIAELVEQVAALHAAGHEVVIVSSGAIAAGFEALGLPERPKTLAEKQALAAVGQVRLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259   85 QLWEQLFSIYGIHVGQMLLTRADMEDRERFLNARDTLRALLDNNIVPVINENDAVATAEIKVGDNDNLSALAAILAGADK 164
Cdd:TIGR01027  81 QLYEQLFSQYGIKVAQILLTRADFSDRERYLNARNTLEALLELGVVPIINENDTVATEEIKFGDNDTLSALVAILVGADL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  165 LLLLTDQKGLYTADPRSNPQAELIKDVYGIDDALRAIAGDSVSGLGTGGMSTKLQAADVACRAGIDTIIAAGSKPGVIGD 244
Cdd:TIGR01027 161 LVLLTDVDGLYDADPRTNPDAKLIPVVEEITDLLLGVAGDSGSSVGTGGMRTKLQAADLATRAGVPVIIASGSKPEKIAD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  245 VMEGISVGTLFHAQATPLENRKRWI-FGAPPAGEITVDEGATAAILERGSSLLPKGIKSVTGNFSRGEVIRICNLEGRDI 323
Cdd:TIGR01027 241 ALEGAPVGTLFHAQARRLRNRKFWIaFASEPAGEITVDAGAEEALLERGKSLLPAGIVGVEGNFSRGEVVEILNPEGQDI 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 253972259  324 AHGVSRYNSDALRRIAGHHSQEIDAILGYEYGPVAVHRDDMIT 366
Cdd:TIGR01027 321 GRGLVNYSSDELEKIKGHKSSEIEAVLGYEYGDEVVHRDDMVL 363
 
Name Accession Description Interval E-value
proB TIGR01027
glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ...
 5-366 0e+00

glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ProB-like domain of delta 1-pyrroline-5-carboxylate synthetase does not hit the C-terminal 100 residues of this model. The noise cutoff is set low enough to hit delta 1-pyrroline-5-carboxylate synthetase and other partial matches to this family. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 162163 [Multi-domain]  Cd Length: 363  Bit Score: 577.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259    5 QTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPELPATIASKQLLAAVGQSRLI 84
Cdd:TIGR01027   1 QRIVVKVGSSSLTGSSGSLDRSHIAELVEQVAALHAAGHEVVIVSSGAIAAGFEALGLPERPKTLAEKQALAAVGQVRLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259   85 QLWEQLFSIYGIHVGQMLLTRADMEDRERFLNARDTLRALLDNNIVPVINENDAVATAEIKVGDNDNLSALAAILAGADK 164
Cdd:TIGR01027  81 QLYEQLFSQYGIKVAQILLTRADFSDRERYLNARNTLEALLELGVVPIINENDTVATEEIKFGDNDTLSALVAILVGADL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  165 LLLLTDQKGLYTADPRSNPQAELIKDVYGIDDALRAIAGDSVSGLGTGGMSTKLQAADVACRAGIDTIIAAGSKPGVIGD 244
Cdd:TIGR01027 161 LVLLTDVDGLYDADPRTNPDAKLIPVVEEITDLLLGVAGDSGSSVGTGGMRTKLQAADLATRAGVPVIIASGSKPEKIAD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  245 VMEGISVGTLFHAQATPLENRKRWI-FGAPPAGEITVDEGATAAILERGSSLLPKGIKSVTGNFSRGEVIRICNLEGRDI 323
Cdd:TIGR01027 241 ALEGAPVGTLFHAQARRLRNRKFWIaFASEPAGEITVDAGAEEALLERGKSLLPAGIVGVEGNFSRGEVVEILNPEGQDI 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 253972259  324 AHGVSRYNSDALRRIAGHHSQEIDAILGYEYGPVAVHRDDMIT 366
Cdd:TIGR01027 321 GRGLVNYSSDELEKIKGHKSSEIEAVLGYEYGDEVVHRDDMVL 363
ProB COG0263
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ...
 1-365 0e+00

Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440033 [Multi-domain]  Cd Length: 371  Bit Score: 573.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259   1 MSDSQTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPELPATIASKQLLAAVGQ 80
Cdd:COG0263    4 LAKARRIVVKIGSSLLTDEGGGLDRARLAALADQIAALRAAGKEVVLVSSGAVAAGRGRLGLPKRPKTLPEKQAAAAVGQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  81 SRLIQLWEQLFSIYGIHVGQMLLTRADMEDRERFLNARDTLRALLDNNIVPVINENDAVATAEIKVGDNDNLSALAAILA 160
Cdd:COG0263   84 GLLMQAYEEAFARHGLTVAQVLLTRDDLEDRRRYLNARNTLETLLELGVVPIINENDTVATDEIRFGDNDRLAALVANLV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 161 GADKLLLLTDQKGLYTADPRSNPQAELIKDVYGIDDALRAIAGDSVSGLGTGGMSTKLQAADVACRAGIDTIIAAGSKPG 240
Cdd:COG0263  164 EADLLVLLTDVDGLYDADPRKDPDAKLIPEVEEITPEIEAMAGGAGSGLGTGGMATKLEAARIATRAGIPTVIASGREPN 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 241 VIGDVMEGISVGTLFHAQATPLENRKRWI-FGAPPAGEITVDEGATAAILERGSSLLPKGIKSVTGNFSRGEVIRICNLE 319
Cdd:COG0263  244 VLLRILAGERVGTLFLPSGEPLSARKRWIaGALQPRGRLVVDAGAVRALRERGKSLLPAGVTAVEGDFERGDVVEIVDPD 323

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 253972259 320 GRDIAHGVSRYNSDALRRIAGHHSQEIDAILGYEYGPVAVHRDDMI 365
Cdd:COG0263  324 GREIARGLVNYSSDELRRIKGRRSDEIEAILGYKGRDEVIHRDNLV 369
AAK_G5K_ProB cd04242
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ...
 6-256 3.14e-136

AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, in the first and controlling step of proline (and, in mammals, ornithine) biosynthesis. G5K is subject to feedback allosteric inhibition by proline or ornithine. In microorganisms and plants, proline plays an important role as an osmoprotectant and, in mammals, ornithine biosynthesis is crucial for proper ammonia detoxification, since a G5K mutation has been shown to cause human hyperammonaemia. Microbial G5K generally consists of two domains: a catalytic G5K domain and one PUA (pseudo uridine synthases and archaeosine-specific transglycosylases) domain, and some lack the PUA domain. G5K requires free Mg for activity, it is tetrameric, and it aggregates to higher forms in a proline-dependent way. G5K lacking the PUA domain remains tetrameric, active, and proline-inhibitable, but the Mg requirement and the proline-triggered aggregation are greatly diminished and abolished, respectively, and more proline is needed for inhibition. Although plant and animal G5Ks are part of a bifunctional polypeptide, delta 1-pyrroline-5-carboxylate synthetase (P5CS), composed of an N-terminal G5K (ProB) and a C-terminal glutamyl 5- phosphate reductase (G5PR; ProA); bacterial and yeast G5Ks are monofunctional single-polypeptide enzymes. In this CD, all three domain architectures are present: G5K, G5K+PUA, and G5K+G5PR.


Pssm-ID: 239775 [Multi-domain]  Cd Length: 251  Bit Score: 387.95  E-value: 3.14e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259   6 TLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPELPATIASKQLLAAVGQSRLIQ 85
Cdd:cd04242    1 RIVVKVGSSLLTDEDGGLDLGRLASLVEQIAELRNQGKEVILVSSGAVAAGRQRLGLEKRPKTLPEKQALAAVGQSLLMA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  86 LWEQLFSIYGIHVGQMLLTRADMEDRERFLNARDTLRALLDNNIVPVINENDAVATAEIKVGDNDNLSALAAILAGADKL 165
Cdd:cd04242   81 LYEQLFAQYGIKVAQILLTRDDFEDRKRYLNARNTLETLLELGVIPIINENDTVATEEIRFGDNDRLSALVAGLVNADLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 166 LLLTDQKGLYTADPRSNPQAELIKDVYGIDDALRAIAGDSVSGLGTGGMSTKLQAADVACRAGIDTIIAAGSKPGVIGDV 245
Cdd:cd04242  161 ILLSDVDGLYDKNPRENPDAKLIPEVEEITDEIEAMAGGSGSSVGTGGMRTKLKAARIATEAGIPVVIANGRKPDVLLDI 240

                        250
                 ....*....|.
gi 253972259 246 MEGISVGTLFH 256
Cdd:cd04242  241 LAGEAVGTLFL 251
PRK12314 PRK12314
gamma-glutamyl kinase; Provisional
 2-259 3.29e-103

gamma-glutamyl kinase; Provisional


Pssm-ID: 183430 [Multi-domain]  Cd Length: 266  Bit Score: 304.86  E-value: 3.29e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259   2 SDSQTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPELPATIASKQLLAAVGQS 81
Cdd:PRK12314   7 ENAKRIVIKVGSSTLSYENGKINLERIEQLVFVISDLMNKGKEVILVSSGAIGAGLTKLKLDKRPTSLAEKQALAAVGQP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  82 RLIQLWEQLFSIYGIHVGQMLLTRADMEDRERFLNARDTLRALLDNNIVPVINENDAVATAEI--KVGDNDNLSALAAIL 159
Cdd:PRK12314  87 ELMSLYSKFFAEYGIVVAQILLTRDDFDSPKSRANVKNTFESLLELGILPIVNENDAVATDEIdtKFGDNDRLSAIVAKL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 160 AGADKLLLLTDQKGLYTADPRSNPQAELIKDVYGIDDALRAIAGDSVSGLGTGGMSTKLQAADVACRAGIDTIIAAGSKP 239
Cdd:PRK12314 167 VKADLLIILSDIDGLYDKNPRINPDAKLRSEVTEITEEILALAGGAGSKFGTGGMVTKLKAAKFLMEAGIKMVLANGFNP 246

                        250       260
                 ....*....|....*....|
gi 253972259 240 GVIGDVMEGISVGTLFHAQA 259
Cdd:PRK12314 247 SDILDFLEGESIGTLFAPKK 266
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 5-234 1.00e-43

Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino acid substrates, as well as uridylate kinase and carbamate kinase. This family includes: Aspartokinase EC:2.7.2.4. Acetylglutamate kinase EC:2.7.2.8. Glutamate 5-kinase EC:2.7.2.11. Uridylate kinase EC:2.7.4.-. Carbamate kinase EC:2.7.2.2.


Pssm-ID: 395565 [Multi-domain]  Cd Length: 232  Bit Score: 150.98  E-value: 1.00e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259    5 QTLVVKLGTSVLTGGSRrlnrahIVELVRQCAQLHAAGHRIVIVTS-GAIAAG---------REHLGYPELPATIASKQL 74
Cdd:pfam00696   1 KRVVIKLGGSSLTDKER------LKRLADEIAALLEEGRKLVVVHGgGAFADGllallglspRFARLTDAETLEVATMDA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259   75 LAAVGQSRLIQLWEQLFSIYGIHVGQMLLTRADMEDRERFLNARDTLRALLDNNIVPVINENDAVATAEIK-VGDNDNLS 153
Cdd:pfam00696  75 LGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVTRIDTEALEELLEAGVVPVITGFIGIDPEGELgRGSSDTLA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  154 ALAAILAGADKLLLLTDQKGLYTADPRSNPQAELIKDVYgIDDALRAIAgdsvSGLGTGGMSTKLQAADVACRAG-IDTI 232
Cdd:pfam00696 155 ALLAEALGADKLIILTDVDGVYTADPRKVPDAKLIPEIS-YDELLELLA----SGLATGGMKVKLPAALEAARRGgIPVV 229


                  ..
gi 253972259  233 IA 234
Cdd:pfam00696 230 IV 231
PUA smart00359
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
276-341 8.08e-14

Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;


Pssm-ID: 214635 [Multi-domain]  Cd Length: 76  Bit Score: 66.13  E-value: 8.08e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 253972259   276 GEITVDEGATAAILeRGSSLLPKGIKSVTGNFSRGEVIRICNLEGRDIAHGVSRYNSDALRRIAGH 341
Cdd:smart00359   1 GKVVVDDGAEKAIL-NGASLLAPGVVRVDGDIKEGDVVVIVDEKGEPLGIGLANMSSEEIARIKGK 65
 
Name Accession Description Interval E-value
proB TIGR01027
glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ...
 5-366 0e+00

glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ProB-like domain of delta 1-pyrroline-5-carboxylate synthetase does not hit the C-terminal 100 residues of this model. The noise cutoff is set low enough to hit delta 1-pyrroline-5-carboxylate synthetase and other partial matches to this family. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 162163 [Multi-domain]  Cd Length: 363  Bit Score: 577.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259    5 QTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPELPATIASKQLLAAVGQSRLI 84
Cdd:TIGR01027   1 QRIVVKVGSSSLTGSSGSLDRSHIAELVEQVAALHAAGHEVVIVSSGAIAAGFEALGLPERPKTLAEKQALAAVGQVRLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259   85 QLWEQLFSIYGIHVGQMLLTRADMEDRERFLNARDTLRALLDNNIVPVINENDAVATAEIKVGDNDNLSALAAILAGADK 164
Cdd:TIGR01027  81 QLYEQLFSQYGIKVAQILLTRADFSDRERYLNARNTLEALLELGVVPIINENDTVATEEIKFGDNDTLSALVAILVGADL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  165 LLLLTDQKGLYTADPRSNPQAELIKDVYGIDDALRAIAGDSVSGLGTGGMSTKLQAADVACRAGIDTIIAAGSKPGVIGD 244
Cdd:TIGR01027 161 LVLLTDVDGLYDADPRTNPDAKLIPVVEEITDLLLGVAGDSGSSVGTGGMRTKLQAADLATRAGVPVIIASGSKPEKIAD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  245 VMEGISVGTLFHAQATPLENRKRWI-FGAPPAGEITVDEGATAAILERGSSLLPKGIKSVTGNFSRGEVIRICNLEGRDI 323
Cdd:TIGR01027 241 ALEGAPVGTLFHAQARRLRNRKFWIaFASEPAGEITVDAGAEEALLERGKSLLPAGIVGVEGNFSRGEVVEILNPEGQDI 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 253972259  324 AHGVSRYNSDALRRIAGHHSQEIDAILGYEYGPVAVHRDDMIT 366
Cdd:TIGR01027 321 GRGLVNYSSDELEKIKGHKSSEIEAVLGYEYGDEVVHRDDMVL 363
ProB COG0263
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ...
 1-365 0e+00

Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440033 [Multi-domain]  Cd Length: 371  Bit Score: 573.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259   1 MSDSQTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPELPATIASKQLLAAVGQ 80
Cdd:COG0263    4 LAKARRIVVKIGSSLLTDEGGGLDRARLAALADQIAALRAAGKEVVLVSSGAVAAGRGRLGLPKRPKTLPEKQAAAAVGQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  81 SRLIQLWEQLFSIYGIHVGQMLLTRADMEDRERFLNARDTLRALLDNNIVPVINENDAVATAEIKVGDNDNLSALAAILA 160
Cdd:COG0263   84 GLLMQAYEEAFARHGLTVAQVLLTRDDLEDRRRYLNARNTLETLLELGVVPIINENDTVATDEIRFGDNDRLAALVANLV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 161 GADKLLLLTDQKGLYTADPRSNPQAELIKDVYGIDDALRAIAGDSVSGLGTGGMSTKLQAADVACRAGIDTIIAAGSKPG 240
Cdd:COG0263  164 EADLLVLLTDVDGLYDADPRKDPDAKLIPEVEEITPEIEAMAGGAGSGLGTGGMATKLEAARIATRAGIPTVIASGREPN 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 241 VIGDVMEGISVGTLFHAQATPLENRKRWI-FGAPPAGEITVDEGATAAILERGSSLLPKGIKSVTGNFSRGEVIRICNLE 319
Cdd:COG0263  244 VLLRILAGERVGTLFLPSGEPLSARKRWIaGALQPRGRLVVDAGAVRALRERGKSLLPAGVTAVEGDFERGDVVEIVDPD 323

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 253972259 320 GRDIAHGVSRYNSDALRRIAGHHSQEIDAILGYEYGPVAVHRDDMI 365
Cdd:COG0263  324 GREIARGLVNYSSDELRRIKGRRSDEIEAILGYKGRDEVIHRDNLV 369
AAK_G5K_ProB cd04242
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ...
 6-256 3.14e-136

AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, in the first and controlling step of proline (and, in mammals, ornithine) biosynthesis. G5K is subject to feedback allosteric inhibition by proline or ornithine. In microorganisms and plants, proline plays an important role as an osmoprotectant and, in mammals, ornithine biosynthesis is crucial for proper ammonia detoxification, since a G5K mutation has been shown to cause human hyperammonaemia. Microbial G5K generally consists of two domains: a catalytic G5K domain and one PUA (pseudo uridine synthases and archaeosine-specific transglycosylases) domain, and some lack the PUA domain. G5K requires free Mg for activity, it is tetrameric, and it aggregates to higher forms in a proline-dependent way. G5K lacking the PUA domain remains tetrameric, active, and proline-inhibitable, but the Mg requirement and the proline-triggered aggregation are greatly diminished and abolished, respectively, and more proline is needed for inhibition. Although plant and animal G5Ks are part of a bifunctional polypeptide, delta 1-pyrroline-5-carboxylate synthetase (P5CS), composed of an N-terminal G5K (ProB) and a C-terminal glutamyl 5- phosphate reductase (G5PR; ProA); bacterial and yeast G5Ks are monofunctional single-polypeptide enzymes. In this CD, all three domain architectures are present: G5K, G5K+PUA, and G5K+G5PR.


Pssm-ID: 239775 [Multi-domain]  Cd Length: 251  Bit Score: 387.95  E-value: 3.14e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259   6 TLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPELPATIASKQLLAAVGQSRLIQ 85
Cdd:cd04242    1 RIVVKVGSSLLTDEDGGLDLGRLASLVEQIAELRNQGKEVILVSSGAVAAGRQRLGLEKRPKTLPEKQALAAVGQSLLMA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  86 LWEQLFSIYGIHVGQMLLTRADMEDRERFLNARDTLRALLDNNIVPVINENDAVATAEIKVGDNDNLSALAAILAGADKL 165
Cdd:cd04242   81 LYEQLFAQYGIKVAQILLTRDDFEDRKRYLNARNTLETLLELGVIPIINENDTVATEEIRFGDNDRLSALVAGLVNADLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 166 LLLTDQKGLYTADPRSNPQAELIKDVYGIDDALRAIAGDSVSGLGTGGMSTKLQAADVACRAGIDTIIAAGSKPGVIGDV 245
Cdd:cd04242  161 ILLSDVDGLYDKNPRENPDAKLIPEVEEITDEIEAMAGGSGSSVGTGGMRTKLKAARIATEAGIPVVIANGRKPDVLLDI 240

                        250
                 ....*....|.
gi 253972259 246 MEGISVGTLFH 256
Cdd:cd04242  241 LAGEAVGTLFL 251
PRK12314 PRK12314
gamma-glutamyl kinase; Provisional
 2-259 3.29e-103

gamma-glutamyl kinase; Provisional


Pssm-ID: 183430 [Multi-domain]  Cd Length: 266  Bit Score: 304.86  E-value: 3.29e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259   2 SDSQTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPELPATIASKQLLAAVGQS 81
Cdd:PRK12314   7 ENAKRIVIKVGSSTLSYENGKINLERIEQLVFVISDLMNKGKEVILVSSGAIGAGLTKLKLDKRPTSLAEKQALAAVGQP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  82 RLIQLWEQLFSIYGIHVGQMLLTRADMEDRERFLNARDTLRALLDNNIVPVINENDAVATAEI--KVGDNDNLSALAAIL 159
Cdd:PRK12314  87 ELMSLYSKFFAEYGIVVAQILLTRDDFDSPKSRANVKNTFESLLELGILPIVNENDAVATDEIdtKFGDNDRLSAIVAKL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 160 AGADKLLLLTDQKGLYTADPRSNPQAELIKDVYGIDDALRAIAGDSVSGLGTGGMSTKLQAADVACRAGIDTIIAAGSKP 239
Cdd:PRK12314 167 VKADLLIILSDIDGLYDKNPRINPDAKLRSEVTEITEEILALAGGAGSKFGTGGMVTKLKAAKFLMEAGIKMVLANGFNP 246

                        250       260
                 ....*....|....*....|
gi 253972259 240 GVIGDVMEGISVGTLFHAQA 259
Cdd:PRK12314 247 SDILDFLEGESIGTLFAPKK 266
AAK_P5CS_ProBA cd04256
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ...
 1-256 1.47e-59

AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta 1-pyrroline-5-carboxylate synthetase (P5CS), composed of an N-terminal G5K (ProB) and a C-terminal glutamyl 5- phosphate reductase (G5PR, ProA), the first and second enzyme catalyzing proline (and, in mammals, ornithine) biosynthesis. G5K transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, and is subject to feedback allosteric inhibition by proline or ornithine. In plants, proline plays an important role as an osmoprotectant and, in mammals, ornithine biosynthesis is crucial for proper ammonia detoxification, since a G5K mutation has been shown to cause human hyperammonaemia.


Pssm-ID: 239789 [Multi-domain]  Cd Length: 284  Bit Score: 193.80  E-value: 1.47e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259   1 MSDSQTLVVKLGTSVLT-GGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGY----------------- 62
Cdd:cd04256    5 LKHAKRIVVKLGSAVVTrEDECGLALGRLASIVEQVSELQSQGREVILVTSGAVAFGKQRLRHeillsssmrqtlksgql 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  63 PELPATIASKQLLAAVGQSRLIQLWEQLFSIYGIHVGQMLLTRADMEDRERFLNARDTLRALLDNNIVPVINENDAVATA 142
Cdd:cd04256   85 KDMPQMELDGRACAAVGQSGLMALYEAMFTQYGITVAQVLVTKPDFYDEQTRRNLNGTLEELLRLNIIPIINTNDAVSPP 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 143 E---------IKVGDNDNLSALAAILAGADKLLLLTDQKGLYTADPRSnPQAELIKDVYGIDdaLRAIAGDSVSGLGTGG 213
Cdd:cd04256  165 PepdedlqgvISIKDNDSLAARLAVELKADLLILLSDVDGLYDGPPGS-DDAKLIHTFYPGD--QQSITFGTKSRVGTGG 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 253972259 214 MSTKLQAADVACRAGIDTIIAAGSKPGVIGDVMEGISVGTLFH 256
Cdd:cd04256  242 MEAKVKAALWALQGGTSVVITNGMAGDVITKILEGKKVGTFFT 284
PLN02418 PLN02418
delta-1-pyrroline-5-carboxylate synthase
 3-287 2.84e-52

delta-1-pyrroline-5-carboxylate synthase


Pssm-ID: 215230  Cd Length: 718  Bit Score: 184.54  E-value: 2.84e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259   3 DSQTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPEL----------PATIASK 72
Cdd:PLN02418  14 DVKRVVIKVGTAVVTRDDGRLALGRLGALCEQIKELNSDGYEVILVSSGAVGVGRQRLRYRRLvnssfadlqkPQMELDG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  73 QLLAAVGQSRLIQLWEQLFSIYGIHVGQMLLTRADMEDRERFLNARDTLRALLDNNIVPVINENDAVAT-------AEIK 145
Cdd:PLN02418  94 KACAAVGQSELMALYDTLFSQLDVTASQLLVTDSDFRDPDFRKQLSETVESLLDLRVIPIFNENDAVSTrrapyedSSGI 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 146 VGDNDNLSALAAILAGADKLLLLTDQKGLYTADPrSNPQAELIKdVYGIDDALRAIAGDSVSGLGTGGMSTKLQAADVAC 225
Cdd:PLN02418 174 FWDNDSLAALLALELKADLLILLSDVEGLYTGPP-SDPSSKLIH-TYIKEKHQDEITFGEKSRVGRGGMTAKVKAAVNAA 251

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 253972259 226 RAGIDTIIAAGSKPGVIGDVMEGISVGTLFHAQATplenrkRWifgaPPAGEITVDEGATAA 287
Cdd:PLN02418 252 SAGIPVVITSGYALDNIRKVLRGERVGTLFHQDAH------LW----APSKEVGAREMAVAA 303
P5CS TIGR01092
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ...
 3-259 1.25e-51

delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, EC 2.7.2.11) region followed by a gamma-glutamyl phosphate reductase (ProA, EC 1.2.1.41) region. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 130164 [Multi-domain]  Cd Length: 715  Bit Score: 182.80  E-value: 1.25e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259    3 DSQTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPEL----------PATIASK 72
Cdd:TIGR01092   6 DVKRIVVKVGTAVVTRGDGRLALGRLGSICEQLSELNSDGREVILVTSGAVAFGRQRLRHRILvnssfadlqkPQPELDG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259   73 QLLAAVGQSRLIQLWEQLFSIYGIHVGQMLLTRADMEDRERFLNARDTLRALLDNNIVPVINENDAVATAEIK------- 145
Cdd:TIGR01092  86 KACAAVGQSGLMALYETMFTQLDITAAQILVTDLDFRDEQFRRQLNETVHELLRMNVVPVVNENDAVSTRAAPysdsqgi 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  146 VGDNDNLSALAAILAGADKLLLLTDQKGLYTADPrSNPQAELIkDVYGIDDALRAIAGDSVSGLGTGGMSTKLQAADVAC 225
Cdd:TIGR01092 166 FWDNDSLAALLALELKADLLILLSDVEGLYDGPP-SDDDSKLI-DTFYKEKHQGEITFGTKSRLGRGGMTAKVKAAVWAA 243

                         250       260       270
                  ....*....|....*....|....*....|....
gi 253972259  226 RAGIDTIIAAGSKPGVIGDVMEGISVGTLFHAQA 259
Cdd:TIGR01092 244 YGGTPVIIASGTAPKNITKVVEGKKVGTLFHEDA 277
PUA_G5K cd21157
PUA domain of gamma-glutamyl kinase, found in archaea, bacteria, and eukarya; Gamma glutamyl ...
 264-365 1.68e-48

PUA domain of gamma-glutamyl kinase, found in archaea, bacteria, and eukarya; Gamma glutamyl kinase (G5K) is an enzyme essential for the biosynthesis of L-proline; it catalyzes the transfer of a phosphate group to glutamate. The resulting glutamate 5-phosphate cyclizes spontaneously to form 5-oxoproline. The PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain functions as an RNA binding domain in many other proteins; however, its role in G5K is not understood. It might play a role in modulating the enzymatic properties of bacterial G5Ks.


Pssm-ID: 409299 [Multi-domain]  Cd Length: 104  Bit Score: 159.17  E-value: 1.68e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 264 NRKRWI-FGAPPAGEITVDEGATAAILERGSSLLPKGIKSVTGNFSRGEVIRICNLEGRDIAHGVSRYNSDALRRIAGHH 342
Cdd:cd21157    1 ARKQWIaFALKPKGKLVVDAGAVKALLEGGKSLLPAGITAVEGDFERGDVVRIVDPDGREIARGLVNYSSEELRKIKGKK 80

                         90       100
                 ....*....|....*....|...
gi 253972259 343 SQEIDAILGYEYGPVAVHRDDMI 365
Cdd:cd21157   81 SSEIEEILGYKYGDEVIHRDNLV 103
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 5-234 1.00e-43

Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino acid substrates, as well as uridylate kinase and carbamate kinase. This family includes: Aspartokinase EC:2.7.2.4. Acetylglutamate kinase EC:2.7.2.8. Glutamate 5-kinase EC:2.7.2.11. Uridylate kinase EC:2.7.4.-. Carbamate kinase EC:2.7.2.2.


Pssm-ID: 395565 [Multi-domain]  Cd Length: 232  Bit Score: 150.98  E-value: 1.00e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259    5 QTLVVKLGTSVLTGGSRrlnrahIVELVRQCAQLHAAGHRIVIVTS-GAIAAG---------REHLGYPELPATIASKQL 74
Cdd:pfam00696   1 KRVVIKLGGSSLTDKER------LKRLADEIAALLEEGRKLVVVHGgGAFADGllallglspRFARLTDAETLEVATMDA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259   75 LAAVGQSRLIQLWEQLFSIYGIHVGQMLLTRADMEDRERFLNARDTLRALLDNNIVPVINENDAVATAEIK-VGDNDNLS 153
Cdd:pfam00696  75 LGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVTRIDTEALEELLEAGVVPVITGFIGIDPEGELgRGSSDTLA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  154 ALAAILAGADKLLLLTDQKGLYTADPRSNPQAELIKDVYgIDDALRAIAgdsvSGLGTGGMSTKLQAADVACRAG-IDTI 232
Cdd:pfam00696 155 ALLAEALGADKLIILTDVDGVYTADPRKVPDAKLIPEIS-YDELLELLA----SGLATGGMKVKLPAALEAARRGgIPVV 229


                  ..
gi 253972259  233 IA 234
Cdd:pfam00696 230 IV 231
PTZ00489 PTZ00489
glutamate 5-kinase; Provisional
 7-260 5.64e-37

glutamate 5-kinase; Provisional


Pssm-ID: 240438 [Multi-domain]  Cd Length: 264  Bit Score: 134.37  E-value: 5.64e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259   7 LVVKLGTSVLTGgSRRLNRAHIVELVRQCAQLHAAgHRIVIVTSGAIAAGREHLGYPElpATIASKQLLAAVGQSRLIQL 86
Cdd:PTZ00489  11 IVVKVGSSILVD-NQEIAAHRIEALCRFIADLQTK-YEVILVTSGAVAAGYTKKEMDK--SYVPNKQALASMGQPLLMHM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  87 WEQLFSIYGIHVGQMLLTRADMEDRERFLNARDTLRALLDNNIVPVINENDAVATAEIKVGDNDNLSALAAILAGADKLL 166
Cdd:PTZ00489  87 YYTELQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALHELVFGDNDRLSALVAHHFKADLLV 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 167 LLTDQKGLYTADPRSNPQAELIKDVYGIDDALRAIAGDSVSGLGTGGMSTKLQAADVACRAGIDTIIAAGSKPGVIGDVM 246
Cdd:PTZ00489 167 ILSDIDGYYTENPRTSTDAKIRSVVHELSPDDLVAEATPNNRFATGGIVTKLQAAQFLLERGGKMYLSSGFHLEKARDFL 246

                        250
                 ....*....|....*.
gi 253972259 247 EGIS--VGTLFHAQAT 260
Cdd:PTZ00489 247 IGGSheIGTLFYPRVS 262
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 8-255 3.83e-28

Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like N-acetylglutamate kinase (NAGK), carbamate kinase (CK), aspartokinase (AK), glutamate-5-kinase (G5K) and UMP kinase (UMPK). The AAK superfamily includes kinases that phosphorylate a variety of amino acid substrates. These kinases catalyze the formation of phosphoric anhydrides, generally with a carboxylate, and use ATP as the source of the phosphoryl group; are involved in amino acid biosynthesis. Some of these kinases control the process via allosteric feed-back inhibition.


Pssm-ID: 239033 [Multi-domain]  Cd Length: 248  Bit Score: 110.22  E-value: 3.83e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259   8 VVKLGTSVLTGGSRRLNRAHIVelvrqcAQLHAAGHRIVIVTSGAIAAGREHLGYPELPA-------TIASKQLLAAVGQ 80
Cdd:cd02115    1 VIKFGGSSVSSEERLRNLARIL------VKLASEGGRVVVVHGAGPQITDELLAHGELLGyarglriTDRETDALAAMGE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  81 SRLIQLWEQLFSIYGIHVGQMLLTRADMEDRERFLNAR------DTLRALLDNNIVPVINENDAVA---TAEIKVGDNDN 151
Cdd:cd02115   75 GMSNLLIAAALEQHGIKAVPLDLTQAGFASPNQGHVGKitkvstDRLKSLLENGILPILSGFGGTDekeTGTLGRGGSDS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 152 LSALAAILAGADKLLLLTDQKGLYTADPRSNPQAELIKDVYgiddalraiAGDSVSGLGTGGMSTKLQAADVACRAGIDT 231
Cdd:cd02115  155 TAALLAAALKADRLVILTDVDGVYTADPRKVPDAKLLSELT---------YEEAAELAYAGAMVLKPKAADPAARAGIPV 225

                        250       260
                 ....*....|....*....|....
gi 253972259 232 IIAAGSKPGVIgDVMEGISVGTLF 255
Cdd:cd02115  226 RIANTENPGAL-ALFTPDGGGTLI 248
PUA pfam01472
PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, ...
 276-350 1.00e-18

PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, was detected in archaeal and eukaryotic pseudouridine synthases, archaeal archaeosine synthases, a family of predicted ATPases that may be involved in RNA modification, a family of predicted archaeal and bacterial rRNA methylases. Additionally, the PUA domain was detected in a family of eukaryotic proteins that also contain a domain homologous to the translation initiation factor eIF1/SUI1; these proteins may comprise a novel type of translation factors. Unexpectedly, the PUA domain was detected also in bacterial and yeast glutamate kinases; this is compatible with the demonstrated role of these enzymes in the regulation of the expression of other genes. It is predicted that the PUA domain is an RNA binding domain.


Pssm-ID: 426278 [Multi-domain]  Cd Length: 74  Bit Score: 79.45  E-value: 1.00e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 253972259  276 GEITVDEGATAAILErGSSLLPKGIKSVTGNFSRGEVIRICNLEGRDIAHGVSRYNSDALRRIAGHHSQEIDAIL 350
Cdd:pfam01472   1 GRVVVDDGAVKAILN-GASLLAPGVVRVDGDFRKGDEVVVVTEKGELVAVGLANYSSEELAKIEGGKAVKVRRVL 74
AAK_UMPK-like cd04239
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ...
 8-254 1.46e-14

AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) enzyme that catalyzes UMP phosphorylation and plays a key role in pyrimidine nucleotide biosynthesis. Regulation of this process is via feed-back control and via gene repression of carbamoyl phosphate synthetase (the first enzyme of the pyrimidine biosynthesis pathway). The UMP kinases of E. coli (Ec) and Pyrococcus furiosus (Pf) are known to function as homohexamers, with GTP and UTP being allosteric effectors. Like other related enzymes (carbamate kinase, aspartokinase, and N-acetylglutamate kinase) the E. coli and most bacterial UMPKs have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs appear to lack this residue and the Pyrococcus furiosus structure has an additional Mg ion bound to the ATP molecule which is proposed to function as the catalysis instead. Also included in this CD are the alpha and beta subunits of the Mo storage protein (MosA and MosB) characterized as an alpha4-beta4 octamer containing an ATP-dependent, polynuclear molybdenum-oxide cluster. These and related sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239772 [Multi-domain]  Cd Length: 229  Bit Score: 72.18  E-value: 1.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259   8 VVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSG------AIAAGREhlgypeLPATIASKQ-LLAAVGQ 80
Cdd:cd04239    3 VLKLSGEALAGEGGGIDPEVLKEIAREIKEVVDLGVEVAIVVGGgniargYIAAARG------MPRATADYIgMLATVMN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  81 SRLIQlweqlFSIYGIHVGQMLLTRADMEDRERFLNARDTLRALLDNNIV-----PVI--NENDAVAtaeikvgdndnls 153
Cdd:cd04239   77 ALALQ-----DALEKLGVKTRVMSAIPMQGVAEPYIRRRAIRHLEKGRIVifgggTGNpgFTTDTAA------------- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 154 ALAAILAGADKLLLLTDQKGLYTADPRSNPQAELIKDVyGIDDALRaiagdsvsgLGTGGMSTKlqAADVACRAGIDTII 233
Cdd:cd04239  139 ALRAEEIGADVLLKATNVDGVYDADPKKNPDAKKYDRI-SYDELLK---------KGLKVMDAT--ALTLCRRNKIPIIV 206

                        250       260
                 ....*....|....*....|.
gi 253972259 234 AAGSKPGVIGDVMEGISVGTL 254
Cdd:cd04239  207 FNGLKPGNLLRALKGEHVGTL 227
PUA cd07953
PUA RNA binding domain; The PUA (PseudoUridine synthase and Archaeosine transglycosylase) ...
 276-337 2.11e-14

PUA RNA binding domain; The PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in archaeal and eukaryotic pseudouridine synthases, archaeal archaeosine synthases, a family of predicted ATPases that may be involved in RNA modification, and a family of predicted archaeal and bacterial rRNA methylases. Additionally, the PUA domain was detected in a family of eukaryotic proteins that also contain a domain homologous to the translation initiation factor eIF1/SUI1; these proteins may comprise a novel type of translation factors. Unexpectedly, the PUA domain was also found in bacterial and yeast glutamate kinases; this is compatible with the demonstrated role of these enzymes in regulating the expression of other genes. It has been shown that the PUA domain acts as an RNA binding domain in at least some of the proteins involved in RNA metabolism.


Pssm-ID: 409289 [Multi-domain]  Cd Length: 73  Bit Score: 67.32  E-value: 2.11e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 253972259 276 GEITVDEGATAAILeRGSSLLPKGIKSVTGNFSRGEVIRICNLEGRDIAHGVSRYNSDALRR 337
Cdd:cd07953    1 PVVVVDKGAEKAVL-NGADLMAPGVVSADGDFKRGDLVRIVSEGGRPLAIGVAEMSSDEMKE 61
PUA smart00359
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
276-341 8.08e-14

Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;


Pssm-ID: 214635 [Multi-domain]  Cd Length: 76  Bit Score: 66.13  E-value: 8.08e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 253972259   276 GEITVDEGATAAILeRGSSLLPKGIKSVTGNFSRGEVIRICNLEGRDIAHGVSRYNSDALRRIAGH 341
Cdd:smart00359   1 GKVVVDDGAEKAIL-NGASLLAPGVVRVDGDIKEGDVVVIVDEKGEPLGIGLANMSSEEIARIKGK 65
AAK_UMPK-PyrH-Pf cd04253
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ...
 154-254 5.88e-10

AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase (uridylate kinase) enzymes that catalyze UMP phosphorylation and play a key role in pyrimidine nucleotide biosynthesis; regulation of this process is via feed-back control and via gene repression of carbamoyl phosphate synthetase (the first enzyme of the pyrimidine biosynthesis pathway). The UMP kinase of Pyrococcus furiosus (Pf) is known to function as a homohexamer, with GTP and UTP being allosteric effectors. Like other related enzymes (carbamate kinase, aspartokinase, and N-acetylglutamate kinase) the E. coli and most bacterial UMPKs have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs (this CD) appear to lack this residue and the Pyrococcus furiosus structure has an additional Mg ion bound to the ATP molecule which is proposed to function as the catalysis instead. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239786 [Multi-domain]  Cd Length: 221  Bit Score: 58.80  E-value: 5.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 154 ALAAILA---GADKLLLLTDQKGLYTADPRSNPQAELIKDVyGIDDaLRAIAGDSVSGLGTGGMSTKLqAADVACRAGID 230
Cdd:cd04253  119 AVAALLAerlGADLLINATNVDGVYSKDPRKDPDAKKFDRL-SADE-LIDIVGKSSWKAGSNEPFDPL-AAKIIERSGIK 195

                         90       100
                 ....*....|....*....|....
gi 253972259 231 TIIAAGSKPGVIGDVMEGISVGTL 254
Cdd:cd04253  196 TIVVDGRDPENLERALKGEFVGTI 219
AAK_FomA-like cd04241
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ...
 6-254 7.49e-10

AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar proteins found in a wide range of organisms. Together, the fomA and fomB genes in the fosfomycin biosynthetic gene cluster of Streptomyces wedmorensis confer high-level fosfomycin resistance. FomA and FomB proteins converted fosfomycin to fosfomycin monophosphate and fosfomycin diphosphate in the presence of ATP and a magnesium ion, indicating that FomA and FomB catalyzed phosphorylations of fosfomycin and fosfomycin monophosphate, respectively. FomA and related sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239774 [Multi-domain]  Cd Length: 252  Bit Score: 58.81  E-value: 7.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259   6 TLVVKLGTSVLTGGSRR--LNRAHIVELVRQCAQlhAAGHRIVIVtSGA-----IAAGREHLGYPELPATIASkqlLAAV 78
Cdd:cd04241    1 MIILKLGGSVITDKDRPetIREENLERIARELAE--AIDEKLVLV-HGGgsfghPKAKEYGLPDGDGSFSAEG---VAET 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  79 GQS--RLIQLWEQLFSIYGI-----HVGQMLLTRADmedreRFLNAR-DTLRALLDNNIVPVINeNDAVATAEIKVG--D 148
Cdd:cd04241   75 HEAmlELNSIVVDALLEAGVpavsvPPSSFFVTENG-----RIVSFDlEVIKELLDRGFVPVLH-GDVVLDEGGGITilS 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 149 NDNLSALAAILAGADKLLLLTDQKGLYTADPrsnPQAELIK--DVYGIDDALraIAGDSVSGLGTGGMSTKLQAADVACR 226
Cdd:cd04241  149 GDDIVVELAKALKPERVIFLTDVDGVYDKPP---PDAKLIPeiDVGSLEDIL--AALGSAGTDVTGGMAGKIEELLELAR 223

                        250       260
                 ....*....|....*....|....*...
gi 253972259 227 AGIDTIIAAGSKPGVIGDVMEGISVGTL 254
Cdd:cd04241  224 RGIEVYIFNGDKPENLYRALLGNFIGTR 251
ArgB COG0548
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ...
 119-256 2.82e-08

N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440314 [Multi-domain]  Cd Length: 283  Bit Score: 54.27  E-value: 2.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 119 DTLRALLDNNIVPVI------------NEN-DAVATAeikvgdndnlsaLAAILaGADKLLLLTDQKGLYtadprsNPQA 185
Cdd:COG0548  155 ELIRALLDAGYIPVIspigysptgevyNINaDTVAGA------------IAAAL-KAEKLILLTDVPGVL------DDPG 215

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 253972259 186 ELIKDVyGIDDALRAIAgdsvSGLGTGGMSTKLQAADVACRAGIDTI-IAAGSKPG-VIGDVMEGISVGTLFH 256
Cdd:COG0548  216 SLISEL-TAAEAEELIA----DGVISGGMIPKLEAALDAVRGGVKRVhIIDGRVPHaLLLELFTDDGIGTMIV 283
PRK00942 PRK00942
acetylglutamate kinase; Provisional
 119-258 3.28e-07

acetylglutamate kinase; Provisional


Pssm-ID: 234869 [Multi-domain]  Cd Length: 283  Bit Score: 51.26  E-value: 3.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 119 DTLRALLDNNIVPVInendavatAEIKVGDNDNL---------SALAAILaGADKLLLLTDQKGLYTADprsnpqAELIK 189
Cdd:PRK00942 153 ALLEALLEAGYIPVI--------SPIGVGEDGETyninadtaaGAIAAAL-GAEKLILLTDVPGVLDDK------GQLIS 217

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 253972259 190 DVyGIDDALRAIAgdsvSGLGTGGMSTKLQAADVACRAGIDTI-IAAGSKP-GVIGDVMEGISVGTLFHAQ 258
Cdd:PRK00942 218 EL-TASEAEELIE----DGVITGGMIPKVEAALDAARGGVRSVhIIDGRVPhALLLELFTDEGIGTMIVPD 283
AAK_UMPK-MosAB cd04255
AAK_UMPK-MosAB: This CD includes the alpha and beta subunits of the Mo storage protein (MosA ...
 155-256 2.28e-06

AAK_UMPK-MosAB: This CD includes the alpha and beta subunits of the Mo storage protein (MosA and MosB) which are related to uridine monophosphate kinase (UMPK) enzymes that catalyze the phosphorylation of UMP by ATP, yielding UDP, and playing a key role in pyrimidine nucleotide biosynthesis. The Mo storage protein from the nitrogen-fixing bacterium, Azotobacter vinelandii, is characterized as an alpha4-beta4 octamer containing a polynuclear molybdenum-oxide cluster which is ATP-dependent to bind Mo and pH-dependent to release Mo. These and related bacterial sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239788 [Multi-domain]  Cd Length: 262  Bit Score: 48.54  E-value: 2.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 155 LAAILAGADKLLLLTDQKGLYTADPRSNPQAELIKDVyGIDDALRAIAGDSVSGLgtgGMSTKLQAADVacragIDTI-I 233
Cdd:cd04255  169 LLAEVIGARNLIFVKDEDGLYTADPKKNKKAEFIPEI-SAAELLKKDLDDLVLER---PVLDLLQNARH-----VKEVqI 239

                         90       100
                 ....*....|....*....|...
gi 253972259 234 AAGSKPGVIGDVMEGISVGTLFH 256
Cdd:cd04255  240 VNGLVPGNLTRALRGEHVGTIIR 262
AAK_NAGK-like cd04238
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ...
 118-242 6.59e-06

AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the Escherichia coli and Pseudomonas aeruginosa type NAGKs which catalyze the phosphorylation of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in bacteria and photosynthetic organisms using either the acetylated, noncyclic (NC), or non-acetylated, cyclic (C) route of ornithine biosynthesis. Also included in this CD is a distinct group of uncharacterized (UC) bacterial and archeal NAGKs. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239771 [Multi-domain]  Cd Length: 256  Bit Score: 47.12  E-value: 6.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 118 RDTLRALLDNNIVPVInendavatAEIKVGDNDNL---------SALAAILaGADKLLLLTDQKGLYTADprsnpqAELI 188
Cdd:cd04238  128 PELLETLLEAGYIPVI--------APIAVDEDGETynvnadtaaGAIAAAL-KAEKLILLTDVPGVLDDP------GSLI 192

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 253972259 189 KDVyGIDDALRAIAGDSVSglgtGGMSTKLQAADVACRAGI-DTIIAAGSKPGVI 242
Cdd:cd04238  193 SEL-TPKEAEELIEDGVIS----GGMIPKVEAALEALEGGVrKVHIIDGRVPHSL 242
AAK_NAGK-C cd04250
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ...
 118-228 7.12e-06

AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in some bacteria and photosynthetic organisms using the non-acetylated, cyclic route of ornithine biosynthesis. In this pathway, glutamate is first N-acetylated and then phosphorylated by NAGK to give phosphoryl NAG, which is converted to NAG-ornithine. There are two variants of this pathway. In one, typified by the pathway in Thermotoga maritima and Pseudomonas aeruginosa, the acetyl group is recycled by reversible transacetylation from acetylornithine to glutamate. The phosphorylation of NAG by NAGK is feedback inhibited by arginine. In photosynthetic organisms, NAGK is the target of the nitrogen-signaling protein PII. Hexameric formation of NAGK domains appears to be essential to both arginine inhibition and NAGK-PII complex formation. NAGK-C are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239783 [Multi-domain]  Cd Length: 279  Bit Score: 47.12  E-value: 7.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 118 RDTLRALLDNNIVPVInendavatAEIKVGDNDNL---------SALAAILaGADKLLLLTDQKGLYTadpRSNPQAELI 188
Cdd:cd04250  148 PELLETLLEAGYIPVI--------APVGVGEDGETyninadtaaGAIAAAL-KAEKLILLTDVAGVLD---DPNDPGSLI 215

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 253972259 189 KDVyGIDDALRAIAGDSVSglgtGGMSTKLQAADVACRAG 228
Cdd:cd04250  216 SEI-SLKEAEELIADGIIS----GGMIPKVEACIEALEGG 250
PRK14058 PRK14058
[LysW]-aminoadipate/[LysW]-glutamate kinase;
119-248 4.78e-05

[LysW]-aminoadipate/[LysW]-glutamate kinase;


Pssm-ID: 237599 [Multi-domain]  Cd Length: 268  Bit Score: 44.51  E-value: 4.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 119 DTLRALLDNNIVPVI------NENDAVATaeikvgDNDNLSALAAILAGADKLLLLTDQKGLYTADPRSNpqaELIkdvy 192
Cdd:PRK14058 140 DLLKLLLKAGYLPVVappalsEEGEPLNV------DGDRAAAAIAGALKAEALVLLSDVPGLLRDPPDEG---SLI---- 206

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 253972259 193 gidDALRAIAGDSVSGLGTGGMSTKLQAADVACRAGIDT-IIAAGSKPGVIGDVMEG 248
Cdd:PRK14058 207 ---ERITPEEAEELSKAAGGGMKKKVLMAAEAVEGGVGRvIIADANVDDPISAALAG 260
AAK_AK cd04234
AAK_AK: Amino Acid Kinase Superfamily (AAK), Aspartokinase (AK); this CD includes the ...
 7-189 1.77e-04

AAK_AK: Amino Acid Kinase Superfamily (AAK), Aspartokinase (AK); this CD includes the N-terminal catalytic domain of aspartokinase (4-L-aspartate-4-phosphotransferase;). AK is the first enzyme in the biosynthetic pathway of the aspartate family of amino acids (lysine, threonine, methionine, and isoleucine) and the bacterial cell wall component, meso-diaminopimelate. It also catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. One mechanism for the regulation of this pathway is by the production of several isoenzymes of aspartokinase with different repressors and allosteric inhibitors. Pairs of ACT domains are proposed to specifically bind amino acids leading to allosteric regulation of the enzyme. In Escherichia coli, three different aspartokinase isoenzymes are regulated specifically by lysine, methionine, and threonine. AK-HSDHI (ThrA) and AK-HSDHII (MetL) are bifunctional enzymes that consist of an N-terminal AK and a C-terminal homoserine dehydrogenase (HSDH). ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. The third isoenzyme, AKIII (LysC), is monofunctional and is involved in lysine synthesis. The three Bacillus subtilis isoenzymes, AKI (DapG), AKII (LysC), and AKIII (YclM), are feedback-inhibited by meso-diaminopimelate, lysine, and lysine plus threonine, respectively. The E. coli lysine-sensitive AK is described as a homodimer, whereas, the B. subtilis lysine-sensitive AK is described as a heterodimeric complex of alpha- and beta- subunits that are formed from two in-frame overlapping genes. A single AK enzyme type has been described in Pseudomonas, Amycolatopsis, and Corynebacterium. The fungal aspartate pathway is regulated at the AK step, with L-Thr being an allosteric inhibitor of the Saccharomyces cerevisiae AK (Hom3). At least two distinct AK isoenzymes can occur in higher plants, one is a monofunctional lysine-sensitive isoenzyme, which is involved in the overall regulation of the pathway and can be synergistically inhibited by S-adenosylmethionine. The other isoenzyme is a bifunctional, threonine-sensitive AK-HSDH protein. Also included in this CD is the catalytic domain of the Methylomicrobium alcaliphilum ectoine AK, the first enzyme of the ectoine biosynthetic pathway, found in this bacterium, and several other halophilic/halotolerant bacteria.


Pssm-ID: 239767 [Multi-domain]  Cd Length: 227  Bit Score: 42.46  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259   7 LVVKLG-TSVLTGGSRRlnraHIVELVRQcaqlHAAGHRIVIVTSgaiAAGR---EHLGYPELPAT--IASKQLLAAVGQ 80
Cdd:cd04234    2 VVQKFGgTSVASAERIK----RVADIIKA----YEKGNRVVVVVS---AMGGvtdLLIELALLLSFgeRLSARLLAAALR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  81 -----SRLIQLWEQLFSIYGIHVgqmlLTRADMEDRERFLNArdtlraLLDNNIVPVI------NENDAVAT-------- 141
Cdd:cd04234   71 drgikARSLDARQAGITTDDNHG----AARIIEISYERLKEL------LAEIGKVPVVtgfigrNEDGEITTlgrggsdy 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 253972259 142 -AeikvgdndnlSALAAILaGADKLLLLTDQKGLYTADPRSNPQAELIK 189
Cdd:cd04234  141 sA----------AALAAAL-GADEVEIWTDVDGIYTADPRIVPEARLIP 178
argB TIGR00761
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ...
 6-229 1.87e-04

acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many prokaryotes and the N-acetylglutamate kinase domains of multifunctional proteins from yeasts. This enzyme is the second step in the "acetylated" ornithine biosynthesis pathway. A related group of enzymes representing the first step of the pathway contain a homologous domain and are excluded from this model. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273256 [Multi-domain]  Cd Length: 231  Bit Score: 42.27  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259    6 TLVVKLGTSVLTGGSRrlnrahivELVRQCAQLHAAGHRIVIVTSGA--IAAGREHLGYP---------ELPATIA-SKQ 73
Cdd:TIGR00761   1 TIVIKIGGAAISDLLE--------AFASDIAFLRAVGIKPVIVHGGGpeINELLEALGIPpefknglrvTDKETLEvVEM 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259   74 LLAAVGQSRLIQLWEQL-FSIYGIHVGQMLLTRADMEDRER--------FLNArDTLRALLDNNIVPVINendAVATAEI 144
Cdd:TIGR00761  73 VLIGQVNKELVALLNKHgINAIGLTGGDGQLFTARYLDKEDlgyvgeikKVNK-ALIEALLKAGYIPVIS---SLALTAE 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  145 KVGDNDNLSALAAILA---GADKLLLLTDQKGLYTADPrsnpqAELIK--DVYGIDDALRaiagdsvSGLGTGGMSTKLQ 219
Cdd:TIGR00761 149 GQALNVNADTAAGALAaalGAEKLVLLTDVPGILNGDG-----QSLISeiPLDEIEQLIK-------QGIIKGGMIPKVN 216

                         250
                  ....*....|
gi 253972259  220 AADVACRAGI 229
Cdd:TIGR00761 217 AALEALRGGV 226
MetL1 COG0527
Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the ...
 12-189 2.02e-04

Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440293 [Multi-domain]  Cd Length: 407  Bit Score: 43.15  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  12 GTSVLTGgSRRLNRAHIVelvrqcAQLHAAGHRIVIVTS---GA----IAAGREHLGYPElPATIAskqLLAAVGqsrli 84
Cdd:COG0527   10 GTSVADA-ERIKRVADIV------KKAKEAGNRVVVVVSamgGVtdllIALAEELLGEPS-PRELD---MLLSTG----- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259  85 qlwEQ----LFSIY----GIHV----GQMLLTRADmedrERFLNAR-------DTLRALLDNNIVPVI------NENDAV 139
Cdd:COG0527   74 ---EQlsaaLLAMAlqelGVPAvsldGRQAGIITD----DNHGKARidlietpERIRELLEEGKVVVVagfqgvTEDGEI 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 253972259 140 AT---------AeikvgdndnlSALAAILaGADKLLLLTDQKGLYTADPRSNPQAELIK 189
Cdd:COG0527  147 TTlgrggsdttA----------VALAAAL-KADECEIWTDVDGVYTADPRIVPDARKLP 194
AAK_AKii-LysC-BS cd04261
AAK_AKii-LysC-BS: Amino Acid Kinase Superfamily (AAK), AKii; this CD includes the N-terminal ...
 112-189 4.10e-04

AAK_AKii-LysC-BS: Amino Acid Kinase Superfamily (AAK), AKii; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis 168, and the lysine plus threonine-sensitive aspartokinase of Corynebacterium glutamicum, and related sequences. In B. subtilis 168, the regulation of the diaminopimelate (Dap)-lysine biosynthetic pathway involves dual control by Dap and lysine, effected through separate Dap- and lysine-sensitive aspartokinase isoenzymes. The B. subtilis 168 AKII is induced by methionine, and repressed and inhibited by lysine. Although Corynebacterium glutamicum is known to contain a single aspartokinase isoenzyme type, both the succinylase and dehydrogenase variant pathways of DAP-lysine synthesis operate simultaneously in this organism. In this organism and other various Gram-positive bacteria, the DAP-lysine pathway is feedback regulated by the concerted action of lysine and theronine. Also included in this CD are the aspartokinases of the extreme thermophile, Thermus thermophilus HB27, the Gram-negative obligate methylotroph, Methylophilus methylotrophus AS1, and those single aspartokinases found in Pseudomons, C. glutamicum, and Amycolatopsis lactamdurans. B. subtilis 168 AKII, and the C. glutamicum, Streptomyces clavuligerus and A. lactamdurans aspartokinases are described as tetramers consisting of two alpha and two beta subunits; the alpha (44 kD) and beta (18 kD) subunits formed by two in-phase overlapping polypeptides.


Pssm-ID: 239794 [Multi-domain]  Cd Length: 239  Bit Score: 41.36  E-value: 4.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 112 ERFLNAR------DTLRALLDNNIVPV------INENDAVATaeIKVGDNDnLSA--LAAILaGADKLLLLTDQKGLYTA 177
Cdd:cd04261  104 GHHGKARiididpDRIRELLEEGDVVIvagfqgINEDGDITT--LGRGGSD-TSAvaLAAAL-GADRCEIYTDVDGVYTA 179

                         90
                 ....*....|..
gi 253972259 178 DPRSNPQAELIK 189
Cdd:cd04261  180 DPRIVPKARKLD 191
AAK_UMPK-PyrH-Ec cd04254
UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) ...
 150-254 7.47e-04

UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) enzyme that catalyzes UMP phosphorylation and plays a key role in pyrimidine nucleotide biosynthesis; regulation of this process is via feed-back control and via gene repression of carbamoyl phosphate synthetase (the first enzyme of the pyrimidine biosynthesis pathway). The UMP kinase of E. coli (Ec) is known to function as a homohexamer, with GTP and UTP being allosteric effectors. Like other related enzymes (carbamate kinase, aspartokinase, and N-acetylglutamate kinase) the E. coli and most bacterial and chloroplast UMPKs (this CD) have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs appear to lack this residue and the Pyrococcus furiosus structure has an additional Mg ion bound to the ATP molecule which is proposed to function as the catalysis instead. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239787 [Multi-domain]  Cd Length: 231  Bit Score: 40.55  E-value: 7.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 150 DNLSALAAILAGADKLLLLTDQKGLYTADPRSNPQAELIKDV-YgiDDALraiagdsvsglgtggmSTKLQAADVA---- 224
Cdd:cd04254  137 DTAAALRAIEINADVILKATKVDGVYDADPKKNPNAKRYDHLtY--DEVL----------------SKGLKVMDATaftl 198

                         90       100       110
                 ....*....|....*....|....*....|.
gi 253972259 225 CR-AGIDTIIAAGSKPGVIGDVMEGISVGTL 254
Cdd:cd04254  199 CRdNNLPIVVFNINEPGNLLKAVKGEGVGTL 229
AAK_AK-DapG-like cd04246
AAK_AK-DapG-like: Amino Acid Kinase Superfamily (AAK), AK-DapG-like; this CD includes the ...
 112-189 8.63e-04

AAK_AK-DapG-like: Amino Acid Kinase Superfamily (AAK), AK-DapG-like; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the diaminopimelate-sensitive aspartokinase isoenzyme AKI (DapG), a monofunctional enzymes found in Bacilli (Bacillus subtilis 168), Clostridia, and Actinobacteria bacterial species, as well as, the catalytic AK domain of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis 168, the lysine plus threonine-sensitive aspartokinase of Corynebacterium glutamicum, and related isoenzymes. In Bacillus subtilis, the regulation of the diaminopimelate-lysine biosynthetic pathway involves dual control by diaminopimelate and lysine, effected through separate diaminopimelate- and lysine-sensitive aspartokinase isoenzymes. The role of the AKI isoenzyme is most likely to provide a constant level of aspartyl-beta-phosphate for the biosynthesis of diaminopimelate for peptidoglycan synthesis and dipicolinate during sporulation. The B. subtilis 168 AKII is induced by methionine, and repressed and inhibited by lysine. In Corynebacterium glutamicum and other various Gram-positive bacteria, the DAP-lysine pathway is feedback regulated by the concerted action of lysine and threonine. Also included in this CD are the aspartokinases of the extreme thermophile, Thermus thermophilus HB27, the Gram-negative obligate methylotroph, Methylophilus methylotrophus AS1, and those single aspartokinase isoenzyme types found in Pseudomonas, C. glutamicum, and Amycolatopsis lactamdurans. The B. subtilis AKI is tetrameric consisting of two alpha and two beta subunits; the alpha (43 kD) and beta (17 kD) subunit formed by two in-phase overlapping genes. The alpha subunit contains the AK catalytic domain and two ACT domains. The beta subunit contains two ACT domains. The B. subtilis 168 AKII aspartokinase is also described as tetrameric consisting of two alpha and two beta subunits. Some archeal aspartokinases in this group lack recognizable ACT domains.


Pssm-ID: 239779 [Multi-domain]  Cd Length: 239  Bit Score: 40.55  E-value: 8.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 112 ERFLNAR------DTLRALLDNNIVPV------INENDAVATaeIKVGDND-NLSALAAILaGADKLLLLTDQKGLYTAD 178
Cdd:cd04246  104 DHHGNARiididpKRILEALEEGDVVVvagfqgVNEDGEITT--LGRGGSDtTAVALAAAL-KADRCEIYTDVDGVYTAD 180

                         90
                 ....*....|.
gi 253972259 179 PRSNPQAELIK 189
Cdd:cd04246  181 PRIVPKARKLD 191
PRK12353 PRK12353
putative amino acid kinase; Reviewed
 119-257 2.63e-03

putative amino acid kinase; Reviewed


Pssm-ID: 237071  Cd Length: 314  Bit Score: 39.37  E-value: 2.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 119 DTLRALLDNNIV---------PVINENDAVATAEiKVGDNDNLSALAAILAGADKLLLLTDQKGLYTadprsN---PQAE 186
Cdd:PRK12353 176 EAIKTLVDAGQVviaaggggiPVIREGGGLKGVE-AVIDKDFASAKLAELVDADLLIILTAVDKVYI-----NfgkPNQK 249

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 253972259 187 LIKDVyGIDDALRAIAGDSvsgLGTGGMSTKLQAAdvacragIDTIIAAGSKPGVIG------DVMEGISvGTLFHA 257
Cdd:PRK12353 250 KLDEV-TVSEAEKYIEEGQ---FAPGSMLPKVEAA-------ISFVESRPGRKAIITslekakEALEGKA-GTVIVK 314
PRK12454 PRK12454
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
 119-176 3.14e-03

carbamate kinase-like carbamoyl phosphate synthetase; Reviewed


Pssm-ID: 183535  Cd Length: 313  Bit Score: 39.21  E-value: 3.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 253972259 119 DTLRALLDNNI---------VPVINENDAVATAEiKVGDNDNLSALAAILAGADKLLLLTDQKGLYT 176
Cdd:PRK12454 176 EVIKALVENGFiviasggggIPVIEEDGELKGVE-AVIDKDLASELLAEELNADIFIILTDVEKVYL 241
PRK08373 PRK08373
aspartate kinase; Validated
 124-188 5.12e-03

aspartate kinase; Validated


Pssm-ID: 236250 [Multi-domain]  Cd Length: 341  Bit Score: 38.50  E-value: 5.12e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 124 LLDNNIVPVI-----NENDAVATAEiKVGDNDNLSALAAILaGADKLLLLTDQKGLYTADPRSNPQAELI 188
Cdd:PRK08373 163 LLERGRVPVVpgfigNLNGFRATLG-RGGSDYSAVALGVLL-NAKAVLIMSDVEGIYTADPKLVPSARLI 230
PLN02512 PLN02512
acetylglutamate kinase
 121-231 5.36e-03

acetylglutamate kinase


Pssm-ID: 178128  Cd Length: 309  Bit Score: 38.13  E-value: 5.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253972259 121 LRALLDNNIVPVINendAVATAEIKVGDNDNLSALAAILA---GADKLLLLTDQKGLYTA--DPRSnpqaeLIKDVyGID 195
Cdd:PLN02512 179 LRPLVDDGHIPVIA---TVAADEDGQAYNINADTAAGEIAaalGAEKLILLTDVAGVLEDkdDPGS-----LVKEL-DIK 249

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 253972259 196 DALRAIAGDSVsglgTGGMSTKLQAADVACRAGIDT 231
Cdd:PLN02512 250 GVRKLIADGKI----AGGMIPKVECCVRSLAQGVKT 281
thrA PRK09436
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional
 156-189 7.78e-03

bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional


Pssm-ID: 181856 [Multi-domain]  Cd Length: 819  Bit Score: 38.21  E-value: 7.78e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 253972259 156 AAILA---GADKLLLLTDQKGLYTADPRSNPQAELIK 189
Cdd:PRK09436 211 AAILAaclDADCCEIWTDVDGVYTADPRVVPDARLLK 247
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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