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Conserved domains on  [gi|549578914|gb|ERN83666|]
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gamma-glutamyl kinase [Salmonella enterica subsp. enterica serovar Kentucky str. 20793]

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

CATH:  2.30.130.10|3.40.1160.10
EC:  2.7.2.11
Gene Ontology:  GO:0016310|GO:0055129|GO:0004349|GO:0005524|GO:0003723

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: 578.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914    5 QTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPELPATIASKQLLAAVGQSRLI 84
Cdd:TIGR01027   1 QRIVVKVGSSSLTGSSGSLDRSHIAELVEQVAALHAAGHEVVIVSSGAIAAGFEALGLPERPKTLAEKQALAAVGQVRLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914   85 QLWEQLFSIYGIHIGQMLLTRADMEDRERFLNARDTLRALLDNHIVPVINENDAVATAEIKVGDNDNLSALAAILAGADK 164
Cdd:TIGR01027  81 QLYEQLFSQYGIKVAQILLTRADFSDRERYLNARNTLEALLELGVVPIINENDTVATEEIKFGDNDTLSALVAILVGADL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  165 LLLLTDQQGLFTADPRSNPQAELIKDVYGVDDALRSIAGDSVSGLGTGGMSTKLQAADVACRAGIDTIIASGSKPGVIGD 244
Cdd:TIGR01027 161 LVLLTDVDGLYDADPRTNPDAKLIPVVEEITDLLLGVAGDSGSSVGTGGMRTKLQAADLATRAGVPVIIASGSKPEKIAD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  245 VMEGISVGTRFHAQASPLENRKRWI-FGAPPAGEITVDEGATAAMLERGSSLLPKGIKSVTGNFSRGEVIRICNLQGRDI 323
Cdd:TIGR01027 241 ALEGAPVGTLFHAQARRLRNRKFWIaFASEPAGEITVDAGAEEALLERGKSLLPAGIVGVEGNFSRGEVVEILNPEGQDI 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 549578914  324 AHGVSRYNSDALRRIAGHHSQQIDAILGYEYGPVAVHRDDMIT 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: 578.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914    5 QTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPELPATIASKQLLAAVGQSRLI 84
Cdd:TIGR01027   1 QRIVVKVGSSSLTGSSGSLDRSHIAELVEQVAALHAAGHEVVIVSSGAIAAGFEALGLPERPKTLAEKQALAAVGQVRLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914   85 QLWEQLFSIYGIHIGQMLLTRADMEDRERFLNARDTLRALLDNHIVPVINENDAVATAEIKVGDNDNLSALAAILAGADK 164
Cdd:TIGR01027  81 QLYEQLFSQYGIKVAQILLTRADFSDRERYLNARNTLEALLELGVVPIINENDTVATEEIKFGDNDTLSALVAILVGADL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  165 LLLLTDQQGLFTADPRSNPQAELIKDVYGVDDALRSIAGDSVSGLGTGGMSTKLQAADVACRAGIDTIIASGSKPGVIGD 244
Cdd:TIGR01027 161 LVLLTDVDGLYDADPRTNPDAKLIPVVEEITDLLLGVAGDSGSSVGTGGMRTKLQAADLATRAGVPVIIASGSKPEKIAD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  245 VMEGISVGTRFHAQASPLENRKRWI-FGAPPAGEITVDEGATAAMLERGSSLLPKGIKSVTGNFSRGEVIRICNLQGRDI 323
Cdd:TIGR01027 241 ALEGAPVGTLFHAQARRLRNRKFWIaFASEPAGEITVDAGAEEALLERGKSLLPAGIVGVEGNFSRGEVVEILNPEGQDI 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 549578914  324 AHGVSRYNSDALRRIAGHHSQQIDAILGYEYGPVAVHRDDMIT 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: 567.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914   1 MSDSQTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPELPATIASKQLLAAVGQ 80
Cdd:COG0263    4 LAKARRIVVKIGSSLLTDEGGGLDRARLAALADQIAALRAAGKEVVLVSSGAVAAGRGRLGLPKRPKTLPEKQAAAAVGQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  81 SRLIQLWEQLFSIYGIHIGQMLLTRADMEDRERFLNARDTLRALLDNHIVPVINENDAVATAEIKVGDNDNLSALAAILA 160
Cdd:COG0263   84 GLLMQAYEEAFARHGLTVAQVLLTRDDLEDRRRYLNARNTLETLLELGVVPIINENDTVATDEIRFGDNDRLAALVANLV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 161 GADKLLLLTDQQGLFTADPRSNPQAELIKDVYGVDDALRSIAGDSVSGLGTGGMSTKLQAADVACRAGIDTIIASGSKPG 240
Cdd:COG0263  164 EADLLVLLTDVDGLYDADPRKDPDAKLIPEVEEITPEIEAMAGGAGSGLGTGGMATKLEAARIATRAGIPTVIASGREPN 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 241 VIGDVMEGISVGTRFHAQASPLENRKRWI-FGAPPAGEITVDEGATAAMLERGSSLLPKGIKSVTGNFSRGEVIRICNLQ 319
Cdd:COG0263  244 VLLRILAGERVGTLFLPSGEPLSARKRWIaGALQPRGRLVVDAGAVRALRERGKSLLPAGVTAVEGDFERGDVVEIVDPD 323

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 549578914 320 GRDIAHGVSRYNSDALRRIAGHHSQQIDAILGYEYGPVAVHRDDMI 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 5.00e-135

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: 385.26  E-value: 5.00e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914   6 TLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPELPATIASKQLLAAVGQSRLIQ 85
Cdd:cd04242    1 RIVVKVGSSLLTDEDGGLDLGRLASLVEQIAELRNQGKEVILVSSGAVAAGRQRLGLEKRPKTLPEKQALAAVGQSLLMA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  86 LWEQLFSIYGIHIGQMLLTRADMEDRERFLNARDTLRALLDNHIVPVINENDAVATAEIKVGDNDNLSALAAILAGADKL 165
Cdd:cd04242   81 LYEQLFAQYGIKVAQILLTRDDFEDRKRYLNARNTLETLLELGVIPIINENDTVATEEIRFGDNDRLSALVAGLVNADLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 166 LLLTDQQGLFTADPRSNPQAELIKDVYGVDDALRSIAGDSVSGLGTGGMSTKLQAADVACRAGIDTIIASGSKPGVIGDV 245
Cdd:cd04242  161 ILLSDVDGLYDKNPRENPDAKLIPEVEEITDEIEAMAGGSGSSVGTGGMRTKLKAARIATEAGIPVVIANGRKPDVLLDI 240

                        250
                 ....*....|.
gi 549578914 246 MEGISVGTRFH 256
Cdd:cd04242  241 LAGEAVGTLFL 251
PRK12314 PRK12314
gamma-glutamyl kinase; Provisional
 2-259 3.04e-100

gamma-glutamyl kinase; Provisional


Pssm-ID: 183430 [Multi-domain]  Cd Length: 266  Bit Score: 297.54  E-value: 3.04e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914   2 SDSQTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPELPATIASKQLLAAVGQS 81
Cdd:PRK12314   7 ENAKRIVIKVGSSTLSYENGKINLERIEQLVFVISDLMNKGKEVILVSSGAIGAGLTKLKLDKRPTSLAEKQALAAVGQP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  82 RLIQLWEQLFSIYGIHIGQMLLTRADMEDRERFLNARDTLRALLDNHIVPVINENDAVATAEI--KVGDNDNLSALAAIL 159
Cdd:PRK12314  87 ELMSLYSKFFAEYGIVVAQILLTRDDFDSPKSRANVKNTFESLLELGILPIVNENDAVATDEIdtKFGDNDRLSAIVAKL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 160 AGADKLLLLTDQQGLFTADPRSNPQAELIKDVYGVDDALRSIAGDSVSGLGTGGMSTKLQAADVACRAGIDTIIASGSKP 239
Cdd:PRK12314 167 VKADLLIILSDIDGLYDKNPRINPDAKLRSEVTEITEEILALAGGAGSKFGTGGMVTKLKAAKFLMEAGIKMVLANGFNP 246

                        250       260
                 ....*....|....*....|
gi 549578914 240 GVIGDVMEGISVGTRFHAQA 259
Cdd:PRK12314 247 SDILDFLEGESIGTLFAPKK 266
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 5-235 3.05e-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: 149.82  E-value: 3.05e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914    5 QTLVVKLGTSVLTGGSRrlnrahIVELVRQCAQLHAAGHRIVIVTS-GAIAAG---------REHLGYPELPATIASKQL 74
Cdd:pfam00696   1 KRVVIKLGGSSLTDKER------LKRLADEIAALLEEGRKLVVVHGgGAFADGllallglspRFARLTDAETLEVATMDA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914   75 LAAVGQSRLIQLWEQLFSIYGIHIGQMLLTRADMEDRERFLNARDTLRALLDNHIVPVINENDAVATAEIK-VGDNDNLS 153
Cdd:pfam00696  75 LGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVTRIDTEALEELLEAGVVPVITGFIGIDPEGELgRGSSDTLA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  154 ALAAILAGADKLLLLTDQQGLFTADPRSNPQAELIKDVYgVDDALRSIAgdsvSGLGTGGMSTKLQAADVACRAG-IDTI 232
Cdd:pfam00696 155 ALLAEALGADKLIILTDVDGVYTADPRKVPDAKLIPEIS-YDELLELLA----SGLATGGMKVKLPAALEAARRGgIPVV 229


                  ...
gi 549578914  233 IAS 235
Cdd:pfam00696 230 IVN 232
PUA smart00359
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
276-341 7.47e-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: 7.47e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549578914   276 GEITVDEGATAAMLeRGSSLLPKGIKSVTGNFSRGEVIRICNLQGRDIAHGVSRYNSDALRRIAGH 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: 578.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914    5 QTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPELPATIASKQLLAAVGQSRLI 84
Cdd:TIGR01027   1 QRIVVKVGSSSLTGSSGSLDRSHIAELVEQVAALHAAGHEVVIVSSGAIAAGFEALGLPERPKTLAEKQALAAVGQVRLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914   85 QLWEQLFSIYGIHIGQMLLTRADMEDRERFLNARDTLRALLDNHIVPVINENDAVATAEIKVGDNDNLSALAAILAGADK 164
Cdd:TIGR01027  81 QLYEQLFSQYGIKVAQILLTRADFSDRERYLNARNTLEALLELGVVPIINENDTVATEEIKFGDNDTLSALVAILVGADL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  165 LLLLTDQQGLFTADPRSNPQAELIKDVYGVDDALRSIAGDSVSGLGTGGMSTKLQAADVACRAGIDTIIASGSKPGVIGD 244
Cdd:TIGR01027 161 LVLLTDVDGLYDADPRTNPDAKLIPVVEEITDLLLGVAGDSGSSVGTGGMRTKLQAADLATRAGVPVIIASGSKPEKIAD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  245 VMEGISVGTRFHAQASPLENRKRWI-FGAPPAGEITVDEGATAAMLERGSSLLPKGIKSVTGNFSRGEVIRICNLQGRDI 323
Cdd:TIGR01027 241 ALEGAPVGTLFHAQARRLRNRKFWIaFASEPAGEITVDAGAEEALLERGKSLLPAGIVGVEGNFSRGEVVEILNPEGQDI 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 549578914  324 AHGVSRYNSDALRRIAGHHSQQIDAILGYEYGPVAVHRDDMIT 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: 567.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914   1 MSDSQTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPELPATIASKQLLAAVGQ 80
Cdd:COG0263    4 LAKARRIVVKIGSSLLTDEGGGLDRARLAALADQIAALRAAGKEVVLVSSGAVAAGRGRLGLPKRPKTLPEKQAAAAVGQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  81 SRLIQLWEQLFSIYGIHIGQMLLTRADMEDRERFLNARDTLRALLDNHIVPVINENDAVATAEIKVGDNDNLSALAAILA 160
Cdd:COG0263   84 GLLMQAYEEAFARHGLTVAQVLLTRDDLEDRRRYLNARNTLETLLELGVVPIINENDTVATDEIRFGDNDRLAALVANLV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 161 GADKLLLLTDQQGLFTADPRSNPQAELIKDVYGVDDALRSIAGDSVSGLGTGGMSTKLQAADVACRAGIDTIIASGSKPG 240
Cdd:COG0263  164 EADLLVLLTDVDGLYDADPRKDPDAKLIPEVEEITPEIEAMAGGAGSGLGTGGMATKLEAARIATRAGIPTVIASGREPN 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 241 VIGDVMEGISVGTRFHAQASPLENRKRWI-FGAPPAGEITVDEGATAAMLERGSSLLPKGIKSVTGNFSRGEVIRICNLQ 319
Cdd:COG0263  244 VLLRILAGERVGTLFLPSGEPLSARKRWIaGALQPRGRLVVDAGAVRALRERGKSLLPAGVTAVEGDFERGDVVEIVDPD 323

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 549578914 320 GRDIAHGVSRYNSDALRRIAGHHSQQIDAILGYEYGPVAVHRDDMI 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 5.00e-135

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: 385.26  E-value: 5.00e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914   6 TLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPELPATIASKQLLAAVGQSRLIQ 85
Cdd:cd04242    1 RIVVKVGSSLLTDEDGGLDLGRLASLVEQIAELRNQGKEVILVSSGAVAAGRQRLGLEKRPKTLPEKQALAAVGQSLLMA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  86 LWEQLFSIYGIHIGQMLLTRADMEDRERFLNARDTLRALLDNHIVPVINENDAVATAEIKVGDNDNLSALAAILAGADKL 165
Cdd:cd04242   81 LYEQLFAQYGIKVAQILLTRDDFEDRKRYLNARNTLETLLELGVIPIINENDTVATEEIRFGDNDRLSALVAGLVNADLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 166 LLLTDQQGLFTADPRSNPQAELIKDVYGVDDALRSIAGDSVSGLGTGGMSTKLQAADVACRAGIDTIIASGSKPGVIGDV 245
Cdd:cd04242  161 ILLSDVDGLYDKNPRENPDAKLIPEVEEITDEIEAMAGGSGSSVGTGGMRTKLKAARIATEAGIPVVIANGRKPDVLLDI 240

                        250
                 ....*....|.
gi 549578914 246 MEGISVGTRFH 256
Cdd:cd04242  241 LAGEAVGTLFL 251
PRK12314 PRK12314
gamma-glutamyl kinase; Provisional
 2-259 3.04e-100

gamma-glutamyl kinase; Provisional


Pssm-ID: 183430 [Multi-domain]  Cd Length: 266  Bit Score: 297.54  E-value: 3.04e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914   2 SDSQTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPELPATIASKQLLAAVGQS 81
Cdd:PRK12314   7 ENAKRIVIKVGSSTLSYENGKINLERIEQLVFVISDLMNKGKEVILVSSGAIGAGLTKLKLDKRPTSLAEKQALAAVGQP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  82 RLIQLWEQLFSIYGIHIGQMLLTRADMEDRERFLNARDTLRALLDNHIVPVINENDAVATAEI--KVGDNDNLSALAAIL 159
Cdd:PRK12314  87 ELMSLYSKFFAEYGIVVAQILLTRDDFDSPKSRANVKNTFESLLELGILPIVNENDAVATDEIdtKFGDNDRLSAIVAKL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 160 AGADKLLLLTDQQGLFTADPRSNPQAELIKDVYGVDDALRSIAGDSVSGLGTGGMSTKLQAADVACRAGIDTIIASGSKP 239
Cdd:PRK12314 167 VKADLLIILSDIDGLYDKNPRINPDAKLRSEVTEITEEILALAGGAGSKFGTGGMVTKLKAAKFLMEAGIKMVLANGFNP 246

                        250       260
                 ....*....|....*....|
gi 549578914 240 GVIGDVMEGISVGTRFHAQA 259
Cdd:PRK12314 247 SDILDFLEGESIGTLFAPKK 266
AAK_P5CS_ProBA cd04256
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ...
 1-256 3.19e-58

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: 190.34  E-value: 3.19e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914   1 MSDSQTLVVKLGTSVLT-GGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGY----------------- 62
Cdd:cd04256    5 LKHAKRIVVKLGSAVVTrEDECGLALGRLASIVEQVSELQSQGREVILVTSGAVAFGKQRLRHeillsssmrqtlksgql 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  63 PELPATIASKQLLAAVGQSRLIQLWEQLFSIYGIHIGQMLLTRADMEDRERFLNARDTLRALLDNHIVPVINENDAVATA 142
Cdd:cd04256   85 KDMPQMELDGRACAAVGQSGLMALYEAMFTQYGITVAQVLVTKPDFYDEQTRRNLNGTLEELLRLNIIPIINTNDAVSPP 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 143 E---------IKVGDNDNLSALAAILAGADKLLLLTDQQGLFTADPRSnPQAELIKDVYGVDdaLRSIAGDSVSGLGTGG 213
Cdd:cd04256  165 PepdedlqgvISIKDNDSLAARLAVELKADLLILLSDVDGLYDGPPGS-DDAKLIHTFYPGD--QQSITFGTKSRVGTGG 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 549578914 214 MSTKLQAADVACRAGIDTIIASGSKPGVIGDVMEGISVGTRFH 256
Cdd:cd04256  242 MEAKVKAALWALQGGTSVVITNGMAGDVITKILEGKKVGTFFT 284
P5CS TIGR01092
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ...
 3-287 7.82e-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: 180.49  E-value: 7.82e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914    3 DSQTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPEL----------PATIASK 72
Cdd:TIGR01092   6 DVKRIVVKVGTAVVTRGDGRLALGRLGSICEQLSELNSDGREVILVTSGAVAFGRQRLRHRILvnssfadlqkPQPELDG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914   73 QLLAAVGQSRLIQLWEQLFSIYGIHIGQMLLTRADMEDRERFLNARDTLRALLDNHIVPVINENDAVATAEIK------- 145
Cdd:TIGR01092  86 KACAAVGQSGLMALYETMFTQLDITAAQILVTDLDFRDEQFRRQLNETVHELLRMNVVPVVNENDAVSTRAAPysdsqgi 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  146 VGDNDNLSALAAILAGADKLLLLTDQQGLFTADPrSNPQAELIkDVYGVDDALRSIAGDSVSGLGTGGMSTKLQAADVAC 225
Cdd:TIGR01092 166 FWDNDSLAALLALELKADLLILLSDVEGLYDGPP-SDDDSKLI-DTFYKEKHQGEITFGTKSRLGRGGMTAKVKAAVWAA 243

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 549578914  226 RAGIDTIIASGSKPGVIGDVMEGISVGTRFHaQASPLenrkrWifgaPPAGEITVDEGATAA 287
Cdd:TIGR01092 244 YGGTPVIIASGTAPKNITKVVEGKKVGTLFH-EDAHL-----W----PTVEQTGERDMAVAA 295
PLN02418 PLN02418
delta-1-pyrroline-5-carboxylate synthase
 3-287 9.52e-51

delta-1-pyrroline-5-carboxylate synthase


Pssm-ID: 215230  Cd Length: 718  Bit Score: 180.31  E-value: 9.52e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914   3 DSQTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPEL----------PATIASK 72
Cdd:PLN02418  14 DVKRVVIKVGTAVVTRDDGRLALGRLGALCEQIKELNSDGYEVILVSSGAVGVGRQRLRYRRLvnssfadlqkPQMELDG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  73 QLLAAVGQSRLIQLWEQLFSIYGIHIGQMLLTRADMEDRERFLNARDTLRALLDNHIVPVINENDAVAT-------AEIK 145
Cdd:PLN02418  94 KACAAVGQSELMALYDTLFSQLDVTASQLLVTDSDFRDPDFRKQLSETVESLLDLRVIPIFNENDAVSTrrapyedSSGI 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 146 VGDNDNLSALAAILAGADKLLLLTDQQGLFTADPrSNPQAELIKdVYGVDDALRSIAGDSVSGLGTGGMSTKLQAADVAC 225
Cdd:PLN02418 174 FWDNDSLAALLALELKADLLILLSDVEGLYTGPP-SDPSSKLIH-TYIKEKHQDEITFGEKSRVGRGGMTAKVKAAVNAA 251

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 549578914 226 RAGIDTIIASGSKPGVIGDVMEGISVGTRFHAQASplenrkRWifgaPPAGEITVDEGATAA 287
Cdd:PLN02418 252 SAGIPVVITSGYALDNIRKVLRGERVGTLFHQDAH------LW----APSKEVGAREMAVAA 303
PUA_G5K cd21157
PUA domain of gamma-glutamyl kinase, found in archaea, bacteria, and eukarya; Gamma glutamyl ...
 264-365 1.45e-47

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: 156.47  E-value: 1.45e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 264 NRKRWI-FGAPPAGEITVDEGATAAMLERGSSLLPKGIKSVTGNFSRGEVIRICNLQGRDIAHGVSRYNSDALRRIAGHH 342
Cdd:cd21157    1 ARKQWIaFALKPKGKLVVDAGAVKALLEGGKSLLPAGITAVEGDFERGDVVRIVDPDGREIARGLVNYSSEELRKIKGKK 80

                         90       100
                 ....*....|....*....|...
gi 549578914 343 SQQIDAILGYEYGPVAVHRDDMI 365
Cdd:cd21157   81 SSEIEEILGYKYGDEVIHRDNLV 103
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 5-235 3.05e-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: 149.82  E-value: 3.05e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914    5 QTLVVKLGTSVLTGGSRrlnrahIVELVRQCAQLHAAGHRIVIVTS-GAIAAG---------REHLGYPELPATIASKQL 74
Cdd:pfam00696   1 KRVVIKLGGSSLTDKER------LKRLADEIAALLEEGRKLVVVHGgGAFADGllallglspRFARLTDAETLEVATMDA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914   75 LAAVGQSRLIQLWEQLFSIYGIHIGQMLLTRADMEDRERFLNARDTLRALLDNHIVPVINENDAVATAEIK-VGDNDNLS 153
Cdd:pfam00696  75 LGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVTRIDTEALEELLEAGVVPVITGFIGIDPEGELgRGSSDTLA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  154 ALAAILAGADKLLLLTDQQGLFTADPRSNPQAELIKDVYgVDDALRSIAgdsvSGLGTGGMSTKLQAADVACRAG-IDTI 232
Cdd:pfam00696 155 ALLAEALGADKLIILTDVDGVYTADPRKVPDAKLIPEIS-YDELLELLA----SGLATGGMKVKLPAALEAARRGgIPVV 229


                  ...
gi 549578914  233 IAS 235
Cdd:pfam00696 230 IVN 232
PTZ00489 PTZ00489
glutamate 5-kinase; Provisional
 7-260 9.81e-36

glutamate 5-kinase; Provisional


Pssm-ID: 240438 [Multi-domain]  Cd Length: 264  Bit Score: 131.29  E-value: 9.81e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914   7 LVVKLGTSVLTGgSRRLNRAHIVELVRQCAQLHAAgHRIVIVTSGAIAAGREHLGYPElpATIASKQLLAAVGQSRLIQL 86
Cdd:PTZ00489  11 IVVKVGSSILVD-NQEIAAHRIEALCRFIADLQTK-YEVILVTSGAVAAGYTKKEMDK--SYVPNKQALASMGQPLLMHM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  87 WEQLFSIYGIHIGQMLLTRADMEDRERFLNARDTLRALLDNHIVPVINENDAVATAEIKVGDNDNLSALAAILAGADKLL 166
Cdd:PTZ00489  87 YYTELQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALHELVFGDNDRLSALVAHHFKADLLV 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 167 LLTDQQGLFTADPRSNPQAELIKDVYGVDDALRSIAGDSVSGLGTGGMSTKLQAADVACRAGIDTIIASGSKPGVIGDVM 246
Cdd:PTZ00489 167 ILSDIDGYYTENPRTSTDAKIRSVVHELSPDDLVAEATPNNRFATGGIVTKLQAAQFLLERGGKMYLSSGFHLEKARDFL 246

                        250
                 ....*....|....*.
gi 549578914 247 EGIS--VGTRFHAQAS 260
Cdd:PTZ00489 247 IGGSheIGTLFYPRVS 262
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 8-255 3.68e-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: 3.68e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914   8 VVKLGTSVLTGGSRRLNRAHIVelvrqcAQLHAAGHRIVIVTSGAIAAGREHLGYPELPA-------TIASKQLLAAVGQ 80
Cdd:cd02115    1 VIKFGGSSVSSEERLRNLARIL------VKLASEGGRVVVVHGAGPQITDELLAHGELLGyarglriTDRETDALAAMGE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  81 SRLIQLWEQLFSIYGIHIGQMLLTRADMEDRERFLNAR------DTLRALLDNHIVPVINENDAVA---TAEIKVGDNDN 151
Cdd:cd02115   75 GMSNLLIAAALEQHGIKAVPLDLTQAGFASPNQGHVGKitkvstDRLKSLLENGILPILSGFGGTDekeTGTLGRGGSDS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 152 LSALAAILAGADKLLLLTDQQGLFTADPRSNPQAELIKDVYgvddalrsiAGDSVSGLGTGGMSTKLQAADVACRAGIDT 231
Cdd:cd02115  155 TAALLAAALKADRLVILTDVDGVYTADPRKVPDAKLLSELT---------YEEAAELAYAGAMVLKPKAADPAARAGIPV 225

                        250       260
                 ....*....|....*....|....
gi 549578914 232 IIASGSKPGVIgDVMEGISVGTRF 255
Cdd:cd02115  226 RIANTENPGAL-ALFTPDGGGTLI 248
PUA pfam01472
PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, ...
 276-350 5.93e-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: 77.52  E-value: 5.93e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549578914  276 GEITVDEGATAAMLErGSSLLPKGIKSVTGNFSRGEVIRICNLQGRDIAHGVSRYNSDALRRIAGHHSQQIDAIL 350
Cdd:pfam01472   1 GRVVVDDGAVKAILN-GASLLAPGVVRVDGDFRKGDEVVVVTEKGELVAVGLANYSSEELAKIEGGKAVKVRRVL 74
AAK_UMPK-like cd04239
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ...
 8-253 3.81e-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: 71.03  E-value: 3.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914   8 VVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSG------AIAAGREhlgypeLPATIASKQ-LLAAVGQ 80
Cdd:cd04239    3 VLKLSGEALAGEGGGIDPEVLKEIAREIKEVVDLGVEVAIVVGGgniargYIAAARG------MPRATADYIgMLATVMN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  81 SRLIQlweqlFSIYGIHIGQMLLTRADMEDRERFLNARDTLRALlDNHIVPV---INENDAVATaeikvgdnDNLSALAA 157
Cdd:cd04239   77 ALALQ-----DALEKLGVKTRVMSAIPMQGVAEPYIRRRAIRHL-EKGRIVIfggGTGNPGFTT--------DTAAALRA 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 158 ILAGADKLLLLTDQQGLFTADPRSNPQAELIKDVyGVDDALRSIAG--DSVsglgtggmstklqAADVACRAGIDTIIAS 235
Cdd:cd04239  143 EEIGADVLLKATNVDGVYDADPKKNPDAKKYDRI-SYDELLKKGLKvmDAT-------------ALTLCRRNKIPIIVFN 208

                        250
                 ....*....|....*...
gi 549578914 236 GSKPGVIGDVMEGISVGT 253
Cdd:cd04239  209 GLKPGNLLRALKGEHVGT 226
PUA smart00359
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
276-341 7.47e-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: 7.47e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549578914   276 GEITVDEGATAAMLeRGSSLLPKGIKSVTGNFSRGEVIRICNLQGRDIAHGVSRYNSDALRRIAGH 341
Cdd:smart00359   1 GKVVVDDGAEKAIL-NGASLLAPGVVRVDGDIKEGDVVVIVDEKGEPLGIGLANMSSEEIARIKGK 65
PUA cd07953
PUA RNA binding domain; The PUA (PseudoUridine synthase and Archaeosine transglycosylase) ...
 276-337 1.32e-13

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: 65.40  E-value: 1.32e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 549578914 276 GEITVDEGATAAMLeRGSSLLPKGIKSVTGNFSRGEVIRICNLQGRDIAHGVSRYNSDALRR 337
Cdd:cd07953    1 PVVVVDKGAEKAVL-NGADLMAPGVVSADGDFKRGDLVRIVSEGGRPLAIGVAEMSSDEMKE 61
AAK_FomA-like cd04241
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ...
 6-254 9.87e-11

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: 61.51  E-value: 9.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914   6 TLVVKLGTSVLTGGSRR--LNRAHIVELVRQCAQlhAAGHRIVIVtSGA-----IAAGREHLGYPELPATIASkqlLAAV 78
Cdd:cd04241    1 MIILKLGGSVITDKDRPetIREENLERIARELAE--AIDEKLVLV-HGGgsfghPKAKEYGLPDGDGSFSAEG---VAET 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  79 GQS--RLIQLWEQLFSIYGI-----HIGQMLLTRADmedreRFLNAR-DTLRALLDNHIVPVINeNDAVATAEIKVG--D 148
Cdd:cd04241   75 HEAmlELNSIVVDALLEAGVpavsvPPSSFFVTENG-----RIVSFDlEVIKELLDRGFVPVLH-GDVVLDEGGGITilS 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 149 NDNLSALAAILAGADKLLLLTDQQGLFTADPrsnPQAELIK--DVYGVDDALrsIAGDSVSGLGTGGMSTKLQAADVACR 226
Cdd:cd04241  149 GDDIVVELAKALKPERVIFLTDVDGVYDKPP---PDAKLIPeiDVGSLEDIL--AALGSAGTDVTGGMAGKIEELLELAR 223

                        250       260
                 ....*....|....*....|....*...
gi 549578914 227 AGIDTIIASGSKPGVIGDVMEGISVGTR 254
Cdd:cd04241  224 RGIEVYIFNGDKPENLYRALLGNFIGTR 251
AAK_UMPK-PyrH-Pf cd04253
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ...
 154-253 2.58e-09

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: 56.87  E-value: 2.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 154 ALAAILA---GADKLLLLTDQQGLFTADPRSNPQAELIKDVyGVDDALRsIAGDSVSGLGTGGMSTKLqAADVACRAGID 230
Cdd:cd04253  119 AVAALLAerlGADLLINATNVDGVYSKDPRKDPDAKKFDRL-SADELID-IVGKSSWKAGSNEPFDPL-AAKIIERSGIK 195

                         90       100
                 ....*....|....*....|...
gi 549578914 231 TIIASGSKPGVIGDVMEGISVGT 253
Cdd:cd04253  196 TIVVDGRDPENLERALKGEFVGT 218
ArgB COG0548
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ...
 119-242 9.82e-09

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: 55.81  E-value: 9.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 119 DTLRALLDNHIVPVI------------NEN-DAVATAeikvgdndnlsaLAAILaGADKLLLLTDQQGLFtadprsNPQA 185
Cdd:COG0548  155 ELIRALLDAGYIPVIspigysptgevyNINaDTVAGA------------IAAAL-KAEKLILLTDVPGVL------DDPG 215

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 549578914 186 ELIKDVyGVDDALRSIAgdsvSGLGTGGMSTKLQAADVACRAGIDTI-IASGSKPGVI 242
Cdd:COG0548  216 SLISEL-TAAEAEELIA----DGVISGGMIPKLEAALDAVRGGVKRVhIIDGRVPHAL 268
PRK00942 PRK00942
acetylglutamate kinase; Provisional
 119-258 1.22e-06

acetylglutamate kinase; Provisional


Pssm-ID: 234869 [Multi-domain]  Cd Length: 283  Bit Score: 49.34  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 119 DTLRALLDNHIVPVInendavatAEIKVGDNDNL---------SALAAILaGADKLLLLTDQQGLFTADprsnpqAELIK 189
Cdd:PRK00942 153 ALLEALLEAGYIPVI--------SPIGVGEDGETyninadtaaGAIAAAL-GAEKLILLTDVPGVLDDK------GQLIS 217

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 549578914 190 DVyGVDDALRSIAgdsvSGLGTGGMSTKLQAADVACRAGIDTI-IASGSKP-GVIGDVMEGISVGTRFHAQ 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 ...
 155-253 1.46e-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: 48.93  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 155 LAAILAGADKLLLLTDQQGLFTADPRSNPQAELIKDVyGVDDALRSIAGDSVSGLgtgGMSTKLQAADVacragIDTI-I 233
Cdd:cd04255  169 LLAEVIGARNLIFVKDEDGLYTADPKKNKKAEFIPEI-SAAELLKKDLDDLVLER---PVLDLLQNARH-----VKEVqI 239

                         90       100
                 ....*....|....*....|
gi 549578914 234 ASGSKPGVIGDVMEGISVGT 253
Cdd:cd04255  240 VNGLVPGNLTRALRGEHVGT 259
AAK_NAGK-like cd04238
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ...
 118-255 7.55e-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: 46.73  E-value: 7.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 118 RDTLRALLDNHIVPVInendavatAEIKVGDNDNL---------SALAAILaGADKLLLLTDQQGLFTADprsnpqAELI 188
Cdd:cd04238  128 PELLETLLEAGYIPVI--------APIAVDEDGETynvnadtaaGAIAAAL-KAEKLILLTDVPGVLDDP------GSLI 192

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549578914 189 KDVyGVDDALRSIAGDSVSglgtGGMSTKLQAADVACRAGI-DTIIASGSKPGVI-GDVMEGISVGTRF 255
Cdd:cd04238  193 SEL-TPKEAEELIEDGVIS----GGMIPKVEAALEALEGGVrKVHIIDGRVPHSLlLELFTDEGIGTMI 256
AAK_NAGK-C cd04250
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ...
 118-228 3.46e-05

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: 44.80  E-value: 3.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 118 RDTLRALLDNHIVPVInendavatAEIKVGDNDNL---------SALAAILaGADKLLLLTDQQGLFTadpRSNPQAELI 188
Cdd:cd04250  148 PELLETLLEAGYIPVI--------APVGVGEDGETyninadtaaGAIAAAL-KAEKLILLTDVAGVLD---DPNDPGSLI 215

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 549578914 189 KDVyGVDDALRSIAGDSVSglgtGGMSTKLQAADVACRAG 228
Cdd:cd04250  216 SEI-SLKEAEELIADGIIS----GGMIPKVEACIEALEGG 250
PRK14058 PRK14058
[LysW]-aminoadipate/[LysW]-glutamate kinase;
119-257 5.83e-05

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


Pssm-ID: 237599 [Multi-domain]  Cd Length: 268  Bit Score: 44.12  E-value: 5.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 119 DTLRALLDNHIVPVI------NENDAVATaeikvgDNDNLSALAAILAGADKLLLLTDQQGLFTADPRSNpqaELIKDVy 192
Cdd:PRK14058 140 DLLKLLLKAGYLPVVappalsEEGEPLNV------DGDRAAAAIAGALKAEALVLLSDVPGLLRDPPDEG---SLIERI- 209

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549578914 193 GVDDAlrsiagDSVSGLGTGGMSTKLQAADVACRAGIDT-IIASGSKPGVIGDVMEGIsvGTRFHA 257
Cdd:PRK14058 210 TPEEA------EELSKAAGGGMKKKVLMAAEAVEGGVGRvIIADANVDDPISAALAGE--GTVIVN 267
argB TIGR00761
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ...
 6-229 2.44e-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: 41.88  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914    6 TLVVKLGTSVLTGGSRrlnrahivELVRQCAQLHAAGHRIVIVTSGA--IAAGREHLGYP---------ELPATIA-SKQ 73
Cdd:TIGR00761   1 TIVIKIGGAAISDLLE--------AFASDIAFLRAVGIKPVIVHGGGpeINELLEALGIPpefknglrvTDKETLEvVEM 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914   74 LLAAVGQSRLIQLWEQL-FSIYGIHIGQMLLTRADMEDRER--------FLNArDTLRALLDNHIVPVINendAVATAEI 144
Cdd:TIGR00761  73 VLIGQVNKELVALLNKHgINAIGLTGGDGQLFTARYLDKEDlgyvgeikKVNK-ALIEALLKAGYIPVIS---SLALTAE 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  145 KVGDNDNLSALAAILA---GADKLLLLTDQQGLFTADPrsnpqAELIkDVYGVDDALRSIAgdsvSGLGTGGMSTKLQAA 221
Cdd:TIGR00761 149 GQALNVNADTAAGALAaalGAEKLVLLTDVPGILNGDG-----QSLI-SEIPLDEIEQLIK----QGIIKGGMIPKVNAA 218


                  ....*...
gi 549578914  222 DVACRAGI 229
Cdd:TIGR00761 219 LEALRGGV 226
AAK_AK cd04234
AAK_AK: Amino Acid Kinase Superfamily (AAK), Aspartokinase (AK); this CD includes the ...
 7-189 4.93e-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: 40.92  E-value: 4.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914   7 LVVKLG-TSVLTGGSRRlnraHIVELVRQcaqlHAAGHRIVIVTSgaiAAGR---EHLGYPELPAT--IASKQLLAAVGQ 80
Cdd:cd04234    2 VVQKFGgTSVASAERIK----RVADIIKA----YEKGNRVVVVVS---AMGGvtdLLIELALLLSFgeRLSARLLAAALR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  81 -----SRLIQLWEQLFSIYGIHigqmLLTRADMEDRERFLNArdtlraLLDNHIVPVI------NENDAVAT-------- 141
Cdd:cd04234   71 drgikARSLDARQAGITTDDNH----GAARIIEISYERLKEL------LAEIGKVPVVtgfigrNEDGEITTlgrggsdy 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 549578914 142 -AeikvgdndnlSALAAILaGADKLLLLTDQQGLFTADPRSNPQAELIK 189
Cdd:cd04234  141 sA----------AALAAAL-GADEVEIWTDVDGIYTADPRIVPEARLIP 178
AAK_AKii-LysC-BS cd04261
AAK_AKii-LysC-BS: Amino Acid Kinase Superfamily (AAK), AKii; this CD includes the N-terminal ...
 112-189 8.18e-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: 40.59  E-value: 8.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 112 ERFLNAR------DTLRALLDNHIVPV------INENDAVATaeIKVGDNDnLSA--LAAILaGADKLLLLTDQQGLFTA 177
Cdd:cd04261  104 GHHGKARiididpDRIRELLEEGDVVIvagfqgINEDGDITT--LGRGGSD-TSAvaLAAAL-GADRCEIYTDVDGVYTA 179

                         90
                 ....*....|..
gi 549578914 178 DPRSNPQAELIK 189
Cdd:cd04261  180 DPRIVPKARKLD 191
PRK12353 PRK12353
putative amino acid kinase; Reviewed
 119-257 1.07e-03

putative amino acid kinase; Reviewed


Pssm-ID: 237071  Cd Length: 314  Bit Score: 40.52  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 119 DTLRALLDN-HIV--------PVINENDAVATAEiKVGDNDNLSALAAILAGADKLLLLTDQQGLFTadprsN---PQAE 186
Cdd:PRK12353 176 EAIKTLVDAgQVViaaggggiPVIREGGGLKGVE-AVIDKDFASAKLAELVDADLLIILTAVDKVYI-----NfgkPNQK 249

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549578914 187 LIKDVyGVDDALRSIAGDSvsgLGTGGMSTKLQAAdvacragIDTIIASGSKPGVIG------DVMEGISvGTRFHA 257
Cdd:PRK12353 250 KLDEV-TVSEAEKYIEEGQ---FAPGSMLPKVEAA-------ISFVESRPGRKAIITslekakEALEGKA-GTVIVK 314
AAK_AK-DapG-like cd04246
AAK_AK-DapG-like: Amino Acid Kinase Superfamily (AAK), AK-DapG-like; this CD includes the ...
 112-189 1.37e-03

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: 39.78  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 112 ERFLNAR------DTLRALLDNHIVPV------INENDAVATaeIKVGDND-NLSALAAILaGADKLLLLTDQQGLFTAD 178
Cdd:cd04246  104 DHHGNARiididpKRILEALEEGDVVVvagfqgVNEDGEITT--LGRGGSDtTAVALAAAL-KADRCEIYTDVDGVYTAD 180

                         90
                 ....*....|.
gi 549578914 179 PRSNPQAELIK 189
Cdd:cd04246  181 PRIVPKARKLD 191
MetL1 COG0527
Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the ...
 12-189 1.86e-03

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: 40.07  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  12 GTSVLTGgSRRLNRAHIVelvrqcAQLHAAGHRIVIVTS---GA----IAAGREHLGYPElPATIAskqLLAAVGqsrli 84
Cdd:COG0527   10 GTSVADA-ERIKRVADIV------KKAKEAGNRVVVVVSamgGVtdllIALAEELLGEPS-PRELD---MLLSTG----- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914  85 qlwEQ----LFSIY----GIHI----GQMLLTRADmedrERFLNAR-------DTLRALLDNHIVPVI------NENDAV 139
Cdd:COG0527   74 ---EQlsaaLLAMAlqelGVPAvsldGRQAGIITD----DNHGKARidlietpERIRELLEEGKVVVVagfqgvTEDGEI 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 549578914 140 AT---------AeikvgdndnlSALAAILaGADKLLLLTDQQGLFTADPRSNPQAELIK 189
Cdd:COG0527  147 TTlgrggsdttA----------VALAAAL-KADECEIWTDVDGVYTADPRIVPDARKLP 194
PRK12454 PRK12454
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
 119-254 4.85e-03

carbamate kinase-like carbamoyl phosphate synthetase; Reviewed


Pssm-ID: 183535  Cd Length: 313  Bit Score: 38.44  E-value: 4.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 119 DTLRALLDNHI---------VPVINENDAVATAEiKVGDNDNLSALAAILAGADKLLLLTDQQGLFTADPRSNPQAeliK 189
Cdd:PRK12454 176 EVIKALVENGFiviasggggIPVIEEDGELKGVE-AVIDKDLASELLAEELNADIFIILTDVEKVYLNYGKPDQKP---L 251

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 549578914 190 DVYGVDDALRSIAGDSVSglgTGGMSTKLQAAdvacragIDTIIASGsKPGVIG------DVMEGiSVGTR 254
Cdd:PRK12454 252 DKVTVEEAKKYYEEGHFK---AGSMGPKILAA-------IRFVENGG-KRAIIAslekavEALEG-KTGTR 310
AAK_UMPK-PyrH-Ec cd04254
UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) ...
 150-253 5.10e-03

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: 37.85  E-value: 5.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 150 DNLSALAAILAGADKLLLLTDQQGLFTADPRSNPQAELIKDV-YgvDDALrsiagdsvsglgtggmSTKLQAADVA---- 224
Cdd:cd04254  137 DTAAALRAIEINADVILKATKVDGVYDADPKKNPNAKRYDHLtY--DEVL----------------SKGLKVMDATaftl 198

                         90       100       110
                 ....*....|....*....|....*....|
gi 549578914 225 CR-AGIDTIIASGSKPGVIGDVMEGISVGT 253
Cdd:cd04254  199 CRdNNLPIVVFNINEPGNLLKAVKGEGVGT 228
AAK_NAGS-ABP cd04237
AAK_NAGS-ABP: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ...
 151-229 5.68e-03

AAK_NAGS-ABP: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the arginine-biosynthesis pathway (ABP) found in gamma- and beta-proteobacteria and higher plant chloroplasts. Domain architecture of these NAGS consisted of an N-terminal NAG kinase-like (ArgB) domain (this CD) and a C-terminal NAG synthase, acetyltransferase (ArgA) domain. Both bacterial and plant sequences in this CD have a conserved N-terminal extension; a similar sequence in the NAG kinases of the cyclic arginine-biosynthesis pathway has been implicated in feedback inhibition sensing. Plant sequences also have an N-terminal chloroplast transit peptide and an insert (approx. 70 residues) in the C-terminal region of ArgB. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239770 [Multi-domain]  Cd Length: 280  Bit Score: 38.31  E-value: 5.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 151 NLSAL-----AAILAGADKLLLLTDQQGLftADPRSNPQAELIkdvygVDDALRSIAGDsvsGLGTGGMSTKLQAADVAC 225
Cdd:cd04237  179 NLSMEdvataVAIALKADKLIFLTDGPGL--LDDDGELIRELT-----AQEAEALLETG---ALLTNDTARLLQAAIEAC 248


                 ....
gi 549578914 226 RAGI 229
Cdd:cd04237  249 RGGV 252
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
105-189 8.01e-03

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 38.14  E-value: 8.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 105 RADMEDRERFLNARDtlRALLDNHIvpvINENDAVATAEIKVGDNDNLSALAAILAGADKLLLLTDQQGLFTADPRSNPQ 184
Cdd:PRK08961 176 QSDPALRERFAAQPA--QVLITQGF---IARNADGGTALLGRGGSDTSAAYFAAKLGASRVEIWTDVPGMFSANPKEVPD 250


                 ....*
gi 549578914 185 AELIK 189
Cdd:PRK08961 251 ARLLT 255
PLN02512 PLN02512
acetylglutamate kinase
 121-231 8.21e-03

acetylglutamate kinase


Pssm-ID: 178128  Cd Length: 309  Bit Score: 37.74  E-value: 8.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549578914 121 LRALLDNHIVPVINendAVATAEIKVGDNDNLSALAAILA---GADKLLLLTDQQGLFTA--DPRSnpqaeLIK--DVYG 193
Cdd:PLN02512 179 LRPLVDDGHIPVIA---TVAADEDGQAYNINADTAAGEIAaalGAEKLILLTDVAGVLEDkdDPGS-----LVKelDIKG 250

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 549578914 194 VDDAlrsIAGDSVsglgTGGMSTKLQAADVACRAGIDT 231
Cdd:PLN02512 251 VRKL---IADGKI----AGGMIPKVECCVRSLAQGVKT 281
 
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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