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Conserved domains on  [gi|2563495933|gb|WLU66878|]
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glutamate 5-kinase [Brucella abortus]

Protein Classification

glutamate 5-kinase( domain architecture ID 11415724)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ProB COG0263
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ...
 5-369 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: 548.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933   5 LKDYRRIVVKIGSALLVDRATGLKRKWLESLGQDIAALQHAGVEVLVVSSGAIALGRTVLGLPKKALKLEESQAAAAAGQ 84
Cdd:COG0263     4 LAKARRIVVKIGSSLLTDEGGGLDRARLAALADQIAALRAAGKEVVLVSSGAVAAGRGRLGLPKRPKTLPEKQAAAAVGQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933  85 IALAKAYADVLGGHGIKSGQILVTLSDTEERRRYLNARATIETLLKLKAVPIINENDTVATTEIRYGDNDRLAARVATMM 164
Cdd:COG0263    84 GLLMQAYEEAFARHGLTVAQVLLTRDDLEDRRRYLNARNTLETLLELGVVPIINENDTVATDEIRFGDNDRLAALVANLV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 165 GADLLILLSDIDGLYTAPPHKNPDAQFLPFVETITPQIEAMAGAAASELSRGGMKTKLDAGKIANAAGTAMIITSGTRFG 244
Cdd:COG0263   164 EADLLVLLTDVDGLYDADPRKDPDAKLIPEVEEITPEIEAMAGGAGSGLGTGGMATKLEAARIATRAGIPTVIASGREPN 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 245 PLSAIDRGER-ATLFEAAHAPVNAWKTWISGNLEPAGRLTVDAGAVKAL-KSGKSLLPAGVKEVDGDFERGDTVAVMNED 322
Cdd:COG0263   244 VLLRILAGERvGTLFLPSGEPLSARKRWIAGALQPRGRLVVDAGAVRALrERGKSLLPAGVTAVEGDFERGDVVEIVDPD 323

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2563495933 323 GREIARGLIAYDAADARKVAGHKSDEISAILGYDARAAMIHRNDLVV 369
Cdd:COG0263   324 GREIARGLVNYSSDELRRIKGRRSDEIEAILGYKGRDEVIHRDNLVL 370
 
Name Accession Description Interval E-value
ProB COG0263
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ...
 5-369 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: 548.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933   5 LKDYRRIVVKIGSALLVDRATGLKRKWLESLGQDIAALQHAGVEVLVVSSGAIALGRTVLGLPKKALKLEESQAAAAAGQ 84
Cdd:COG0263     4 LAKARRIVVKIGSSLLTDEGGGLDRARLAALADQIAALRAAGKEVVLVSSGAVAAGRGRLGLPKRPKTLPEKQAAAAVGQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933  85 IALAKAYADVLGGHGIKSGQILVTLSDTEERRRYLNARATIETLLKLKAVPIINENDTVATTEIRYGDNDRLAARVATMM 164
Cdd:COG0263    84 GLLMQAYEEAFARHGLTVAQVLLTRDDLEDRRRYLNARNTLETLLELGVVPIINENDTVATDEIRFGDNDRLAALVANLV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 165 GADLLILLSDIDGLYTAPPHKNPDAQFLPFVETITPQIEAMAGAAASELSRGGMKTKLDAGKIANAAGTAMIITSGTRFG 244
Cdd:COG0263   164 EADLLVLLTDVDGLYDADPRKDPDAKLIPEVEEITPEIEAMAGGAGSGLGTGGMATKLEAARIATRAGIPTVIASGREPN 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 245 PLSAIDRGER-ATLFEAAHAPVNAWKTWISGNLEPAGRLTVDAGAVKAL-KSGKSLLPAGVKEVDGDFERGDTVAVMNED 322
Cdd:COG0263   244 VLLRILAGERvGTLFLPSGEPLSARKRWIAGALQPRGRLVVDAGAVRALrERGKSLLPAGVTAVEGDFERGDVVEIVDPD 323

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2563495933 323 GREIARGLIAYDAADARKVAGHKSDEISAILGYDARAAMIHRNDLVV 369
Cdd:COG0263   324 GREIARGLVNYSSDELRRIKGRRSDEIEAILGYKGRDEVIHRDNLVL 370
proB TIGR01027
glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ...
 9-369 3.20e-130

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: 377.80  E-value: 3.20e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933   9 RRIVVKIGSALLVDRATGLKRKWLESLGQDIAALQHAGVEVLVVSSGAIALGRTVLGLPKKALKLEESQAAAAAGQIALA 88
Cdd:TIGR01027   1 QRIVVKVGSSSLTGSSGSLDRSHIAELVEQVAALHAAGHEVVIVSSGAIAAGFEALGLPERPKTLAEKQALAAVGQVRLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933  89 KAYADVLGGHGIKSGQILVTLSDTEERRRYLNARATIETLLKLKAVPIINENDTVATTEIRYGDNDRLAARVATMMGADL 168
Cdd:TIGR01027  81 QLYEQLFSQYGIKVAQILLTRADFSDRERYLNARNTLEALLELGVVPIINENDTVATEEIKFGDNDTLSALVAILVGADL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 169 LILLSDIDGLYTAPPHKNPDAQFLPFVETITPQIEAMAGAAASELSRGGMKTKLDAGKIANAAGTAMIITSGTRFGPLSA 248
Cdd:TIGR01027 161 LVLLTDVDGLYDADPRTNPDAKLIPVVEEITDLLLGVAGDSGSSVGTGGMRTKLQAADLATRAGVPVIIASGSKPEKIAD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 249 IDRGER-ATLFEAAHAPVNAWKTWISGNLEPAGRLTVDAGAVKALKS-GKSLLPAGVKEVDGDFERGDTVAVMNEDGREI 326
Cdd:TIGR01027 241 ALEGAPvGTLFHAQARRLRNRKFWIAFASEPAGEITVDAGAEEALLErGKSLLPAGIVGVEGNFSRGEVVEILNPEGQDI 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 2563495933 327 ARGLIAYDAADARKVAGHKSDEISAILGYDARAAMIHRNDLVV 369
Cdd:TIGR01027 321 GRGLVNYSSDELEKIKGHKSSEIEAVLGYEYGDEVVHRDDMVL 363
AAK_G5K_ProB cd04242
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ...
 10-258 6.35e-117

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: 339.42  E-value: 6.35e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933  10 RIVVKIGSALLVDRATGLKRKWLESLGQDIAALQHAGVEVLVVSSGAIALGRTVLGLPKKALKLEESQAAAAAGQIALAK 89
Cdd:cd04242     1 RIVVKVGSSLLTDEDGGLDLGRLASLVEQIAELRNQGKEVILVSSGAVAAGRQRLGLEKRPKTLPEKQALAAVGQSLLMA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933  90 AYADVLGGHGIKSGQILVTLSDTEERRRYLNARATIETLLKLKAVPIINENDTVATTEIRYGDNDRLAARVATMMGADLL 169
Cdd:cd04242    81 LYEQLFAQYGIKVAQILLTRDDFEDRKRYLNARNTLETLLELGVIPIINENDTVATEEIRFGDNDRLSALVAGLVNADLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 170 ILLSDIDGLYTAPPHKNPDAQFLPFVETITPQIEAMAGAAASELSRGGMKTKLDAGKIANAAGTAMIITSGTRFGPLSAI 249
Cdd:cd04242   161 ILLSDVDGLYDKNPRENPDAKLIPEVEEITDEIEAMAGGSGSSVGTGGMRTKLKAARIATEAGIPVVIANGRKPDVLLDI 240

                         250
                  ....*....|
gi 2563495933 250 DRGE-RATLF 258
Cdd:cd04242   241 LAGEaVGTLF 250
PRK12314 PRK12314
gamma-glutamyl kinase; Provisional
 1-258 2.66e-90

gamma-glutamyl kinase; Provisional


Pssm-ID: 183430 [Multi-domain]  Cd Length: 266  Bit Score: 272.50  E-value: 2.66e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933   1 MLKKLKDYRRIVVKIGSALLVDRATGLKRKWLESLGQDIAALQHAGVEVLVVSSGAIALGRTVLGLPKKALKLEESQAAA 80
Cdd:PRK12314    2 MRRQLENAKRIVIKVGSSTLSYENGKINLERIEQLVFVISDLMNKGKEVILVSSGAIGAGLTKLKLDKRPTSLAEKQALA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933  81 AAGQIALAKAYADVLGGHGIKSGQILVTLSDTEERRRYLNARATIETLLKLKAVPIINENDTVATTEI--RYGDNDRLAA 158
Cdd:PRK12314   82 AVGQPELMSLYSKFFAEYGIVVAQILLTRDDFDSPKSRANVKNTFESLLELGILPIVNENDAVATDEIdtKFGDNDRLSA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 159 RVATMMGADLLILLSDIDGLYTAPPHKNPDAQFLPFVETITPQIEAMAGAAASELSRGGMKTKLDAGKIANAAGTAMIIT 238
Cdd:PRK12314  162 IVAKLVKADLLIILSDIDGLYDKNPRINPDAKLRSEVTEITEEILALAGGAGSKFGTGGMVTKLKAAKFLMEAGIKMVLA 241

                         250       260
                  ....*....|....*....|.
gi 2563495933 239 SGTRFGPLSAIDRGE-RATLF 258
Cdd:PRK12314  242 NGFNPSDILDFLEGEsIGTLF 262
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 9-239 1.33e-35

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: 130.18  E-value: 1.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933   9 RRIVVKIGSALLVDRATglkrkwLESLGQDIAALQHAGVEVLVVSSG-------AIALG---RTVLGLPKKALKLEESQA 78
Cdd:pfam00696   1 KRVVIKLGGSSLTDKER------LKRLADEIAALLEEGRKLVVVHGGgafadglLALLGlspRFARLTDAETLEVATMDA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933  79 AAAAGQIALAKAYADVLGGHGIKSGQILVTLSDTEERRRYLNARATIETLLKLKAVPIINENDTVATTEIRY-GDNDRLA 157
Cdd:pfam00696  75 LGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVTRIDTEALEELLEAGVVPVITGFIGIDPEGELGrGSSDTLA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 158 ARVATMMGADLLILLSDIDGLYTAPPHKNPDAQFLPFVEtitpqIEAMAGAAASELSRGGMKTKLDAG-KIANAAGTAMI 236
Cdd:pfam00696 155 ALLAEALGADKLIILTDVDGVYTADPRKVPDAKLIPEIS-----YDELLELLASGLATGGMKVKLPAAlEAARRGGIPVV 229


                  ...
gi 2563495933 237 ITS 239
Cdd:pfam00696 230 IVN 232
PUA smart00359
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
280-344 4.49e-16

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


Pssm-ID: 214635 [Multi-domain]  Cd Length: 76  Bit Score: 72.29  E-value: 4.49e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2563495933  280 GRLTVDAGAVKALKSGKSLLPAGVKEVDGDFERGDTVAVMNEDGREIARGLIAYDAADARKVAGH 344
Cdd:smart00359   1 GKVVVDDGAEKAILNGASLLAPGVVRVDGDIKEGDVVVIVDEKGEPLGIGLANMSSEEIARIKGK 65
 
Name Accession Description Interval E-value
ProB COG0263
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ...
 5-369 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: 548.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933   5 LKDYRRIVVKIGSALLVDRATGLKRKWLESLGQDIAALQHAGVEVLVVSSGAIALGRTVLGLPKKALKLEESQAAAAAGQ 84
Cdd:COG0263     4 LAKARRIVVKIGSSLLTDEGGGLDRARLAALADQIAALRAAGKEVVLVSSGAVAAGRGRLGLPKRPKTLPEKQAAAAVGQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933  85 IALAKAYADVLGGHGIKSGQILVTLSDTEERRRYLNARATIETLLKLKAVPIINENDTVATTEIRYGDNDRLAARVATMM 164
Cdd:COG0263    84 GLLMQAYEEAFARHGLTVAQVLLTRDDLEDRRRYLNARNTLETLLELGVVPIINENDTVATDEIRFGDNDRLAALVANLV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 165 GADLLILLSDIDGLYTAPPHKNPDAQFLPFVETITPQIEAMAGAAASELSRGGMKTKLDAGKIANAAGTAMIITSGTRFG 244
Cdd:COG0263   164 EADLLVLLTDVDGLYDADPRKDPDAKLIPEVEEITPEIEAMAGGAGSGLGTGGMATKLEAARIATRAGIPTVIASGREPN 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 245 PLSAIDRGER-ATLFEAAHAPVNAWKTWISGNLEPAGRLTVDAGAVKAL-KSGKSLLPAGVKEVDGDFERGDTVAVMNED 322
Cdd:COG0263   244 VLLRILAGERvGTLFLPSGEPLSARKRWIAGALQPRGRLVVDAGAVRALrERGKSLLPAGVTAVEGDFERGDVVEIVDPD 323

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2563495933 323 GREIARGLIAYDAADARKVAGHKSDEISAILGYDARAAMIHRNDLVV 369
Cdd:COG0263   324 GREIARGLVNYSSDELRRIKGRRSDEIEAILGYKGRDEVIHRDNLVL 370
proB TIGR01027
glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ...
 9-369 3.20e-130

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: 377.80  E-value: 3.20e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933   9 RRIVVKIGSALLVDRATGLKRKWLESLGQDIAALQHAGVEVLVVSSGAIALGRTVLGLPKKALKLEESQAAAAAGQIALA 88
Cdd:TIGR01027   1 QRIVVKVGSSSLTGSSGSLDRSHIAELVEQVAALHAAGHEVVIVSSGAIAAGFEALGLPERPKTLAEKQALAAVGQVRLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933  89 KAYADVLGGHGIKSGQILVTLSDTEERRRYLNARATIETLLKLKAVPIINENDTVATTEIRYGDNDRLAARVATMMGADL 168
Cdd:TIGR01027  81 QLYEQLFSQYGIKVAQILLTRADFSDRERYLNARNTLEALLELGVVPIINENDTVATEEIKFGDNDTLSALVAILVGADL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 169 LILLSDIDGLYTAPPHKNPDAQFLPFVETITPQIEAMAGAAASELSRGGMKTKLDAGKIANAAGTAMIITSGTRFGPLSA 248
Cdd:TIGR01027 161 LVLLTDVDGLYDADPRTNPDAKLIPVVEEITDLLLGVAGDSGSSVGTGGMRTKLQAADLATRAGVPVIIASGSKPEKIAD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 249 IDRGER-ATLFEAAHAPVNAWKTWISGNLEPAGRLTVDAGAVKALKS-GKSLLPAGVKEVDGDFERGDTVAVMNEDGREI 326
Cdd:TIGR01027 241 ALEGAPvGTLFHAQARRLRNRKFWIAFASEPAGEITVDAGAEEALLErGKSLLPAGIVGVEGNFSRGEVVEILNPEGQDI 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 2563495933 327 ARGLIAYDAADARKVAGHKSDEISAILGYDARAAMIHRNDLVV 369
Cdd:TIGR01027 321 GRGLVNYSSDELEKIKGHKSSEIEAVLGYEYGDEVVHRDDMVL 363
AAK_G5K_ProB cd04242
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ...
 10-258 6.35e-117

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: 339.42  E-value: 6.35e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933  10 RIVVKIGSALLVDRATGLKRKWLESLGQDIAALQHAGVEVLVVSSGAIALGRTVLGLPKKALKLEESQAAAAAGQIALAK 89
Cdd:cd04242     1 RIVVKVGSSLLTDEDGGLDLGRLASLVEQIAELRNQGKEVILVSSGAVAAGRQRLGLEKRPKTLPEKQALAAVGQSLLMA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933  90 AYADVLGGHGIKSGQILVTLSDTEERRRYLNARATIETLLKLKAVPIINENDTVATTEIRYGDNDRLAARVATMMGADLL 169
Cdd:cd04242    81 LYEQLFAQYGIKVAQILLTRDDFEDRKRYLNARNTLETLLELGVIPIINENDTVATEEIRFGDNDRLSALVAGLVNADLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 170 ILLSDIDGLYTAPPHKNPDAQFLPFVETITPQIEAMAGAAASELSRGGMKTKLDAGKIANAAGTAMIITSGTRFGPLSAI 249
Cdd:cd04242   161 ILLSDVDGLYDKNPRENPDAKLIPEVEEITDEIEAMAGGSGSSVGTGGMRTKLKAARIATEAGIPVVIANGRKPDVLLDI 240

                         250
                  ....*....|
gi 2563495933 250 DRGE-RATLF 258
Cdd:cd04242   241 LAGEaVGTLF 250
PRK12314 PRK12314
gamma-glutamyl kinase; Provisional
 1-258 2.66e-90

gamma-glutamyl kinase; Provisional


Pssm-ID: 183430 [Multi-domain]  Cd Length: 266  Bit Score: 272.50  E-value: 2.66e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933   1 MLKKLKDYRRIVVKIGSALLVDRATGLKRKWLESLGQDIAALQHAGVEVLVVSSGAIALGRTVLGLPKKALKLEESQAAA 80
Cdd:PRK12314    2 MRRQLENAKRIVIKVGSSTLSYENGKINLERIEQLVFVISDLMNKGKEVILVSSGAIGAGLTKLKLDKRPTSLAEKQALA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933  81 AAGQIALAKAYADVLGGHGIKSGQILVTLSDTEERRRYLNARATIETLLKLKAVPIINENDTVATTEI--RYGDNDRLAA 158
Cdd:PRK12314   82 AVGQPELMSLYSKFFAEYGIVVAQILLTRDDFDSPKSRANVKNTFESLLELGILPIVNENDAVATDEIdtKFGDNDRLSA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 159 RVATMMGADLLILLSDIDGLYTAPPHKNPDAQFLPFVETITPQIEAMAGAAASELSRGGMKTKLDAGKIANAAGTAMIIT 238
Cdd:PRK12314  162 IVAKLVKADLLIILSDIDGLYDKNPRINPDAKLRSEVTEITEEILALAGGAGSKFGTGGMVTKLKAAKFLMEAGIKMVLA 241

                         250       260
                  ....*....|....*....|.
gi 2563495933 239 SGTRFGPLSAIDRGE-RATLF 258
Cdd:PRK12314  242 NGFNPSDILDFLEGEsIGTLF 262
PUA_G5K cd21157
PUA domain of gamma-glutamyl kinase, found in archaea, bacteria, and eukarya; Gamma glutamyl ...
 267-369 5.25e-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: 158.01  E-value: 5.25e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 267 AWKTWISGNLEPAGRLTVDAGAVKALKS-GKSLLPAGVKEVDGDFERGDTVAVMNEDGREIARGLIAYDAADARKVAGHK 345
Cdd:cd21157     1 ARKQWIAFALKPKGKLVVDAGAVKALLEgGKSLLPAGITAVEGDFERGDVVRIVDPDGREIARGLVNYSSEELRKIKGKK 80

                          90       100
                  ....*....|....*....|....
gi 2563495933 346 SDEISAILGYDARAAMIHRNDLVV 369
Cdd:cd21157    81 SSEIEEILGYKYGDEVIHRDNLVL 104
AAK_P5CS_ProBA cd04256
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ...
 5-258 1.33e-44

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: 155.28  E-value: 1.33e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933   5 LKDYRRIVVKIGSALLV-DRATGLKRKWLESLGQDIAALQHAGVEVLVVSSGAIALGRTVLG---LPKKALK--LEESQA 78
Cdd:cd04256     5 LKHAKRIVVKLGSAVVTrEDECGLALGRLASIVEQVSELQSQGREVILVTSGAVAFGKQRLRheiLLSSSMRqtLKSGQL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933  79 AAAAGQIALAKAYADV------------LGGHGIKSGQILVTLSD--TEERRRYLNAraTIETLLKLKAVPIINENDTVA 144
Cdd:cd04256    85 KDMPQMELDGRACAAVgqsglmalyeamFTQYGITVAQVLVTKPDfyDEQTRRNLNG--TLEELLRLNIIPIINTNDAVS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 145 TTEIRYG---------DNDRLAARVATMMGADLLILLSDIDGLYTAPPhKNPDAQFLpfvETITPQIEA-MAGAAASELS 214
Cdd:cd04256   163 PPPEPDEdlqgvisikDNDSLAARLAVELKADLLILLSDVDGLYDGPP-GSDDAKLI---HTFYPGDQQsITFGTKSRVG 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2563495933 215 RGGMKTKLDAGKIANAAGTAMIITSGTRFGPLSAIDRGER-ATLF 258
Cdd:cd04256   239 TGGMEAKVKAALWALQGGTSVVITNGMAGDVITKILEGKKvGTFF 283
PLN02418 PLN02418
delta-1-pyrroline-5-carboxylate synthase
 5-268 1.56e-42

delta-1-pyrroline-5-carboxylate synthase


Pssm-ID: 215230  Cd Length: 718  Bit Score: 157.58  E-value: 1.56e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933   5 LKDYRRIVVKIGSALlVDRATG---LKRkwLESLGQDIAALQHAGVEVLVVSSGAIALGRTVL---GLPKKALK-LEESQ 77
Cdd:PLN02418   12 LRDVKRVVIKVGTAV-VTRDDGrlaLGR--LGALCEQIKELNSDGYEVILVSSGAVGVGRQRLryrRLVNSSFAdLQKPQ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933  78 AAAAAgqialaKAYADV------------LGGHGIKSGQILVTLSDTEERRRYLNARATIETLLKLKAVPIINENDTVAT 145
Cdd:PLN02418   89 MELDG------KACAAVgqselmalydtlFSQLDVTASQLLVTDSDFRDPDFRKQLSETVESLLDLRVIPIFNENDAVST 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 146 TEIRY-------GDNDRLAARVATMMGADLLILLSDIDGLYTAPPhKNPDAQFLPFVETITPQIEAMAGaAASELSRGGM 218
Cdd:PLN02418  163 RRAPYedssgifWDNDSLAALLALELKADLLILLSDVEGLYTGPP-SDPSSKLIHTYIKEKHQDEITFG-EKSRVGRGGM 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2563495933 219 KTKLDAGKIANAAGTAMIITSGTRFGPLSAIDRGER-ATLFeaaHAPVNAW 268
Cdd:PLN02418  241 TAKVKAAVNAASAGIPVVITSGYALDNIRKVLRGERvGTLF---HQDAHLW 288
PTZ00489 PTZ00489
glutamate 5-kinase; Provisional
 1-240 1.81e-38

glutamate 5-kinase; Provisional


Pssm-ID: 240438 [Multi-domain]  Cd Length: 264  Bit Score: 138.61  E-value: 1.81e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933   1 MLKKLKDYRRIVVKIGSALLVDRATgLKRKWLESLGQDIAALQhAGVEVLVVSSGAIALGRTVLGLPKKALKleESQAAA 80
Cdd:PTZ00489    1 MADILKSVKRIVVKVGSSILVDNQE-IAAHRIEALCRFIADLQ-TKYEVILVTSGAVAAGYTKKEMDKSYVP--NKQALA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933  81 AAGQIALAKAYADVLGGHGIKSGQILVTLSDTEERRRYLNARATIETLLKLKAVPIINENDTVATTEIRYGDNDRLAARV 160
Cdd:PTZ00489   77 SMGQPLLMHMYYTELQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALHELVFGDNDRLSALV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 161 ATMMGADLLILLSDIDGLYTAPPHKNPDAQFLPFVETITPQIEAMAGAAASELSRGGMKTKLDAGKIANAAGTAMIITSG 240
Cdd:PTZ00489  157 AHHFKADLLVILSDIDGYYTENPRTSTDAKIRSVVHELSPDDLVAEATPNNRFATGGIVTKLQAAQFLLERGGKMYLSSG 236
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 9-239 1.33e-35

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: 130.18  E-value: 1.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933   9 RRIVVKIGSALLVDRATglkrkwLESLGQDIAALQHAGVEVLVVSSG-------AIALG---RTVLGLPKKALKLEESQA 78
Cdd:pfam00696   1 KRVVIKLGGSSLTDKER------LKRLADEIAALLEEGRKLVVVHGGgafadglLALLGlspRFARLTDAETLEVATMDA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933  79 AAAAGQIALAKAYADVLGGHGIKSGQILVTLSDTEERRRYLNARATIETLLKLKAVPIINENDTVATTEIRY-GDNDRLA 157
Cdd:pfam00696  75 LGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVTRIDTEALEELLEAGVVPVITGFIGIDPEGELGrGSSDTLA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 158 ARVATMMGADLLILLSDIDGLYTAPPHKNPDAQFLPFVEtitpqIEAMAGAAASELSRGGMKTKLDAG-KIANAAGTAMI 236
Cdd:pfam00696 155 ALLAEALGADKLIILTDVDGVYTADPRKVPDAKLIPEIS-----YDELLELLASGLATGGMKVKLPAAlEAARRGGIPVV 229


                  ...
gi 2563495933 237 ITS 239
Cdd:pfam00696 230 IVN 232
P5CS TIGR01092
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ...
 5-263 2.31e-35

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: 137.35  E-value: 2.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933   5 LKDYRRIVVKIGSALLVDRATGLKRKWLESLGQDIAALQHAGVEVLVVSSGAIALGR-----------TVLGLPKKALKL 73
Cdd:TIGR01092   4 LKDVKRIVVKVGTAVVTRGDGRLALGRLGSICEQLSELNSDGREVILVTSGAVAFGRqrlrhrilvnsSFADLQKPQPEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933  74 EeSQAAAAAGQIALAKAYADVLGGHGIKSGQILVTLSDTEERRRYLNARATIETLLKLKAVPIINENDTVATTEIRYGD- 152
Cdd:TIGR01092  84 D-GKACAAVGQSGLMALYETMFTQLDITAAQILVTDLDFRDEQFRRQLNETVHELLRMNVVPVVNENDAVSTRAAPYSDs 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 153 ------NDRLAARVATMMGADLLILLSDIDGLYTAPPhKNPDAQFLPFVETITPQIEAMAGaAASELSRGGMKTKLDAGK 226
Cdd:TIGR01092 163 qgifwdNDSLAALLALELKADLLILLSDVEGLYDGPP-SDDDSKLIDTFYKEKHQGEITFG-TKSRLGRGGMTAKVKAAV 240

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2563495933 227 IANAAGTAMIITSGTRFGPLSAIDRGER-ATLF-EAAHA 263
Cdd:TIGR01092 241 WAAYGGTPVIIASGTAPKNITKVVEGKKvGTLFhEDAHL 279
PUA pfam01472
PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, ...
 280-353 5.56e-24

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: 93.70  E-value: 5.56e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2563495933 280 GRLTVDAGAVKALKSGKSLLPAGVKEVDGDFERGDTVAVMNEDGREIARGLIAYDAADARKVAGHKSDEISAIL 353
Cdd:pfam01472   1 GRVVVDDGAVKAILNGASLLAPGVVRVDGDFRKGDEVVVVTEKGELVAVGLANYSSEELAKIEGGKAVKVRRVL 74
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 12-258 9.71e-20

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: 87.50  E-value: 9.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933  12 VVKIGSALLVDRATglkrkwLESLGQDIAALQHAGVEVLVVSSGAIALGRTVLGLPKKALKLEESQAAAAAGQ------- 84
Cdd:cd02115     1 VIKFGGSSVSSEER------LRNLARILVKLASEGGRVVVVHGAGPQITDELLAHGELLGYARGLRITDRETDalaamge 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933  85 IALAKAYADVLGGHGIKSGQILVTLSDTEERRRYLNARAT------IETLLKLKAVPIINENDTVA---TTEIRYGDNDR 155
Cdd:cd02115    75 GMSNLLIAAALEQHGIKAVPLDLTQAGFASPNQGHVGKITkvstdrLKSLLENGILPILSGFGGTDekeTGTLGRGGSDS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 156 LAARVATMMGADLLILLSDIDGLYTAPPHKNPDAQFLPfveTITPQIeamagaAASELSRGGMKTKLDAGKIANAAGTAM 235
Cdd:cd02115   155 TAALLAAALKADRLVILTDVDGVYTADPRKVPDAKLLS---ELTYEE------AAELAYAGAMVLKPKAADPAARAGIPV 225

                         250       260
                  ....*....|....*....|...
gi 2563495933 236 IITSGTRFGPLSAIDRGERATLF 258
Cdd:cd02115   226 RIANTENPGALALFTPDGGGTLI 248
PUA smart00359
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
280-344 4.49e-16

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


Pssm-ID: 214635 [Multi-domain]  Cd Length: 76  Bit Score: 72.29  E-value: 4.49e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2563495933  280 GRLTVDAGAVKALKSGKSLLPAGVKEVDGDFERGDTVAVMNEDGREIARGLIAYDAADARKVAGH 344
Cdd:smart00359   1 GKVVVDDGAEKAILNGASLLAPGVVRVDGDIKEGDVVVIVDEKGEPLGIGLANMSSEEIARIKGK 65
PUA cd07953
PUA RNA binding domain; The PUA (PseudoUridine synthase and Archaeosine transglycosylase) ...
 280-340 2.53e-11

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: 58.85  E-value: 2.53e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2563495933 280 GRLTVDAGAVKALKSGKSLLPAGVKEVDGDFERGDTVAVMNEDGREIARGLIAYDAADARK 340
Cdd:cd07953     1 PVVVVDKGAEKAVLNGADLMAPGVVSADGDFKRGDLVRIVSEGGRPLAIGVAEMSSDEMKE 61
AAK_UMPK-like cd04239
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ...
 10-230 2.81e-11

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: 62.55  E-value: 2.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933  10 RIVVKIGSALLVDRATGLKRKWLESLGQDIAALQHAGVEVLVVSSGaialGRTVLGLPKKALKLEESQAAAAAGQIALAK 89
Cdd:cd04239     1 RIVLKLSGEALAGEGGGIDPEVLKEIAREIKEVVDLGVEVAIVVGG----GNIARGYIAAARGMPRATADYIGMLATVMN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933  90 AYA--DVLGGHGIKSgQILVTLSDTEERRRYlNARATIEtLLKLKAVPIinendTVATTEIRYGDNDRLAARVATMMGAD 167
Cdd:cd04239    77 ALAlqDALEKLGVKT-RVMSAIPMQGVAEPY-IRRRAIR-HLEKGRIVI-----FGGGTGNPGFTTDTAAALRAEEIGAD 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 168 LLILLSDIDGLYTAPPHKNPDAQFLP---FVETITPQIEAMAGAAASELSRGGMKTK----LDAGKIANA 230
Cdd:cd04239   149 VLLKATNVDGVYDADPKKNPDAKKYDrisYDELLKKGLKVMDATALTLCRRNKIPIIvfngLKPGNLLRA 218
AAK_FomA-like cd04241
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ...
 123-253 2.89e-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: 59.97  E-value: 2.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 123 ATIETLLKLKAVPIINEN---DTVATTEIRYGDNdrLAARVATMMGADLLILLSDIDGLYTAPPhknPDAQFLPFVETIT 199
Cdd:cd04241   118 EVIKELLDRGFVPVLHGDvvlDEGGGITILSGDD--IVVELAKALKPERVIFLTDVDGVYDKPP---PDAKLIPEIDVGS 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2563495933 200 P-QIEAMAGAAASELSrGGMKTKLDAGKIANAAGTAMIITSGTRFGPLSAIDRGE 253
Cdd:cd04241   193 LeDILAALGSAGTDVT-GGMAGKIEELLELARRGIEVYIFNGDKPENLYRALLGN 246
PRK14058 PRK14058
[LysW]-aminoadipate/[LysW]-glutamate kinase;
125-242 1.05e-08

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


Pssm-ID: 237599 [Multi-domain]  Cd Length: 268  Bit Score: 55.68  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 125 IETLLKLKAVPII------NENDTVATteirygDNDRLAARVATMMGADLLILLSDIDGLYTAPPHKNpdaqflPFVETI 198
Cdd:PRK14058  142 LKLLLKAGYLPVVappalsEEGEPLNV------DGDRAAAAIAGALKAEALVLLSDVPGLLRDPPDEG------SLIERI 209

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2563495933 199 TP-QIEAMAGAAaselsRGGMKTKLDAGKIANAAGTAMIITSGTR 242
Cdd:PRK14058  210 TPeEAEELSKAA-----GGGMKKKVLMAAEAVEGGVGRVIIADAN 249
Tma20 COG2016
Predicted ribosome-associated RNA-binding protein Tma20, contains PUA domain [Translation, ...
 280-340 3.54e-07

Predicted ribosome-associated RNA-binding protein Tma20, contains PUA domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441619 [Multi-domain]  Cd Length: 154  Bit Score: 49.40  E-value: 3.54e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2563495933 280 GRLTVDAGAVKALKSGKSLLPAGVKEVDGDFERGDTVAVMNED-GREIARGLIAYDAADARK 340
Cdd:COG2016    74 PVVTVDMGAVKFVSNGADVMRPGIVEADGEIKEGDIVVIVEEKhGKPLAVGRALVDGEEMVE 135
PRK13795 PRK13795
hypothetical protein; Provisional
 283-337 4.45e-07

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 51.92  E-value: 4.45e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2563495933 283 TVDAGAVKALKSGKSLLPAGVKEVDGDFERGDTVAVMNEDGREIARGLIAYDAAD 337
Cdd:PRK13795  130 IVDKGALEPIKNGKNVLAPGVVEADLDIKKGDEVVVVTEDGEVVGVGRAKMDGDD 184
arCOG00985 TIGR03684
arCOG04150 universal archaeal PUA-domain protein; This universal archaeal protein contains a ...
 280-338 5.41e-07

arCOG04150 universal archaeal PUA-domain protein; This universal archaeal protein contains a domain possibly associated with RNA binding (pfam01472, TIGR00451).


Pssm-ID: 274723 [Multi-domain]  Cd Length: 150  Bit Score: 48.76  E-value: 5.41e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 280 GRLTVDAGAVKALKSGKSLLPAGVKEVDGDFERGDTVAVMNE-DGREIARGLIAYDAADA 338
Cdd:TIGR03684  70 NVVVVDEGAVKFIINGADIMAPGIVEADPSIKEGDIVFVVDEtHGKPLAVGIALMDAEEM 129
AAK_UMPK-PyrH-Pf cd04253
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ...
 154-253 8.79e-07

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: 49.17  E-value: 8.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 154 DRLAARVATMMGADLLILLSDIDGLYTAPPHKNPDAQFLPfveTITPQiEAMAGAAASELsRGGMKTKLD--AGKIANAA 231
Cdd:cd04253   118 DAVAALLAERLGADLLINATNVDGVYSKDPRKDPDAKKFD---RLSAD-ELIDIVGKSSW-KAGSNEPFDplAAKIIERS 192

                          90       100
                  ....*....|....*....|..
gi 2563495933 232 GTAMIITSGTRFGPLSAIDRGE 253
Cdd:cd04253   193 GIKTIVVDGRDPENLERALKGE 214
PUA_MJ1432-like cd21154
PUA RNA-binding domain of MJ1432, TA1423, PH0734, and similar proteins; The RNA-binding PUA ...
 280-340 1.48e-06

PUA RNA-binding domain of MJ1432, TA1423, PH0734, and similar proteins; The RNA-binding PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in a number of proteins involved in RNA metabolism. Members of this mostly archaeal family have not been characterized functionally; they may bind to RNA. This family includes Pyrococcus horikoshii PH0734 where the N-terminal domain may modulate the binding target of the C-terminal PUA domain using its characteristic electropositive surface.


Pssm-ID: 409296 [Multi-domain]  Cd Length: 84  Bit Score: 45.57  E-value: 1.48e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2563495933 280 GRLTVDAGAVKALKSGKSLLPAGVKEVDGDFERGDTVAVMNED-GREIARGLIAYDAADARK 340
Cdd:cd21154     3 PRVVVDMGAVKFVANGADVMRPGIVEADEEIKKGDIVVVVDERhGKPLAVGIALMSGEEMVE 64
PUA_3 pfam17785
PUA-like domain; This PUA-like domain is found at the N-terminus of SAM-dependent ...
 282-331 4.24e-06

PUA-like domain; This PUA-like domain is found at the N-terminus of SAM-dependent methyltransferases.


Pssm-ID: 436043 [Multi-domain]  Cd Length: 64  Bit Score: 44.00  E-value: 4.24e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2563495933 282 LTVDAGAVKALKSGKSLLPAG-VKEVDGDFERGDTVAVMNEDGREIARGLI 331
Cdd:pfam17785   1 VTLKKKAEKRLKRGHPWIYSNeIERVEGDLEEGDLVRVVDSDGRFLGTGYY 51
argB TIGR00761
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ...
 11-228 6.32e-06

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: 46.89  E-value: 6.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933  11 IVVKIGSALLVDRatglkrkwLESLGQDIAALQHAGVEVLVVSSG-------AIALG---RTVLGL---PKKALKLEEsq 77
Cdd:TIGR00761   2 IVIKIGGAAISDL--------LEAFASDIAFLRAVGIKPVIVHGGgpeinelLEALGippEFKNGLrvtDKETLEVVE-- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933  78 aaaAAGQIALAKAYADVLGGHGIKS-------GQILVTLSDTEERRRY------LNARAtIETLLKLKAVPIINENDTVA 144
Cdd:TIGR00761  72 ---MVLIGQVNKELVALLNKHGINAigltggdGQLFTARYLDKEDLGYvgeikkVNKAL-IEALLKAGYIPVISSLALTA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 145 TTEIRYGDNDRLAARVATMMGADLLILLSDIDGLYtapphkNPDAQFLpfVETITP-QIEAMAGaaaSELSRGGMKTKLD 223
Cdd:TIGR00761 148 EGQALNVNADTAAGALAAALGAEKLVLLTDVPGIL------NGDGQSL--ISEIPLdEIEQLIK---QGIIKGGMIPKVN 216


                  ....*
gi 2563495933 224 AGKIA 228
Cdd:TIGR00761 217 AALEA 221
PRK14560 PRK14560
putative RNA-binding protein; Provisional
 280-338 1.11e-05

putative RNA-binding protein; Provisional


Pssm-ID: 237757 [Multi-domain]  Cd Length: 160  Bit Score: 45.23  E-value: 1.11e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 280 GRLTVDAGAVKALKSGKSLLPAGVKEVDGDFERGDTVAVMNE-DGREIARGLIAYDAADA 338
Cdd:PRK14560   77 RRVVVDAGAVKFVSNGADVMAPGIVEADEDIKEGDIVFVVEEtHGKPLAVGRALMDGDEM 136
PUA_RlmI cd21153
PUA RNA-binding domain of the SAM-dependent methyltransferase RlmI and related proteins; The ...
 281-331 4.66e-05

PUA RNA-binding domain of the SAM-dependent methyltransferase RlmI and related proteins; The RNA-binding PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in a number of proteins involved in RNA metabolism. Members of this subfamily contain PUA domains that co-occur N-terminal to SAM-dependent methyltransferase domains and include Escherichia coli RlmI (rRNA large subunit methyltransferase gene I, also called YccW) and Thermus thermophilus methyltransferase RlmO, which are 5-methylcytosine methyltransferases (m5C MTases) that play a role in modifying 23S rRNA. This subfamily also includes Pyrococcus horikoshii PH1915 that may play a role as a 5-methyluridine MTase, and/or perform similar roles.


Pssm-ID: 409295 [Multi-domain]  Cd Length: 70  Bit Score: 41.03  E-value: 4.66e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2563495933 281 RLTVDAGAVKALKSGKSLLPAG-VKEVDGDFERGDTVAVMNEDGREIARGLI 331
Cdd:cd21153     2 RIVLKKGKEKSLRRGHPWIFSGaIDRIEGKPEPGDLVDVYDHKGKFLGTGLY 53
AAK_NAGK-UC cd04251
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ...
 152-253 7.42e-05

AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar to Escherichia coli and Pseudomonas aeruginosa NAGKs which catalyze the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis. These uncharacterized domain sequences are found in some bacteria (Deinococci and Chloroflexi) and archea and belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239784 [Multi-domain]  Cd Length: 257  Bit Score: 43.90  E-value: 7.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 152 DNDRLAARVATMMGADLLILLSDIDGLYTapphknpDAQFLPfvETITPQIEAMAGAAaselsRGGMKTKLDAGKIANAA 231
Cdd:cd04251   165 DGDRAAAAIAAALKAERLILLTDVEGLYL-------DGRVIE--RITVSDAESLLEKA-----GGGMKRKLLAAAEAVEG 230

                          90       100
                  ....*....|....*....|...
gi 2563495933 232 GTA-MIITSGTRFGPLSAIDRGE 253
Cdd:cd04251   231 GVReVVIGDARADSPISSALNGG 253
AAK_NAGK-like cd04238
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ...
 125-237 9.31e-05

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: 43.65  E-value: 9.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 125 IETLLKLKAVPIINendTVATTE--IRYGDN-DRLAARVATMMGADLLILLSDIDGLYtapphKNPDAqflpFVETITP- 200
Cdd:cd04238   131 LETLLEAGYIPVIA---PIAVDEdgETYNVNaDTAAGAIAAALKAEKLILLTDVPGVL-----DDPGS----LISELTPk 198

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2563495933 201 QIEAMagaAASELSRGGMKTKLDAGK--IANAAGTAMII 237
Cdd:cd04238   199 EAEEL---IEDGVISGGMIPKVEAALeaLEGGVRKVHII 234
PRK13794 PRK13794
hypothetical protein; Provisional
 282-340 2.14e-04

hypothetical protein; Provisional


Pssm-ID: 237509 [Multi-domain]  Cd Length: 479  Bit Score: 43.12  E-value: 2.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 282 LTVDAGAVKALK-SGKSLLPAGVKEVDGDFERGDTVAVMNEDGREIARGLIAYDAADARK 340
Cdd:PRK13794  127 IVVKDDVPKFIRnKGASVLRPGVAEASEDIEEGDDVIILDENGDVVGVGRARMSYEEIVN 186
PRK04270 PRK04270
RNA-guided pseudouridylation complex pseudouridine synthase subunit Cbf5;
281-337 4.01e-04

RNA-guided pseudouridylation complex pseudouridine synthase subunit Cbf5;


Pssm-ID: 179806 [Multi-domain]  Cd Length: 300  Bit Score: 41.77  E-value: 4.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2563495933 281 RLTVDAGAVKALKSGKSLLPAGVKEVDGDFERGDTVAVMNEDGREIARGLIAYDAAD 337
Cdd:PRK04270  227 KIIIKDSAVDAIAHGAPLYAPGIAKLEKGIKKGDLVAVFTLKGELVALGKALMDSDE 283
AAK_AK cd04234
AAK_AK: Amino Acid Kinase Superfamily (AAK), Aspartokinase (AK); this CD includes the ...
 157-219 4.02e-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: 41.30  E-value: 4.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2563495933 157 AARVATMMGADLLILLSDIDGLYTAPPHKNPDAQFLPFvetITPQiEAMagaaasELSRGGMK 219
Cdd:cd04234   142 AAALAAALGADEVEIWTDVDGIYTADPRIVPEARLIPE---ISYD-EAL------ELAYFGAK 194
PRK06291 PRK06291
aspartate kinase; Provisional
 118-219 8.20e-04

aspartate kinase; Provisional


Pssm-ID: 235773 [Multi-domain]  Cd Length: 465  Bit Score: 41.07  E-value: 8.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 118 YLNARATIETLLKLKAVPIIN----ENDTVATTEIRYGDNDRLAARVATMMGADLLILLSDIDGLYTAPPHKNPDAQFLP 193
Cdd:PRK06291  174 YERVKERLEPLLKEGVIPVVTgfigETEEGIITTLGRGGSDYSAAIIGAALDADEIWIWTDVDGVMTTDPRIVPEARVIP 253

                          90       100
                  ....*....|....*....|....*.
gi 2563495933 194 FVEtitpQIEAMagaaasELSRGGMK 219
Cdd:PRK06291  254 KIS----YIEAM------ELSYFGAK 269
unchar_dom_2 TIGR00451
uncharacterized domain 2; This uncharacterized domain is found a number of enzymes and ...
 276-330 9.90e-04

uncharacterized domain 2; This uncharacterized domain is found a number of enzymes and uncharacterized proteins, often at the C-terminus. It is found in some but not all members of a family of related tRNA-guanine transglycosylases (tgt), which exchange a guanine base for some modified base without breaking the phosphodiester backbone of the tRNA. It is also found in rRNA pseudouridine synthase, another enzyme of RNA base modification not otherwise homologous to tgt. It is found, again at the C-terminus, in two putative glutamate 5-kinases. It is also found in a family of small, uncharacterized archaeal proteins consisting mostly of this domain.


Pssm-ID: 129543 [Multi-domain]  Cd Length: 107  Bit Score: 38.18  E-value: 9.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2563495933 276 LEPAGRLTVDAGAVKALKSGKSLLPAGVKEVDGDFERGDTVAVMNEDG-REIARGL 330
Cdd:TIGR00451  27 MEDKKIVVVDNGAVKFLKNGADVMRPGIVDADEDIKEGDDVVVVDENKdRPLAVGI 82
AAK_CK cd04235
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ...
 134-239 1.09e-03

AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and carbamoyl phosphate (CP) utilization with the production of ATP from ADP and CP. Both CK (this CD) and nonhomologous CP synthetase synthesize carbamoyl phosphate, an essential precursor of arginine and pyrimidine bases, in the presence of ATP, bicarbonate, and ammonia. CK is a homodimer of 33 kDa subunits and is a member of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239768  Cd Length: 308  Bit Score: 40.57  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 134 VPIINENDTVATTE--IrygDNDRLAARVATMMGADLLILLSDIDGLYTAppHKNPDAQFLpfvETITPQiEAMAGAAAS 211
Cdd:cd04235   192 IPVVREGGGLKGVEavI---DKDLASALLAEEINADLLVILTDVDNVYIN--FGKPNQKAL---EQVTVE-ELEKYIEEG 262

                          90       100
                  ....*....|....*....|....*....
gi 2563495933 212 ELSRGGMKTKLDAG-KIANAAGTAMIITS 239
Cdd:cd04235   263 QFAPGSMGPKVEAAiRFVESGGKKAIITS 291
PRK12454 PRK12454
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
 134-239 1.45e-03

carbamate kinase-like carbamoyl phosphate synthetase; Reviewed


Pssm-ID: 183535  Cd Length: 313  Bit Score: 39.98  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 134 VPIINENDTVATTE--IrygDNDRLAARVATMMGADLLILLSDIDGLYTAppHKNPDAQFLpfvETITPQiEAMAGAAAS 211
Cdd:PRK12454  196 IPVIEEDGELKGVEavI---DKDLASELLAEELNADIFIILTDVEKVYLN--YGKPDQKPL---DKVTVE-EAKKYYEEG 266

                          90       100
                  ....*....|....*....|....*....
gi 2563495933 212 ELSRGGMKTKLDAG-KIANAAGTAMIITS 239
Cdd:PRK12454  267 HFKAGSMGPKILAAiRFVENGGKRAIIAS 295
AAK_UMPK-MosAB cd04255
AAK_UMPK-MosAB: This CD includes the alpha and beta subunits of the Mo storage protein (MosA ...
 161-193 2.13e-03

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: 39.30  E-value: 2.13e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2563495933 161 ATMMGADLLILLSDIDGLYTAPPHKNPDAQFLP 193
Cdd:cd04255   171 AEVIGARNLIFVKDEDGLYTADPKKNKKAEFIP 203
PUA_archaeosine_TGT cd21149
PUA RNA-binding domain of archaeosine tRNA-guanine transglycosylase; The RNA-binding PUA ...
 278-340 2.39e-03

PUA RNA-binding domain of archaeosine tRNA-guanine transglycosylase; The RNA-binding PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in a number of proteins involved in RNA metabolism. Members of this archaeosine tRNA-guanine transglycosylase (TGT) family are responsible for the exchange of a guanine residue in archaeal tRNAs with a preQ0 base (7-cyano-7-deazaguanine), which constitutes the initial step in archaeosine biosynthesis. Archaeosine is a modified RNA base specific to archaea (7-formamidino-7deazaguanosine), found at position 15 in tRNAs. It has been shown that the PUA domain of archaeosine TGT is not required for its specificity for position 15.


Pssm-ID: 409291 [Multi-domain]  Cd Length: 75  Bit Score: 36.44  E-value: 2.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2563495933 278 PAGRLTVDAGAVKALKSGKSLLPAGVKEVDGDFERGDTVAVMNEDGREIARGLIAYDAADARK 340
Cdd:cd21149     1 PENRVVVNKESAPFVRKGGSVFAKGVVDADENIRPGDEVLVVDEDDRLLAVGRAVLSGKEMKE 63
AAK_AKii-LysC-BS cd04261
AAK_AKii-LysC-BS: Amino Acid Kinase Superfamily (AAK), AKii; this CD includes the N-terminal ...
 117-193 2.40e-03

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: 39.05  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 117 RYLNAR------ATIETLLKLKAVPI------INENDTVaTTEIRyGDNDRLAARVATMMGADLLILLSDIDGLYTAPPH 184
Cdd:cd04261   105 HHGKARiididpDRIRELLEEGDVVIvagfqgINEDGDI-TTLGR-GGSDTSAVALAAALGADRCEIYTDVDGVYTADPR 182


                  ....*....
gi 2563495933 185 KNPDAQFLP 193
Cdd:cd04261   183 IVPKARKLD 191
AAK_UMPK-PyrH-Ec cd04254
UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) ...
 157-211 3.47e-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: 38.63  E-value: 3.47e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2563495933 157 AARVATMMGADLLILLSDIDGLYTAPPHKNPDAQFLP---FVETITPQIEAMAGAAAS 211
Cdd:cd04254   140 AALRAIEINADVILKATKVDGVYDADPKKNPNAKRYDhltYDEVLSKGLKVMDATAFT 197
AAK_AK-DapG-like cd04246
AAK_AK-DapG-like: Amino Acid Kinase Superfamily (AAK), AK-DapG-like; this CD includes the ...
 117-195 6.38e-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: 37.86  E-value: 6.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 117 RYLNAR------ATIETLLKLKAVPI------INENDTVATteIRYGDNDRLAARVATMMGADLLILLSDIDGLYTAPPH 184
Cdd:cd04246   105 HHGNARiididpKRILEALEEGDVVVvagfqgVNEDGEITT--LGRGGSDTTAVALAAALKADRCEIYTDVDGVYTADPR 182

                          90
                  ....*....|.
gi 2563495933 185 KNPDAQFLPFV 195
Cdd:cd04246   183 IVPKARKLDVI 193
AAK_AK-LysC-like cd04244
AAK_AK-LysC-like: Amino Acid Kinase Superfamily (AAK), AK-LysC-like; this CD includes the ...
 118-205 6.43e-03

AAK_AK-LysC-like: Amino Acid Kinase Superfamily (AAK), AK-LysC-like; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the lysine-sensitive AK isoenzyme found in higher plants. The lysine-sensitive AK isoenzyme is a monofunctional protein. It is involved in the overall regulation of the aspartate pathway and can be synergistically inhibited by S-adenosylmethionine. Also included in this CD is an uncharacterized LysC-like AK found in Euryarchaeota and some bacteria. AK catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP.


Pssm-ID: 239777 [Multi-domain]  Cd Length: 298  Bit Score: 38.12  E-value: 6.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2563495933 118 YLNARATIETLLKLKAVPI----INENDTVATTEIRYGDNDRLAARVATMMGADLLILLSDIDGLYTAPPHKNPDAQFLP 193
Cdd:cd04244   170 YERVRKRLLPMLEDGKIPVvtgfIGATEDGAITTLGRGGSDYSATIIGAALDADEIWIWKDVDGVMTADPRIVPEARTIP 249

                          90
                  ....*....|..
gi 2563495933 194 FVEtitpQIEAM 205
Cdd:cd04244   250 RLS----YAEAM 257
 
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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