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Conserved domains on  [gi|502754671|ref|WP_012989655|]
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glutamate 5-kinase [Xenorhabdus bovienii]

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 ...
 1-366 0e+00

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


:

Pssm-ID: 440033 [Multi-domain]  Cd Length: 371  Bit Score: 573.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671   1 MNGSQTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQQHEKGHRIIIVTSGAIAAGREHLGYPDLPATIASKQLLAAVGQ 80
Cdd:COG0263    4 LAKARRIVVKIGSSLLTDEGGGLDRARLAALADQIAALRAAGKEVVLVSSGAVAAGRGRLGLPKRPKTLPEKQAAAAVGQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  81 SRLIQLWEQLFSIYGIHVGQMLLTRADLEDRERFLNARDTLQALLDNHIIPIINENDAVATAEIKVGDNDNLSALAAILG 160
Cdd:COG0263   84 GLLMQAYEEAFARHGLTVAQVLLTRDDLEDRRRYLNARNTLETLLELGVVPIINENDTVATDEIRFGDNDRLAALVANLV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 161 SADKLLLLTDIEGLYTADPRNNPEAKLIPEVHDISDELKMMAGDSVSGLGTGGMATKLQAAGIAGRAGVDVIIAAGNRPE 240
Cdd:COG0263  164 EADLLVLLTDVDGLYDADPRKDPDAKLIPEVEEITPEIEAMAGGAGSGLGTGGMATKLEAARIATRAGIPTVIASGREPN 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 241 VVADVIEGKSVGTRFHGQACPMENRKRWI-FGAPPAGEIIVDHGAEAAILEKGSSLLPKGIKNVKGNFSRGEVIRVRSLS 319
Cdd:COG0263  244 VLLRILAGERVGTLFLPSGEPLSARKRWIaGALQPRGRLVVDAGAVRALRERGKSLLPAGVTAVEGDFERGDVVEIVDPD 323

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 502754671 320 GKELARGVCRYNSDALRLIAGHHSQQISQILGYEYGAVAVHRDDMIV 366
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 ...
 1-366 0e+00

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


Pssm-ID: 440033 [Multi-domain]  Cd Length: 371  Bit Score: 573.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671   1 MNGSQTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQQHEKGHRIIIVTSGAIAAGREHLGYPDLPATIASKQLLAAVGQ 80
Cdd:COG0263    4 LAKARRIVVKIGSSLLTDEGGGLDRARLAALADQIAALRAAGKEVVLVSSGAVAAGRGRLGLPKRPKTLPEKQAAAAVGQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  81 SRLIQLWEQLFSIYGIHVGQMLLTRADLEDRERFLNARDTLQALLDNHIIPIINENDAVATAEIKVGDNDNLSALAAILG 160
Cdd:COG0263   84 GLLMQAYEEAFARHGLTVAQVLLTRDDLEDRRRYLNARNTLETLLELGVVPIINENDTVATDEIRFGDNDRLAALVANLV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 161 SADKLLLLTDIEGLYTADPRNNPEAKLIPEVHDISDELKMMAGDSVSGLGTGGMATKLQAAGIAGRAGVDVIIAAGNRPE 240
Cdd:COG0263  164 EADLLVLLTDVDGLYDADPRKDPDAKLIPEVEEITPEIEAMAGGAGSGLGTGGMATKLEAARIATRAGIPTVIASGREPN 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 241 VVADVIEGKSVGTRFHGQACPMENRKRWI-FGAPPAGEIIVDHGAEAAILEKGSSLLPKGIKNVKGNFSRGEVIRVRSLS 319
Cdd:COG0263  244 VLLRILAGERVGTLFLPSGEPLSARKRWIaGALQPRGRLVVDAGAVRALRERGKSLLPAGVTAVEGDFERGDVVEIVDPD 323

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 502754671 320 GKELARGVCRYNSDALRLIAGHHSQQISQILGYEYGAVAVHRDDMIV 366
Cdd:COG0263  324 GREIARGLVNYSSDELRRIKGRRSDEIEAILGYKGRDEVIHRDNLVL 370
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: 554.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671    5 QTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQQHEKGHRIIIVTSGAIAAGREHLGYPDLPATIASKQLLAAVGQSRLI 84
Cdd:TIGR01027   1 QRIVVKVGSSSLTGSSGSLDRSHIAELVEQVAALHAAGHEVVIVSSGAIAAGFEALGLPERPKTLAEKQALAAVGQVRLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671   85 QLWEQLFSIYGIHVGQMLLTRADLEDRERFLNARDTLQALLDNHIIPIINENDAVATAEIKVGDNDNLSALAAILGSADK 164
Cdd:TIGR01027  81 QLYEQLFSQYGIKVAQILLTRADFSDRERYLNARNTLEALLELGVVPIINENDTVATEEIKFGDNDTLSALVAILVGADL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  165 LLLLTDIEGLYTADPRNNPEAKLIPEVHDISDELKMMAGDSVSGLGTGGMATKLQAAGIAGRAGVDVIIAAGNRPEVVAD 244
Cdd:TIGR01027 161 LVLLTDVDGLYDADPRTNPDAKLIPVVEEITDLLLGVAGDSGSSVGTGGMRTKLQAADLATRAGVPVIIASGSKPEKIAD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  245 VIEGKSVGTRFHGQACPMENRKRWI-FGAPPAGEIIVDHGAEAAILEKGSSLLPKGIKNVKGNFSRGEVIRVRSLSGKEL 323
Cdd:TIGR01027 241 ALEGAPVGTLFHAQARRLRNRKFWIaFASEPAGEITVDAGAEEALLERGKSLLPAGIVGVEGNFSRGEVVEILNPEGQDI 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 502754671  324 ARGVCRYNSDALRLIAGHHSQQISQILGYEYGAVAVHRDDMIV 366
Cdd:TIGR01027 321 GRGLVNYSSDELEKIKGHKSSEIEAVLGYEYGDEVVHRDDMVL 363
AAK_G5K_ProB cd04242
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ...
 6-256 6.42e-140

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: 397.58  E-value: 6.42e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671   6 TLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQQHEKGHRIIIVTSGAIAAGREHLGYPDLPATIASKQLLAAVGQSRLIQ 85
Cdd:cd04242    1 RIVVKVGSSLLTDEDGGLDLGRLASLVEQIAELRNQGKEVILVSSGAVAAGRQRLGLEKRPKTLPEKQALAAVGQSLLMA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  86 LWEQLFSIYGIHVGQMLLTRADLEDRERFLNARDTLQALLDNHIIPIINENDAVATAEIKVGDNDNLSALAAILGSADKL 165
Cdd:cd04242   81 LYEQLFAQYGIKVAQILLTRDDFEDRKRYLNARNTLETLLELGVIPIINENDTVATEEIRFGDNDRLSALVAGLVNADLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 166 LLLTDIEGLYTADPRNNPEAKLIPEVHDISDELKMMAGDSVSGLGTGGMATKLQAAGIAGRAGVDVIIAAGNRPEVVADV 245
Cdd:cd04242  161 ILLSDVDGLYDKNPRENPDAKLIPEVEEITDEIEAMAGGSGSSVGTGGMRTKLKAARIATEAGIPVVIANGRKPDVLLDI 240

                        250
                 ....*....|.
gi 502754671 246 IEGKSVGTRFH 256
Cdd:cd04242  241 LAGEAVGTLFL 251
PRK12314 PRK12314
gamma-glutamyl kinase; Provisional
 7-259 1.20e-107

gamma-glutamyl kinase; Provisional


Pssm-ID: 183430 [Multi-domain]  Cd Length: 266  Bit Score: 316.03  E-value: 1.20e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671   7 LVVKLGTSVLTGGSRRLNRAHIVELVRQCAQQHEKGHRIIIVTSGAIAAGREHLGYPDLPATIASKQLLAAVGQSRLIQL 86
Cdd:PRK12314  12 IVIKVGSSTLSYENGKINLERIEQLVFVISDLMNKGKEVILVSSGAIGAGLTKLKLDKRPTSLAEKQALAAVGQPELMSL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  87 WEQLFSIYGIHVGQMLLTRADLEDRERFLNARDTLQALLDNHIIPIINENDAVATAEI--KVGDNDNLSALAAILGSADK 164
Cdd:PRK12314  92 YSKFFAEYGIVVAQILLTRDDFDSPKSRANVKNTFESLLELGILPIVNENDAVATDEIdtKFGDNDRLSAIVAKLVKADL 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 165 LLLLTDIEGLYTADPRNNPEAKLIPEVHDISDELKMMAGDSVSGLGTGGMATKLQAAGIAGRAGVDVIIAAGNRPEVVAD 244
Cdd:PRK12314 172 LIILSDIDGLYDKNPRINPDAKLRSEVTEITEEILALAGGAGSKFGTGGMVTKLKAAKFLMEAGIKMVLANGFNPSDILD 251

                        250
                 ....*....|....*
gi 502754671 245 VIEGKSVGTRFHGQA 259
Cdd:PRK12314 252 FLEGESIGTLFAPKK 266
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 5-234 6.40e-42

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: 146.36  E-value: 6.40e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671    5 QTLVVKLGTSVLTGGSRrlnrahIVELVRQCAQQHEKGHRIIIVTS-GAIAAG---------REHLGYPDLPATIASKQL 74
Cdd:pfam00696   1 KRVVIKLGGSSLTDKER------LKRLADEIAALLEEGRKLVVVHGgGAFADGllallglspRFARLTDAETLEVATMDA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671   75 LAAVGQSRLIQLWEQLFSIYGIHVGQMLLTRADLEDRERFLNARDTLQALLDNHIIPIINENDAVATAEIK-VGDNDNLS 153
Cdd:pfam00696  75 LGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVTRIDTEALEELLEAGVVPVITGFIGIDPEGELgRGSSDTLA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  154 ALAAILGSADKLLLLTDIEGLYTADPRNNPEAKLIPEVhDISDELKMMAgdsvSGLGTGGMATKLQAAGIAGRAGV-DVI 232
Cdd:pfam00696 155 ALLAEALGADKLIILTDVDGVYTADPRKVPDAKLIPEI-SYDELLELLA----SGLATGGMKVKLPAALEAARRGGiPVV 229


                  ..
gi 502754671  233 IA 234
Cdd:pfam00696 230 IV 231
PUA smart00359
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
276-341 1.26e-12

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


Pssm-ID: 214635 [Multi-domain]  Cd Length: 76  Bit Score: 62.66  E-value: 1.26e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502754671   276 GEIIVDHGAEAAILeKGSSLLPKGIKNVKGNFSRGEVIRVRSLSGKELARGVCRYNSDALRLIAGH 341
Cdd:smart00359   1 GKVVVDDGAEKAIL-NGASLLAPGVVRVDGDIKEGDVVVIVDEKGEPLGIGLANMSSEEIARIKGK 65
 
Name Accession Description Interval E-value
ProB COG0263
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ...
 1-366 0e+00

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


Pssm-ID: 440033 [Multi-domain]  Cd Length: 371  Bit Score: 573.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671   1 MNGSQTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQQHEKGHRIIIVTSGAIAAGREHLGYPDLPATIASKQLLAAVGQ 80
Cdd:COG0263    4 LAKARRIVVKIGSSLLTDEGGGLDRARLAALADQIAALRAAGKEVVLVSSGAVAAGRGRLGLPKRPKTLPEKQAAAAVGQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  81 SRLIQLWEQLFSIYGIHVGQMLLTRADLEDRERFLNARDTLQALLDNHIIPIINENDAVATAEIKVGDNDNLSALAAILG 160
Cdd:COG0263   84 GLLMQAYEEAFARHGLTVAQVLLTRDDLEDRRRYLNARNTLETLLELGVVPIINENDTVATDEIRFGDNDRLAALVANLV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 161 SADKLLLLTDIEGLYTADPRNNPEAKLIPEVHDISDELKMMAGDSVSGLGTGGMATKLQAAGIAGRAGVDVIIAAGNRPE 240
Cdd:COG0263  164 EADLLVLLTDVDGLYDADPRKDPDAKLIPEVEEITPEIEAMAGGAGSGLGTGGMATKLEAARIATRAGIPTVIASGREPN 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 241 VVADVIEGKSVGTRFHGQACPMENRKRWI-FGAPPAGEIIVDHGAEAAILEKGSSLLPKGIKNVKGNFSRGEVIRVRSLS 319
Cdd:COG0263  244 VLLRILAGERVGTLFLPSGEPLSARKRWIaGALQPRGRLVVDAGAVRALRERGKSLLPAGVTAVEGDFERGDVVEIVDPD 323

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 502754671 320 GKELARGVCRYNSDALRLIAGHHSQQISQILGYEYGAVAVHRDDMIV 366
Cdd:COG0263  324 GREIARGLVNYSSDELRRIKGRRSDEIEAILGYKGRDEVIHRDNLVL 370
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: 554.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671    5 QTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQQHEKGHRIIIVTSGAIAAGREHLGYPDLPATIASKQLLAAVGQSRLI 84
Cdd:TIGR01027   1 QRIVVKVGSSSLTGSSGSLDRSHIAELVEQVAALHAAGHEVVIVSSGAIAAGFEALGLPERPKTLAEKQALAAVGQVRLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671   85 QLWEQLFSIYGIHVGQMLLTRADLEDRERFLNARDTLQALLDNHIIPIINENDAVATAEIKVGDNDNLSALAAILGSADK 164
Cdd:TIGR01027  81 QLYEQLFSQYGIKVAQILLTRADFSDRERYLNARNTLEALLELGVVPIINENDTVATEEIKFGDNDTLSALVAILVGADL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  165 LLLLTDIEGLYTADPRNNPEAKLIPEVHDISDELKMMAGDSVSGLGTGGMATKLQAAGIAGRAGVDVIIAAGNRPEVVAD 244
Cdd:TIGR01027 161 LVLLTDVDGLYDADPRTNPDAKLIPVVEEITDLLLGVAGDSGSSVGTGGMRTKLQAADLATRAGVPVIIASGSKPEKIAD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  245 VIEGKSVGTRFHGQACPMENRKRWI-FGAPPAGEIIVDHGAEAAILEKGSSLLPKGIKNVKGNFSRGEVIRVRSLSGKEL 323
Cdd:TIGR01027 241 ALEGAPVGTLFHAQARRLRNRKFWIaFASEPAGEITVDAGAEEALLERGKSLLPAGIVGVEGNFSRGEVVEILNPEGQDI 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 502754671  324 ARGVCRYNSDALRLIAGHHSQQISQILGYEYGAVAVHRDDMIV 366
Cdd:TIGR01027 321 GRGLVNYSSDELEKIKGHKSSEIEAVLGYEYGDEVVHRDDMVL 363
AAK_G5K_ProB cd04242
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ...
 6-256 6.42e-140

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: 397.58  E-value: 6.42e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671   6 TLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQQHEKGHRIIIVTSGAIAAGREHLGYPDLPATIASKQLLAAVGQSRLIQ 85
Cdd:cd04242    1 RIVVKVGSSLLTDEDGGLDLGRLASLVEQIAELRNQGKEVILVSSGAVAAGRQRLGLEKRPKTLPEKQALAAVGQSLLMA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  86 LWEQLFSIYGIHVGQMLLTRADLEDRERFLNARDTLQALLDNHIIPIINENDAVATAEIKVGDNDNLSALAAILGSADKL 165
Cdd:cd04242   81 LYEQLFAQYGIKVAQILLTRDDFEDRKRYLNARNTLETLLELGVIPIINENDTVATEEIRFGDNDRLSALVAGLVNADLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 166 LLLTDIEGLYTADPRNNPEAKLIPEVHDISDELKMMAGDSVSGLGTGGMATKLQAAGIAGRAGVDVIIAAGNRPEVVADV 245
Cdd:cd04242  161 ILLSDVDGLYDKNPRENPDAKLIPEVEEITDEIEAMAGGSGSSVGTGGMRTKLKAARIATEAGIPVVIANGRKPDVLLDI 240

                        250
                 ....*....|.
gi 502754671 246 IEGKSVGTRFH 256
Cdd:cd04242  241 LAGEAVGTLFL 251
PRK12314 PRK12314
gamma-glutamyl kinase; Provisional
 7-259 1.20e-107

gamma-glutamyl kinase; Provisional


Pssm-ID: 183430 [Multi-domain]  Cd Length: 266  Bit Score: 316.03  E-value: 1.20e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671   7 LVVKLGTSVLTGGSRRLNRAHIVELVRQCAQQHEKGHRIIIVTSGAIAAGREHLGYPDLPATIASKQLLAAVGQSRLIQL 86
Cdd:PRK12314  12 IVIKVGSSTLSYENGKINLERIEQLVFVISDLMNKGKEVILVSSGAIGAGLTKLKLDKRPTSLAEKQALAAVGQPELMSL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  87 WEQLFSIYGIHVGQMLLTRADLEDRERFLNARDTLQALLDNHIIPIINENDAVATAEI--KVGDNDNLSALAAILGSADK 164
Cdd:PRK12314  92 YSKFFAEYGIVVAQILLTRDDFDSPKSRANVKNTFESLLELGILPIVNENDAVATDEIdtKFGDNDRLSAIVAKLVKADL 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 165 LLLLTDIEGLYTADPRNNPEAKLIPEVHDISDELKMMAGDSVSGLGTGGMATKLQAAGIAGRAGVDVIIAAGNRPEVVAD 244
Cdd:PRK12314 172 LIILSDIDGLYDKNPRINPDAKLRSEVTEITEEILALAGGAGSKFGTGGMVTKLKAAKFLMEAGIKMVLANGFNPSDILD 251

                        250
                 ....*....|....*
gi 502754671 245 VIEGKSVGTRFHGQA 259
Cdd:PRK12314 252 FLEGESIGTLFAPKK 266
AAK_P5CS_ProBA cd04256
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ...
 4-256 2.54e-59

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


Pssm-ID: 239789 [Multi-domain]  Cd Length: 284  Bit Score: 193.42  E-value: 2.54e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671   4 SQTLVVKLGTSVLT-GGSRRLNRAHIVELVRQCAQQHEKGHRIIIVTSGAIAAGREHLGY-----------------PDL 65
Cdd:cd04256    8 AKRIVVKLGSAVVTrEDECGLALGRLASIVEQVSELQSQGREVILVTSGAVAFGKQRLRHeillsssmrqtlksgqlKDM 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  66 PATIASKQLLAAVGQSRLIQLWEQLFSIYGIHVGQMLLTRADLEDRERFLNARDTLQALLDNHIIPIINENDAVATAE-- 143
Cdd:cd04256   88 PQMELDGRACAAVGQSGLMALYEAMFTQYGITVAQVLVTKPDFYDEQTRRNLNGTLEELLRLNIIPIINTNDAVSPPPep 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 144 -------IKVGDNDNLSALAAILGSADKLLLLTDIEGLYTADPRnNPEAKLIPEVHDIsDELKMMAGDSvSGLGTGGMAT 216
Cdd:cd04256  168 dedlqgvISIKDNDSLAARLAVELKADLLILLSDVDGLYDGPPG-SDDAKLIHTFYPG-DQQSITFGTK-SRVGTGGMEA 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 502754671 217 KLQAAGIAGRAGVDVIIAAGNRPEVVADVIEGKSVGTRFH 256
Cdd:cd04256  245 KVKAALWALQGGTSVVITNGMAGDVITKILEGKKVGTFFT 284
PLN02418 PLN02418
delta-1-pyrroline-5-carboxylate synthase
 7-259 2.37e-53

delta-1-pyrroline-5-carboxylate synthase


Pssm-ID: 215230  Cd Length: 718  Bit Score: 187.62  E-value: 2.37e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671   7 LVVKLGTSVLTGGSRRLNRAHIVELVRQCAQQHEKGHRIIIVTSGAIAAGREHLGYPDL----------PATIASKQLLA 76
Cdd:PLN02418  18 VVIKVGTAVVTRDDGRLALGRLGALCEQIKELNSDGYEVILVSSGAVGVGRQRLRYRRLvnssfadlqkPQMELDGKACA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  77 AVGQSRLIQLWEQLFSIYGIHVGQMLLTRADLEDRERFLNARDTLQALLDNHIIPIINENDAVAT-------AEIKVGDN 149
Cdd:PLN02418  98 AVGQSELMALYDTLFSQLDVTASQLLVTDSDFRDPDFRKQLSETVESLLDLRVIPIFNENDAVSTrrapyedSSGIFWDN 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 150 DNLSALAAILGSADKLLLLTDIEGLYTADPrNNPEAKLIPEVHDISDELKMMAGDSvSGLGTGGMATKLQAAGIAGRAGV 229
Cdd:PLN02418 178 DSLAALLALELKADLLILLSDVEGLYTGPP-SDPSSKLIHTYIKEKHQDEITFGEK-SRVGRGGMTAKVKAAVNAASAGI 255

                        250       260       270
                 ....*....|....*....|....*....|
gi 502754671 230 DVIIAAGNRPEVVADVIEGKSVGTRFHGQA 259
Cdd:PLN02418 256 PVVITSGYALDNIRKVLRGERVGTLFHQDA 285
P5CS TIGR01092
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ...
 7-256 1.49e-51

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


Pssm-ID: 130164 [Multi-domain]  Cd Length: 715  Bit Score: 182.42  E-value: 1.49e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671    7 LVVKLGTSVLTGGSRRLNRAHIVELVRQCAQQHEKGHRIIIVTSGAIAAGREHLGYPDL----------PATIASKQLLA 76
Cdd:TIGR01092  10 IVVKVGTAVVTRGDGRLALGRLGSICEQLSELNSDGREVILVTSGAVAFGRQRLRHRILvnssfadlqkPQPELDGKACA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671   77 AVGQSRLIQLWEQLFSIYGIHVGQMLLTRADLEDRERFLNARDTLQALLDNHIIPIINENDAVATAEIK-------VGDN 149
Cdd:TIGR01092  90 AVGQSGLMALYETMFTQLDITAAQILVTDLDFRDEQFRRQLNETVHELLRMNVVPVVNENDAVSTRAAPysdsqgiFWDN 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  150 DNLSALAAILGSADKLLLLTDIEGLYTADPrNNPEAKLIPEVHDISDELKMMAGDSvSGLGTGGMATKLQAAGIAGRAGV 229
Cdd:TIGR01092 170 DSLAALLALELKADLLILLSDVEGLYDGPP-SDDDSKLIDTFYKEKHQGEITFGTK-SRLGRGGMTAKVKAAVWAAYGGT 247

                         250       260
                  ....*....|....*....|....*..
gi 502754671  230 DVIIAAGNRPEVVADVIEGKSVGTRFH 256
Cdd:TIGR01092 248 PVIIASGTAPKNITKVVEGKKVGTLFH 274
PUA_G5K cd21157
PUA domain of gamma-glutamyl kinase, found in archaea, bacteria, and eukarya; Gamma glutamyl ...
 264-366 9.05e-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: 154.55  E-value: 9.05e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 264 NRKRWI-FGAPPAGEIIVDHGAEAAILEKGSSLLPKGIKNVKGNFSRGEVIRVRSLSGKELARGVCRYNSDALRLIAGHH 342
Cdd:cd21157    1 ARKQWIaFALKPKGKLVVDAGAVKALLEGGKSLLPAGITAVEGDFERGDVVRIVDPDGREIARGLVNYSSEELRKIKGKK 80

                         90       100
                 ....*....|....*....|....
gi 502754671 343 SQQISQILGYEYGAVAVHRDDMIV 366
Cdd:cd21157   81 SSEIEEILGYKYGDEVIHRDNLVL 104
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 5-234 6.40e-42

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: 146.36  E-value: 6.40e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671    5 QTLVVKLGTSVLTGGSRrlnrahIVELVRQCAQQHEKGHRIIIVTS-GAIAAG---------REHLGYPDLPATIASKQL 74
Cdd:pfam00696   1 KRVVIKLGGSSLTDKER------LKRLADEIAALLEEGRKLVVVHGgGAFADGllallglspRFARLTDAETLEVATMDA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671   75 LAAVGQSRLIQLWEQLFSIYGIHVGQMLLTRADLEDRERFLNARDTLQALLDNHIIPIINENDAVATAEIK-VGDNDNLS 153
Cdd:pfam00696  75 LGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVTRIDTEALEELLEAGVVPVITGFIGIDPEGELgRGSSDTLA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  154 ALAAILGSADKLLLLTDIEGLYTADPRNNPEAKLIPEVhDISDELKMMAgdsvSGLGTGGMATKLQAAGIAGRAGV-DVI 232
Cdd:pfam00696 155 ALLAEALGADKLIILTDVDGVYTADPRKVPDAKLIPEI-SYDELLELLA----SGLATGGMKVKLPAALEAARRGGiPVV 229


                  ..
gi 502754671  233 IA 234
Cdd:pfam00696 230 IV 231
PTZ00489 PTZ00489
glutamate 5-kinase; Provisional
 7-256 2.51e-41

glutamate 5-kinase; Provisional


Pssm-ID: 240438 [Multi-domain]  Cd Length: 264  Bit Score: 145.93  E-value: 2.51e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671   7 LVVKLGTSVLTGGSRRlnRAHIVELVRQCAQQHEKGHRIIIVTSGAIAAGREHLGYPDlpATIASKQLLAAVGQSRLIQL 86
Cdd:PTZ00489  11 IVVKVGSSILVDNQEI--AAHRIEALCRFIADLQTKYEVILVTSGAVAAGYTKKEMDK--SYVPNKQALASMGQPLLMHM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  87 WEQLFSIYGIHVGQMLLTRADLEDRERFLNARDTLQALLDNHIIPIINENDAVATAEIKVGDNDNLSALAAILGSADKLL 166
Cdd:PTZ00489  87 YYTELQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALHELVFGDNDRLSALVAHHFKADLLV 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 167 LLTDIEGLYTADPRNNPEAKLIPEVHDISDELKMMAGDSVSGLGTGGMATKLQAAGIAGRAGVDVIIAAGNRPEVVADVI 246
Cdd:PTZ00489 167 ILSDIDGYYTENPRTSTDAKIRSVVHELSPDDLVAEATPNNRFATGGIVTKLQAAQFLLERGGKMYLSSGFHLEKARDFL 246

                        250
                 ....*....|..
gi 502754671 247 EGKS--VGTRFH 256
Cdd:PTZ00489 247 IGGSheIGTLFY 258
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 8-255 4.38e-30

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: 115.62  E-value: 4.38e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671   8 VVKLGTSVLTGGSRRLNRAHIVELVrqcaqqHEKGHRIIIVTSGAIAAGREHLGYPDLPA-------TIASKQLLAAVGQ 80
Cdd:cd02115    1 VIKFGGSSVSSEERLRNLARILVKL------ASEGGRVVVVHGAGPQITDELLAHGELLGyarglriTDRETDALAAMGE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  81 SRLIQLWEQLFSIYGIHVGQMLLTRADLEDRERFLNAR------DTLQALLDNHIIPIINENDAVA---TAEIKVGDNDN 151
Cdd:cd02115   75 GMSNLLIAAALEQHGIKAVPLDLTQAGFASPNQGHVGKitkvstDRLKSLLENGILPILSGFGGTDekeTGTLGRGGSDS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 152 LSALAAILGSADKLLLLTDIEGLYTADPRNNPEAKLIPEVH-DISDELkmmagdsvsgLGTGGMATKLQAAGIAGRAGVD 230
Cdd:cd02115  155 TAALLAAALKADRLVILTDVDGVYTADPRKVPDAKLLSELTyEEAAEL----------AYAGAMVLKPKAADPAARAGIP 224

                        250       260
                 ....*....|....*....|....*
gi 502754671 231 VIIAAGNRPEVVAdVIEGKSVGTRF 255
Cdd:cd02115  225 VRIANTENPGALA-LFTPDGGGTLI 248
PUA pfam01472
PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, ...
 276-350 6.42e-17

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: 74.44  E-value: 6.42e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502754671  276 GEIIVDHGAEAAILeKGSSLLPKGIKNVKGNFSRGEVIRVRSLSGKELARGVCRYNSDALRLIAGHHSQQISQIL 350
Cdd:pfam01472   1 GRVVVDDGAVKAIL-NGASLLAPGVVRVDGDFRKGDEVVVVTEKGELVAVGLANYSSEELAKIEGGKAVKVRRVL 74
AAK_UMPK-like cd04239
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ...
 8-253 2.59e-15

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: 74.50  E-value: 2.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671   8 VVKLGTSVLTGGSRRLNRAHIVELVRQCAQQHEKGHRIIIVTSG------AIAAGRehlgypDLPATIASKQ-LLAAVGQ 80
Cdd:cd04239    3 VLKLSGEALAGEGGGIDPEVLKEIAREIKEVVDLGVEVAIVVGGgniargYIAAAR------GMPRATADYIgMLATVMN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  81 SRLIQlweQLFSIYGI----HVGQMLLTRADLEDRERFLNArdtlqalLDNHIIPI---INENDAVATaeikvgdnDNLS 153
Cdd:cd04239   77 ALALQ---DALEKLGVktrvMSAIPMQGVAEPYIRRRAIRH-------LEKGRIVIfggGTGNPGFTT--------DTAA 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 154 ALAAILGSADKLLLLTDIEGLYTADPRNNPEAKLIPEV-HD--ISDELKMMagDSVsglgtggmatklqAAGIAGRAGVD 230
Cdd:cd04239  139 ALRAEEIGADVLLKATNVDGVYDADPKKNPDAKKYDRIsYDelLKKGLKVM--DAT-------------ALTLCRRNKIP 203

                        250       260
                 ....*....|....*....|...
gi 502754671 231 VIIAAGNRPEVVADVIEGKSVGT 253
Cdd:cd04239  204 IIVFNGLKPGNLLRALKGEHVGT 226
AAK_FomA-like cd04241
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ...
 6-254 2.39e-14

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: 71.91  E-value: 2.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671   6 TLVVKLGTSVLTGGSRR--LNRAHIVELVRQCAQQheKGHRIIIVtSGA-----IAAGREHLGYPDLPATIASkqlLAAV 78
Cdd:cd04241    1 MIILKLGGSVITDKDRPetIREENLERIARELAEA--IDEKLVLV-HGGgsfghPKAKEYGLPDGDGSFSAEG---VAET 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  79 GQS--RLIQLWEQLFSIYGI-----HVGQMLLTRADledreRFLNAR-DTLQALLDNHIIPIINeNDAVATAEIKVG--D 148
Cdd:cd04241   75 HEAmlELNSIVVDALLEAGVpavsvPPSSFFVTENG-----RIVSFDlEVIKELLDRGFVPVLH-GDVVLDEGGGITilS 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 149 NDNLSALAAILGSADKLLLLTDIEGLYTADPrnnPEAKLIPEVH--DISDELKMMAGDSVSGlgTGGMATKLQAAGIAGR 226
Cdd:cd04241  149 GDDIVVELAKALKPERVIFLTDVDGVYDKPP---PDAKLIPEIDvgSLEDILAALGSAGTDV--TGGMAGKIEELLELAR 223

                        250       260
                 ....*....|....*....|....*...
gi 502754671 227 AGVDVIIAAGNRPEVVADVIEGKSVGTR 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 7.29e-13

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: 67.27  E-value: 7.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 154 ALAAILG---SADKLLLLTDIEGLYTADPRNNPEAKLIPEVHdiSDELKMMAGDSVSGLGTGGMATKLqAAGIAGRAGVD 230
Cdd:cd04253  119 AVAALLAerlGADLLINATNVDGVYSKDPRKDPDAKKFDRLS--ADELIDIVGKSSWKAGSNEPFDPL-AAKIIERSGIK 195

                         90       100
                 ....*....|....*....|...
gi 502754671 231 VIIAAGNRPEVVADVIEGKSVGT 253
Cdd:cd04253  196 TIVVDGRDPENLERALKGEFVGT 218
PUA smart00359
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
276-341 1.26e-12

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


Pssm-ID: 214635 [Multi-domain]  Cd Length: 76  Bit Score: 62.66  E-value: 1.26e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502754671   276 GEIIVDHGAEAAILeKGSSLLPKGIKNVKGNFSRGEVIRVRSLSGKELARGVCRYNSDALRLIAGH 341
Cdd:smart00359   1 GKVVVDDGAEKAIL-NGASLLAPGVVRVDGDIKEGDVVVIVDEKGEPLGIGLANMSSEEIARIKGK 65
AAK_NAGK-like cd04238
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ...
 118-255 1.28e-10

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: 60.99  E-value: 1.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 118 RDTLQALLDNHIIPIInendavatAEIKVGDNDNL---------SALAAILGsADKLLLLTDIEGLYTAdprnnpEAKLI 188
Cdd:cd04238  128 PELLETLLEAGYIPVI--------APIAVDEDGETynvnadtaaGAIAAALK-AEKLILLTDVPGVLDD------PGSLI 192

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502754671 189 PEVHdiSDELKMMAGDsvsGLGTGGMATKLQAAGIAGRAGV-DVIIAAGNRPEVVADVIEG-KSVGTRF 255
Cdd:cd04238  193 SELT--PKEAEELIED---GVISGGMIPKVEAALEALEGGVrKVHIIDGRVPHSLLLELFTdEGIGTMI 256
PRK00942 PRK00942
acetylglutamate kinase; Provisional
 119-258 2.34e-10

acetylglutamate kinase; Provisional


Pssm-ID: 234869 [Multi-domain]  Cd Length: 283  Bit Score: 60.51  E-value: 2.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 119 DTLQALLDNHIIPIInendavatAEIKVGDNDNL---------SALAAILGsADKLLLLTDIEGLYTADprnnpeAKLIP 189
Cdd:PRK00942 153 ALLEALLEAGYIPVI--------SPIGVGEDGETyninadtaaGAIAAALG-AEKLILLTDVPGVLDDK------GQLIS 217

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502754671 190 EVhDISDELKMMAgdsvSGLGTGGMATKLQAAGIAGRAGVD-VIIAAGNRPEVV-ADVIEGKSVGTRFHGQ 258
Cdd:PRK00942 218 EL-TASEAEELIE----DGVITGGMIPKVEAALDAARGGVRsVHIIDGRVPHALlLELFTDEGIGTMIVPD 283
PUA cd07953
PUA RNA binding domain; The PUA (PseudoUridine synthase and Archaeosine transglycosylase) ...
 276-336 3.62e-09

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: 52.68  E-value: 3.62e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502754671 276 GEIIVDHGAEAAILeKGSSLLPKGIKNVKGNFSRGEVIRVRSLSGKELARGVCRYNSDALR 336
Cdd:cd07953    1 PVVVVDKGAEKAVL-NGADLMAPGVVSADGDFKRGDLVRIVSEGGRPLAIGVAEMSSDEMK 60
AAK_AK cd04234
AAK_AK: Amino Acid Kinase Superfamily (AAK), Aspartokinase (AK); this CD includes the ...
 7-202 1.78e-08

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: 54.40  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671   7 LVVKLGTSVLTGGSRRLNRAHIVelvrqcaQQHEKGHRIIIVTSgaiAAGrehlGYPDLPATIAskqLLAAVGQ---SRL 83
Cdd:cd04234    2 VVQKFGGTSVASAERIKRVADII-------KAYEKGNRVVVVVS---AMG----GVTDLLIELA---LLLSFGErlsARL 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  84 IQLweqLFSIYGIHVGQMLLTRADLEDRERFLNARDT-------LQALLDNHIIPII------NENDAVAT--------- 141
Cdd:cd04234   65 LAA---ALRDRGIKARSLDARQAGITTDDNHGAARIIeisyerlKELLAEIGKVPVVtgfigrNEDGEITTlgrggsdys 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502754671 142 AeikvgdndnlSALAAILGsADKLLLLTDIEGLYTADPRNNPEAKLIPEvhdIS-DELKMMA 202
Cdd:cd04234  142 A----------AALAAALG-ADEVEIWTDVDGIYTADPRIVPEARLIPE---ISyDEALELA 189
ArgB COG0548
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ...
 119-229 2.69e-08

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


Pssm-ID: 440314 [Multi-domain]  Cd Length: 283  Bit Score: 54.27  E-value: 2.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 119 DTLQALLDNHIIPII------------NEN-DAVATAeikvgdndnlsaLAAILGsADKLLLLTDIEGLYtadprnNPEA 185
Cdd:COG0548  155 ELIRALLDAGYIPVIspigysptgevyNINaDTVAGA------------IAAALK-AEKLILLTDVPGVL------DDPG 215

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 502754671 186 KLIPEVhDISDELKMMAgdsvSGLGTGGMATKLQAAGIAGRAGV 229
Cdd:COG0548  216 SLISEL-TAAEAEELIA----DGVISGGMIPKLEAALDAVRGGV 254
PRK14058 PRK14058
[LysW]-aminoadipate/[LysW]-glutamate kinase;
119-253 4.15e-08

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


Pssm-ID: 237599 [Multi-domain]  Cd Length: 268  Bit Score: 53.75  E-value: 4.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 119 DTLQALLDNHIIPII------NENDAVATaeikvgDNDNLSALAAILGSADKLLLLTDIEGLYtADPRNnpEAKLIPEVH 192
Cdd:PRK14058 140 DLLKLLLKAGYLPVVappalsEEGEPLNV------DGDRAAAAIAGALKAEALVLLSDVPGLL-RDPPD--EGSLIERIT 210

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502754671 193 diSDELKmmagdSVSGLGTGGMATKLQAAGIAGRAGVD-VIIAAGNRPEVVADVIEGKsvGT 253
Cdd:PRK14058 211 --PEEAE-----ELSKAAGGGMKKKVLMAAEAVEGGVGrVIIADANVDDPISAALAGE--GT 263
MetL1 COG0527
Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the ...
 12-191 5.91e-08

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: 53.93  E-value: 5.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  12 GTSVLTGgSRRLNRAHIVelvrqcAQQHEKGHRIIIVTS---GA----IAAGREHLGYPDlPATIAskqLLAAVGqsrli 84
Cdd:COG0527   10 GTSVADA-ERIKRVADIV------KKAKEAGNRVVVVVSamgGVtdllIALAEELLGEPS-PRELD---MLLSTG----- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  85 qlwEQ----LFSIY----GIHV----GQMLLTRADledrERFLNAR-------DTLQALLDNHIIPII------NENDAV 139
Cdd:COG0527   74 ---EQlsaaLLAMAlqelGVPAvsldGRQAGIITD----DNHGKARidlietpERIRELLEEGKVVVVagfqgvTEDGEI 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502754671 140 AT---------AeikvgdndnlSALAAILGsADKLLLLTDIEGLYTADPRNNPEAKLIPEV 191
Cdd:COG0527  147 TTlgrggsdttA----------VALAAALK-ADECEIWTDVDGVYTADPRIVPDARKLPEI 196
AAK_AKii-LysC-BS cd04261
AAK_AKii-LysC-BS: Amino Acid Kinase Superfamily (AAK), AKii; this CD includes the N-terminal ...
 112-192 2.27e-07

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: 51.38  E-value: 2.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 112 ERFLNAR------DTLQALLDNHIIPI------INENDAVATaeIKVGDNDnLSA--LAAILGsADKLLLLTDIEGLYTA 177
Cdd:cd04261  104 GHHGKARiididpDRIRELLEEGDVVIvagfqgINEDGDITT--LGRGGSD-TSAvaLAAALG-ADRCEIYTDVDGVYTA 179

                         90
                 ....*....|....*
gi 502754671 178 DPRNNPEAKLIPEVH 192
Cdd:cd04261  180 DPRIVPKARKLDEIS 194
AAK_NAGK-C cd04250
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ...
 118-229 2.63e-07

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: 51.35  E-value: 2.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 118 RDTLQALLDNHIIPIInendavatAEIKVGDNDNL---------SALAAILGsADKLLLLTDIEGLYTadpRNNPEAKLI 188
Cdd:cd04250  148 PELLETLLEAGYIPVI--------APVGVGEDGETyninadtaaGAIAAALK-AEKLILLTDVAGVLD---DPNDPGSLI 215

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 502754671 189 PEVhDISDELKMMAGDSVSglgtGGMATKLQAAGIAGRAGV 229
Cdd:cd04250  216 SEI-SLKEAEELIADGIIS----GGMIPKVEACIEALEGGV 251
AAK_AK-DapG-like cd04246
AAK_AK-DapG-like: Amino Acid Kinase Superfamily (AAK), AK-DapG-like; this CD includes the ...
 112-191 6.55e-07

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: 49.80  E-value: 6.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 112 ERFLNAR------DTLQALLDNHIIPI------INENDAVATaeIKVGDND-NLSALAAILGsADKLLLLTDIEGLYTAD 178
Cdd:cd04246  104 DHHGNARiididpKRILEALEEGDVVVvagfqgVNEDGEITT--LGRGGSDtTAVALAAALK-ADRCEIYTDVDGVYTAD 180

                         90
                 ....*....|...
gi 502754671 179 PRNNPEAKLIPEV 191
Cdd:cd04246  181 PRIVPKARKLDVI 193
argB TIGR00761
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ...
 6-233 7.33e-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: 46.51  E-value: 7.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671    6 TLVVKLGTSVLTGGSRrlnrahivELVRQCAQQHEKGHRIIIVTSGA--IAAGREHLGYP----------DLPATIASKQ 73
Cdd:TIGR00761   1 TIVIKIGGAAISDLLE--------AFASDIAFLRAVGIKPVIVHGGGpeINELLEALGIPpefknglrvtDKETLEVVEM 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671   74 LLAAVGQSRLIQLWEQL-FSIYGIHVGQMLLTRADLEDRER--------FLNArDTLQALLDNHIIPIINENDAVATAEI 144
Cdd:TIGR00761  73 VLIGQVNKELVALLNKHgINAIGLTGGDGQLFTARYLDKEDlgyvgeikKVNK-ALIEALLKAGYIPVISSLALTAEGQA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  145 KVGDNDNL-SALAAILGsADKLLLLTDIEGLYtadprNNPEAKLIPEVHdiSDELKMMAGdsvSGLGTGGMATKLQAAGI 223
Cdd:TIGR00761 152 LNVNADTAaGALAAALG-AEKLVLLTDVPGIL-----NGDGQSLISEIP--LDEIEQLIK---QGIIKGGMIPKVNAALE 220

                         250
                  ....*....|.
gi 502754671  224 AGRAGV-DVII 233
Cdd:TIGR00761 221 ALRGGVrSVHI 231
PRK06291 PRK06291
aspartate kinase; Provisional
 105-191 1.06e-05

aspartate kinase; Provisional


Pssm-ID: 235773 [Multi-domain]  Cd Length: 465  Bit Score: 47.23  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 105 RADLEDRERflnARDTLQALLDNHIIPII------NENDAVATaeIKVGDNDnLSAlaAILGS---ADKLLLLTDIEGLY 175
Cdd:PRK06291 168 RPLPKTYER---VKERLEPLLKEGVIPVVtgfigeTEEGIITT--LGRGGSD-YSA--AIIGAaldADEIWIWTDVDGVM 239

                         90
                 ....*....|....*.
gi 502754671 176 TADPRNNPEAKLIPEV 191
Cdd:PRK06291 240 TTDPRIVPEARVIPKI 255
PRK08373 PRK08373
aspartate kinase; Validated
 121-189 1.37e-05

aspartate kinase; Validated


Pssm-ID: 236250 [Multi-domain]  Cd Length: 341  Bit Score: 46.59  E-value: 1.37e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502754671 121 LQALLDNHIIPII-----NENDAVATaeIKVGDNDNLSALAAILGSADKLLLLTDIEGLYTADPRNNPEAKLIP 189
Cdd:PRK08373 160 LYELLERGRVPVVpgfigNLNGFRAT--LGRGGSDYSAVALGVLLNAKAVLIMSDVEGIYTADPKLVPSARLIP 231
AAK_UMPK-PyrH-Ec cd04254
UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) ...
 150-253 1.56e-05

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: 45.56  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 150 DNLSALAAILGSADKLLLLTDIEGLYTADPRNNPEAKLIPEV-HD--ISDELKMMagDSVsglgtggmatklqAAGIAGR 226
Cdd:cd04254  137 DTAAALRAIEINADVILKATKVDGVYDADPKKNPNAKRYDHLtYDevLSKGLKVM--DAT-------------AFTLCRD 201

                         90       100
                 ....*....|....*....|....*..
gi 502754671 227 AGVDVIIAAGNRPEVVADVIEGKSVGT 253
Cdd:cd04254  202 NNLPIVVFNINEPGNLLKAVKGEGVGT 228
PRK12454 PRK12454
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
 119-254 1.96e-05

carbamate kinase-like carbamoyl phosphate synthetase; Reviewed


Pssm-ID: 183535  Cd Length: 313  Bit Score: 45.76  E-value: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 119 DTLQALLDNHI---------IPIINENDAVATAEiKVGDNDNLSALAAILGSADKLLLLTDIEGLYTAdpRNNPEAKLIP 189
Cdd:PRK12454 176 EVIKALVENGFiviasggggIPVIEEDGELKGVE-AVIDKDLASELLAEELNADIFIILTDVEKVYLN--YGKPDQKPLD 252

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502754671 190 EVHdiSDELK--MMAGDsvsgLGTGGMATKLQAA-GIAGRAGVDVIIAAgnrPEVVADVIEGKSvGTR 254
Cdd:PRK12454 253 KVT--VEEAKkyYEEGH----FKAGSMGPKILAAiRFVENGGKRAIIAS---LEKAVEALEGKT-GTR 310
PLN02512 PLN02512
acetylglutamate kinase
 121-229 6.26e-05

acetylglutamate kinase


Pssm-ID: 178128  Cd Length: 309  Bit Score: 44.29  E-value: 6.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 121 LQALLDNHIIPIINendAVATAEIKVGDNDNLS----ALAAILGsADKLLLLTDIEGLYTadpRNNPEAKLIPEVhDISD 196
Cdd:PLN02512 179 LRPLVDDGHIPVIA---TVAADEDGQAYNINADtaagEIAAALG-AEKLILLTDVAGVLE---DKDDPGSLVKEL-DIKG 250

                         90       100       110
                 ....*....|....*....|....*....|...
gi 502754671 197 ELKMMAGDSVsglgTGGMATKLQAAGIAGRAGV 229
Cdd:PLN02512 251 VRKLIADGKI----AGGMIPKVECCVRSLAQGV 279
AAK_NAGK-NC cd04249
AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation ...
 121-255 9.02e-05

AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis using the acetylated, noncyclic route of ornithine biosynthesis. There are two variants of this pathway. In one, typified by the pathway in Escherichia coli, glutamate is acetylated by acetyl-CoA and acetylornithine is deacylated hydrolytically. In this pathway, feedback inhibition by arginine occurs at the initial acetylation of glutamate and not at the phosphorylation of NAG by NAGK. Homodimeric NAGK-NC are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239782 [Multi-domain]  Cd Length: 252  Bit Score: 43.56  E-value: 9.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 121 LQALLDNHIIPIINENDAVATAE-IKVGDNDNLSALAAILGsADkLLLLTDIEGLYTADprnnpeAKLIPEVHDisdelK 199
Cdd:cd04249  129 LNDLLKAGFLPIISSIGADDQGQlMNVNADQAATAIAQLLN-AD-LVLLSDVSGVLDAD------KQLISELNA-----K 195

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 502754671 200 MMAGDSVSGLGTGGMATKLQAAGIAGRA-GVDVIIAAGNRPEVVADVIEGKSVGTRF 255
Cdd:cd04249  196 QAAELIEQGVITDGMIVKVNAALDAAQSlRRGIDIASWQYPEQLTALLAGEPVGTKI 252
PRK06635 PRK06635
aspartate kinase; Reviewed
 112-202 9.12e-05

aspartate kinase; Reviewed


Pssm-ID: 235843 [Multi-domain]  Cd Length: 404  Bit Score: 43.95  E-value: 9.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 112 ERFLNAR------DTLQALLDNHIIPII------NENDAVAT---------AeikVgdndnlsALAAILGsADKLLLLTD 170
Cdd:PRK06635 106 SAHGKARitdidpSRIREALDEGDVVVVagfqgvDEDGEITTlgrggsdttA---V-------ALAAALK-ADECEIYTD 174

                         90       100       110
                 ....*....|....*....|....*....|...
gi 502754671 171 IEGLYTADPRNNPEAKLIPEvhdIS-DELKMMA 202
Cdd:PRK06635 175 VDGVYTTDPRIVPKARKLDK---ISyEEMLELA 204
AAK_UMPK-MosAB cd04255
AAK_UMPK-MosAB: This CD includes the alpha and beta subunits of the Mo storage protein (MosA ...
 155-253 9.55e-05

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: 43.54  E-value: 9.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 155 LAAILGSADkLLLLTDIEGLYTADPRNNPEAKLIPEVhDISDELKMMAGDSVSGLgtgGMATKLQAAgiagRAGVDVIIA 234
Cdd:cd04255  170 LAEVIGARN-LIFVKDEDGLYTADPKKNKKAEFIPEI-SAAELLKKDLDDLVLER---PVLDLLQNA----RHVKEVQIV 240

                         90
                 ....*....|....*....
gi 502754671 235 AGNRPEVVADVIEGKSVGT 253
Cdd:cd04255  241 NGLVPGNLTRALRGEHVGT 259
AAK_AK-HSDH-like cd04243
AAK_AK-HSDH-like: Amino Acid Kinase Superfamily (AAK), AK-HSDH-like; this family includes the ...
 156-192 1.44e-04

AAK_AK-HSDH-like: Amino Acid Kinase Superfamily (AAK), AK-HSDH-like; this family includes the N-terminal catalytic domain of aspartokinase (AK) of the bifunctional enzyme AK- homoserine dehydrogenase (HSDH). These aspartokinases are found in such bacteria as E. coli (AKI-HSDHI, ThrA and AKII-HSDHII, MetL) and in higher plants (Z. mays AK-HSDH). AK and HSDH are the first and third enzymes in the biosynthetic pathway of the aspartate family of amino acids. AK catalyzes the phosphorylation of Asp to P-aspartyl phosphate. HSDH catalyzes the NADPH-dependent conversion of Asp 3-semialdehyde to homoserine. ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. In E. coli, ThrA is subject to allosteric regulation by the end product L-threonine and the native enzyme is reported to be tetrameric. As with bacteria, plant AK and HSDH are feedback inhibited by pathway end products. Maize AK-HSDH is a Thr-sensitive 180-kD enzyme. Arabidopsis AK-HSDH is an alanine-activated, threonine-sensitive enzyme whose ACT domains, located C-terminal to the AK catalytic domain, were shown to be involved in allosteric activation. Also included in this CD is the catalytic domain of the aspartokinase (AK) of the lysine-sensitive aspartokinase isoenzyme AKIII, a monofunctional class enzyme (LysC) found in some bacteria such as E. coli. In E. coli, LysC is reported to be a homodimer of 50 kD subunits. Also included in this CD is the catalytic domain of aspartokinase (AK) of the bifunctional enzyme AK - DAP decarboxylase (DapDC) found in some bacteria. DapDC, which is the lysA gene product, catalyzes the decarboxylation of DAP to lysine.


Pssm-ID: 239776 [Multi-domain]  Cd Length: 293  Bit Score: 42.93  E-value: 1.44e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 502754671 156 AAILGS---ADKLLLLTDIEGLYTADPRNNPEAKLIPEVH 192
Cdd:cd04243  208 AALLAAlldAEEVEIWTDVDGVYTADPRKVPDARLLKELS 247
AAK_AK-LysC-like cd04244
AAK_AK-LysC-like: Amino Acid Kinase Superfamily (AAK), AK-LysC-like; this CD includes the ...
 117-191 2.07e-04

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: 42.74  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 117 ARDTLQALLDNHIIPI----INENDAVATAEIKVGDNDnLSA--LAAILGsADKLLLLTDIEGLYTADPRNNPEAKLIPE 190
Cdd:cd04244  173 VRKRLLPMLEDGKIPVvtgfIGATEDGAITTLGRGGSD-YSAtiIGAALD-ADEIWIWKDVDGVMTADPRIVPEARTIPR 250


                 .
gi 502754671 191 V 191
Cdd:cd04244  251 L 251
PRK07431 PRK07431
aspartate kinase; Provisional
 154-191 2.27e-04

aspartate kinase; Provisional


Pssm-ID: 236018 [Multi-domain]  Cd Length: 587  Bit Score: 42.98  E-value: 2.27e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 502754671 154 ALAAILGsADKLLLLTDIEGLYTADPRNNPEAKLIPEV 191
Cdd:PRK07431 161 ALAAALG-ADACEIYTDVPGVLTTDPRLVPEAQLMDEI 197
PyrH COG0528
Uridylate kinase [Nucleotide transport and metabolism]; Uridylate kinase is part of the ...
 153-257 3.15e-04

Uridylate kinase [Nucleotide transport and metabolism]; Uridylate kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440294 [Multi-domain]  Cd Length: 238  Bit Score: 41.54  E-value: 3.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 153 SALAAILGSADKLLLLTDIEGLYTADPRNNPEAKLIPEV-HD--ISDELKMMagDSvsglgtggmatklQAAGIAGRAGV 229
Cdd:COG0528  146 AALRAIEIGADVLLKATKVDGVYDADPKKNPDAKKYDRLtYDevLAKGLKVM--DA-------------TAFSLCRDNNL 210

                         90       100
                 ....*....|....*....|....*...
gi 502754671 230 DVIIAAGNRPEVVADVIEGKSVGTRFHG 257
Cdd:COG0528  211 PIIVFNMNKPGNLLRAVLGEKIGTLVSG 238
AAK_AK-Hom3 cd04247
AAK_AK-Hom3: Amino Acid Kinase Superfamily (AAK), AK-Hom3; this CD includes the N-terminal ...
 142-191 3.57e-04

AAK_AK-Hom3: Amino Acid Kinase Superfamily (AAK), AK-Hom3; this CD includes the N-terminal catalytic domain of the aspartokinase HOM3, a monofunctional class enzyme found in Saccharomyces cerevisiae and other related AK domains. Aspartokinase, the first enzyme in the aspartate metabolic pathway, catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP, and in fungi, is responsible for the production of threonine, isoleucine and methionine. S. cerevisiae has a single aspartokinase isoenzyme type, which is regulated by feedback, allosteric inhibition by L-threonine. Recent studies show that the allosteric transition triggered by binding of threonine to AK involves a large change in the conformation of the native hexameric enzyme that is converted to an inactive one of different shape and substantially smaller hydrodynamic size.


Pssm-ID: 239780 [Multi-domain]  Cd Length: 306  Bit Score: 42.04  E-value: 3.57e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 502754671 142 AEIKVGDNDNLSALAAILGSADKLLLLTDIEGLYTADPRNNPEAKLIPEV 191
Cdd:cd04247  208 SQIGRGYTDLCAALCAVGLNADELQIWKEVDGIFTADPRKVPTARLLPSI 257
AAK_NAGK-UC cd04251
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ...
 117-249 5.01e-04

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: 41.20  E-value: 5.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 117 ARDTLQALLDNHIIPIINendAVATAEIKVG---DNDNLSA-LAAILGsADKLLLLTDIEGLYTadprnnpEAKLIPEVh 192
Cdd:cd04251  134 NSDLIEALLDAGYLPVVS---PVAYSEEGEPlnvDGDRAAAaIAAALK-AERLILLTDVEGLYL-------DGRVIERI- 201

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 193 DISD--ELKMMAGdsvsglgtGGMATKLQAAGIAGRAGV-DVIIAAGNRPEVVADVIEGK 249
Cdd:cd04251  202 TVSDaeSLLEKAG--------GGMKRKLLAAAEAVEGGVrEVVIGDARADSPISSALNGG 253
AAK_AK-HSDH cd04257
AAK_AK-HSDH: Amino Acid Kinase Superfamily (AAK), AK-HSDH; this CD includes the N-terminal ...
 156-191 5.16e-04

AAK_AK-HSDH: Amino Acid Kinase Superfamily (AAK), AK-HSDH; this CD includes the N-terminal catalytic domain of aspartokinase (AK) of the bifunctional enzyme AK - homoserine dehydrogenase (HSDH). These aspartokinases are found in bacteria (E. coli AKI-HSDHI, ThrA and E. coli AKII-HSDHII, MetL) and higher plants (Z. mays AK-HSDH). AK and HSDH are the first and third enzymes in the biosynthetic pathway of the aspartate family of amino acids. AK catalyzes the phosphorylation of Asp to P-aspartyl phosphate. HSDH catalyzes the NADPH-dependent conversion of Asp 3-semialdehyde to homoserine. ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. In E. coli, ThrA is subject to allosteric regulation by the end product L-threonine and the native enzyme is reported to be tetrameric. As with bacteria, plant AK and HSDH are feedback inhibited by pathway end products. Maize AK-HSDH is a Thr-sensitive 180-kD enzyme. Arabidopsis AK-HSDH is an alanine-activated, threonine-sensitive enzyme whose ACT domains, located C-terminal to the AK catalytic domain, were shown to be involved in allosteric activation.


Pssm-ID: 239790 [Multi-domain]  Cd Length: 294  Bit Score: 41.41  E-value: 5.16e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 502754671 156 AAILGS---ADKLLLLTDIEGLYTADPRNNPEAKLIPEV 191
Cdd:cd04257  209 AAILAAlldADQVEIWTDVDGVYSADPRKVKDARLLPSL 247
thrA PRK09436
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional
 156-190 5.17e-04

bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional


Pssm-ID: 181856 [Multi-domain]  Cd Length: 819  Bit Score: 42.07  E-value: 5.17e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 502754671 156 AAILGS---ADKLLLLTDIEGLYTADPRNNPEAKLIPE 190
Cdd:PRK09436 211 AAILAAcldADCCEIWTDVDGVYTADPRVVPDARLLKS 248
PRK05925 PRK05925
aspartate kinase; Provisional
 133-191 1.26e-03

aspartate kinase; Provisional


Pssm-ID: 235646 [Multi-domain]  Cd Length: 440  Bit Score: 40.57  E-value: 1.26e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502754671 133 INENDAVATAEIKVGDNDNLSALAAILGSADKLLLLTDIEGLYTADPRNNPEAKLIPEV 191
Cdd:PRK05925 174 IGANSSGKTTVLGRGGSDFSASLIAELCKAREVRIYTDVNGIYTMDPKIIKDAQLIPEL 232
PRK09084 PRK09084
aspartate kinase III; Validated
 156-190 1.68e-03

aspartate kinase III; Validated


Pssm-ID: 236376 [Multi-domain]  Cd Length: 448  Bit Score: 40.19  E-value: 1.68e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 502754671 156 AAILG---SADKLLLLTDIEGLYTADPRNNPEAKLIPE 190
Cdd:PRK09084 203 AALLAealNASRVEIWTDVPGIYTTDPRIVPAAKRIDE 240
AAK_AKiii-LysC-EC cd04258
AAK_AKiii-LysC-EC: Amino Acid Kinase Superfamily (AAK), AKiii-LysC-EC: this CD includes the ...
 156-191 2.18e-03

AAK_AKiii-LysC-EC: Amino Acid Kinase Superfamily (AAK), AKiii-LysC-EC: this CD includes the N-terminal catalytic aspartokinase (AK) domain of the lysine-sensitive aspartokinase isoenzyme AKIII. AKIII is a monofunctional class enzyme (LysC) found in some bacteria such as E. coli. Aspartokinase is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. In E. coli, LysC is reported to be a homodimer of 50 kD subunits.


Pssm-ID: 239791 [Multi-domain]  Cd Length: 292  Bit Score: 39.65  E-value: 2.18e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 502754671 156 AAILG---SADKLLLLTDIEGLYTADPRNNPEAKLIPEV 191
Cdd:cd04258  207 AALLAealHAEELQIWTDVAGIYTTDPRICPAARAIKEI 245
AAK_CK cd04235
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ...
 119-256 2.64e-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: 39.42  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 119 DTLQALLDN-HI--------IPIINENDAVATAEiKVGDNDNLSALAAILGSADKLLLLTDIEGLYTAdpRNNPEAKLIP 189
Cdd:cd04235  172 EAIKTLVDNgVIviaaggggIPVVREGGGLKGVE-AVIDKDLASALLAEEINADLLVILTDVDNVYIN--FGKPNQKALE 248

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502754671 190 EVHdISDELKMMAGDSvsgLGTGGMATKLQAA-GIAGRAGVDVIIAAgnrPEVVADVIEGKSvGTRFH 256
Cdd:cd04235  249 QVT-VEELEKYIEEGQ---FAPGSMGPKVEAAiRFVESGGKKAIITS---LENAEAALEGKA-GTVIV 308
AAK_AK-DapDC cd04259
AAK_AK-DapDC: Amino Acid Kinase Superfamily (AAK), AK-DapDC; this CD includes the N-terminal ...
 147-246 4.55e-03

AAK_AK-DapDC: Amino Acid Kinase Superfamily (AAK), AK-DapDC; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the bifunctional enzyme AK - DAP decarboxylase (DapDC) found in some bacteria. Aspartokinase is the first enzyme in the aspartate metabolic pathway, catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. DapDC, which is the lysA gene product, catalyzes the decarboxylation of DAP to lysine.


Pssm-ID: 239792 [Multi-domain]  Cd Length: 295  Bit Score: 38.67  E-value: 4.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671 147 GDNDNLSALAAILGSADKLLLLTDIEGLYTADPRNNPEAKLIPEV-HDISDELKMMagdsvsglgtGGMATKLQAAGIAG 225
Cdd:cd04259  204 GGSDTSAAYFAAKLQAARCEIWTDVPGLFTANPHEVPHARLLKRLdYDEAQEIATM----------GAKVLHPRCIPPAR 273

                         90       100
                 ....*....|....*....|.
gi 502754671 226 RAGVDVIIAAGNRPEVVADVI 246
Cdd:cd04259  274 RANIPMVVRSTERPELSGTLI 294
AAK_AKi-DapG-BS cd04260
AAK_AKi-DapG-BS: Amino Acid Kinase Superfamily (AAK), AKi-DapG; this CD includes the ...
 12-191 7.88e-03

AAK_AKi-DapG-BS: Amino Acid Kinase Superfamily (AAK), AKi-DapG; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the diaminopimelate-sensitive aspartokinase isoenzyme AKI (DapG), a monofunctional class enzyme found in Bacilli (Bacillus subtilis 168), Clostridia, and Actinobacteria bacterial species. 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. AKI activity is invariant during the exponential and stationary phases of growth and is not altered by addition of amino acids to the growth medium. The role of this 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 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.


Pssm-ID: 239793 [Multi-domain]  Cd Length: 244  Bit Score: 37.37  E-value: 7.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  12 GTSVLTGGSRRlnrahivELVRQCAQQHEKGHRIIIVTSgaiAAGRE----------HLGYPDLPA-TIASKQLLAAVGQ 80
Cdd:cd04260    8 GTSVSTKERRE-------QVAKKVKQAVDEGYKPVVVVS---AMGRKgdpyatdtliNLVYAENSDiSPRELDLLMSCGE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754671  81 SRLIQLWEQLFSIYGIHVGQMLLTRADLEDRERFLNAR------DTLQALLDNHIIPII------NENDAVATaeIKVGD 148
Cdd:cd04260   78 IISAVVLTSTLRAQGLKAVALTGAQAGILTDDNYSNAKiikvnpKKILSALKEGDVVVVagfqgvTEDGEVTT--LGRGG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 502754671 149 NDNLsalAAILGSA---DKLLLLTDIEGLYTADPRNNPEAKLIPEV 191
Cdd:cd04260  156 SDTT---AAALGAAlnaEYVEIYTDVDGIMTADPRVVPNARILDVV 198
 
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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