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Conserved domains on  [gi|505309309|ref|WP_015496411|]
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glutamate 5-kinase [Octadecabacter arcticus]

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 ...
 12-366 5.03e-149

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: 425.99  E-value: 5.03e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  12 GSSLLANSDRlTLRYAFMNGLMSDLAQLQKEGYDIILTSSGSVALGLNMIG--KRPEDagIMDKQAAAACGQPLLMNAYR 89
Cdd:COG0263   15 GSSLLTDEGG-GLDRARLAALADQIAALRAAGKEVVLVSSGAVAAGRGRLGlpKRPKT--LPEKQAAAAVGQGLLMQAYE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  90 QVASEHGMDVGQMLVTVDDMEERRRFLNIKNTMSRLFESDIMPIINENDSVATHDLRVGDNDRLSAKVAQMIEADVLIIL 169
Cdd:COG0263   92 EAFARHGLTVAQVLLTRDDLEDRRRYLNARNTLETLLELGVVPIINENDTVATDEIRFGDNDRLAALVANLVEADLLVLL 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 170 TSVEGLYDRDPS-DPDAKFIAEIKDVSEHLESTTG--VSALGSGGMLTKMQAASMAQNAGVETIIADGIIERPVSSVLKN 246
Cdd:COG0263  172 TDVDGLYDADPRkDPDAKLIPEVEEITPEIEAMAGgaGSGLGTGGMATKLEAARIATRAGIPTVIASGREPNVLLRILAG 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 247 ERRYTRCLVTGKTASPLKVWLSNRLQVAGTLVVSTEVAASVIAGECGITRQDVISIQGDFSKGDVLHVYDEDGTEVARGL 326
Cdd:COG0263  252 ERVGTLFLPSGEPLSARKRWIAGALQPRGRLVVDAGAVRALRERGKSLLPAGVTAVEGDFERGDVVEIVDPDGREIARGL 331

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 505309309 327 TNFSSEETMLMARHIDMPIEDVIGYKTKSDVIAAANMLVL 366
Cdd:COG0263  332 VNYSSDELRRIKGRRSDEIEAILGYKGRDEVIHRDNLVLL 371
 
Name Accession Description Interval E-value
ProB COG0263
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ...
 12-366 5.03e-149

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: 425.99  E-value: 5.03e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  12 GSSLLANSDRlTLRYAFMNGLMSDLAQLQKEGYDIILTSSGSVALGLNMIG--KRPEDagIMDKQAAAACGQPLLMNAYR 89
Cdd:COG0263   15 GSSLLTDEGG-GLDRARLAALADQIAALRAAGKEVVLVSSGAVAAGRGRLGlpKRPKT--LPEKQAAAAVGQGLLMQAYE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  90 QVASEHGMDVGQMLVTVDDMEERRRFLNIKNTMSRLFESDIMPIINENDSVATHDLRVGDNDRLSAKVAQMIEADVLIIL 169
Cdd:COG0263   92 EAFARHGLTVAQVLLTRDDLEDRRRYLNARNTLETLLELGVVPIINENDTVATDEIRFGDNDRLAALVANLVEADLLVLL 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 170 TSVEGLYDRDPS-DPDAKFIAEIKDVSEHLESTTG--VSALGSGGMLTKMQAASMAQNAGVETIIADGIIERPVSSVLKN 246
Cdd:COG0263  172 TDVDGLYDADPRkDPDAKLIPEVEEITPEIEAMAGgaGSGLGTGGMATKLEAARIATRAGIPTVIASGREPNVLLRILAG 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 247 ERRYTRCLVTGKTASPLKVWLSNRLQVAGTLVVSTEVAASVIAGECGITRQDVISIQGDFSKGDVLHVYDEDGTEVARGL 326
Cdd:COG0263  252 ERVGTLFLPSGEPLSARKRWIAGALQPRGRLVVDAGAVRALRERGKSLLPAGVTAVEGDFERGDVVEIVDPDGREIARGL 331

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 505309309 327 TNFSSEETMLMARHIDMPIEDVIGYKTKSDVIAAANMLVL 366
Cdd:COG0263  332 VNYSSDELRRIKGRRSDEIEAILGYKGRDEVIHRDNLVLL 371
AAK_G5K_ProB cd04242
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ...
 12-252 1.01e-101

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: 301.28  E-value: 1.01e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  12 GSSLLANSDRlTLRYAFMNGLMSDLAQLQKEGYDIILTSSGSVALGLNMIGKRPEDAGIMDKQAAAACGQPLLMNAYRQV 91
Cdd:cd04242    7 GSSLLTDEDG-GLDLGRLASLVEQIAELRNQGKEVILVSSGAVAAGRQRLGLEKRPKTLPEKQALAAVGQSLLMALYEQL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  92 ASEHGMDVGQMLVTVDDMEERRRFLNIKNTMSRLFESDIMPIINENDSVATHDLRVGDNDRLSAKVAQMIEADVLIILTS 171
Cdd:cd04242   86 FAQYGIKVAQILLTRDDFEDRKRYLNARNTLETLLELGVIPIINENDTVATEEIRFGDNDRLSALVAGLVNADLLILLSD 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 172 VEGLYDRDPS-DPDAKFIAEIKDVSEHLESTTG--VSALGSGGMLTKMQAASMAQNAGVETIIADGIIERPVSSVLKNER 248
Cdd:cd04242  166 VDGLYDKNPReNPDAKLIPEVEEITDEIEAMAGgsGSSVGTGGMRTKLKAARIATEAGIPVVIANGRKPDVLLDILAGEA 245


                 ....
gi 505309309 249 RYTR 252
Cdd:cd04242  246 VGTL 249
proB TIGR01027
glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ...
 12-365 6.79e-100

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: 300.76  E-value: 6.79e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309   12 GSSLLANSDRlTLRYAFMNGLMSDLAQLQKEGYDIILTSSGSVALGLNMIG--KRPEDagIMDKQAAAACGQPLLMNAYR 89
Cdd:TIGR01027   8 GSSSLTGSSG-SLDRSHIAELVEQVAALHAAGHEVVIVSSGAIAAGFEALGlpERPKT--LAEKQALAAVGQVRLMQLYE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309   90 QVASEHGMDVGQMLVTVDDMEERRRFLNIKNTMSRLFESDIMPIINENDSVATHDLRVGDNDRLSAKVAQMIEADVLIIL 169
Cdd:TIGR01027  85 QLFSQYGIKVAQILLTRADFSDRERYLNARNTLEALLELGVVPIINENDTVATEEIKFGDNDTLSALVAILVGADLLVLL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  170 TSVEGLYDRDP-SDPDAKFIAEIKDVSEHLES--TTGVSALGSGGMLTKMQAASMAQNAGVETIIADGIIERPVSSVLKN 246
Cdd:TIGR01027 165 TDVDGLYDADPrTNPDAKLIPVVEEITDLLLGvaGDSGSSVGTGGMRTKLQAADLATRAGVPVIIASGSKPEKIADALEG 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  247 ERRYTRCLVTGKTASPLKVWLSNRLQVAGTLVVSTEVAASVIAGECGITRQDVISIQGDFSKGDVLHVYDEDGTEVARGL 326
Cdd:TIGR01027 245 APVGTLFHAQARRLRNRKFWIAFASEPAGEITVDAGAEEALLERGKSLLPAGIVGVEGNFSRGEVVEILNPEGQDIGRGL 324

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 505309309  327 TNFSSEETMLMARHIDMPIEDVIGYKTKSDVIAAANMLV 365
Cdd:TIGR01027 325 VNYSSDELEKIKGHKSSEIEAVLGYEYGDEVVHRDDMVL 363
PRK12314 PRK12314
gamma-glutamyl kinase; Provisional
 12-247 3.25e-76

gamma-glutamyl kinase; Provisional


Pssm-ID: 183430 [Multi-domain]  Cd Length: 266  Bit Score: 236.68  E-value: 3.25e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  12 GSSLLANSDRlTLRYAFMNGLMSDLAQLQKEGYDIILTSSGSVALGLNMIG--KRPEDagIMDKQAAAACGQPLLMNAYR 89
Cdd:PRK12314  17 GSSTLSYENG-KINLERIEQLVFVISDLMNKGKEVILVSSGAIGAGLTKLKldKRPTS--LAEKQALAAVGQPELMSLYS 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  90 QVASEHGMDVGQMLVTVDDMEERRRFLNIKNTMSRLFESDIMPIINENDSVATHDL--RVGDNDRLSAKVAQMIEADVLI 167
Cdd:PRK12314  94 KFFAEYGIVVAQILLTRDDFDSPKSRANVKNTFESLLELGILPIVNENDAVATDEIdtKFGDNDRLSAIVAKLVKADLLI 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 168 ILTSVEGLYDRDPS-DPDAKFIAEIKDVSEHLESTTG--VSALGSGGMLTKMQAASMAQNAGVETIIADGIIERPVSSVL 244
Cdd:PRK12314 174 ILSDIDGLYDKNPRiNPDAKLRSEVTEITEEILALAGgaGSKFGTGGMVTKLKAAKFLMEAGIKMVLANGFNPSDILDFL 253


                 ...
gi 505309309 245 KNE 247
Cdd:PRK12314 254 EGE 256
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 12-233 2.03e-32

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: 121.70  E-value: 2.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309   12 GSSLLANSDRLtlryafmNGLMSDLAQLQKEGYDIILTSS-GSVALGLNMIGKRPED---------AGIMDKQAAAACGQ 81
Cdd:pfam00696   8 GGSSLTDKERL-------KRLADEIAALLEEGRKLVVVHGgGAFADGLLALLGLSPRfarltdaetLEVATMDALGSLGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309   82 PLLMNAYRQVASEHGMDVGQMLVTVDDMEERRRFLNIKNTMSRLFESDIMPIINENDSVATHDLR-VGDNDRLSAKVAQM 160
Cdd:pfam00696  81 RLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVTRIDTEALEELLEAGVVPVITGFIGIDPEGELgRGSSDTLAALLAEA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505309309  161 IEADVLIILTSVEGLYDRDPS-DPDAKFIAEIkDVSEHLESTTGVsaLGSGGMLTKMQAA-SMAQNAGVETIIAD 233
Cdd:pfam00696 161 LGADKLIILTDVDGVYTADPRkVPDAKLIPEI-SYDELLELLASG--LATGGMKVKLPAAlEAARRGGIPVVIVN 232
PUA smart00359
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
275-358 1.60e-05

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


Pssm-ID: 214635 [Multi-domain]  Cd Length: 76  Bit Score: 42.63  E-value: 1.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309   275 GTLVVSTEVAASVIAGEcGITRQDVISIQGDFSKGDVLHVYDEDGTEVARGLTNFSSEETMLMARHidmpiedVIGYKTK 354
Cdd:smart00359   1 GKVVVDDGAEKAILNGA-SLLAPGVVRVDGDIKEGDVVVIVDEKGEPLGIGLANMSSEEIARIKGK-------GLAVKVR 72


                   ....
gi 505309309   355 SDVI 358
Cdd:smart00359  73 RAVM 76
 
Name Accession Description Interval E-value
ProB COG0263
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ...
 12-366 5.03e-149

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: 425.99  E-value: 5.03e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  12 GSSLLANSDRlTLRYAFMNGLMSDLAQLQKEGYDIILTSSGSVALGLNMIG--KRPEDagIMDKQAAAACGQPLLMNAYR 89
Cdd:COG0263   15 GSSLLTDEGG-GLDRARLAALADQIAALRAAGKEVVLVSSGAVAAGRGRLGlpKRPKT--LPEKQAAAAVGQGLLMQAYE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  90 QVASEHGMDVGQMLVTVDDMEERRRFLNIKNTMSRLFESDIMPIINENDSVATHDLRVGDNDRLSAKVAQMIEADVLIIL 169
Cdd:COG0263   92 EAFARHGLTVAQVLLTRDDLEDRRRYLNARNTLETLLELGVVPIINENDTVATDEIRFGDNDRLAALVANLVEADLLVLL 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 170 TSVEGLYDRDPS-DPDAKFIAEIKDVSEHLESTTG--VSALGSGGMLTKMQAASMAQNAGVETIIADGIIERPVSSVLKN 246
Cdd:COG0263  172 TDVDGLYDADPRkDPDAKLIPEVEEITPEIEAMAGgaGSGLGTGGMATKLEAARIATRAGIPTVIASGREPNVLLRILAG 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 247 ERRYTRCLVTGKTASPLKVWLSNRLQVAGTLVVSTEVAASVIAGECGITRQDVISIQGDFSKGDVLHVYDEDGTEVARGL 326
Cdd:COG0263  252 ERVGTLFLPSGEPLSARKRWIAGALQPRGRLVVDAGAVRALRERGKSLLPAGVTAVEGDFERGDVVEIVDPDGREIARGL 331

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 505309309 327 TNFSSEETMLMARHIDMPIEDVIGYKTKSDVIAAANMLVL 366
Cdd:COG0263  332 VNYSSDELRRIKGRRSDEIEAILGYKGRDEVIHRDNLVLL 371
AAK_G5K_ProB cd04242
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ...
 12-252 1.01e-101

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: 301.28  E-value: 1.01e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  12 GSSLLANSDRlTLRYAFMNGLMSDLAQLQKEGYDIILTSSGSVALGLNMIGKRPEDAGIMDKQAAAACGQPLLMNAYRQV 91
Cdd:cd04242    7 GSSLLTDEDG-GLDLGRLASLVEQIAELRNQGKEVILVSSGAVAAGRQRLGLEKRPKTLPEKQALAAVGQSLLMALYEQL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  92 ASEHGMDVGQMLVTVDDMEERRRFLNIKNTMSRLFESDIMPIINENDSVATHDLRVGDNDRLSAKVAQMIEADVLIILTS 171
Cdd:cd04242   86 FAQYGIKVAQILLTRDDFEDRKRYLNARNTLETLLELGVIPIINENDTVATEEIRFGDNDRLSALVAGLVNADLLILLSD 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 172 VEGLYDRDPS-DPDAKFIAEIKDVSEHLESTTG--VSALGSGGMLTKMQAASMAQNAGVETIIADGIIERPVSSVLKNER 248
Cdd:cd04242  166 VDGLYDKNPReNPDAKLIPEVEEITDEIEAMAGgsGSSVGTGGMRTKLKAARIATEAGIPVVIANGRKPDVLLDILAGEA 245


                 ....
gi 505309309 249 RYTR 252
Cdd:cd04242  246 VGTL 249
proB TIGR01027
glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ...
 12-365 6.79e-100

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: 300.76  E-value: 6.79e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309   12 GSSLLANSDRlTLRYAFMNGLMSDLAQLQKEGYDIILTSSGSVALGLNMIG--KRPEDagIMDKQAAAACGQPLLMNAYR 89
Cdd:TIGR01027   8 GSSSLTGSSG-SLDRSHIAELVEQVAALHAAGHEVVIVSSGAIAAGFEALGlpERPKT--LAEKQALAAVGQVRLMQLYE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309   90 QVASEHGMDVGQMLVTVDDMEERRRFLNIKNTMSRLFESDIMPIINENDSVATHDLRVGDNDRLSAKVAQMIEADVLIIL 169
Cdd:TIGR01027  85 QLFSQYGIKVAQILLTRADFSDRERYLNARNTLEALLELGVVPIINENDTVATEEIKFGDNDTLSALVAILVGADLLVLL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  170 TSVEGLYDRDP-SDPDAKFIAEIKDVSEHLES--TTGVSALGSGGMLTKMQAASMAQNAGVETIIADGIIERPVSSVLKN 246
Cdd:TIGR01027 165 TDVDGLYDADPrTNPDAKLIPVVEEITDLLLGvaGDSGSSVGTGGMRTKLQAADLATRAGVPVIIASGSKPEKIADALEG 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  247 ERRYTRCLVTGKTASPLKVWLSNRLQVAGTLVVSTEVAASVIAGECGITRQDVISIQGDFSKGDVLHVYDEDGTEVARGL 326
Cdd:TIGR01027 245 APVGTLFHAQARRLRNRKFWIAFASEPAGEITVDAGAEEALLERGKSLLPAGIVGVEGNFSRGEVVEILNPEGQDIGRGL 324

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 505309309  327 TNFSSEETMLMARHIDMPIEDVIGYKTKSDVIAAANMLV 365
Cdd:TIGR01027 325 VNYSSDELEKIKGHKSSEIEAVLGYEYGDEVVHRDDMVL 363
PRK12314 PRK12314
gamma-glutamyl kinase; Provisional
 12-247 3.25e-76

gamma-glutamyl kinase; Provisional


Pssm-ID: 183430 [Multi-domain]  Cd Length: 266  Bit Score: 236.68  E-value: 3.25e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  12 GSSLLANSDRlTLRYAFMNGLMSDLAQLQKEGYDIILTSSGSVALGLNMIG--KRPEDagIMDKQAAAACGQPLLMNAYR 89
Cdd:PRK12314  17 GSSTLSYENG-KINLERIEQLVFVISDLMNKGKEVILVSSGAIGAGLTKLKldKRPTS--LAEKQALAAVGQPELMSLYS 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  90 QVASEHGMDVGQMLVTVDDMEERRRFLNIKNTMSRLFESDIMPIINENDSVATHDL--RVGDNDRLSAKVAQMIEADVLI 167
Cdd:PRK12314  94 KFFAEYGIVVAQILLTRDDFDSPKSRANVKNTFESLLELGILPIVNENDAVATDEIdtKFGDNDRLSAIVAKLVKADLLI 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 168 ILTSVEGLYDRDPS-DPDAKFIAEIKDVSEHLESTTG--VSALGSGGMLTKMQAASMAQNAGVETIIADGIIERPVSSVL 244
Cdd:PRK12314 174 ILSDIDGLYDKNPRiNPDAKLRSEVTEITEEILALAGgaGSKFGTGGMVTKLKAAKFLMEAGIKMVLANGFNPSDILDFL 253


                 ...
gi 505309309 245 KNE 247
Cdd:PRK12314 254 EGE 256
AAK_P5CS_ProBA cd04256
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ...
 12-248 4.87e-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: 154.13  E-value: 4.87e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  12 GSSLLANSDRLTLRYAFMNGLMSDLAQLQKEGYDIILTSSGSVALG-----------------LNMIGKRPEDAGIMDKQ 74
Cdd:cd04256   16 GSAVVTREDECGLALGRLASIVEQVSELQSQGREVILVTSGAVAFGkqrlrheillsssmrqtLKSGQLKDMPQMELDGR 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  75 AAAACGQPLLMNAYRQVASEHGMDVGQMLVTVDDMEERRRFLNIKNTMSRLFESDIMPIINENDSVATHD---------L 145
Cdd:cd04256   96 ACAAVGQSGLMALYEAMFTQYGITVAQVLVTKPDFYDEQTRRNLNGTLEELLRLNIIPIINTNDAVSPPPepdedlqgvI 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 146 RVGDNDRLSAKVAQMIEADVLIILTSVEGLYDRDPSDPDAKFIAEIkdVSEHLESTT--GVSALGSGGMLTKMQAASMAQ 223
Cdd:cd04256  176 SIKDNDSLAARLAVELKADLLILLSDVDGLYDGPPGSDDAKLIHTF--YPGDQQSITfgTKSRVGTGGMEAKVKAALWAL 253

                        250       260
                 ....*....|....*....|....*
gi 505309309 224 NAGVETIIADGIIERPVSSVLKNER 248
Cdd:cd04256  254 QGGTSVVITNGMAGDVITKILEGKK 278
PLN02418 PLN02418
delta-1-pyrroline-5-carboxylate synthase
 12-248 2.75e-39

delta-1-pyrroline-5-carboxylate synthase


Pssm-ID: 215230  Cd Length: 718  Bit Score: 148.72  E-value: 2.75e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  12 GSSLLANSD-RLTLryAFMNGLMSDLAQLQKEGYDIILTSSGSVALGLNMIGKR------------PEDAgiMDKQAAAA 78
Cdd:PLN02418  23 GTAVVTRDDgRLAL--GRLGALCEQIKELNSDGYEVILVSSGAVGVGRQRLRYRrlvnssfadlqkPQME--LDGKACAA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  79 CGQPLLMNAYRQVASEHGMDVGQMLVTVDDMEERRRFLNIKNTMSRLFESDIMPIINENDSVAThdlRVG---------- 148
Cdd:PLN02418  99 VGQSELMALYDTLFSQLDVTASQLLVTDSDFRDPDFRKQLSETVESLLDLRVIPIFNENDAVST---RRApyedssgifw 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 149 DNDRLSAKVAQMIEADVLIILTSVEGLYDRDPSDPDAKFIAEIKDVSEHLESTTGV-SALGSGGMLTKMQAASMAQNAGV 227
Cdd:PLN02418 176 DNDSLAALLALELKADLLILLSDVEGLYTGPPSDPSSKLIHTYIKEKHQDEITFGEkSRVGRGGMTAKVKAAVNAASAGI 255

                        250       260
                 ....*....|....*....|.
gi 505309309 228 ETIIADGIIERPVSSVLKNER 248
Cdd:PLN02418 256 PVVITSGYALDNIRKVLRGER 276
PTZ00489 PTZ00489
glutamate 5-kinase; Provisional
 12-234 1.31e-35

glutamate 5-kinase; Provisional


Pssm-ID: 240438 [Multi-domain]  Cd Length: 264  Bit Score: 131.29  E-value: 1.31e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  12 GSSLLANSDRLTLRYafMNGLMSDLAQLQKEgYDIILTSSGSVALGLNMigKRPEDAGIMDKQAAAACGQPLLMNAYRQV 91
Cdd:PTZ00489  16 GSSILVDNQEIAAHR--IEALCRFIADLQTK-YEVILVTSGAVAAGYTK--KEMDKSYVPNKQALASMGQPLLMHMYYTE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  92 ASEHGMDVGQMLVTVDDMEERRRFLNIKNTMSRLFESDIMPIINENDSVATHDLRVGDNDRLSAKVAQMIEADVLIILTS 171
Cdd:PTZ00489  91 LQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALHELVFGDNDRLSALVAHHFKADLLVILSD 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505309309 172 VEGLYDRDP-SDPDAKFIAEIKDV--SEHLESTTGVSALGSGGMLTKMQAASMAQNAGVETIIADG 234
Cdd:PTZ00489 171 IDGYYTENPrTSTDAKIRSVVHELspDDLVAEATPNNRFATGGIVTKLQAAQFLLERGGKMYLSSG 236
P5CS TIGR01092
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ...
 12-248 6.02e-33

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: 130.41  E-value: 6.02e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309   12 GSSLLANSD-RLTLryAFMNGLMSDLAQLQKEGYDIILTSSGSVALG---------LNMIGKRPEDAGI-MDKQAAAACG 80
Cdd:TIGR01092  15 GTAVVTRGDgRLAL--GRLGSICEQLSELNSDGREVILVTSGAVAFGrqrlrhrilVNSSFADLQKPQPeLDGKACAAVG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309   81 QPLLMNAYRQVASEHGMDVGQMLVTVDDMEERRRFLNIKNTMSRLFESDIMPIINENDSVAT-----HDLR--VGDNDRL 153
Cdd:TIGR01092  93 QSGLMALYETMFTQLDITAAQILVTDLDFRDEQFRRQLNETVHELLRMNVVPVVNENDAVSTraapySDSQgiFWDNDSL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  154 SAKVAQMIEADVLIILTSVEGLYDRDPSDPDAKFIAEIKDVSEHLESTTGV-SALGSGGMLTKMQAASMAQNAGVETIIA 232
Cdd:TIGR01092 173 AALLALELKADLLILLSDVEGLYDGPPSDDDSKLIDTFYKEKHQGEITFGTkSRLGRGGMTAKVKAAVWAAYGGTPVIIA 252

                         250
                  ....*....|....*.
gi 505309309  233 DGIIERPVSSVLKNER 248
Cdd:TIGR01092 253 SGTAPKNITKVVEGKK 268
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 12-233 2.03e-32

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: 121.70  E-value: 2.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309   12 GSSLLANSDRLtlryafmNGLMSDLAQLQKEGYDIILTSS-GSVALGLNMIGKRPED---------AGIMDKQAAAACGQ 81
Cdd:pfam00696   8 GGSSLTDKERL-------KRLADEIAALLEEGRKLVVVHGgGAFADGLLALLGLSPRfarltdaetLEVATMDALGSLGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309   82 PLLMNAYRQVASEHGMDVGQMLVTVDDMEERRRFLNIKNTMSRLFESDIMPIINENDSVATHDLR-VGDNDRLSAKVAQM 160
Cdd:pfam00696  81 RLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVTRIDTEALEELLEAGVVPVITGFIGIDPEGELgRGSSDTLAALLAEA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505309309  161 IEADVLIILTSVEGLYDRDPS-DPDAKFIAEIkDVSEHLESTTGVsaLGSGGMLTKMQAA-SMAQNAGVETIIAD 233
Cdd:pfam00696 161 LGADKLIILTDVDGVYTADPRkVPDAKLIPEI-SYDELLELLASG--LATGGMKVKLPAAlEAARRGGIPVVIVN 232
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 25-234 7.71e-18

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: 82.10  E-value: 7.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  25 RYAFMNGLMSDLAQLQKEGYDIILTSSGSVALGlNMIGKRPEDAGIMD--------KQAAAACGQPLLMNAYRQVASEHG 96
Cdd:cd02115   11 SEERLRNLARILVKLASEGGRVVVVHGAGPQIT-DELLAHGELLGYARglritdreTDALAAMGEGMSNLLIAAALEQHG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309  97 MDVGQMLVT-VDDMEERRRFLNIKNTMS-----RLFESDIMPIINENDSVATHDLRV---GDNDRLSAKVAQMIEADVLI 167
Cdd:cd02115   90 IKAVPLDLTqAGFASPNQGHVGKITKVStdrlkSLLENGILPILSGFGGTDEKETGTlgrGGSDSTAALLAAALKADRLV 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505309309 168 ILTSVEGLYDRDPS-DPDAKFIAEIKDvSEHLESTTGvsalgsGGMLTKMQAASMAQNAGVETIIADG 234
Cdd:cd02115  170 ILTDVDGVYTADPRkVPDAKLLSELTY-EEAAELAYA------GAMVLKPKAADPAARAGIPVRIANT 230
PUA_G5K cd21157
PUA domain of gamma-glutamyl kinase, found in archaea, bacteria, and eukarya; Gamma glutamyl ...
 264-365 6.33e-17

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: 75.58  E-value: 6.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 264 KVWLSNRLQVAGTLVVSTEVAASVIAGECGITRQDVISIQGDFSKGDVLHVYDEDGTEVARGLTNFSSEETMLMARHIDM 343
Cdd:cd21157    3 KQWIAFALKPKGKLVVDAGAVKALLEGGKSLLPAGITAVEGDFERGDVVRIVDPDGREIARGLVNYSSEELRKIKGKKSS 82

                         90       100
                 ....*....|....*....|..
gi 505309309 344 PIEDVIGYKTKSDVIAAANMLV 365
Cdd:cd21157   83 EIEEILGYKYGDEVIHRDNLVL 104
PRK14058 PRK14058
[LysW]-aminoadipate/[LysW]-glutamate kinase;
149-244 2.16e-10

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


Pssm-ID: 237599 [Multi-domain]  Cd Length: 268  Bit Score: 60.68  E-value: 2.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 149 DNDRLSAKVAQMIEADVLIILTSVEGLYdRDPSDPdAKFIAEIKdvsehLESTTGVSALGSGGMLTKMQAASMAQNAGV- 227
Cdd:PRK14058 169 DGDRAAAAIAGALKAEALVLLSDVPGLL-RDPPDE-GSLIERIT-----PEEAEELSKAAGGGMKKKVLMAAEAVEGGVg 241

                         90
                 ....*....|....*..
gi 505309309 228 ETIIADGIIERPVSSVL 244
Cdd:PRK14058 242 RVIIADANVDDPISAAL 258
AAK_UMPK-PyrH-Pf cd04253
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ...
 151-247 4.12e-10

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


Pssm-ID: 239786 [Multi-domain]  Cd Length: 221  Bit Score: 59.18  E-value: 4.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 151 DRLSAKVAQMIEADVLIILTSVEGLYDRDP-SDPDAKFIAEIKdVSEHLESTTGVSALGSGGMLTKMQAASMAQNAGVET 229
Cdd:cd04253  118 DAVAALLAERLGADLLINATNVDGVYSKDPrKDPDAKKFDRLS-ADELIDIVGKSSWKAGSNEPFDPLAAKIIERSGIKT 196

                         90
                 ....*....|....*...
gi 505309309 230 IIADGIIERPVSSVLKNE 247
Cdd:cd04253  197 IVVDGRDPENLERALKGE 214
AAK_UMPK-like cd04239
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ...
 154-251 2.96e-08

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: 53.70  E-value: 2.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 154 SAKVAQMIEADVLIILTSVEGLYDRDP-SDPDAKFIAEIKdvseHLEsttgvsALGSGGMLTKMQAASMAQNAGVETIIA 232
Cdd:cd04239  138 AALRAEEIGADVLLKATNVDGVYDADPkKNPDAKKYDRIS----YDE------LLKKGLKVMDATALTLCRRNKIPIIVF 207

                         90
                 ....*....|....*....
gi 505309309 233 DGIIERPVSSVLKNERRYT 251
Cdd:cd04239  208 NGLKPGNLLRALKGEHVGT 226
PUA pfam01472
PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, ...
 299-349 7.26e-08

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: 49.02  E-value: 7.26e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 505309309  299 VISIQGDFSKGDVLHVYDEDGTEVARGLTNFSSEETMLMARHIDMPIEDVI 349
Cdd:pfam01472  24 VVRVDGDFRKGDEVVVVTEKGELVAVGLANYSSEELAKIEGGKAVKVRRVL 74
AAK_NAGK-UC cd04251
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ...
 149-244 2.15e-07

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: 51.60  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 149 DNDRLSAKVAQMIEADVLIILTSVEGLYdrdpsdPDAKFIAEIkDVSEHLESTTGVsalgSGGMLTKMQAASMAQNAGV- 227
Cdd:cd04251  165 DGDRAAAAIAAALKAERLILLTDVEGLY------LDGRVIERI-TVSDAESLLEKA----GGGMKRKLLAAAEAVEGGVr 233

                         90
                 ....*....|....*..
gi 505309309 228 ETIIADGIIERPVSSVL 244
Cdd:cd04251  234 EVVIGDARADSPISSAL 250
AAK_CK cd04235
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ...
 147-233 4.84e-07

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: 50.97  E-value: 4.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 147 VGDNDRLSAKVAQMIEADVLIILTSVEGLYdRDPSDPDAKFIAEIkDVSEhLESTTGVSALGSGGMLTKMQAA-SMAQNA 225
Cdd:cd04235  207 VIDKDLASALLAEEINADLLVILTDVDNVY-INFGKPNQKALEQV-TVEE-LEKYIEEGQFAPGSMGPKVEAAiRFVESG 283


                 ....*...
gi 505309309 226 GVETIIAD 233
Cdd:cd04235  284 GKKAIITS 291
AAK_FomA-like cd04241
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ...
 151-252 6.53e-07

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: 49.95  E-value: 6.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 151 DRLSAKVAQMIEADVLIILTSVEGLYDRDPsdPDAKFIAEIKDVS-EHLESTTGVSALG-SGGMLTKMQAASMAQNAGVE 228
Cdd:cd04241  150 DDIVVELAKALKPERVIFLTDVDGVYDKPP--PDAKLIPEIDVGSlEDILAALGSAGTDvTGGMAGKIEELLELARRGIE 227

                         90       100
                 ....*....|....*....|....
gi 505309309 229 TIIADGIIERPVSSVLKNERRYTR 252
Cdd:cd04241  228 VYIFNGDKPENLYRALLGNFIGTR 251
PRK12454 PRK12454
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
 132-233 1.01e-06

carbamate kinase-like carbamoyl phosphate synthetase; Reviewed


Pssm-ID: 183535  Cd Length: 313  Bit Score: 50.00  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 132 PIINENDSVatHDLR-VGDNDRLSAKVAQMIEADVLIILTSVEGLYdRDPSDPDAKFIAEIKdVSEhLESTTGVSALGSG 210
Cdd:PRK12454 197 PVIEEDGEL--KGVEaVIDKDLASELLAEELNADIFIILTDVEKVY-LNYGKPDQKPLDKVT-VEE-AKKYYEEGHFKAG 271

                         90       100
                 ....*....|....*....|....
gi 505309309 211 GMLTKMQAA-SMAQNAGVETIIAD 233
Cdd:PRK12454 272 SMGPKILAAiRFVENGGKRAIIAS 295
PRK12353 PRK12353
putative amino acid kinase; Reviewed
 147-219 1.07e-06

putative amino acid kinase; Reviewed


Pssm-ID: 237071  Cd Length: 314  Bit Score: 49.77  E-value: 1.07e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505309309 147 VGDNDRLSAKVAQMIEADVLIILTSVEGLYdRDPSDPDAKFIAEIkDVSE---HLEstTGVSALGSggMLTKMQAA 219
Cdd:PRK12353 211 VIDKDFASAKLAELVDADLLIILTAVDKVY-INFGKPNQKKLDEV-TVSEaekYIE--EGQFAPGS--MLPKVEAA 280
PRK12686 PRK12686
carbamate kinase; Reviewed
 147-231 1.54e-06

carbamate kinase; Reviewed


Pssm-ID: 183683  Cd Length: 312  Bit Score: 49.27  E-value: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 147 VGDNDRLSAKVAQMIEADVLIILTSVEGLYdRDPSDPDAKFIAEIkDVSEhLESTTGVSALGSGGMLTKMQAA-SMAQNA 225
Cdd:PRK12686 209 VIDKDFASEKLAEQIDADLLIILTGVENVF-INFNKPNQQKLDDI-TVAE-AKQYIAEGQFAPGSMLPKVEAAiDFVESG 285


                 ....*..
gi 505309309 226 -GVETII 231
Cdd:PRK12686 286 eGKKAII 292
ArcC COG0549
Carbamate kinase [Amino acid transport and metabolism];
149-233 1.98e-06

Carbamate kinase [Amino acid transport and metabolism];


Pssm-ID: 440315  Cd Length: 313  Bit Score: 48.92  E-value: 1.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 149 DNDRLSAKVAQMIEADVLIILTSVEGLYdRDPSDPDAKFIAEIKdVSEhLESTTGVSALGSGGMLTKMQAA-SMAQNAGV 227
Cdd:COG0549  213 DKDLASALLAEELDADLLLILTDVDKVY-INFGKPDQRALDEVT-VAE-AKKYIEEGHFAAGSMGPKVEAAiRFVEATGK 289


                 ....*.
gi 505309309 228 ETIIAD 233
Cdd:COG0549  290 RAIITS 295
AAK_NAGK-like cd04238
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ...
 125-244 2.71e-06

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


Pssm-ID: 239771 [Multi-domain]  Cd Length: 256  Bit Score: 48.27  E-value: 2.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 125 LFESDIMPIINendSVATHDLRVGDN---DRLSAKVAQMIEADVLIILTSVEGLYDrdpsDPDaKFIAEI--KDVSEHLE 199
Cdd:cd04238  134 LLEAGYIPVIA---PIAVDEDGETYNvnaDTAAGAIAAALKAEKLILLTDVPGVLD----DPG-SLISELtpKEAEELIE 205

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 505309309 200 STTgvsalGSGGMLTKMQAASMAQNAGV-ETIIADGIIERPVSSVL 244
Cdd:cd04238  206 DGV-----ISGGMIPKVEAALEALEGGVrKVHIIDGRVPHSLLLEL 246
PUA smart00359
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
275-358 1.60e-05

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


Pssm-ID: 214635 [Multi-domain]  Cd Length: 76  Bit Score: 42.63  E-value: 1.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309   275 GTLVVSTEVAASVIAGEcGITRQDVISIQGDFSKGDVLHVYDEDGTEVARGLTNFSSEETMLMARHidmpiedVIGYKTK 354
Cdd:smart00359   1 GKVVVDDGAEKAILNGA-SLLAPGVVRVDGDIKEGDVVVIVDEKGEPLGIGLANMSSEEIARIKGK-------GLAVKVR 72


                   ....
gi 505309309   355 SDVI 358
Cdd:smart00359  73 RAVM 76
PRK00942 PRK00942
acetylglutamate kinase; Provisional
 125-237 4.42e-05

acetylglutamate kinase; Provisional


Pssm-ID: 234869 [Multi-domain]  Cd Length: 283  Bit Score: 44.71  E-value: 4.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 125 LFESDIMPIINendSVAthdlrVGDN--------DRLSAKVAQMIEADVLIILTSVEGLYDrdpsDPDaKFIAEI--KDV 194
Cdd:PRK00942 158 LLEAGYIPVIS---PIG-----VGEDgetyninaDTAAGAIAAALGAEKLILLTDVPGVLD----DKG-QLISELtaSEA 224

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 505309309 195 SEHLESttGVSalgSGGMLTKMQAASMAQNAGVETI-IADGIIE 237
Cdd:PRK00942 225 EELIED--GVI---TGGMIPKVEAALDAARGGVRSVhIIDGRVP 263
ArgB COG0548
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ...
 155-234 6.21e-05

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: 44.25  E-value: 6.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 155 AKVAQMIEADVLIILTSVEGLYDrdpsdPDAKFIAEI--KDVSEHLESTTGvsalgSGGMLTKMQAASMAQNAGVETI-I 231
Cdd:COG0548  190 GAIAAALKAEKLILLTDVPGVLD-----DPGSLISELtaAEAEELIADGVI-----SGGMIPKLEAALDAVRGGVKRVhI 259


                 ...
gi 505309309 232 ADG 234
Cdd:COG0548  260 IDG 262
AAK_NAGK-C cd04250
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ...
 155-237 1.16e-04

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: 43.26  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505309309 155 AKVAQMIEADVLIILTSVEGLYDrDPSDPDaKFIAEI--KDVSEHLESttGVSalgSGGMLTKMQAASMAQNAGVETI-I 231
Cdd:cd04250  184 GAIAAALKAEKLILLTDVAGVLD-DPNDPG-SLISEIslKEAEELIAD--GII---SGGMIPKVEACIEALEGGVKAAhI 256


                 ....*.
gi 505309309 232 ADGIIE 237
Cdd:cd04250  257 IDGRVP 262
PRK12354 PRK12354
carbamate kinase; Reviewed
 147-219 8.49e-04

carbamate kinase; Reviewed


Pssm-ID: 183466  Cd Length: 307  Bit Score: 40.97  E-value: 8.49e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505309309 147 VGDNDRLSAKVAQMIEADVLIILTSVEGLYdRDPSDPDAKFIAEIkdvsehleSTTGVSALG--SGGMLTKMQAA 219
Cdd:PRK12354 202 VIDKDLAAALLAEQLDADLLLILTDVDAVY-LDWGKPTQRAIAQA--------TPDELRELGfaAGSMGPKVEAA 267
PyrH COG0528
Uridylate kinase [Nucleotide transport and metabolism]; Uridylate kinase is part of the ...
 161-191 1.14e-03

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: 40.00  E-value: 1.14e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 505309309 161 IEADVLIILTSVEGLYDRDPS-DPDAKFIAEI 191
Cdd:COG0528  153 IGADVLLKATKVDGVYDADPKkNPDAKKYDRL 184
PUA_3 pfam17785
PUA-like domain; This PUA-like domain is found at the N-terminus of SAM-dependent ...
 277-328 2.70e-03

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: 35.92  E-value: 2.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 505309309  277 LVVSTEVAASVIAGECGITRQDVISIQGDFSKGDVLHVYDEDGTEVARGLTN 328
Cdd:pfam17785   1 VTLKKKAEKRLKRGHPWIYSNEIERVEGDLEEGDLVRVVDSDGRFLGTGYYN 52
AAK_UMPK-PyrH-Ec cd04254
UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) ...
 158-191 4.57e-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: 38.24  E-value: 4.57e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 505309309 158 AQMIEADVLIILTSVEGLYDRDPS-DPDAKFIAEI 191
Cdd:cd04254  144 AIEINADVILKATKVDGVYDADPKkNPNAKRYDHL 178
 
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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