|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00489 |
PTZ00489 |
glutamate 5-kinase; Provisional |
1-264 |
4.01e-175 |
|
glutamate 5-kinase; Provisional
Pssm-ID: 240438 [Multi-domain] Cd Length: 264 Bit Score: 482.98 E-value: 4.01e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 1 MADILKSVKRIVVKVGSSILVDNQEIAAHRIEALCAFIADLQTKYEVILVTSGAVAAGYTKKEMDKSYVPNKQALASMGQ 80
Cdd:PTZ00489 1 MADILKSVKRIVVKVGSSILVDNQEIAAHRIEALCRFIADLQTKYEVILVTSGAVAAGYTKKEMDKSYVPNKQALASMGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 81 PLLMHMYYTEFQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALHELVFGDNDRLSALVAHHF 160
Cdd:PTZ00489 81 PLLMHMYYTELQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALHELVFGDNDRLSALVAHHF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 161 KADLLVILSDIDGYYTENPRTSTDAKRRPVVHELSPADLVAEATPNNRFATGGIVTKLQAAQFLLDRGGKMYLSSGFHLD 240
Cdd:PTZ00489 161 KADLLVILSDIDGYYTENPRTSTDAKIRSVVHELSPDDLVAEATPNNRFATGGIVTKLQAAQFLLERGGKMYLSSGFHLE 240
|
250 260
....*....|....*....|....
gi 401424176 241 KAREFLLGGTYEIGTLFYPRASSS 264
Cdd:PTZ00489 241 KARDFLIGGSHEIGTLFYPRVSSA 264
|
|
| AAK_G5K_ProB |
cd04242 |
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ... |
10-257 |
3.50e-119 |
|
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: 340.57 E-value: 3.50e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 10 RIVVKVGSSILVD-NQEIAAHRIEALCAFIADLQTK-YEVILVTSGAVAAGYTK---KEMDKSyVPNKQALASMGQPLLM 84
Cdd:cd04242 1 RIVVKVGSSLLTDeDGGLDLGRLASLVEQIAELRNQgKEVILVSSGAVAAGRQRlglEKRPKT-LPEKQALAAVGQSLLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 85 HMYYTEFQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALHELVFGDNDRLSALVAHHFKADL 164
Cdd:cd04242 80 ALYEQLFAQYGIKVAQILLTRDDFEDRKRYLNARNTLETLLELGVIPIINENDTVATEEIRFGDNDRLSALVAGLVNADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 165 LVILSDIDGYYTENPRTSTDAKRRPVVHELSPADLVAEATPNNRFATGGIVTKLQAAQFLLDRGGKMYLSSGFHLDKARE 244
Cdd:cd04242 160 LILLSDVDGLYDKNPRENPDAKLIPEVEEITDEIEAMAGGSGSSVGTGGMRTKLKAARIATEAGIPVVIANGRKPDVLLD 239
|
250
....*....|...
gi 401424176 245 FLLGGtyEIGTLF 257
Cdd:cd04242 240 ILAGE--AVGTLF 250
|
|
| ProB |
COG0263 |
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ... |
3-262 |
1.75e-97 |
|
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: 290.01 E-value: 1.75e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 3 DILKSVKRIVVKVGSSILVD-NQEIAAHRIEALCAFIADL-QTKYEVILVTSGAVAAGYTK---KEMDKSyVPNKQALAS 77
Cdd:COG0263 2 EALAKARRIVVKIGSSLLTDeGGGLDRARLAALADQIAALrAAGKEVVLVSSGAVAAGRGRlglPKRPKT-LPEKQAAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 78 MGQPLLMHMYYTEFQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALHELVFGDNDRLSALVA 157
Cdd:COG0263 81 VGQGLLMQAYEEAFARHGLTVAQVLLTRDDLEDRRRYLNARNTLETLLELGVVPIINENDTVATDEIRFGDNDRLAALVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 158 HHFKADLLVILSDIDGYYTENPRTSTDAKRRPVVHELSPADLVAEATPNNRFATGGIVTKLQAAQFLLDRGGKMYLSSGF 237
Cdd:COG0263 161 NLVEADLLVLLTDVDGLYDADPRKDPDAKLIPEVEEITPEIEAMAGGAGSGLGTGGMATKLEAARIATRAGIPTVIASGR 240
|
250 260
....*....|....*....|....*
gi 401424176 238 HLDKAREFLLGGtyEIGTLFYPRAS 262
Cdd:COG0263 241 EPNVLLRILAGE--RVGTLFLPSGE 263
|
|
| proB |
TIGR01027 |
glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ... |
9-263 |
3.28e-78 |
|
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: 240.67 E-value: 3.28e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 9 KRIVVKVGSSILVDNQ-EIAAHRIEALCAFIADLQTK-YEVILVTSGAVAAG-----YTKKEMDksyVPNKQALASMGQP 81
Cdd:TIGR01027 1 QRIVVKVGSSSLTGSSgSLDRSHIAELVEQVAALHAAgHEVVIVSSGAIAAGfealgLPERPKT---LAEKQALAAVGQV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 82 LLMHMYYTEFQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALHELVFGDNDRLSALVAHHFK 161
Cdd:TIGR01027 78 RLMQLYEQLFSQYGIKVAQILLTRADFSDRERYLNARNTLEALLELGVVPIINENDTVATEEIKFGDNDTLSALVAILVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 162 ADLLVILSDIDGYYTENPRTSTDAKRRPVVHELSPADLVAEATPNNRFATGGIVTKLQAAQFLLDRGGKMYLSSGFHLDK 241
Cdd:TIGR01027 158 ADLLVLLTDVDGLYDADPRTNPDAKLIPVVEEITDLLLGVAGDSGSSVGTGGMRTKLQAADLATRAGVPVIIASGSKPEK 237
|
250 260
....*....|....*....|..
gi 401424176 242 AREFLLGGTyeIGTLFYPRASS 263
Cdd:TIGR01027 238 IADALEGAP--VGTLFHAQARR 257
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
9-229 |
1.54e-40 |
|
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: 139.81 E-value: 1.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 9 KRIVVKVGSSILVDnqeiaAHRIEALCAFIADLQTK-YEVILVTS-GAVAAGYTKK-----------EMDKSYVPNKQAL 75
Cdd:pfam00696 1 KRVVIKLGGSSLTD-----KERLKRLADEIAALLEEgRKLVVVHGgGAFADGLLALlglsprfarltDAETLEVATMDAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 76 ASMGQPLLMHMYYTEFQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALHELV-FGDNDRLSA 154
Cdd:pfam00696 76 GSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVTRIDTEALEELLEAGVVPVITGFIGIDPEGELgRGSSDTLAA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 401424176 155 LVAHHFKADLLVILSDIDGYYTENPRTSTDAKRrpvVHELSPADlvAEATPNNRFATGGIVTKLQAAQFLLDRGG 229
Cdd:pfam00696 156 LLAEALGADKLIILTDVDGVYTADPRKVPDAKL---IPEISYDE--LLELLASGLATGGMKVKLPAALEAARRGG 225
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00489 |
PTZ00489 |
glutamate 5-kinase; Provisional |
1-264 |
4.01e-175 |
|
glutamate 5-kinase; Provisional
Pssm-ID: 240438 [Multi-domain] Cd Length: 264 Bit Score: 482.98 E-value: 4.01e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 1 MADILKSVKRIVVKVGSSILVDNQEIAAHRIEALCAFIADLQTKYEVILVTSGAVAAGYTKKEMDKSYVPNKQALASMGQ 80
Cdd:PTZ00489 1 MADILKSVKRIVVKVGSSILVDNQEIAAHRIEALCRFIADLQTKYEVILVTSGAVAAGYTKKEMDKSYVPNKQALASMGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 81 PLLMHMYYTEFQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALHELVFGDNDRLSALVAHHF 160
Cdd:PTZ00489 81 PLLMHMYYTELQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALHELVFGDNDRLSALVAHHF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 161 KADLLVILSDIDGYYTENPRTSTDAKRRPVVHELSPADLVAEATPNNRFATGGIVTKLQAAQFLLDRGGKMYLSSGFHLD 240
Cdd:PTZ00489 161 KADLLVILSDIDGYYTENPRTSTDAKIRSVVHELSPDDLVAEATPNNRFATGGIVTKLQAAQFLLERGGKMYLSSGFHLE 240
|
250 260
....*....|....*....|....
gi 401424176 241 KAREFLLGGTYEIGTLFYPRASSS 264
Cdd:PTZ00489 241 KARDFLIGGSHEIGTLFYPRVSSA 264
|
|
| PRK12314 |
PRK12314 |
gamma-glutamyl kinase; Provisional |
5-261 |
3.45e-128 |
|
gamma-glutamyl kinase; Provisional
Pssm-ID: 183430 [Multi-domain] Cd Length: 266 Bit Score: 364.18 E-value: 3.45e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 5 LKSVKRIVVKVGSSILV-DNQEIAAHRIEALCAFIADLQTK-YEVILVTSGAVAAGYTKKEMDKSY--VPNKQALASMGQ 80
Cdd:PRK12314 6 LENAKRIVIKVGSSTLSyENGKINLERIEQLVFVISDLMNKgKEVILVSSGAIGAGLTKLKLDKRPtsLAEKQALAAVGQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 81 PLLMHMYYTEFQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALHELV--FGDNDRLSALVAH 158
Cdd:PRK12314 86 PELMSLYSKFFAEYGIVVAQILLTRDDFDSPKSRANVKNTFESLLELGILPIVNENDAVATDEIDtkFGDNDRLSAIVAK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 159 HFKADLLVILSDIDGYYTENPRTSTDAKRRPVVHELSPADLVAEATPNNRFATGGIVTKLQAAQFLLDRGGKMYLSSGFH 238
Cdd:PRK12314 166 LVKADLLIILSDIDGLYDKNPRINPDAKLRSEVTEITEEILALAGGAGSKFGTGGMVTKLKAAKFLMEAGIKMVLANGFN 245
|
250 260
....*....|....*....|...
gi 401424176 239 LDKAREFLLGGtyEIGTLFYPRA 261
Cdd:PRK12314 246 PSDILDFLEGE--SIGTLFAPKK 266
|
|
| AAK_G5K_ProB |
cd04242 |
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ... |
10-257 |
3.50e-119 |
|
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: 340.57 E-value: 3.50e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 10 RIVVKVGSSILVD-NQEIAAHRIEALCAFIADLQTK-YEVILVTSGAVAAGYTK---KEMDKSyVPNKQALASMGQPLLM 84
Cdd:cd04242 1 RIVVKVGSSLLTDeDGGLDLGRLASLVEQIAELRNQgKEVILVSSGAVAAGRQRlglEKRPKT-LPEKQALAAVGQSLLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 85 HMYYTEFQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALHELVFGDNDRLSALVAHHFKADL 164
Cdd:cd04242 80 ALYEQLFAQYGIKVAQILLTRDDFEDRKRYLNARNTLETLLELGVIPIINENDTVATEEIRFGDNDRLSALVAGLVNADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 165 LVILSDIDGYYTENPRTSTDAKRRPVVHELSPADLVAEATPNNRFATGGIVTKLQAAQFLLDRGGKMYLSSGFHLDKARE 244
Cdd:cd04242 160 LILLSDVDGLYDKNPRENPDAKLIPEVEEITDEIEAMAGGSGSSVGTGGMRTKLKAARIATEAGIPVVIANGRKPDVLLD 239
|
250
....*....|...
gi 401424176 245 FLLGGtyEIGTLF 257
Cdd:cd04242 240 ILAGE--AVGTLF 250
|
|
| ProB |
COG0263 |
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ... |
3-262 |
1.75e-97 |
|
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: 290.01 E-value: 1.75e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 3 DILKSVKRIVVKVGSSILVD-NQEIAAHRIEALCAFIADL-QTKYEVILVTSGAVAAGYTK---KEMDKSyVPNKQALAS 77
Cdd:COG0263 2 EALAKARRIVVKIGSSLLTDeGGGLDRARLAALADQIAALrAAGKEVVLVSSGAVAAGRGRlglPKRPKT-LPEKQAAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 78 MGQPLLMHMYYTEFQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALHELVFGDNDRLSALVA 157
Cdd:COG0263 81 VGQGLLMQAYEEAFARHGLTVAQVLLTRDDLEDRRRYLNARNTLETLLELGVVPIINENDTVATDEIRFGDNDRLAALVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 158 HHFKADLLVILSDIDGYYTENPRTSTDAKRRPVVHELSPADLVAEATPNNRFATGGIVTKLQAAQFLLDRGGKMYLSSGF 237
Cdd:COG0263 161 NLVEADLLVLLTDVDGLYDADPRKDPDAKLIPEVEEITPEIEAMAGGAGSGLGTGGMATKLEAARIATRAGIPTVIASGR 240
|
250 260
....*....|....*....|....*
gi 401424176 238 HLDKAREFLLGGtyEIGTLFYPRAS 262
Cdd:COG0263 241 EPNVLLRILAGE--RVGTLFLPSGE 263
|
|
| proB |
TIGR01027 |
glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ... |
9-263 |
3.28e-78 |
|
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: 240.67 E-value: 3.28e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 9 KRIVVKVGSSILVDNQ-EIAAHRIEALCAFIADLQTK-YEVILVTSGAVAAG-----YTKKEMDksyVPNKQALASMGQP 81
Cdd:TIGR01027 1 QRIVVKVGSSSLTGSSgSLDRSHIAELVEQVAALHAAgHEVVIVSSGAIAAGfealgLPERPKT---LAEKQALAAVGQV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 82 LLMHMYYTEFQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALHELVFGDNDRLSALVAHHFK 161
Cdd:TIGR01027 78 RLMQLYEQLFSQYGIKVAQILLTRADFSDRERYLNARNTLEALLELGVVPIINENDTVATEEIKFGDNDTLSALVAILVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 162 ADLLVILSDIDGYYTENPRTSTDAKRRPVVHELSPADLVAEATPNNRFATGGIVTKLQAAQFLLDRGGKMYLSSGFHLDK 241
Cdd:TIGR01027 158 ADLLVLLTDVDGLYDADPRTNPDAKLIPVVEEITDLLLGVAGDSGSSVGTGGMRTKLQAADLATRAGVPVIIASGSKPEK 237
|
250 260
....*....|....*....|..
gi 401424176 242 AREFLLGGTyeIGTLFYPRASS 263
Cdd:TIGR01027 238 IADALEGAP--VGTLFHAQARR 257
|
|
| AAK_P5CS_ProBA |
cd04256 |
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ... |
5-257 |
5.09e-52 |
|
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: 171.08 E-value: 5.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 5 LKSVKRIVVKVGSSILV--DNQEIAAHRIEALCAFIADLQTK-YEVILVTSGAVAAGYTK----KEMDKSY--------- 68
Cdd:cd04256 5 LKHAKRIVVKLGSAVVTreDECGLALGRLASIVEQVSELQSQgREVILVTSGAVAFGKQRlrheILLSSSMrqtlksgql 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 69 ------VPNKQALASMGQPLLMHMYYTEFQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALH 142
Cdd:cd04256 85 kdmpqmELDGRACAAVGQSGLMALYEAMFTQYGITVAQVLVTKPDFYDEQTRRNLNGTLEELLRLNIIPIINTNDAVSPP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 143 -------ELVFG--DNDRLSALVAHHFKADLLVILSDIDGYYTENPRtSTDAKrrpVVHELSPADL-VAEATPNNRFATG 212
Cdd:cd04256 165 pepdedlQGVISikDNDSLAARLAVELKADLLILLSDVDGLYDGPPG-SDDAK---LIHTFYPGDQqSITFGTKSRVGTG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 401424176 213 GIVTKLQAAQFLLDRGGKMYLSSGFHLDKAREFLLGgtYEIGTLF 257
Cdd:cd04256 241 GMEAKVKAALWALQGGTSVVITNGMAGDVITKILEG--KKVGTFF 283
|
|
| PLN02418 |
PLN02418 |
delta-1-pyrroline-5-carboxylate synthase |
5-261 |
1.30e-43 |
|
delta-1-pyrroline-5-carboxylate synthase
Pssm-ID: 215230 Cd Length: 718 Bit Score: 156.81 E-value: 1.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 5 LKSVKRIVVKVGSSILV-DNQEIAAHRIEALCAFIADL-QTKYEVILVTSGAVAAGYTK----KEMDKSYVP-------- 70
Cdd:PLN02418 12 LRDVKRVVIKVGTAVVTrDDGRLALGRLGALCEQIKELnSDGYEVILVSSGAVGVGRQRlryrRLVNSSFADlqkpqmel 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 71 NKQALASMGQPLLMHMYYTEFQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALH-------E 143
Cdd:PLN02418 92 DGKACAAVGQSELMALYDTLFSQLDVTASQLLVTDSDFRDPDFRKQLSETVESLLDLRVIPIFNENDAVSTRrapyedsS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 144 LVFGDNDRLSALVAHHFKADLLVILSDIDGYYTeNPRTSTDAKRRPVVHELSPADLVAEATpNNRFATGGIVTKLQAAQF 223
Cdd:PLN02418 172 GIFWDNDSLAALLALELKADLLILLSDVEGLYT-GPPSDPSSKLIHTYIKEKHQDEITFGE-KSRVGRGGMTAKVKAAVN 249
|
250 260 270
....*....|....*....|....*....|....*...
gi 401424176 224 LLDRGGKMYLSSGFHLDKAREFLLGGtyEIGTLFYPRA 261
Cdd:PLN02418 250 AASAGIPVVITSGYALDNIRKVLRGE--RVGTLFHQDA 285
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
9-229 |
1.54e-40 |
|
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: 139.81 E-value: 1.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 9 KRIVVKVGSSILVDnqeiaAHRIEALCAFIADLQTK-YEVILVTS-GAVAAGYTKK-----------EMDKSYVPNKQAL 75
Cdd:pfam00696 1 KRVVIKLGGSSLTD-----KERLKRLADEIAALLEEgRKLVVVHGgGAFADGLLALlglsprfarltDAETLEVATMDAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 76 ASMGQPLLMHMYYTEFQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALHELV-FGDNDRLSA 154
Cdd:pfam00696 76 GSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVTRIDTEALEELLEAGVVPVITGFIGIDPEGELgRGSSDTLAA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 401424176 155 LVAHHFKADLLVILSDIDGYYTENPRTSTDAKRrpvVHELSPADlvAEATPNNRFATGGIVTKLQAAQFLLDRGG 229
Cdd:pfam00696 156 LLAEALGADKLIILTDVDGVYTADPRKVPDAKL---IPEISYDE--LLELLASGLATGGMKVKLPAALEAARRGG 225
|
|
| P5CS |
TIGR01092 |
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ... |
5-258 |
1.22e-37 |
|
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: 140.04 E-value: 1.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 5 LKSVKRIVVKVGSSILVDNQE-IAAHRIEALCAFIADLQTK-YEVILVTSGAVAAGYTK----KEMDKSY--------VP 70
Cdd:TIGR01092 4 LKDVKRIVVKVGTAVVTRGDGrLALGRLGSICEQLSELNSDgREVILVTSGAVAFGRQRlrhrILVNSSFadlqkpqpEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 71 NKQALASMGQPLLMHMYYTEFQKHGILCAQMLLAAYDL-DSRKRTiNAHNTIEVLISHKVIPIINENDATALHEL----- 144
Cdd:TIGR01092 84 DGKACAAVGQSGLMALYETMFTQLDITAAQILVTDLDFrDEQFRR-QLNETVHELLRMNVVPVVNENDAVSTRAApysds 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 145 --VFGDNDRLSALVAHHFKADLLVILSDIDGYYTeNPRTSTDAKrrpVVHELSPADLVAEAT--PNNRFATGGIVTKLQA 220
Cdd:TIGR01092 163 qgIFWDNDSLAALLALELKADLLILLSDVEGLYD-GPPSDDDSK---LIDTFYKEKHQGEITfgTKSRLGRGGMTAKVKA 238
|
250 260 270
....*....|....*....|....*....|....*...
gi 401424176 221 AQFLLDRGGKMYLSSGFHLDKAREFLLGgtYEIGTLFY 258
Cdd:TIGR01092 239 AVWAAYGGTPVIIASGTAPKNITKVVEG--KKVGTLFH 274
|
|
| AAK |
cd02115 |
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ... |
12-257 |
6.03e-24 |
|
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: 96.74 E-value: 6.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 12 VVKVGSSILVDNQEIA--AHRIEALCAFiadlqtKYEVILVTSGAVAAGYTKKEMDKSY---------VPNKQALASMGQ 80
Cdd:cd02115 1 VIKFGGSSVSSEERLRnlARILVKLASE------GGRVVVVHGAGPQITDELLAHGELLgyarglritDRETDALAAMGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 81 PLLMHMYYTEFQKHGILCAQMLLAAYDLDSRKRTINAH------NTIEVLISHKVIPIINENDATALHE---LVFGDNDR 151
Cdd:cd02115 75 GMSNLLIAAALEQHGIKAVPLDLTQAGFASPNQGHVGKitkvstDRLKSLLENGILPILSGFGGTDEKEtgtLGRGGSDS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 152 LSALVAHHFKADLLVILSDIDGYYTENPRTSTDAKRrpvVHELSPADLvAEATpnnrfATGGIVTKLQAAQFLLDRGGKM 231
Cdd:cd02115 155 TAALLAAALKADRLVILTDVDGVYTADPRKVPDAKL---LSELTYEEA-AELA-----YAGAMVLKPKAADPAARAGIPV 225
|
250 260
....*....|....*....|....*.
gi 401424176 232 YLSSGFHLDKAREFLLGGTyeiGTLF 257
Cdd:cd02115 226 RIANTENPGALALFTPDGG---GTLI 248
|
|
| AAK_UMPK-PyrH-Pf |
cd04253 |
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ... |
10-200 |
1.29e-09 |
|
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase (uridylate kinase) enzymes that catalyze UMP phosphorylation and play a key role in pyrimidine nucleotide biosynthesis; regulation of this process is via feed-back control and via gene repression of carbamoyl phosphate synthetase (the first enzyme of the pyrimidine biosynthesis pathway). The UMP kinase of Pyrococcus furiosus (Pf) is known to function as a homohexamer, with GTP and UTP being allosteric effectors. Like other related enzymes (carbamate kinase, aspartokinase, and N-acetylglutamate kinase) the E. coli and most bacterial UMPKs have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs (this CD) appear to lack this residue and the Pyrococcus furiosus structure has an additional Mg ion bound to the ATP molecule which is proposed to function as the catalysis instead. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239786 [Multi-domain] Cd Length: 221 Bit Score: 56.87 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 10 RIVVKVGSSILVDNQEIAahRIEALCAFIADLQTKYEVILVTSG-AVAAGYTKKEmdKSYVPNKQALASMGqpllmhMYY 88
Cdd:cd04253 1 RIVISLGGSVLAPEKDAD--FIKEYANVLRKISDGHKVAVVVGGgRLAREYISVA--RKLGASEAFLDEIG------IMA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 89 TEfqkhgiLCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVipiinendatalheLVFG------DNDRLSALVAHHFKA 162
Cdd:cd04253 71 TR------LNARLLIAALGDAYPPVPTSYEEALEAMFTGKI--------------VVMGgtepgqSTDAVAALLAERLGA 130
|
170 180 190
....*....|....*....|....*....|....*...
gi 401424176 163 DLLVILSDIDGYYTENPRTSTDAKRRPvvhELSPADLV 200
Cdd:cd04253 131 DLLINATNVDGVYSKDPRKDPDAKKFD---RLSADELI 165
|
|
| AAK_FomA-like |
cd04241 |
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ... |
10-256 |
1.02e-08 |
|
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: 54.57 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 10 RIVVKVGSSILVDNQE---IAAHRIEALCAFIADLQTKyEVILVtSGA------VAAGYTKKEMDKSYVPNKQALASMGQ 80
Cdd:cd04241 1 MIILKLGGSVITDKDRpetIREENLERIARELAEAIDE-KLVLV-HGGgsfghpKAKEYGLPDGDGSFSAEGVAETHEAM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 81 PLLMHMYYTEFQKHGIL-----CAQMLLAAYDLDSRKRTinahNTIEVLISHKVIPII-------NENDATALhelvfgD 148
Cdd:cd04241 79 LELNSIVVDALLEAGVPavsvpPSSFFVTENGRIVSFDL----EVIKELLDRGFVPVLhgdvvldEGGGITIL------S 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 149 NDRLSALVAHHFKADLLVILSDIDGYYTENPRtstDAKRRPVVHELSPADLVAEATPNNRFATGGIVTKLQAAQFLLDRG 228
Cdd:cd04241 149 GDDIVVELAKALKPERVIFLTDVDGVYDKPPP---DAKLIPEIDVGSLEDILAALGSAGTDVTGGMAGKIEELLELARRG 225
|
250 260
....*....|....*....|....*...
gi 401424176 229 GKMYLSSGFHLDKAREFLLGgtYEIGTL 256
Cdd:cd04241 226 IEVYIFNGDKPENLYRALLG--NFIGTR 251
|
|
| AAK_UMPK-like |
cd04239 |
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ... |
10-201 |
1.56e-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: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 10 RIVVKVGSSILVDNQ-EIAAHRIEALCAFIADLQ-TKYEVILVT-SGAVAAGYTKKEMDKsyvpNKQALASMGqpllmhM 86
Cdd:cd04239 1 RIVLKLSGEALAGEGgGIDPEVLKEIAREIKEVVdLGVEVAIVVgGGNIARGYIAAARGM----PRATADYIG------M 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 87 YYTefqkhgILCAQML---LAAYDLDSRKRT-INAHNTIEVLISHKVIPIINENDAtalheLVFG---DN-----DRLSA 154
Cdd:cd04239 71 LAT------VMNALALqdaLEKLGVKTRVMSaIPMQGVAEPYIRRRAIRHLEKGRI-----VIFGggtGNpgfttDTAAA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 401424176 155 LVAHHFKADLLVILSDIDGYYTENPRTSTDAKRRPvvhELSPADLVA 201
Cdd:cd04239 140 LRAEEIGADVLLKATNVDGVYDADPKKNPDAKKYD---RISYDELLK 183
|
|
| PRK12454 |
PRK12454 |
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed |
130-259 |
2.70e-08 |
|
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
Pssm-ID: 183535 Cd Length: 313 Bit Score: 53.85 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 130 IPIINENDATALHELVFgDNDRLSALVAHHFKADLLVILSDIDGYYTENPRTSTDAKRRPVVHELSpaDLVAEAtpnnRF 209
Cdd:PRK12454 196 IPVIEEDGELKGVEAVI-DKDLASELLAEELNADIFIILTDVEKVYLNYGKPDQKPLDKVTVEEAK--KYYEEG----HF 268
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 401424176 210 ATGGIVTKLQAAQFLLDRGGKMYLSSgfHLDKAREFLLGGTyeiGTLFYP 259
Cdd:PRK12454 269 KAGSMGPKILAAIRFVENGGKRAIIA--SLEKAVEALEGKT---GTRIIP 313
|
|
| PRK12353 |
PRK12353 |
putative amino acid kinase; Reviewed |
118-259 |
5.20e-07 |
|
putative amino acid kinase; Reviewed
Pssm-ID: 237071 Cd Length: 314 Bit Score: 49.77 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 118 HNTIEVLISHKV---------IPIINENDAtaLH--ELVFgDNDRLSALVAHHFKADLLVILSDIDGYY----TENPR-- 180
Cdd:PRK12353 175 IEAIKTLVDAGQvviaaggggIPVIREGGG--LKgvEAVI-DKDFASAKLAELVDADLLIILTAVDKVYinfgKPNQKkl 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 181 ---TSTDAKRrpvvhelspadLVAEatpnNRFATGGIVTKLQAA-QFLLDRGGK-MYLSSgfhLDKAREFLLGGTyeiGT 255
Cdd:PRK12353 252 devTVSEAEK-----------YIEE----GQFAPGSMLPKVEAAiSFVESRPGRkAIITS---LEKAKEALEGKA---GT 310
|
....
gi 401424176 256 LFYP 259
Cdd:PRK12353 311 VIVK 314
|
|
| argB |
TIGR00761 |
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ... |
11-230 |
1.74e-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: 47.66 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 11 IVVKVGSSILVDNQEiaahriealcAFIADL-----QTKYEVILVTSGAVAAGYTKK---EMDKS---YVPNKQ------ 73
Cdd:TIGR00761 2 IVIKIGGAAISDLLE----------AFASDIaflraVGIKPVIVHGGGPEINELLEAlgiPPEFKnglRVTDKEtlevve 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 74 -ALASMGQPLLMhmyyTEFQKHGI----LCAQ--MLLAAYDLDSRKR----TINAHNT--IEVLISHKVIPIINENDATA 140
Cdd:TIGR00761 72 mVLIGQVNKELV----ALLNKHGInaigLTGGdgQLFTARYLDKEDLgyvgEIKKVNKalIEALLKAGYIPVISSLALTA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 141 LHELVFGDNDRLSALVAHHFKADLLVILSDIDGYYTENPRTstdakrrpVVHELSPADlvAEATPNNRFATGGIVTKLQA 220
Cdd:TIGR00761 148 EGQALNVNADTAAGALAAALGAEKLVLLTDVPGILNGDGQS--------LISEIPLDE--IEQLIKQGIIKGGMIPKVNA 217
|
250
....*....|
gi 401424176 221 AQFLLDRGGK 230
Cdd:TIGR00761 218 ALEALRGGVR 227
|
|
| AAK_CK |
cd04235 |
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ... |
118-250 |
2.03e-06 |
|
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: 47.89 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 118 HNTIEVLISHKV---------IPIINENDATALHELVFgDNDRLSALVAHHFKADLLVILSDIDGYY----TENPRtstd 184
Cdd:cd04235 171 IEAIKTLVDNGViviaaggggIPVVREGGGLKGVEAVI-DKDLASALLAEEINADLLVILTDVDNVYinfgKPNQK---- 245
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 401424176 185 akrrpVVHELSPADLvAEATPNNRFATGGIVTKLQAA-QFLLDRGGKMYLSSgfhLDKAREFLLG--GT 250
Cdd:cd04235 246 -----ALEQVTVEEL-EKYIEEGQFAPGSMGPKVEAAiRFVESGGKKAIITS---LENAEAALEGkaGT 305
|
|
| PRK14058 |
PRK14058 |
[LysW]-aminoadipate/[LysW]-glutamate kinase; |
148-228 |
1.08e-05 |
|
[LysW]-aminoadipate/[LysW]-glutamate kinase;
Pssm-ID: 237599 [Multi-domain] Cd Length: 268 Bit Score: 45.66 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 148 DNDRLSALVAHHFKADLLVILSDIDGYYTENPRTSTdakrrpVVHELSPADlvAEATpnNRFATGGIVTKLQAAQFLLDR 227
Cdd:PRK14058 169 DGDRAAAAIAGALKAEALVLLSDVPGLLRDPPDEGS------LIERITPEE--AEEL--SKAAGGGMKKKVLMAAEAVEG 238
|
.
gi 401424176 228 G 228
Cdd:PRK14058 239 G 239
|
|
| ArcC |
COG0549 |
Carbamate kinase [Amino acid transport and metabolism]; |
130-259 |
2.18e-05 |
|
Carbamate kinase [Amino acid transport and metabolism];
Pssm-ID: 440315 Cd Length: 313 Bit Score: 44.68 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 130 IPIINENDATaLH--ELVFgDNDRLSALVAHHFKADLLVILSDIDGYY----TENPRtstdakrrpVVHELSPADL---V 200
Cdd:COG0549 195 IPVVRDEDGG-LKgvEAVI-DKDLASALLAEELDADLLLILTDVDKVYinfgKPDQR---------ALDEVTVAEAkkyI 263
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 201 AEatpnNRFATGGIVTKLQAA-QFLLDRGGKMYLSSgfhLDKAREFLLGGTyeiGTLFYP 259
Cdd:COG0549 264 EE----GHFAAGSMGPKVEAAiRFVEATGKRAIITS---LEKAEEALAGKA---GTRIVP 313
|
|
| PRK12354 |
PRK12354 |
carbamate kinase; Reviewed |
130-262 |
6.53e-05 |
|
carbamate kinase; Reviewed
Pssm-ID: 183466 Cd Length: 307 Bit Score: 43.28 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401424176 130 IPIINENDATaLH--ELVFgDNDRLSALVAHHFKADLLVILSDIDGYYtENPRTSTdakRRPvVHELSPADLVAEatpnn 207
Cdd:PRK12354 186 IPVVYDADGK-LHgvEAVI-DKDLAAALLAEQLDADLLLILTDVDAVY-LDWGKPT---QRA-IAQATPDELREL----- 253
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 401424176 208 RFATGGIVTKLQAA-QFLLDRGGKMYLSSgfhLDKAREFLLGgtyEIGTLFYPRAS 262
Cdd:PRK12354 254 GFAAGSMGPKVEAAcEFVRATGKIAGIGS---LEDIQAILAG---EAGTRISPETA 303
|
|
| AAK_UC |
cd04240 |
AAK_UC: Uncharacterized (UC) amino acid kinase-like proteins found mainly in archaea and a few ... |
150-185 |
8.19e-03 |
|
AAK_UC: Uncharacterized (UC) amino acid kinase-like proteins found mainly in archaea and a few bacteria. Sequences in this CD are members of the Amino Acid Kinase (AAK) superfamily.
Pssm-ID: 239773 [Multi-domain] Cd Length: 203 Bit Score: 36.57 E-value: 8.19e-03
10 20 30
....*....|....*....|....*....|....*.
gi 401424176 150 DRLSALVAHHFKADLLVILSDIDGYYTENPRTSTDA 185
Cdd:cd04240 117 DSIAAWLAKKLGAKRLVIVTDVDGIYEKDGKLVNEI 152
|
|
| PRK06291 |
PRK06291 |
aspartate kinase; Provisional |
119-191 |
8.48e-03 |
|
aspartate kinase; Provisional
Pssm-ID: 235773 [Multi-domain] Cd Length: 465 Bit Score: 37.21 E-value: 8.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 401424176 119 NTIEVLISHKVIPIIN----ENDATALHELVFGDNDRLSALVAHHFKADLLVILSDIDGYYTENPRTSTDAKRRPVV 191
Cdd:PRK06291 179 ERLEPLLKEGVIPVVTgfigETEEGIITTLGRGGSDYSAAIIGAALDADEIWIWTDVDGVMTTDPRIVPEARVIPKI 255
|
|
| |
