|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12354 |
PRK12354 |
carbamate kinase; Reviewed |
5-303 |
0e+00 |
|
carbamate kinase; Reviewed
Pssm-ID: 183466 Cd Length: 307 Bit Score: 566.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 5 PTLVVALGGNALLKRGEPLEAEIQRQNIEQAARTIAGLTAQWRVVLVHGNGPQVGLLALQNSAYDKVTPYPLDVLGAESQ 84
Cdd:PRK12354 1 MRIVVALGGNALLRRGEPLTAENQRANIRIAAEQIAKIAREHELVIVHGNGPQVGLLALQNAAYKDVTPYPLDVLGAETE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 85 GMIGYMLQQALKNSLPQREVSVLLTQVEVDAADPAFSNPTKYIGPVYSEAQAKTLAAEKGWVFKADGSYVRRVVPSPQPK 164
Cdd:PRK12354 81 GMIGYMLEQELGNLLPERPVATLLTQVEVDANDPAFANPTKPIGPVYDEAEAERLAAEKGWTIKPDGDYFRRVVPSPRPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 165 RIVESDAITALIQRDHLVICNGGGGVPVVEQAKG-YRGIEAVIDKDLSAALLARQIEADALLILTDADAVYLDWGKPTQR 243
Cdd:PRK12354 161 RIVEIRPIRWLLEKGHLVICAGGGGIPVVYDADGkLHGVEAVIDKDLAAALLAEQLDADLLLILTDVDAVYLDWGKPTQR 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 244 PLAQVTPELLRGMQFDAGSMGPKVAACREFVEACNGIAGIGALADGAEILAGEKGTLIRN 303
Cdd:PRK12354 241 AIAQATPDELRELGFAAGSMGPKVEAACEFVRATGKIAGIGSLEDIQAILAGEAGTRISP 300
|
|
| ArcC |
COG0549 |
Carbamate kinase [Amino acid transport and metabolism]; |
4-303 |
5.48e-176 |
|
Carbamate kinase [Amino acid transport and metabolism];
Pssm-ID: 440315 Cd Length: 313 Bit Score: 488.43 E-value: 5.48e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 4 KPTLVVALGGNALLKRGEPLEAEIQRQNIEQAARTIAGLTAQ-WRVVLVHGNGPQVGLLALQNSAY-DKVTPYPLDVLGA 81
Cdd:COG0549 2 KKRIVVALGGNALLRRGEPGTAEEQRENVREAAKALADLIEAgHEVVITHGNGPQVGLLLLQNEAAkKKVPPMPLDVCGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 82 ESQGMIGYMLQQALKNSLPQR----EVSVLLTQVEVDAADPAFSNPTKYIGPVYSEAQAKTLAAEKGWVFKAD-GSYVRR 156
Cdd:COG0549 82 MTQGMIGYMLQQALRNELPKRgidkPVATLVTQVEVDPDDPAFQNPTKPIGPFYTEEEAEELAKEKGWTFKEDaGRGYRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 157 VVPSPQPKRIVESDAITALIQRDHLVICNGGGGVPVVEQAKG-YRGIEAVIDKDLSAALLARQIEADALLILTDADAVYL 235
Cdd:COG0549 162 VVPSPKPKRIVEIDAIKALLEAGVIVIAAGGGGIPVVRDEDGgLKGVEAVIDKDLASALLAEELDADLLLILTDVDKVYI 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1545108536 236 DWGKPTQRPLAQVTPELLRGM----QFDAGSMGPKVAACREFVEACNGIAGIGALADGAEILAGEKGTLIRN 303
Cdd:COG0549 242 NFGKPDQRALDEVTVAEAKKYieegHFAAGSMGPKVEAAIRFVEATGKRAIITSLEKAEEALAGKAGTRIVP 313
|
|
| AAK_CK |
cd04235 |
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ... |
6-302 |
2.36e-169 |
|
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: 471.61 E-value: 2.36e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 6 TLVVALGGNALLKRGEPLEAEIQRQNIEQAARTIAGLTAQ-WRVVLVHGNGPQVGLLALQNSAYDKVTP-YPLDVLGAES 83
Cdd:cd04235 1 RIVVALGGNALLRRGEPGTAEEQRENVKIAAKALADLIKNgHEVVITHGNGPQVGNLLLQNEAAAEKVPaYPLDVCGAMS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 84 QGMIGYMLQQALKNSLPQR----EVSVLLTQVEVDAADPAFSNPTKYIGPVYSEAQAKTLAAEKGWVFKAD-GSYVRRVV 158
Cdd:cd04235 81 QGMIGYMLQQALDNELPKRgidkPVVTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEKGWTFKEDaGRGYRRVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 159 PSPQPKRIVESDAITALIQRDHLVICNGGGGVPVVEQAKGYRGIEAVIDKDLSAALLARQIEADALLILTDADAVYLDWG 238
Cdd:cd04235 161 PSPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREGGGLKGVEAVIDKDLASALLAEEINADLLVILTDVDNVYINFG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1545108536 239 KPTQRPLAQVTP-ELLRGM---QFDAGSMGPKVAACREFVEACNGIAGIGALADGAEILAGEKGTLIR 302
Cdd:cd04235 241 KPNQKALEQVTVeELEKYIeegQFAPGSMGPKVEAAIRFVESGGKKAIITSLENAEAALEGKAGTVIV 308
|
|
| arcC |
TIGR00746 |
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes ... |
6-301 |
3.46e-139 |
|
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes carbamoyl phosphate to convert ADP into ATP. In the pathway in Pyrococcus furiosus, the enzyme acts instead to generate carbamoyl phosphate.The seed alignment for this model includes experimentally confirmed examples from a set of phylogenetically distinct species. In a neighbor-joining tree constructed from an alignment of candidate carbamate kinases and several acetylglutamate kinases, the latter group forms a clear outgroup which roots the tree of carbamate kinase-like proteins. This analysis suggests that in E. coli, the ArcC paralog YqeA may be a second isozyme, while the paralog YahI branches as an outlier and is less likely to be an authentic carbamate kinase. The homolog from Mycoplasma pneumoniae likewise branches outside the set containing known carbamate kinases and also scores below the trusted cutoff. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273248 Cd Length: 310 Bit Score: 395.29 E-value: 3.46e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 6 TLVVALGGNALLKRGEPLEAEIQRQNIEQAARTIAGLTAQ-WRVVLVHGNGPQVGLLALQNSAYDKVTP-YPLDVLGAES 83
Cdd:TIGR00746 2 RVVVALGGNALLQRGEKGSAEAQRDNVRQTAPQIAKLIKRgYELVITHGNGPQVGNLLLQNQAADSEVPaMPLDVLGAMS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 84 QGMIGYMLQQALKNSLPQR----EVSVLLTQVEVDAADPAFSNPTKYIGPVYSEAQAKTLAAEKGWVFK-ADGSYVRRVV 158
Cdd:TIGR00746 82 QGMIGYMLQQALNNELPKRgmekPVATVLTQTIVDPKDPAFQNPTKPIGPFYTEEEAKRLAAEKGWIVKeDAGRGWRRVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 159 PSPQPKRIVESDAITALIQRDHLVICNGGGGVPVVEQAKGYRGIEAVIDKDLSAALLARQIEADALLILTDADAVYLDWG 238
Cdd:TIGR00746 162 PSPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEGAELKGVEAVIDKDLASEKLAEEVNADILVILTDVDAVYINYG 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1545108536 239 KPTQRPLAQVTPELLRGM----QFDAGSMGPKVAACREFVEACNGIAGIGALADGAEILAGEKGTLI 301
Cdd:TIGR00746 242 KPDEKALREVTVEELEDYykagHFAAGSMGPKVEAAIEFVESGGKRAIITSLENAVEALEGKAGTRV 308
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
6-278 |
9.93e-18 |
|
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: 80.49 E-value: 9.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 6 TLVVALGGNALLKRGepleaeiqrqNIEQAARTIAGLTAQW-RVVLVHGNGPQVGLLALQNsaydKVTPYPLDVLGAESq 84
Cdd:pfam00696 2 RVVIKLGGSSLTDKE----------RLKRLADEIAALLEEGrKLVVVHGGGAFADGLLALL----GLSPRFARLTDAET- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 85 gmiGYMLQQALKNSLPQREVSVLLtqvevDAADPAFSNPTKYIgpvyseaqaktlaaekgwvfkadgsYVRRVVPSPQPK 164
Cdd:pfam00696 67 ---LEVATMDALGSLGERLNAALL-----AAGLPAVGLPAAQL-------------------------LATEAGFIDDVV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 165 RIVESDAITALIQRDHLVICNGGGGVPVVEQAkgyrgieAVIDKDLSAALLARQIEADALLILTDADAVYLDWGK--PTQ 242
Cdd:pfam00696 114 TRIDTEALEELLEAGVVPVITGFIGIDPEGEL-------GRGSSDTLAALLAEALGADKLIILTDVDGVYTADPRkvPDA 186
|
250 260 270
....*....|....*....|....*....|....*....
gi 1545108536 243 RPLAQVTPELLRGM---QFDAGSMGPKVAACREFVEACN 278
Cdd:pfam00696 187 KLIPEISYDELLELlasGLATGGMKVKLPAALEAARRGG 225
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12354 |
PRK12354 |
carbamate kinase; Reviewed |
5-303 |
0e+00 |
|
carbamate kinase; Reviewed
Pssm-ID: 183466 Cd Length: 307 Bit Score: 566.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 5 PTLVVALGGNALLKRGEPLEAEIQRQNIEQAARTIAGLTAQWRVVLVHGNGPQVGLLALQNSAYDKVTPYPLDVLGAESQ 84
Cdd:PRK12354 1 MRIVVALGGNALLRRGEPLTAENQRANIRIAAEQIAKIAREHELVIVHGNGPQVGLLALQNAAYKDVTPYPLDVLGAETE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 85 GMIGYMLQQALKNSLPQREVSVLLTQVEVDAADPAFSNPTKYIGPVYSEAQAKTLAAEKGWVFKADGSYVRRVVPSPQPK 164
Cdd:PRK12354 81 GMIGYMLEQELGNLLPERPVATLLTQVEVDANDPAFANPTKPIGPVYDEAEAERLAAEKGWTIKPDGDYFRRVVPSPRPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 165 RIVESDAITALIQRDHLVICNGGGGVPVVEQAKG-YRGIEAVIDKDLSAALLARQIEADALLILTDADAVYLDWGKPTQR 243
Cdd:PRK12354 161 RIVEIRPIRWLLEKGHLVICAGGGGIPVVYDADGkLHGVEAVIDKDLAAALLAEQLDADLLLILTDVDAVYLDWGKPTQR 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 244 PLAQVTPELLRGMQFDAGSMGPKVAACREFVEACNGIAGIGALADGAEILAGEKGTLIRN 303
Cdd:PRK12354 241 AIAQATPDELRELGFAAGSMGPKVEAACEFVRATGKIAGIGSLEDIQAILAGEAGTRISP 300
|
|
| ArcC |
COG0549 |
Carbamate kinase [Amino acid transport and metabolism]; |
4-303 |
5.48e-176 |
|
Carbamate kinase [Amino acid transport and metabolism];
Pssm-ID: 440315 Cd Length: 313 Bit Score: 488.43 E-value: 5.48e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 4 KPTLVVALGGNALLKRGEPLEAEIQRQNIEQAARTIAGLTAQ-WRVVLVHGNGPQVGLLALQNSAY-DKVTPYPLDVLGA 81
Cdd:COG0549 2 KKRIVVALGGNALLRRGEPGTAEEQRENVREAAKALADLIEAgHEVVITHGNGPQVGLLLLQNEAAkKKVPPMPLDVCGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 82 ESQGMIGYMLQQALKNSLPQR----EVSVLLTQVEVDAADPAFSNPTKYIGPVYSEAQAKTLAAEKGWVFKAD-GSYVRR 156
Cdd:COG0549 82 MTQGMIGYMLQQALRNELPKRgidkPVATLVTQVEVDPDDPAFQNPTKPIGPFYTEEEAEELAKEKGWTFKEDaGRGYRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 157 VVPSPQPKRIVESDAITALIQRDHLVICNGGGGVPVVEQAKG-YRGIEAVIDKDLSAALLARQIEADALLILTDADAVYL 235
Cdd:COG0549 162 VVPSPKPKRIVEIDAIKALLEAGVIVIAAGGGGIPVVRDEDGgLKGVEAVIDKDLASALLAEELDADLLLILTDVDKVYI 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1545108536 236 DWGKPTQRPLAQVTPELLRGM----QFDAGSMGPKVAACREFVEACNGIAGIGALADGAEILAGEKGTLIRN 303
Cdd:COG0549 242 NFGKPDQRALDEVTVAEAKKYieegHFAAGSMGPKVEAAIRFVEATGKRAIITSLEKAEEALAGKAGTRIVP 313
|
|
| AAK_CK |
cd04235 |
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ... |
6-302 |
2.36e-169 |
|
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: 471.61 E-value: 2.36e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 6 TLVVALGGNALLKRGEPLEAEIQRQNIEQAARTIAGLTAQ-WRVVLVHGNGPQVGLLALQNSAYDKVTP-YPLDVLGAES 83
Cdd:cd04235 1 RIVVALGGNALLRRGEPGTAEEQRENVKIAAKALADLIKNgHEVVITHGNGPQVGNLLLQNEAAAEKVPaYPLDVCGAMS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 84 QGMIGYMLQQALKNSLPQR----EVSVLLTQVEVDAADPAFSNPTKYIGPVYSEAQAKTLAAEKGWVFKAD-GSYVRRVV 158
Cdd:cd04235 81 QGMIGYMLQQALDNELPKRgidkPVVTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEKGWTFKEDaGRGYRRVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 159 PSPQPKRIVESDAITALIQRDHLVICNGGGGVPVVEQAKGYRGIEAVIDKDLSAALLARQIEADALLILTDADAVYLDWG 238
Cdd:cd04235 161 PSPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREGGGLKGVEAVIDKDLASALLAEEINADLLVILTDVDNVYINFG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1545108536 239 KPTQRPLAQVTP-ELLRGM---QFDAGSMGPKVAACREFVEACNGIAGIGALADGAEILAGEKGTLIR 302
Cdd:cd04235 241 KPNQKALEQVTVeELEKYIeegQFAPGSMGPKVEAAIRFVESGGKKAIITSLENAEAALEGKAGTVIV 308
|
|
| arcC |
TIGR00746 |
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes ... |
6-301 |
3.46e-139 |
|
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes carbamoyl phosphate to convert ADP into ATP. In the pathway in Pyrococcus furiosus, the enzyme acts instead to generate carbamoyl phosphate.The seed alignment for this model includes experimentally confirmed examples from a set of phylogenetically distinct species. In a neighbor-joining tree constructed from an alignment of candidate carbamate kinases and several acetylglutamate kinases, the latter group forms a clear outgroup which roots the tree of carbamate kinase-like proteins. This analysis suggests that in E. coli, the ArcC paralog YqeA may be a second isozyme, while the paralog YahI branches as an outlier and is less likely to be an authentic carbamate kinase. The homolog from Mycoplasma pneumoniae likewise branches outside the set containing known carbamate kinases and also scores below the trusted cutoff. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273248 Cd Length: 310 Bit Score: 395.29 E-value: 3.46e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 6 TLVVALGGNALLKRGEPLEAEIQRQNIEQAARTIAGLTAQ-WRVVLVHGNGPQVGLLALQNSAYDKVTP-YPLDVLGAES 83
Cdd:TIGR00746 2 RVVVALGGNALLQRGEKGSAEAQRDNVRQTAPQIAKLIKRgYELVITHGNGPQVGNLLLQNQAADSEVPaMPLDVLGAMS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 84 QGMIGYMLQQALKNSLPQR----EVSVLLTQVEVDAADPAFSNPTKYIGPVYSEAQAKTLAAEKGWVFK-ADGSYVRRVV 158
Cdd:TIGR00746 82 QGMIGYMLQQALNNELPKRgmekPVATVLTQTIVDPKDPAFQNPTKPIGPFYTEEEAKRLAAEKGWIVKeDAGRGWRRVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 159 PSPQPKRIVESDAITALIQRDHLVICNGGGGVPVVEQAKGYRGIEAVIDKDLSAALLARQIEADALLILTDADAVYLDWG 238
Cdd:TIGR00746 162 PSPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEGAELKGVEAVIDKDLASEKLAEEVNADILVILTDVDAVYINYG 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1545108536 239 KPTQRPLAQVTPELLRGM----QFDAGSMGPKVAACREFVEACNGIAGIGALADGAEILAGEKGTLI 301
Cdd:TIGR00746 242 KPDEKALREVTVEELEDYykagHFAAGSMGPKVEAAIEFVESGGKRAIITSLENAVEALEGKAGTRV 308
|
|
| PRK12353 |
PRK12353 |
putative amino acid kinase; Reviewed |
4-302 |
1.18e-138 |
|
putative amino acid kinase; Reviewed
Pssm-ID: 237071 Cd Length: 314 Bit Score: 394.14 E-value: 1.18e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 4 KPTLVVALGGNALLKRGEplEAEIQRQNIEQAARTIAGLTAQ-WRVVLVHGNGPQVGLLALQNSA----YDKVTPYPLDV 78
Cdd:PRK12353 2 MKKIVVALGGNALGSTPE--EATAQLEAVKKTAKSLVDLIEEgHEVVITHGNGPQVGNILLAQEAaaseKNKVPAMPLDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 79 LGAESQGMIGYMLQQALKNSLPQR----EVSVLLTQVEVDAADPAFSNPTKYIGPVYSEAQAKTLAAEKGWVFKAD--GS 152
Cdd:PRK12353 80 CGAMSQGYIGYHLQNALRNELLKRgidkPVATVVTQVVVDANDPAFKNPTKPIGPFYTEEEAEKLAKEKGYTFKEDagRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 153 YvRRVVPSPQPKRIVESDAITALIQRDHLVICNGGGGVPVVEQAKGYRGIEAVIDKDLSAALLARQIEADALLILTDADA 232
Cdd:PRK12353 160 Y-RRVVPSPKPVDIVEIEAIKTLVDAGQVVIAAGGGGIPVIREGGGLKGVEAVIDKDFASAKLAELVDADLLIILTAVDK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1545108536 233 VYLDWGKPTQRPLAQVTPELLRGM----QFDAGSMGPKVAACREFVEACNG-IAGIGALADGAEILAGEKGTLIR 302
Cdd:PRK12353 239 VYINFGKPNQKKLDEVTVSEAEKYieegQFAPGSMLPKVEAAISFVESRPGrKAIITSLEKAKEALEGKAGTVIV 313
|
|
| PRK09411 |
PRK09411 |
carbamate kinase; Reviewed |
4-302 |
4.39e-136 |
|
carbamate kinase; Reviewed
Pssm-ID: 181831 Cd Length: 297 Bit Score: 386.85 E-value: 4.39e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 4 KPTLVVALGGNALLKRGEPLEAEIQRQNIEQAARTIAGLTAQWRVVLVHGNGPQVGLLALQNSAYDKVTPYPLDVLGAES 83
Cdd:PRK09411 1 MKTLVVALGGNALLQRGEALTAENQYRNIASAVPALARLARSYRLAIVHGNGPQVGLLALQNLAWKEVEPYPLDVLVAES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 84 QGMIGYMLQQALKNSLPQREVSVLLTQVEVDAADPAFSNPTKYIGPVYSEAQAKTLAAEKGWVFKADGSYVRRVVPSPQP 163
Cdd:PRK09411 81 QGMIGYMLAQSLSAQPQMPPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAYGWQMKRDGKYLRRVVASPQP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 164 KRIVESDAITALIQRDHLVICNGGGGVPVVEQAKgyrGIEAVIDKDLSAALLARQIEADALLILTDADAVYLDWGKPTQR 243
Cdd:PRK09411 161 RKILDSEAIELLLKEGHVVICSGGGGVPVTEDGA---GSEAVIDKDLAAALLAEQINADGLVILTDADAVYENWGTPQQR 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1545108536 244 PLAQVTPELLRGMQFDAGSMGPKVAACREFVEACNGIAGIGALADGAEILAGEKGTLIR 302
Cdd:PRK09411 238 AIRHATPDELAPFAKADGAMGPKVTAVSGYVRSRGKPAWIGALSRIEETLAGEAGTCIS 296
|
|
| PRK12454 |
PRK12454 |
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed |
4-301 |
3.15e-134 |
|
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
Pssm-ID: 183535 Cd Length: 313 Bit Score: 382.81 E-value: 3.15e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 4 KPTLVVALGGNALLKRGEPLEAEIQRQNIEQAARTIAGLTAQ-WRVVLVHGNGPQVGLLALQNSAYDKV--TPYPLDVLG 80
Cdd:PRK12454 2 KKRIVIALGGNALLQPGEKGTAENQMKNVRKTAKQIADLIEEgYEVVITHGNGPQVGNLLLQMDAAKDVgiPPFPLDVAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 81 AESQGMIGYMLQQALKNSLPQ----REVSVLLTQVEVDAADPAFSNPTKYIGPVYSEAQAKTLAAEKGWVFKAD-GSYVR 155
Cdd:PRK12454 82 AMTQGWIGYMIQQALRNELAKrgieKQVATIVTQVIVDKNDPAFQNPTKPVGPFYDEEEAKKLAKEKGWIVKEDaGRGWR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 156 RVVPSPQPKRIVESDAITALIQRDHLVICNGGGGVPVVEQAKGYRGIEAVIDKDLSAALLARQIEADALLILTDADAVYL 235
Cdd:PRK12454 162 RVVPSPDPLGIVEIEVIKALVENGFIVIASGGGGIPVIEEDGELKGVEAVIDKDLASELLAEELNADIFIILTDVEKVYL 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 236 DWGKPTQRPLAQVTPE----LLRGMQFDAGSMGPKVAACREFVEACNGIAGIGALADGAEILAGEKGTLI 301
Cdd:PRK12454 242 NYGKPDQKPLDKVTVEeakkYYEEGHFKAGSMGPKILAAIRFVENGGKRAIIASLEKAVEALEGKTGTRI 311
|
|
| PRK12686 |
PRK12686 |
carbamate kinase; Reviewed |
4-301 |
1.66e-112 |
|
carbamate kinase; Reviewed
Pssm-ID: 183683 Cd Length: 312 Bit Score: 327.77 E-value: 1.66e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 4 KPTLVVALGGNALLKRGEPLEAeiQRQNIEQAARTIAGLTAQ-WRVVLVHGNGPQVGLLALQ--NSAYDKVTPYPLDVLG 80
Cdd:PRK12686 2 KEKIVIALGGNAILQTEATAEA--QQTAVREAAQHLVDLIEAgHDIVITHGNGPQVGNLLLQqaESNSNKVPAMPLDTCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 81 AESQGMIGYMLQQALKNSLPQR----EVSVLLTQVEVDAADPAFSNPTKYIGPVYSEAQAKTLAAEKGWVFKAD-GSYVR 155
Cdd:PRK12686 80 AMSQGMIGYWLQNALNNELTERgidkPVITLVTQVEVDKDDPAFANPTKPIGPFYTEEEAKQQAEQPGSTFKEDaGRGYR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 156 RVVPSPQPKRIVESDAITALIQRDHLVICNGGGGVPVVEQAKGYRGIEAVIDKDLSAALLARQIEADALLILTDADAVYL 235
Cdd:PRK12686 160 RVVPSPKPQEIIEHDTIRTLVDGGNIVIACGGGGIPVIRDDNTLKGVEAVIDKDFASEKLAEQIDADLLIILTGVENVFI 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1545108536 236 DWGKPTQRPLAQVT----PELLRGMQFDAGSMGPKVAACREFVEACNGIAG-IGALADGAEILAGEKGTLI 301
Cdd:PRK12686 240 NFNKPNQQKLDDITvaeaKQYIAEGQFAPGSMLPKVEAAIDFVESGEGKKAiITSLEQAKEALAGNAGTHI 310
|
|
| PRK12352 |
PRK12352 |
putative carbamate kinase; Reviewed |
4-303 |
1.16e-88 |
|
putative carbamate kinase; Reviewed
Pssm-ID: 183464 Cd Length: 316 Bit Score: 267.44 E-value: 1.16e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 4 KPTLVVALGGNALLKRGEPLEAEIQRQNIEQAARTIAGLTAQ-WRVVLVHGNGPQVGLLALQN---SAYDKVTPYPLDVL 79
Cdd:PRK12352 2 KELVVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASdYDIVLTHGNGPQVGLDLRRAeiaHEREGLPLTPLANC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 80 GAESQGMIGYMLQQALKNSLPQR---EVSVLLTQVEVDAADPAFSNPTKYIGPVYSEAQAKTL-AAEKGWVFKAD-GSYV 154
Cdd:PRK12352 82 VADTQGGIGYLIQQALNNRLARHgekKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDELqKANPDWRFVEDaGRGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 155 RRVVPSPQPKRIVESDAITALIQRDHLVICNGGGGVPVVEQAKG-YRGIEAVIDKDLSAALLARQIEADALLILTDADAV 233
Cdd:PRK12352 162 RRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDAGdYQSVDAVIDKDLSTALLAREIHADILVITTGVEKV 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1545108536 234 YLDWGKPTQRPLAQVT-PELLRGMQ---FDAGSMGPKVAACREFVEACNGIAGIGALADGAEILAGEKGTLIRN 303
Cdd:PRK12352 242 CIHFGKPQQQALDRVDiATMTRYMQeghFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHIIK 315
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
6-278 |
9.93e-18 |
|
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: 80.49 E-value: 9.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 6 TLVVALGGNALLKRGepleaeiqrqNIEQAARTIAGLTAQW-RVVLVHGNGPQVGLLALQNsaydKVTPYPLDVLGAESq 84
Cdd:pfam00696 2 RVVIKLGGSSLTDKE----------RLKRLADEIAALLEEGrKLVVVHGGGAFADGLLALL----GLSPRFARLTDAET- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 85 gmiGYMLQQALKNSLPQREVSVLLtqvevDAADPAFSNPTKYIgpvyseaqaktlaaekgwvfkadgsYVRRVVPSPQPK 164
Cdd:pfam00696 67 ---LEVATMDALGSLGERLNAALL-----AAGLPAVGLPAAQL-------------------------LATEAGFIDDVV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 165 RIVESDAITALIQRDHLVICNGGGGVPVVEQAkgyrgieAVIDKDLSAALLARQIEADALLILTDADAVYLDWGK--PTQ 242
Cdd:pfam00696 114 TRIDTEALEELLEAGVVPVITGFIGIDPEGEL-------GRGSSDTLAALLAEALGADKLIILTDVDGVYTADPRkvPDA 186
|
250 260 270
....*....|....*....|....*....|....*....
gi 1545108536 243 RPLAQVTPELLRGM---QFDAGSMGPKVAACREFVEACN 278
Cdd:pfam00696 187 KLIPEISYDELLELlasGLATGGMKVKLPAALEAARRGG 225
|
|
| AAK |
cd02115 |
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ... |
8-301 |
1.98e-14 |
|
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: 71.32 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 8 VVALGGNaLLKRGEPLEaEIQRQNIEQAARtiagltaQWRVVLVHGNGPQVG------LLALQNSAYDKVTPYPLDVLGA 81
Cdd:cd02115 1 VIKFGGS-SVSSEERLR-NLARILVKLASE-------GGRVVVVHGAGPQITdellahGELLGYARGLRITDRETDALAA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 82 ESQGMIGYMLQQALKNSlpqrevSVLLTQVEVDAADPAfSNPTKYIGPVYSeaqaktlaaekgwvfkadgsyvrrvvpsp 161
Cdd:cd02115 72 MGEGMSNLLIAAALEQH------GIKAVPLDLTQAGFA-SPNQGHVGKITK----------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 162 qpkriVESDAITALIQRDHLVICNGGGGVPVVEqakgyRGIEAVIDKDLSAALLARQIEADALLILTDADAVYLDWGK-- 239
Cdd:cd02115 116 -----VSTDRLKSLLENGILPILSGFGGTDEKE-----TGTLGRGGSDSTAALLAAALKADRLVILTDVDGVYTADPRkv 185
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1545108536 240 PTQRPLAQVTPELLRGMQFdAGSMGPKVAACREFVEACNGIAGIGALADGAEILAGEK--GTLI 301
Cdd:cd02115 186 PDAKLLSELTYEEAAELAY-AGAMVLKPKAADPAARAGIPVRIANTENPGALALFTPDggGTLI 248
|
|
| AAK_G5K_ProB |
cd04242 |
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ... |
207-302 |
2.42e-06 |
|
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: 47.82 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 207 DKDLSAALLARQIEADALLILTDADAVYlDwGKPTQRPLAQVTPEL------LRGMQFDAGS------MGPKVAACREFV 274
Cdd:cd04242 143 DNDRLSALVAGLVNADLLILLSDVDGLY-D-KNPRENPDAKLIPEVeeitdeIEAMAGGSGSsvgtggMRTKLKAARIAT 220
|
90 100 110
....*....|....*....|....*....|....*
gi 1545108536 275 EAcnGIAGIgaLADGAE------ILAGEK-GTLIR 302
Cdd:cd04242 221 EA--GIPVV--IANGRKpdvlldILAGEAvGTLFL 251
|
|
| AAK_NAGK-UC |
cd04251 |
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ... |
186-301 |
1.11e-04 |
|
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar to Escherichia coli and Pseudomonas aeruginosa NAGKs which catalyze the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis. These uncharacterized domain sequences are found in some bacteria (Deinococci and Chloroflexi) and archea and belong to the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239784 [Multi-domain] Cd Length: 257 Bit Score: 42.74 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 186 GGGGVPVVEQ-AKGYRGIEAVIDKDLSAALLARQIEADALLILTDADAVYLDwgkptQRPLAQVTPELLRG-MQFDAGSM 263
Cdd:cd04251 143 DAGYLPVVSPvAYSEEGEPLNVDGDRAAAAIAAALKAERLILLTDVEGLYLD-----GRVIERITVSDAESlLEKAGGGM 217
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1545108536 264 GPKVAACREFVEACNGIAGIGALADGAEILA--GEKGTLI 301
Cdd:cd04251 218 KRKLLAAAEAVEGGVREVVIGDARADSPISSalNGGGTVI 257
|
|
| AAK_NAGK-C |
cd04250 |
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ... |
206-283 |
1.87e-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: 42.11 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 206 IDKDLSAALLARQIEADALLILTDADAVYLDWGKPTQRpLAQVTPELLRGMQFD---AGSMGPKVAACREFVEACNGIAG 282
Cdd:cd04250 177 INADTAAGAIAAALKAEKLILLTDVAGVLDDPNDPGSL-ISEISLKEAEELIADgiiSGGMIPKVEACIEALEGGVKAAH 255
|
.
gi 1545108536 283 I 283
Cdd:cd04250 256 I 256
|
|
| AAK_P5CS_ProBA |
cd04256 |
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ... |
190-300 |
3.56e-04 |
|
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: 41.26 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 190 VPVVEQAKGYRGIEAVIDKDLSAALLARQIEADALLILTDADAVYLDW-GKPTQRPLAQVTPELLRGMQFDA------GS 262
Cdd:cd04256 162 SPPPEPDEDLQGVISIKDNDSLAARLAVELKADLLILLSDVDGLYDGPpGSDDAKLIHTFYPGDQQSITFGTksrvgtGG 241
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1545108536 263 MGPKVAACREFVEA------CNGIAGIGALadgaEILAGEK-GTL 300
Cdd:cd04256 242 MEAKVKAALWALQGgtsvviTNGMAGDVIT----KILEGKKvGTF 282
|
|
| PLN02418 |
PLN02418 |
delta-1-pyrroline-5-carboxylate synthase |
207-300 |
8.01e-04 |
|
delta-1-pyrroline-5-carboxylate synthase
Pssm-ID: 215230 Cd Length: 718 Bit Score: 40.86 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 207 DKDLSAALLARQIEADALLILTDADAVYldwGKPTQRPLAQVTPELLRGMQFDA-----------GSMGPKVAACREFVE 275
Cdd:PLN02418 176 DNDSLAALLALELKADLLILLSDVEGLY---TGPPSDPSSKLIHTYIKEKHQDEitfgeksrvgrGGMTAKVKAAVNAAS 252
|
90 100 110
....*....|....*....|....*....|
gi 1545108536 276 AcnGIAGI---GALADG-AEILAGEK-GTL 300
Cdd:PLN02418 253 A--GIPVVitsGYALDNiRKVLRGERvGTL 280
|
|
| ProB |
COG0263 |
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ... |
212-302 |
1.04e-03 |
|
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: 40.41 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545108536 212 AALLARQIEADALLILTDADAVYlDwGKPTQRPLAQ-------VTPELLRgMQFDAGS------MGPKVAACRefVEACN 278
Cdd:COG0263 156 AALVANLVEADLLVLLTDVDGLY-D-ADPRKDPDAKlipeveeITPEIEA-MAGGAGSglgtggMATKLEAAR--IATRA 230
|
90 100 110
....*....|....*....|....*....|.
gi 1545108536 279 GIAGIgaLADGAE------ILAGEK-GTLIR 302
Cdd:COG0263 231 GIPTV--IASGREpnvllrILAGERvGTLFL 259
|
|
| |
