|
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: 540.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 5 TVVVALGGNALLRRGEPLEADVQRRNIETAVKTISEIAKVYNVVLVHGNGPQVGLLALQGLEYKKVNPYPLDVLGSETQG 84
Cdd:PRK12354 2 RIVVALGGNALLRRGEPLTAENQRANIRIAAEQIAKIAREHELVIVHGNGPQVGLLALQNAAYKDVTPYPLDVLGAETEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 85 MIGYMLMQEFKNYLPNRNISCMLTQMTVDPNDPAFADPTKPIGPIYEEAEARELAEKFHWIVKPDGQHFRRVVPSPRPTG 164
Cdd:PRK12354 82 MIGYMLEQELGNLLPERPVATLLTQVEVDANDPAFANPTKPIGPVYDEAEAERLAAEKGWTIKPDGDYFRRVVPSPRPKR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 165 IVEHEAITQLIDAGHLVICTGGGGIPV-KKENGKLVGVEAVIDKDMSAAFLAKQLDADALLILTDADAVYLDWGKPTQHA 243
Cdd:PRK12354 162 IVEIRPIRWLLEKGHLVICAGGGGIPVvYDADGKLHGVEAVIDKDLAAALLAEQLDADLLLILTDVDAVYLDWGKPTQRA 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 244 LRSTTPSELAMFEFDAGSMGPKIEASCEFIEQGGKVVGIGALEDGLQILQGQAGTNITKG 303
Cdd:PRK12354 242 IAQATPDELRELGFAAGSMGPKVEAACEFVRATGKIAGIGSLEDIQAILAGEAGTRISPE 301
|
|
| ArcC |
COG0549 |
Carbamate kinase [Amino acid transport and metabolism]; |
3-302 |
4.43e-163 |
|
Carbamate kinase [Amino acid transport and metabolism];
Pssm-ID: 440315 Cd Length: 313 Bit Score: 456.07 E-value: 4.43e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 3 KQTVVVALGGNALLRRGEPLEADVQRRNIETAVKTISEIAKV-YNVVLVHGNGPQVGLLALQGLEYKKVNP-YPLDVLGS 80
Cdd:COG0549 2 KKRIVVALGGNALLRRGEPGTAEEQRENVREAAKALADLIEAgHEVVITHGNGPQVGLLLLQNEAAKKKVPpMPLDVCGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 81 ETQGMIGYMLMQEFKNYLPNRNI----SCMLTQMTVDPNDPAFADPTKPIGPIYEEAEARELAEKFHWIVKPD-GQHFRR 155
Cdd:COG0549 82 MTQGMIGYMLQQALRNELPKRGIdkpvATLVTQVEVDPDDPAFQNPTKPIGPFYTEEEAEELAKEKGWTFKEDaGRGYRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 156 VVPSPRPTGIVEHEAITQLIDAGHLVICTGGGGIPV-KKENGKLVGVEAVIDKDMSAAFLAKQLDADALLILTDADAVYL 234
Cdd:COG0549 162 VVPSPKPKRIVEIDAIKALLEAGVIVIAAGGGGIPVvRDEDGGLKGVEAVIDKDLASALLAEELDADLLLILTDVDKVYI 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1515577847 235 DWGKPTQHALRSTTPSEL----AMFEFDAGSMGPKIEASCEFIEQGGKVVGIGALEDGLQILQGQAGTNITK 302
Cdd:COG0549 242 NFGKPDQRALDEVTVAEAkkyiEEGHFAAGSMGPKVEAAIRFVEATGKRAIITSLEKAEEALAGKAGTRIVP 313
|
|
| AAK_CK |
cd04235 |
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ... |
5-301 |
9.96e-161 |
|
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: 449.65 E-value: 9.96e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 5 TVVVALGGNALLRRGEPLEADVQRRNIETAVKTISEIAK-VYNVVLVHGNGPQVGLLALQGLEYKKVNP-YPLDVLGSET 82
Cdd:cd04235 1 RIVVALGGNALLRRGEPGTAEEQRENVKIAAKALADLIKnGHEVVITHGNGPQVGNLLLQNEAAAEKVPaYPLDVCGAMS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 83 QGMIGYMLMQEFKNYLPNRNIS----CMLTQMTVDPNDPAFADPTKPIGPIYEEAEARELAEKFHWIVKPD-GQHFRRVV 157
Cdd:cd04235 81 QGMIGYMLQQALDNELPKRGIDkpvvTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEKGWTFKEDaGRGYRRVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 158 PSPRPTGIVEHEAITQLIDAGHLVICTGGGGIPVKKENGKLVGVEAVIDKDMSAAFLAKQLDADALLILTDADAVYLDWG 237
Cdd:cd04235 161 PSPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREGGGLKGVEAVIDKDLASALLAEEINADLLVILTDVDNVYINFG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1515577847 238 KPTQHALRSTTPSELAMF----EFDAGSMGPKIEASCEFIEQGGKVVGIGALEDGLQILQGQAGTNIT 301
Cdd:cd04235 241 KPNQKALEQVTVEELEKYieegQFAPGSMGPKVEAAIRFVESGGKKAIITSLENAEAALEGKAGTVIV 308
|
|
| arcC |
TIGR00746 |
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes ... |
5-302 |
1.92e-135 |
|
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: 386.04 E-value: 1.92e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 5 TVVVALGGNALLRRGEPLEADVQRRNIETAVKTISEIAKV-YNVVLVHGNGPQVGLLALQGLEYKKVNP-YPLDVLGSET 82
Cdd:TIGR00746 2 RVVVALGGNALLQRGEKGSAEAQRDNVRQTAPQIAKLIKRgYELVITHGNGPQVGNLLLQNQAADSEVPaMPLDVLGAMS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 83 QGMIGYMLMQEFKNYLPNRNI----SCMLTQMTVDPNDPAFADPTKPIGPIYEEAEARELAEKFHWIVKPD-GQHFRRVV 157
Cdd:TIGR00746 82 QGMIGYMLQQALNNELPKRGMekpvATVLTQTIVDPKDPAFQNPTKPIGPFYTEEEAKRLAAEKGWIVKEDaGRGWRRVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 158 PSPRPTGIVEHEAITQLIDAGHLVICTGGGGIPVKKENGKLVGVEAVIDKDMSAAFLAKQLDADALLILTDADAVYLDWG 237
Cdd:TIGR00746 162 PSPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEGAELKGVEAVIDKDLASEKLAEEVNADILVILTDVDAVYINYG 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1515577847 238 KPTQHALRSTTPSELAMF----EFDAGSMGPKIEASCEFIEQGGKVVGIGALEDGLQILQGQAGTNITK 302
Cdd:TIGR00746 242 KPDEKALREVTVEELEDYykagHFAAGSMGPKVEAAIEFVESGGKRAIITSLENAVEALEGKAGTRVTK 310
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
4-277 |
3.03e-21 |
|
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: 90.12 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 4 QTVVVALGGNALlrrgepleadVQRRNIETAVKTISEI-AKVYNVVLVHGNGPQV-GLLALQGLEYKKVNPYPLDVLGSE 81
Cdd:pfam00696 1 KRVVIKLGGSSL----------TDKERLKRLADEIAALlEEGRKLVVVHGGGAFAdGLLALLGLSPRFARLTDAETLEVA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 82 TQGMIG----YMLMQEFKNYLPNRNIScmltqmtvdpndPAFADPTKpigpiyeeaearelaekfhwIVKPDGQHFRRVV 157
Cdd:pfam00696 71 TMDALGslgeRLNAALLAAGLPAVGLP------------AAQLLATE--------------------AGFIDDVVTRIDT 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 158 psprptgivehEAITQLIDAGHLVICTGGGGIPVKKENGklvgveaVIDKDMSAAFLAKQLDADALLILTDADAVYLDWG 237
Cdd:pfam00696 119 -----------EALEELLEAGVVPVITGFIGIDPEGELG-------RGSSDTLAALLAEALGADKLIILTDVDGVYTADP 180
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1515577847 238 KPTQHA--LRSTTPSELA---MFEFDAGSMGPKIEASCEFIEQGG 277
Cdd:pfam00696 181 RKVPDAklIPEISYDELLellASGLATGGMKVKLPAALEAARRGG 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: 540.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 5 TVVVALGGNALLRRGEPLEADVQRRNIETAVKTISEIAKVYNVVLVHGNGPQVGLLALQGLEYKKVNPYPLDVLGSETQG 84
Cdd:PRK12354 2 RIVVALGGNALLRRGEPLTAENQRANIRIAAEQIAKIAREHELVIVHGNGPQVGLLALQNAAYKDVTPYPLDVLGAETEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 85 MIGYMLMQEFKNYLPNRNISCMLTQMTVDPNDPAFADPTKPIGPIYEEAEARELAEKFHWIVKPDGQHFRRVVPSPRPTG 164
Cdd:PRK12354 82 MIGYMLEQELGNLLPERPVATLLTQVEVDANDPAFANPTKPIGPVYDEAEAERLAAEKGWTIKPDGDYFRRVVPSPRPKR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 165 IVEHEAITQLIDAGHLVICTGGGGIPV-KKENGKLVGVEAVIDKDMSAAFLAKQLDADALLILTDADAVYLDWGKPTQHA 243
Cdd:PRK12354 162 IVEIRPIRWLLEKGHLVICAGGGGIPVvYDADGKLHGVEAVIDKDLAAALLAEQLDADLLLILTDVDAVYLDWGKPTQRA 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 244 LRSTTPSELAMFEFDAGSMGPKIEASCEFIEQGGKVVGIGALEDGLQILQGQAGTNITKG 303
Cdd:PRK12354 242 IAQATPDELRELGFAAGSMGPKVEAACEFVRATGKIAGIGSLEDIQAILAGEAGTRISPE 301
|
|
| ArcC |
COG0549 |
Carbamate kinase [Amino acid transport and metabolism]; |
3-302 |
4.43e-163 |
|
Carbamate kinase [Amino acid transport and metabolism];
Pssm-ID: 440315 Cd Length: 313 Bit Score: 456.07 E-value: 4.43e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 3 KQTVVVALGGNALLRRGEPLEADVQRRNIETAVKTISEIAKV-YNVVLVHGNGPQVGLLALQGLEYKKVNP-YPLDVLGS 80
Cdd:COG0549 2 KKRIVVALGGNALLRRGEPGTAEEQRENVREAAKALADLIEAgHEVVITHGNGPQVGLLLLQNEAAKKKVPpMPLDVCGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 81 ETQGMIGYMLMQEFKNYLPNRNI----SCMLTQMTVDPNDPAFADPTKPIGPIYEEAEARELAEKFHWIVKPD-GQHFRR 155
Cdd:COG0549 82 MTQGMIGYMLQQALRNELPKRGIdkpvATLVTQVEVDPDDPAFQNPTKPIGPFYTEEEAEELAKEKGWTFKEDaGRGYRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 156 VVPSPRPTGIVEHEAITQLIDAGHLVICTGGGGIPV-KKENGKLVGVEAVIDKDMSAAFLAKQLDADALLILTDADAVYL 234
Cdd:COG0549 162 VVPSPKPKRIVEIDAIKALLEAGVIVIAAGGGGIPVvRDEDGGLKGVEAVIDKDLASALLAEELDADLLLILTDVDKVYI 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1515577847 235 DWGKPTQHALRSTTPSEL----AMFEFDAGSMGPKIEASCEFIEQGGKVVGIGALEDGLQILQGQAGTNITK 302
Cdd:COG0549 242 NFGKPDQRALDEVTVAEAkkyiEEGHFAAGSMGPKVEAAIRFVEATGKRAIITSLEKAEEALAGKAGTRIVP 313
|
|
| AAK_CK |
cd04235 |
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ... |
5-301 |
9.96e-161 |
|
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: 449.65 E-value: 9.96e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 5 TVVVALGGNALLRRGEPLEADVQRRNIETAVKTISEIAK-VYNVVLVHGNGPQVGLLALQGLEYKKVNP-YPLDVLGSET 82
Cdd:cd04235 1 RIVVALGGNALLRRGEPGTAEEQRENVKIAAKALADLIKnGHEVVITHGNGPQVGNLLLQNEAAAEKVPaYPLDVCGAMS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 83 QGMIGYMLMQEFKNYLPNRNIS----CMLTQMTVDPNDPAFADPTKPIGPIYEEAEARELAEKFHWIVKPD-GQHFRRVV 157
Cdd:cd04235 81 QGMIGYMLQQALDNELPKRGIDkpvvTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEKGWTFKEDaGRGYRRVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 158 PSPRPTGIVEHEAITQLIDAGHLVICTGGGGIPVKKENGKLVGVEAVIDKDMSAAFLAKQLDADALLILTDADAVYLDWG 237
Cdd:cd04235 161 PSPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREGGGLKGVEAVIDKDLASALLAEEINADLLVILTDVDNVYINFG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1515577847 238 KPTQHALRSTTPSELAMF----EFDAGSMGPKIEASCEFIEQGGKVVGIGALEDGLQILQGQAGTNIT 301
Cdd:cd04235 241 KPNQKALEQVTVEELEKYieegQFAPGSMGPKVEAAIRFVESGGKKAIITSLENAEAALEGKAGTVIV 308
|
|
| arcC |
TIGR00746 |
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes ... |
5-302 |
1.92e-135 |
|
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: 386.04 E-value: 1.92e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 5 TVVVALGGNALLRRGEPLEADVQRRNIETAVKTISEIAKV-YNVVLVHGNGPQVGLLALQGLEYKKVNP-YPLDVLGSET 82
Cdd:TIGR00746 2 RVVVALGGNALLQRGEKGSAEAQRDNVRQTAPQIAKLIKRgYELVITHGNGPQVGNLLLQNQAADSEVPaMPLDVLGAMS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 83 QGMIGYMLMQEFKNYLPNRNI----SCMLTQMTVDPNDPAFADPTKPIGPIYEEAEARELAEKFHWIVKPD-GQHFRRVV 157
Cdd:TIGR00746 82 QGMIGYMLQQALNNELPKRGMekpvATVLTQTIVDPKDPAFQNPTKPIGPFYTEEEAKRLAAEKGWIVKEDaGRGWRRVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 158 PSPRPTGIVEHEAITQLIDAGHLVICTGGGGIPVKKENGKLVGVEAVIDKDMSAAFLAKQLDADALLILTDADAVYLDWG 237
Cdd:TIGR00746 162 PSPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEGAELKGVEAVIDKDLASEKLAEEVNADILVILTDVDAVYINYG 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1515577847 238 KPTQHALRSTTPSELAMF----EFDAGSMGPKIEASCEFIEQGGKVVGIGALEDGLQILQGQAGTNITK 302
Cdd:TIGR00746 242 KPDEKALREVTVEELEDYykagHFAAGSMGPKVEAAIEFVESGGKRAIITSLENAVEALEGKAGTRVTK 310
|
|
| PRK09411 |
PRK09411 |
carbamate kinase; Reviewed |
3-302 |
1.49e-133 |
|
carbamate kinase; Reviewed
Pssm-ID: 181831 Cd Length: 297 Bit Score: 380.68 E-value: 1.49e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 3 KQTVVVALGGNALLRRGEPLEADVQRRNIETAVKTISEIAKVYNVVLVHGNGPQVGLLALQGLEYKKVNPYPLDVLGSET 82
Cdd:PRK09411 1 MKTLVVALGGNALLQRGEALTAENQYRNIASAVPALARLARSYRLAIVHGNGPQVGLLALQNLAWKEVEPYPLDVLVAES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 83 QGMIGYMLMQEFKNYLPNRNISCMLTQMTVDPNDPAFADPTKPIGPIYEEAEARELAEKFHWIVKPDGQHFRRVVPSPRP 162
Cdd:PRK09411 81 QGMIGYMLAQSLSAQPQMPPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAYGWQMKRDGKYLRRVVASPQP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 163 TGIVEHEAITQLIDAGHLVICTGGGGIPVKKENGklvGVEAVIDKDMSAAFLAKQLDADALLILTDADAVYLDWGKPTQH 242
Cdd:PRK09411 161 RKILDSEAIELLLKEGHVVICSGGGGVPVTEDGA---GSEAVIDKDLAAALLAEQINADGLVILTDADAVYENWGTPQQR 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 243 ALRSTTPSELAMFEFDAGSMGPKIEASCEFIEQGGKVVGIGALEDGLQILQGQAGTNITK 302
Cdd:PRK09411 238 AIRHATPDELAPFAKADGAMGPKVTAVSGYVRSRGKPAWIGALSRIEETLAGEAGTCISL 297
|
|
| PRK12454 |
PRK12454 |
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed |
3-302 |
2.13e-131 |
|
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
Pssm-ID: 183535 Cd Length: 313 Bit Score: 375.87 E-value: 2.13e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 3 KQTVVVALGGNALLRRGEPLEADVQRRNIETAVKTISE-IAKVYNVVLVHGNGPQVGLLALQGLEYKKVN--PYPLDVLG 79
Cdd:PRK12454 2 KKRIVIALGGNALLQPGEKGTAENQMKNVRKTAKQIADlIEEGYEVVITHGNGPQVGNLLLQMDAAKDVGipPFPLDVAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 80 SETQGMIGYMLMQEFKNYLP----NRNISCMLTQMTVDPNDPAFADPTKPIGPIYEEAEARELAEKFHWIVKPD-GQHFR 154
Cdd:PRK12454 82 AMTQGWIGYMIQQALRNELAkrgiEKQVATIVTQVIVDKNDPAFQNPTKPVGPFYDEEEAKKLAKEKGWIVKEDaGRGWR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 155 RVVPSPRPTGIVEHEAITQLIDAGHLVICTGGGGIPVKKENGKLVGVEAVIDKDMSAAFLAKQLDADALLILTDADAVYL 234
Cdd:PRK12454 162 RVVPSPDPLGIVEIEVIKALVENGFIVIASGGGGIPVIEEDGELKGVEAVIDKDLASELLAEELNADIFIILTDVEKVYL 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1515577847 235 DWGKPTQHALRSTTPSELAMF----EFDAGSMGPKIEASCEFIEQGGKVVGIGALEDGLQILQGQAGTNITK 302
Cdd:PRK12454 242 NYGKPDQKPLDKVTVEEAKKYyeegHFKAGSMGPKILAAIRFVENGGKRAIIASLEKAVEALEGKTGTRIIP 313
|
|
| PRK12353 |
PRK12353 |
putative amino acid kinase; Reviewed |
2-302 |
7.63e-128 |
|
putative amino acid kinase; Reviewed
Pssm-ID: 237071 Cd Length: 314 Bit Score: 366.79 E-value: 7.63e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 2 TKQTVVVALGGNALLRRGEplEADVQRRNIETAVKTISE-IAKVYNVVLVHGNGPQVGLLALQGLEYKKVN----PYPLD 76
Cdd:PRK12353 1 MMKKIVVALGGNALGSTPE--EATAQLEAVKKTAKSLVDlIEEGHEVVITHGNGPQVGNILLAQEAAASEKnkvpAMPLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 77 VLGSETQGMIGYMLMQEFKNYLPNRNI----SCMLTQMTVDPNDPAFADPTKPIGPIYEEAEARELAEKFHWIVKPD-GQ 151
Cdd:PRK12353 79 VCGAMSQGYIGYHLQNALRNELLKRGIdkpvATVVTQVVVDANDPAFKNPTKPIGPFYTEEEAEKLAKEKGYTFKEDaGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 152 HFRRVVPSPRPTGIVEHEAITQLIDAGHLVICTGGGGIPVKKENGKLVGVEAVIDKDMSAAFLAKQLDADALLILTDADA 231
Cdd:PRK12353 159 GYRRVVPSPKPVDIVEIEAIKTLVDAGQVVIAAGGGGIPVIREGGGLKGVEAVIDKDFASAKLAELVDADLLIILTAVDK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1515577847 232 VYLDWGKPTQHALRSTTPSELAMF----EFDAGSMGPKIEASCEFI-EQGGKVVGIGALEDGLQILQGQAGTNITK 302
Cdd:PRK12353 239 VYINFGKPNQKKLDEVTVSEAEKYieegQFAPGSMLPKVEAAISFVeSRPGRKAIITSLEKAKEALEGKAGTVIVK 314
|
|
| PRK12686 |
PRK12686 |
carbamate kinase; Reviewed |
2-302 |
3.16e-107 |
|
carbamate kinase; Reviewed
Pssm-ID: 183683 Cd Length: 312 Bit Score: 314.29 E-value: 3.16e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 2 TKQTVVVALGGNALLRRGEPLEAdvQRRNIETAVKTISE-IAKVYNVVLVHGNGPQVGLLALQ--GLEYKKVNPYPLDVL 78
Cdd:PRK12686 1 MKEKIVIALGGNAILQTEATAEA--QQTAVREAAQHLVDlIEAGHDIVITHGNGPQVGNLLLQqaESNSNKVPAMPLDTC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 79 GSETQGMIGYMLMQEFKNYLPNRNIS----CMLTQMTVDPNDPAFADPTKPIGPIYEEAEARELAEKFHWIVKPD-GQHF 153
Cdd:PRK12686 79 VAMSQGMIGYWLQNALNNELTERGIDkpviTLVTQVEVDKDDPAFANPTKPIGPFYTEEEAKQQAEQPGSTFKEDaGRGY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 154 RRVVPSPRPTGIVEHEAITQLIDAGHLVICTGGGGIPVKKENGKLVGVEAVIDKDMSAAFLAKQLDADALLILTDADAVY 233
Cdd:PRK12686 159 RRVVPSPKPQEIIEHDTIRTLVDGGNIVIACGGGGIPVIRDDNTLKGVEAVIDKDFASEKLAEQIDADLLIILTGVENVF 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1515577847 234 LDWGKPTQHALRSTTPSELAMF----EFDAGSMGPKIEASCEFIEQG-GKVVGIGALEDGLQILQGQAGTNITK 302
Cdd:PRK12686 239 INFNKPNQQKLDDITVAEAKQYiaegQFAPGSMLPKVEAAIDFVESGeGKKAIITSLEQAKEALAGNAGTHITL 312
|
|
| PRK12352 |
PRK12352 |
putative carbamate kinase; Reviewed |
3-302 |
4.47e-82 |
|
putative carbamate kinase; Reviewed
Pssm-ID: 183464 Cd Length: 316 Bit Score: 250.49 E-value: 4.47e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 3 KQTVVVALGGNALLRRGEPLEADVQRRNIETAVKTISE-IAKVYNVVLVHGNGPQVGLLALQ---GLEYKKVNPYPLDVL 78
Cdd:PRK12352 2 KELVVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEmLASDYDIVLTHGNGPQVGLDLRRaeiAHEREGLPLTPLANC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 79 GSETQGMIGYMLMQEFKNYLP---NRNISCMLTQMTVDPNDPAFADPTKPIGPIYEEAEARELAEKF-HWIVKPD-GQHF 153
Cdd:PRK12352 82 VADTQGGIGYLIQQALNNRLArhgEKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDELQKANpDWRFVEDaGRGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 154 RRVVPSPRPTGIVEHEAITQLIDAGHLVICTGGGGIPV-KKENGKLVGVEAVIDKDMSAAFLAKQLDADALLILTDADAV 232
Cdd:PRK12352 162 RRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVvRTDAGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEKV 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1515577847 233 YLDWGKPTQHALRSTTPSELAMF----EFDAGSMGPKIEASCEFIEQGGKVVGIGALEDGLQILQGQAGTNITK 302
Cdd:PRK12352 242 CIHFGKPQQQALDRVDIATMTRYmqegHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHIIK 315
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
4-277 |
3.03e-21 |
|
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: 90.12 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 4 QTVVVALGGNALlrrgepleadVQRRNIETAVKTISEI-AKVYNVVLVHGNGPQV-GLLALQGLEYKKVNPYPLDVLGSE 81
Cdd:pfam00696 1 KRVVIKLGGSSL----------TDKERLKRLADEIAALlEEGRKLVVVHGGGAFAdGLLALLGLSPRFARLTDAETLEVA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 82 TQGMIG----YMLMQEFKNYLPNRNIScmltqmtvdpndPAFADPTKpigpiyeeaearelaekfhwIVKPDGQHFRRVV 157
Cdd:pfam00696 71 TMDALGslgeRLNAALLAAGLPAVGLP------------AAQLLATE--------------------AGFIDDVVTRIDT 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 158 psprptgivehEAITQLIDAGHLVICTGGGGIPVKKENGklvgveaVIDKDMSAAFLAKQLDADALLILTDADAVYLDWG 237
Cdd:pfam00696 119 -----------EALEELLEAGVVPVITGFIGIDPEGELG-------RGSSDTLAALLAEALGADKLIILTDVDGVYTADP 180
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1515577847 238 KPTQHA--LRSTTPSELA---MFEFDAGSMGPKIEASCEFIEQGG 277
Cdd:pfam00696 181 RKVPDAklIPEISYDELLellASGLATGGMKVKLPAALEAARRGG 225
|
|
| AAK |
cd02115 |
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ... |
7-268 |
9.70e-13 |
|
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: 66.70 E-value: 9.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 7 VVALGGNALLRRGepleadvQRRNIETAVKTISEIAkvYNVVLVHGNGPQVG---LLALQGLEYKK---VNPYPLDVLGS 80
Cdd:cd02115 1 VIKFGGSSVSSEE-------RLRNLARILVKLASEG--GRVVVVHGAGPQITdelLAHGELLGYARglrITDRETDALAA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 81 ETQGMIGYMLMQefknYLPNRNIScmLTQMTVDPNDPAFADptkpigpiyeeaearelaekfhwivkpdgQHFRRVVPSp 160
Cdd:cd02115 72 MGEGMSNLLIAA----ALEQHGIK--AVPLDLTQAGFASPN-----------------------------QGHVGKITK- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 161 rptgiVEHEAITQLIDAGHLVICTGGGGIPVKkengkLVGVEAVIDKDMSAAFLAKQLDADALLILTDADAVYLDWGKPT 240
Cdd:cd02115 116 -----VSTDRLKSLLENGILPILSGFGGTDEK-----ETGTLGRGGSDSTAALLAAALKADRLVILTDVDGVYTADPRKV 185
|
250 260 270
....*....|....*....|....*....|
gi 1515577847 241 QHA--LRSTTPSELAMFEFdAGSMGPKIEA 268
Cdd:cd02115 186 PDAklLSELTYEEAAELAY-AGAMVLKPKA 214
|
|
| AAK_NAGK-like |
cd04238 |
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ... |
166-282 |
2.67e-08 |
|
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: 53.67 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 166 VEHEAITQLIDAGHL-VICTGGGGipvkkENGKLVGVEAvidkDMSAAFLAKQLDADALLILTDADAVYLDWGKPtqhaL 244
Cdd:cd04238 126 VNPELLETLLEAGYIpVIAPIAVD-----EDGETYNVNA----DTAAGAIAAALKAEKLILLTDVPGVLDDPGSL----I 192
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1515577847 245 RSTTPSELAMFEFD---AGSMGPKIEASCEFIEQGGKVVGI 282
Cdd:cd04238 193 SELTPKEAEELIEDgviSGGMIPKVEAALEALEGGVRKVHI 233
|
|
| ArgB |
COG0548 |
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ... |
4-278 |
2.46e-07 |
|
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: 51.19 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 4 QTVVVALGGNALlrrgeplEADVQRRNIetaVKTISEIAKV-YNVVLVHGNGPQVG-LLALQGLEYKKVN---------- 71
Cdd:COG0548 24 KTFVIKYGGEAM-------EDEELKAAL---AQDIALLKSLgIRPVLVHGGGPQINeLLKRLGIESEFVNglrvtdeetl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 72 PYPLDVLGsetqGMIGYMLMQEFKNYLPN-RNIS----CMLTqmtvdpndpafADPTKPIGPIyeeaearelaekfhwiv 146
Cdd:COG0548 94 EVVEMVLA----GKVNKEIVALLSQGGGNaVGLSgkdgNLIT-----------ARPLGVGDGV----------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 147 kpDGQHfrrvvpsprpTGIVEH---EAITQLIDAGHLVI--CTGGGgipvkkENGKLVGVEAvidkDMSAAFLAKQLDAD 221
Cdd:COG0548 142 --DLGH----------VGEVRRvdpELIRALLDAGYIPVisPIGYS------PTGEVYNINA----DTVAGAIAAALKAE 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 222 ALLILTDADAVYldwGKPTQHaLRSTTPSEL-AMFE--FDAGSMGPKIEASCEFIEQGGK 278
Cdd:COG0548 200 KLILLTDVPGVL---DDPGSL-ISELTAAEAeELIAdgVISGGMIPKLEAALDAVRGGVK 255
|
|
| AAK_NAGK-UC |
cd04251 |
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ... |
163-300 |
5.68e-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: 49.67 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 163 TGIVEH---EAITQLIDAGHLVICT----GGGGIPVKkengklvgveavIDKDMSAAFLAKQLDADALLILTDADAVYLD 235
Cdd:cd04251 127 TGKVEKvnsDLIEALLDAGYLPVVSpvaySEEGEPLN------------VDGDRAAAAIAAALKAERLILLTDVEGLYLD 194
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1515577847 236 wGKptqhALRSTTPSEL-AMFEFDAGSMGPKIEASCEFIEQGGKVVGIG-ALEDG--LQILQGQaGTNI 300
Cdd:cd04251 195 -GR----VIERITVSDAeSLLEKAGGGMKRKLLAAAEAVEGGVREVVIGdARADSpiSSALNGG-GTVI 257
|
|
| AAK_NAGK-C |
cd04250 |
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ... |
169-282 |
7.23e-06 |
|
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: 46.73 E-value: 7.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 169 EAITQLIDAGHL-VICTGGGGipvkkENGKLVGVEAvidkDMSAAFLAKQLDADALLILTDADAVYLDWGKPTQhALRST 247
Cdd:cd04250 149 ELLETLLEAGYIpVIAPVGVG-----EDGETYNINA----DTAAGAIAAALKAEKLILLTDVAGVLDDPNDPGS-LISEI 218
|
90 100 110
....*....|....*....|....*....|....*...
gi 1515577847 248 TPSELAMFEFD---AGSMGPKIEASCEFIEQGGKVVGI 282
Cdd:cd04250 219 SLKEAEELIADgiiSGGMIPKVEACIEALEGGVKAAHI 256
|
|
| PRK00942 |
PRK00942 |
acetylglutamate kinase; Provisional |
169-303 |
8.27e-06 |
|
acetylglutamate kinase; Provisional
Pssm-ID: 234869 [Multi-domain] Cd Length: 283 Bit Score: 46.25 E-value: 8.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 169 EAITQLIDAGHL-VICTGGGGipvkkENGKLVGVEAvidkDMSAAFLAKQLDADALLILTDADAVYLDWGKPtqhaLRST 247
Cdd:PRK00942 153 ALLEALLEAGYIpVISPIGVG-----EDGETYNINA----DTAAGAIAAALGAEKLILLTDVPGVLDDKGQL----ISEL 219
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1515577847 248 TPSELAMFEFD---AGSMGPKIEASCEFIEQGGKVVGIGaleDG-------LQILQGQA-GTNITKG 303
Cdd:PRK00942 220 TASEAEELIEDgviTGGMIPKVEAALDAARGGVRSVHII---DGrvphallLELFTDEGiGTMIVPD 283
|
|
| argB |
TIGR00761 |
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ... |
166-282 |
4.30e-05 |
|
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: 43.81 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515577847 166 VEHEAITQLIDAGHLVICTGgggiPVKKENGKLVGVEAvidkDMSAAFLAKQLDADALLILTDADAVYLDWGKPTQHALR 245
Cdd:TIGR00761 123 VNKALIEALLKAGYIPVISS----LALTAEGQALNVNA----DTAAGALAAALGAEKLVLLTDVPGILNGDGQSLISEIP 194
|
90 100 110
....*....|....*....|....*....|....*..
gi 1515577847 246 STTPSELAMFEFDAGSMGPKIEASCEFIEQGGKVVGI 282
Cdd:TIGR00761 195 LDEIEQLIKQGIIKGGMIPKVNAALEALRGGVRSVHI 231
|
|
| AAK_G5K_ProB |
cd04242 |
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ... |
206-233 |
1.06e-03 |
|
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: 39.73 E-value: 1.06e-03
10 20
....*....|....*....|....*...
gi 1515577847 206 DKDMSAAFLAKQLDADALLILTDADAVY 233
Cdd:cd04242 143 DNDRLSALVAGLVNADLLILLSDVDGLY 170
|
|
| |
