|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09411 |
PRK09411 |
carbamate kinase; Reviewed |
1-297 |
0e+00 |
|
carbamate kinase; Reviewed
Pssm-ID: 181831 Cd Length: 297 Bit Score: 582.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 1 MKTLVVALGGNALLQRGEALTAENQYRNIASAVPALARLARSYRLAIVHGNGPQVGLLALQNLAWKEVEPYPLDVLVAES 80
Cdd:PRK09411 1 MKTLVVALGGNALLQRGEALTAENQYRNIASAVPALARLARSYRLAIVHGNGPQVGLLALQNLAWKEVEPYPLDVLVAES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 81 QGMIGYMLAQSLSAQPQMPPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAYGWQMKRDGKYLRRVVASPQP 160
Cdd:PRK09411 81 QGMIGYMLAQSLSAQPQMPPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAYGWQMKRDGKYLRRVVASPQP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 161 RKILDSEAIELLLKEGHVVICSGGGGVPVTDDGAGSEAVIDKDLAAALLAEQINADGLVILTDADAVYENWGTPQQRAIR 240
Cdd:PRK09411 161 RKILDSEAIELLLKEGHVVICSGGGGVPVTEDGAGSEAVIDKDLAAALLAEQINADGLVILTDADAVYENWGTPQQRAIR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446778123 241 HATPDELAPFAKADGSMGPNVTAVSGYVRSRGKPAWIGALSRIEETLAGEAGTCISL 297
Cdd:PRK09411 241 HATPDELAPFAKADGAMGPKVTAVSGYVRSRGKPAWIGALSRIEETLAGEAGTCISL 297
|
|
| arcC |
TIGR00746 |
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes ... |
2-297 |
1.43e-164 |
|
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: 459.23 E-value: 1.43e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 2 KTLVVALGGNALLQRGEALTAENQYRNIASAVPALARLA-RSYRLAIVHGNGPQVGLLALQNLAWK-EVEPYPLDVLVAE 79
Cdd:TIGR00746 1 KRVVVALGGNALLQRGEKGSAEAQRDNVRQTAPQIAKLIkRGYELVITHGNGPQVGNLLLQNQAADsEVPAMPLDVLGAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 80 SQGMIGYMLAQSLS----AQPQMPPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAYGWQMKRD-GKYLRRV 154
Cdd:TIGR00746 81 SQGMIGYMLQQALNnelpKRGMEKPVATVLTQTIVDPKDPAFQNPTKPIGPFYTEEEAKRLAAEKGWIVKEDaGRGWRRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 155 VASPQPRKILDSEAIELLLKEGHVVICSGGGGVPVTDDGA---GSEAVIDKDLAAALLAEQINADGLVILTDADAVYENW 231
Cdd:TIGR00746 161 VPSPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEGAelkGVEAVIDKDLASEKLAEEVNADILVILTDVDAVYINY 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 232 GTPQQRAIRHATPDELAPFAK----ADGSMGPNVTAVSGYVRSRGKPAWIGALSRIEETLAGEAGTCISL 297
Cdd:TIGR00746 241 GKPDEKALREVTVEELEDYYKaghfAAGSMGPKVEAAIEFVESGGKRAIITSLENAVEALEGKAGTRVTK 310
|
|
| ArcC |
COG0549 |
Carbamate kinase [Amino acid transport and metabolism]; |
1-296 |
1.48e-161 |
|
Carbamate kinase [Amino acid transport and metabolism];
Pssm-ID: 440315 Cd Length: 313 Bit Score: 451.84 E-value: 1.48e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 1 MKTLVVALGGNALLQRGEALTAENQYRNIASAVPALARLARS-YRLAIVHGNGPQVGLLALQNLAWK-EVEPYPLDVLVA 78
Cdd:COG0549 2 KKRIVVALGGNALLRRGEPGTAEEQRENVREAAKALADLIEAgHEVVITHGNGPQVGLLLLQNEAAKkKVPPMPLDVCGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 79 ESQGMIGYMLAQS----LSAQPQMPPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAYGWQMKRD-GKYLRR 153
Cdd:COG0549 82 MTQGMIGYMLQQAlrneLPKRGIDKPVATLVTQVEVDPDDPAFQNPTKPIGPFYTEEEAEELAKEKGWTFKEDaGRGYRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 154 VVASPQPRKILDSEAIELLLKEGHVVICSGGGGVPVTDDGAGS----EAVIDKDLAAALLAEQINADGLVILTDADAVYE 229
Cdd:COG0549 162 VVPSPKPKRIVEIDAIKALLEAGVIVIAAGGGGIPVVRDEDGGlkgvEAVIDKDLASALLAEELDADLLLILTDVDKVYI 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446778123 230 NWGTPQQRAIRHATPDELAPFAK----ADGSMGPNVTAVSGYVRSRGKPAWIGALSRIEETLAGEAGTCIS 296
Cdd:COG0549 242 NFGKPDQRALDEVTVAEAKKYIEeghfAAGSMGPKVEAAIRFVEATGKRAIITSLEKAEEALAGKAGTRIV 312
|
|
| AAK_CK |
cd04235 |
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ... |
3-296 |
8.87e-157 |
|
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: 439.64 E-value: 8.87e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 3 TLVVALGGNALLQRGEALTAENQYRNIASAVPALARLARS-YRLAIVHGNGPQVGLLALQNLAW-KEVEPYPLDVLVAES 80
Cdd:cd04235 1 RIVVALGGNALLRRGEPGTAEEQRENVKIAAKALADLIKNgHEVVITHGNGPQVGNLLLQNEAAaEKVPAYPLDVCGAMS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 81 QGMIGYMLAQSLSAQPQM----PPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAYGWQMKRD-GKYLRRVV 155
Cdd:cd04235 81 QGMIGYMLQQALDNELPKrgidKPVVTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEKGWTFKEDaGRGYRRVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 156 ASPQPRKILDSEAIELLLKEGHVVICSGGGGVPVTDDG---AGSEAVIDKDLAAALLAEQINADGLVILTDADAVYENWG 232
Cdd:cd04235 161 PSPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREGgglKGVEAVIDKDLASALLAEEINADLLVILTDVDNVYINFG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446778123 233 TPQQRAIRHATPDELAPFAK----ADGSMGPNVTAVSGYVRSRGKPAWIGALSRIEETLAGEAGTCIS 296
Cdd:cd04235 241 KPNQKALEQVTVEELEKYIEegqfAPGSMGPKVEAAIRFVESGGKKAIITSLENAEAALEGKAGTVIV 308
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
2-277 |
2.14e-19 |
|
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: 84.73 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 2 KTLVVALGGNALlqrgealTAENQYRNIASAVPALarLARSYRLAIVHGNGPQV-GLLALQNLAWKEV--------EPYP 72
Cdd:pfam00696 1 KRVVIKLGGSSL-------TDKERLKRLADEIAAL--LEEGRKLVVVHGGGAFAdGLLALLGLSPRFArltdaetlEVAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 73 LDVLVAESQGMIGYMLAQSLSAQPqMPPVTTVLTRIEVSPDdpaflqpekfigpvyqpeeqealeaaygwqmkrdgkylr 152
Cdd:pfam00696 72 MDALGSLGERLNAALLAAGLPAVG-LPAAQLLATEAGFIDD--------------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 153 rvvaspqPRKILDSEAIELLLKEGHVVICSGGGGVpvtdDGAGSEAVIDKDLAAALLAEQINADGLVILTDADAVYENWG 232
Cdd:pfam00696 112 -------VVTRIDTEALEELLEAGVVPVITGFIGI----DPEGELGRGSSDTLAALLAEALGADKLIILTDVDGVYTADP 180
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446778123 233 TPQQRA-----IRHATPDELAPFAKADGSMGPNVTAVSGYVRSRGKPAWI 277
Cdd:pfam00696 181 RKVPDAklipeISYDELLELLASGLATGGMKVKLPAALEAARRGGIPVVI 230
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09411 |
PRK09411 |
carbamate kinase; Reviewed |
1-297 |
0e+00 |
|
carbamate kinase; Reviewed
Pssm-ID: 181831 Cd Length: 297 Bit Score: 582.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 1 MKTLVVALGGNALLQRGEALTAENQYRNIASAVPALARLARSYRLAIVHGNGPQVGLLALQNLAWKEVEPYPLDVLVAES 80
Cdd:PRK09411 1 MKTLVVALGGNALLQRGEALTAENQYRNIASAVPALARLARSYRLAIVHGNGPQVGLLALQNLAWKEVEPYPLDVLVAES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 81 QGMIGYMLAQSLSAQPQMPPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAYGWQMKRDGKYLRRVVASPQP 160
Cdd:PRK09411 81 QGMIGYMLAQSLSAQPQMPPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAYGWQMKRDGKYLRRVVASPQP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 161 RKILDSEAIELLLKEGHVVICSGGGGVPVTDDGAGSEAVIDKDLAAALLAEQINADGLVILTDADAVYENWGTPQQRAIR 240
Cdd:PRK09411 161 RKILDSEAIELLLKEGHVVICSGGGGVPVTEDGAGSEAVIDKDLAAALLAEQINADGLVILTDADAVYENWGTPQQRAIR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446778123 241 HATPDELAPFAKADGSMGPNVTAVSGYVRSRGKPAWIGALSRIEETLAGEAGTCISL 297
Cdd:PRK09411 241 HATPDELAPFAKADGAMGPKVTAVSGYVRSRGKPAWIGALSRIEETLAGEAGTCISL 297
|
|
| PRK12354 |
PRK12354 |
carbamate kinase; Reviewed |
3-296 |
1.73e-166 |
|
carbamate kinase; Reviewed
Pssm-ID: 183466 Cd Length: 307 Bit Score: 463.92 E-value: 1.73e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 3 TLVVALGGNALLQRGEALTAENQYRNIASAVPALARLARSYRLAIVHGNGPQVGLLALQNLAWKEVEPYPLDVLVAESQG 82
Cdd:PRK12354 2 RIVVALGGNALLRRGEPLTAENQRANIRIAAEQIAKIAREHELVIVHGNGPQVGLLALQNAAYKDVTPYPLDVLGAETEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 83 MIGYMLAQSLsaQPQMP--PVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAYGWQMKRDGKYLRRVVASPQP 160
Cdd:PRK12354 82 MIGYMLEQEL--GNLLPerPVATLLTQVEVDANDPAFANPTKPIGPVYDEAEAERLAAEKGWTIKPDGDYFRRVVPSPRP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 161 RKILDSEAIELLLKEGHVVICSGGGGVPVTDDGAGS----EAVIDKDLAAALLAEQINADGLVILTDADAVYENWGTPQQ 236
Cdd:PRK12354 160 KRIVEIRPIRWLLEKGHLVICAGGGGIPVVYDADGKlhgvEAVIDKDLAAALLAEQLDADLLLILTDVDAVYLDWGKPTQ 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 237 RAIRHATPDELAPFAKADGSMGPNVTAVSGYVRSRGKPAWIGALSRIEETLAGEAGTCIS 296
Cdd:PRK12354 240 RAIAQATPDELRELGFAAGSMGPKVEAACEFVRATGKIAGIGSLEDIQAILAGEAGTRIS 299
|
|
| arcC |
TIGR00746 |
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes ... |
2-297 |
1.43e-164 |
|
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: 459.23 E-value: 1.43e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 2 KTLVVALGGNALLQRGEALTAENQYRNIASAVPALARLA-RSYRLAIVHGNGPQVGLLALQNLAWK-EVEPYPLDVLVAE 79
Cdd:TIGR00746 1 KRVVVALGGNALLQRGEKGSAEAQRDNVRQTAPQIAKLIkRGYELVITHGNGPQVGNLLLQNQAADsEVPAMPLDVLGAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 80 SQGMIGYMLAQSLS----AQPQMPPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAYGWQMKRD-GKYLRRV 154
Cdd:TIGR00746 81 SQGMIGYMLQQALNnelpKRGMEKPVATVLTQTIVDPKDPAFQNPTKPIGPFYTEEEAKRLAAEKGWIVKEDaGRGWRRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 155 VASPQPRKILDSEAIELLLKEGHVVICSGGGGVPVTDDGA---GSEAVIDKDLAAALLAEQINADGLVILTDADAVYENW 231
Cdd:TIGR00746 161 VPSPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEGAelkGVEAVIDKDLASEKLAEEVNADILVILTDVDAVYINY 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 232 GTPQQRAIRHATPDELAPFAK----ADGSMGPNVTAVSGYVRSRGKPAWIGALSRIEETLAGEAGTCISL 297
Cdd:TIGR00746 241 GKPDEKALREVTVEELEDYYKaghfAAGSMGPKVEAAIEFVESGGKRAIITSLENAVEALEGKAGTRVTK 310
|
|
| ArcC |
COG0549 |
Carbamate kinase [Amino acid transport and metabolism]; |
1-296 |
1.48e-161 |
|
Carbamate kinase [Amino acid transport and metabolism];
Pssm-ID: 440315 Cd Length: 313 Bit Score: 451.84 E-value: 1.48e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 1 MKTLVVALGGNALLQRGEALTAENQYRNIASAVPALARLARS-YRLAIVHGNGPQVGLLALQNLAWK-EVEPYPLDVLVA 78
Cdd:COG0549 2 KKRIVVALGGNALLRRGEPGTAEEQRENVREAAKALADLIEAgHEVVITHGNGPQVGLLLLQNEAAKkKVPPMPLDVCGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 79 ESQGMIGYMLAQS----LSAQPQMPPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAYGWQMKRD-GKYLRR 153
Cdd:COG0549 82 MTQGMIGYMLQQAlrneLPKRGIDKPVATLVTQVEVDPDDPAFQNPTKPIGPFYTEEEAEELAKEKGWTFKEDaGRGYRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 154 VVASPQPRKILDSEAIELLLKEGHVVICSGGGGVPVTDDGAGS----EAVIDKDLAAALLAEQINADGLVILTDADAVYE 229
Cdd:COG0549 162 VVPSPKPKRIVEIDAIKALLEAGVIVIAAGGGGIPVVRDEDGGlkgvEAVIDKDLASALLAEELDADLLLILTDVDKVYI 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446778123 230 NWGTPQQRAIRHATPDELAPFAK----ADGSMGPNVTAVSGYVRSRGKPAWIGALSRIEETLAGEAGTCIS 296
Cdd:COG0549 242 NFGKPDQRALDEVTVAEAKKYIEeghfAAGSMGPKVEAAIRFVEATGKRAIITSLEKAEEALAGKAGTRIV 312
|
|
| AAK_CK |
cd04235 |
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ... |
3-296 |
8.87e-157 |
|
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: 439.64 E-value: 8.87e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 3 TLVVALGGNALLQRGEALTAENQYRNIASAVPALARLARS-YRLAIVHGNGPQVGLLALQNLAW-KEVEPYPLDVLVAES 80
Cdd:cd04235 1 RIVVALGGNALLRRGEPGTAEEQRENVKIAAKALADLIKNgHEVVITHGNGPQVGNLLLQNEAAaEKVPAYPLDVCGAMS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 81 QGMIGYMLAQSLSAQPQM----PPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAYGWQMKRD-GKYLRRVV 155
Cdd:cd04235 81 QGMIGYMLQQALDNELPKrgidKPVVTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEKGWTFKEDaGRGYRRVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 156 ASPQPRKILDSEAIELLLKEGHVVICSGGGGVPVTDDG---AGSEAVIDKDLAAALLAEQINADGLVILTDADAVYENWG 232
Cdd:cd04235 161 PSPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREGgglKGVEAVIDKDLASALLAEEINADLLVILTDVDNVYINFG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446778123 233 TPQQRAIRHATPDELAPFAK----ADGSMGPNVTAVSGYVRSRGKPAWIGALSRIEETLAGEAGTCIS 296
Cdd:cd04235 241 KPNQKALEQVTVEELEKYIEegqfAPGSMGPKVEAAIRFVESGGKKAIITSLENAEAALEGKAGTVIV 308
|
|
| PRK12353 |
PRK12353 |
putative amino acid kinase; Reviewed |
1-295 |
2.77e-121 |
|
putative amino acid kinase; Reviewed
Pssm-ID: 237071 Cd Length: 314 Bit Score: 349.84 E-value: 2.77e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 1 MKTLVVALGGNALLQRGEALTAenQYRNIASAVPALARL-ARSYRLAIVHGNGPQVGLLALQNLAWKEVE----PYPLDV 75
Cdd:PRK12353 2 MKKIVVALGGNALGSTPEEATA--QLEAVKKTAKSLVDLiEEGHEVVITHGNGPQVGNILLAQEAAASEKnkvpAMPLDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 76 LVAESQGMIGYMLAQS----LSAQPQMPPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAYGWQMKRD-GKY 150
Cdd:PRK12353 80 CGAMSQGYIGYHLQNAlrneLLKRGIDKPVATVVTQVVVDANDPAFKNPTKPIGPFYTEEEAEKLAKEKGYTFKEDaGRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 151 LRRVVASPQPRKILDSEAIELLLKEGHVVICSGGGGVPVTDDG---AGSEAVIDKDLAAALLAEQINADGLVILTDADAV 227
Cdd:PRK12353 160 YRRVVPSPKPVDIVEIEAIKTLVDAGQVVIAAGGGGIPVIREGgglKGVEAVIDKDFASAKLAELVDADLLIILTAVDKV 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446778123 228 YENWGTPQQRAIRHATPDELAPFAK----ADGSMGPNVTAVSGYVRSR-GKPAWIGALSRIEETLAGEAGTCI 295
Cdd:PRK12353 240 YINFGKPNQKKLDEVTVSEAEKYIEegqfAPGSMLPKVEAAISFVESRpGRKAIITSLEKAKEALEGKAGTVI 312
|
|
| PRK12454 |
PRK12454 |
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed |
1-296 |
8.05e-120 |
|
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
Pssm-ID: 183535 Cd Length: 313 Bit Score: 346.21 E-value: 8.05e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 1 MKTLVVALGGNALLQRGEALTAENQYRNIASAVPALARL-ARSYRLAIVHGNGPQVGLLALQNLAWKEV--EPYPLDVLV 77
Cdd:PRK12454 2 KKRIVIALGGNALLQPGEKGTAENQMKNVRKTAKQIADLiEEGYEVVITHGNGPQVGNLLLQMDAAKDVgiPPFPLDVAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 78 AESQGMIGYMLAQSLsaQPQMP------PVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAYGWQMKRD-GKY 150
Cdd:PRK12454 82 AMTQGWIGYMIQQAL--RNELAkrgiekQVATIVTQVIVDKNDPAFQNPTKPVGPFYDEEEAKKLAKEKGWIVKEDaGRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 151 LRRVVASPQPRKILDSEAIELLLKEGHVVICSGGGGVPVTDDGA---GSEAVIDKDLAAALLAEQINADGLVILTDADAV 227
Cdd:PRK12454 160 WRRVVPSPDPLGIVEIEVIKALVENGFIVIASGGGGIPVIEEDGelkGVEAVIDKDLASELLAEELNADIFIILTDVEKV 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446778123 228 YENWGTPQQRAIRHATPDELAPFAK----ADGSMGPNVTAVSGYVRSRGKPAWIGALSRIEETLAGEAGTCIS 296
Cdd:PRK12454 240 YLNYGKPDQKPLDKVTVEEAKKYYEeghfKAGSMGPKILAAIRFVENGGKRAIIASLEKAVEALEGKTGTRII 312
|
|
| PRK12686 |
PRK12686 |
carbamate kinase; Reviewed |
1-297 |
2.60e-98 |
|
carbamate kinase; Reviewed
Pssm-ID: 183683 Cd Length: 312 Bit Score: 291.56 E-value: 2.60e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 1 MKTLVVALGGNALLQRGEalTAENQYRNIASAVPALARL-ARSYRLAIVHGNGPQVGLLALQ--NLAWKEVEPYPLDVLV 77
Cdd:PRK12686 2 KEKIVIALGGNAILQTEA--TAEAQQTAVREAAQHLVDLiEAGHDIVITHGNGPQVGNLLLQqaESNSNKVPAMPLDTCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 78 AESQGMIGYMLAQSLSAQPQM----PPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAYGWQMKRD-GKYLR 152
Cdd:PRK12686 80 AMSQGMIGYWLQNALNNELTErgidKPVITLVTQVEVDKDDPAFANPTKPIGPFYTEEEAKQQAEQPGSTFKEDaGRGYR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 153 RVVASPQPRKILDSEAIELLLKEGHVVICSGGGGVPVTDDGA---GSEAVIDKDLAAALLAEQINADGLVILTDADAVYE 229
Cdd:PRK12686 160 RVVPSPKPQEIIEHDTIRTLVDGGNIVIACGGGGIPVIRDDNtlkGVEAVIDKDFASEKLAEQIDADLLIILTGVENVFI 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446778123 230 NWGTPQQRAIRHATPDELAPFAK----ADGSMGPNVTAVSGYVRSR-GKPAWIGALSRIEETLAGEAGTCISL 297
Cdd:PRK12686 240 NFNKPNQQKLDDITVAEAKQYIAegqfAPGSMLPKVEAAIDFVESGeGKKAIITSLEQAKEALAGNAGTHITL 312
|
|
| PRK12352 |
PRK12352 |
putative carbamate kinase; Reviewed |
1-295 |
1.78e-75 |
|
putative carbamate kinase; Reviewed
Pssm-ID: 183464 Cd Length: 316 Bit Score: 233.54 E-value: 1.78e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 1 MKTL-VVALGGNALLQRGEALTAENQYRNI-ASAVPALARLARSYRLAIVHGNGPQVGLLALQNLAWKEVEPYP---LDV 75
Cdd:PRK12352 1 MKELvVVAIGGNSIIKDNASQSIEHQAEAVkAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHEREGLPltpLAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 76 LVAESQGMIGYMLAQSLS---AQPQMPPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAY-GWQMKRD-GKY 150
Cdd:PRK12352 81 CVADTQGGIGYLIQQALNnrlARHGEKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDELQKANpDWRFVEDaGRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 151 LRRVVASPQPRKILDSEAIELLLKEGHVVICSGGGGVPVTDDGAGS----EAVIDKDLAAALLAEQINADGLVILTDADA 226
Cdd:PRK12352 161 YRRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDAGDyqsvDAVIDKDLSTALLAREIHADILVITTGVEK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446778123 227 VYENWGTPQQRAIRHATPDELAPFAK----ADGSMGPNVTAVSGYVRSRGKPAWIGALSRIEETLAGEAGTCI 295
Cdd:PRK12352 241 VCIHFGKPQQQALDRVDIATMTRYMQeghfPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHI 313
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
2-277 |
2.14e-19 |
|
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: 84.73 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 2 KTLVVALGGNALlqrgealTAENQYRNIASAVPALarLARSYRLAIVHGNGPQV-GLLALQNLAWKEV--------EPYP 72
Cdd:pfam00696 1 KRVVIKLGGSSL-------TDKERLKRLADEIAAL--LEEGRKLVVVHGGGAFAdGLLALLGLSPRFArltdaetlEVAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 73 LDVLVAESQGMIGYMLAQSLSAQPqMPPVTTVLTRIEVSPDdpaflqpekfigpvyqpeeqealeaaygwqmkrdgkylr 152
Cdd:pfam00696 72 MDALGSLGERLNAALLAAGLPAVG-LPAAQLLATEAGFIDD--------------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 153 rvvaspqPRKILDSEAIELLLKEGHVVICSGGGGVpvtdDGAGSEAVIDKDLAAALLAEQINADGLVILTDADAVYENWG 232
Cdd:pfam00696 112 -------VVTRIDTEALEELLEAGVVPVITGFIGI----DPEGELGRGSSDTLAALLAEALGADKLIILTDVDGVYTADP 180
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446778123 233 TPQQRA-----IRHATPDELAPFAKADGSMGPNVTAVSGYVRSRGKPAWI 277
Cdd:pfam00696 181 RKVPDAklipeISYDELLELLASGLATGGMKVKLPAALEAARRGGIPVVI 230
|
|
| AAK |
cd02115 |
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ... |
5-295 |
1.48e-16 |
|
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: 77.48 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 5 VVALGGNaLLQRGEALtaenqyRNIASAVPALARLArsYRLAIVHGNGPQVG--LLALQNLAW----KEVEPYPLDVLVA 78
Cdd:cd02115 1 VIKFGGS-SVSSEERL------RNLARILVKLASEG--GRVVVVHGAGPQITdeLLAHGELLGyargLRITDRETDALAA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 79 ESQGMIGYMLAQSLSaqpqmppvttvltrievspddpaflqpEKFIGPVYQpeeqealeAAYGWQMKRDGKYLRRVVASp 158
Cdd:cd02115 72 MGEGMSNLLIAAALE---------------------------QHGIKAVPL--------DLTQAGFASPNQGHVGKITK- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 159 qprkiLDSEAIELLLKEGHVVICSGGGGVPvtDDGAGSEAVIDKDLAAALLAEQINADGLVILTDADAVYENWGT--PQQ 236
Cdd:cd02115 116 -----VSTDRLKSLLENGILPILSGFGGTD--EKETGTLGRGGSDSTAALLAAALKADRLVILTDVDGVYTADPRkvPDA 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446778123 237 RAIRHATPDELAPFAKAdGSMGPNVTAVSGYVRSrGKPAWIGA---LSRIEETLAGEAGTCI 295
Cdd:cd02115 189 KLLSELTYEEAAELAYA-GAMVLKPKAADPAARA-GIPVRIANtenPGALALFTPDGGGTLI 248
|
|
| AAK_UMPK-like |
cd04239 |
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ... |
167-247 |
1.91e-07 |
|
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: 51.00 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 167 EAIELLlKEGHVVICSGGGGVP--VTDDgagseavidkdlAAALLAEQINADGLVILTDADAVYE-----NwgtPQQRAI 239
Cdd:cd04239 110 RAIRHL-EKGRIVIFGGGTGNPgfTTDT------------AAALRAEEIGADVLLKATNVDGVYDadpkkN---PDAKKY 173
|
....*...
gi 446778123 240 RHATPDEL 247
Cdd:cd04239 174 DRISYDEL 181
|
|
| AAK_NAGK-like |
cd04238 |
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ... |
165-263 |
1.14e-06 |
|
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the Escherichia coli and Pseudomonas aeruginosa type NAGKs which catalyze the phosphorylation of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in bacteria and photosynthetic organisms using either the acetylated, noncyclic (NC), or non-acetylated, cyclic (C) route of ornithine biosynthesis. Also included in this CD is a distinct group of uncharacterized (UC) bacterial and archeal NAGKs. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239771 [Multi-domain] Cd Length: 256 Bit Score: 48.66 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 165 DSEAIELLLKEGHV-VICSggggVPVTDDGagsEAV-IDKDLAAALLAEQINADGLVILTDADAVYENWGTPqqraIRHA 242
Cdd:cd04238 127 NPELLETLLEAGYIpVIAP----IAVDEDG---ETYnVNADTAAGAIAAALKAEKLILLTDVPGVLDDPGSL----ISEL 195
|
90 100
....*....|....*....|....
gi 446778123 243 TPDE---LAPFAKADGSMGPNVTA 263
Cdd:cd04238 196 TPKEaeeLIEDGVISGGMIPKVEA 219
|
|
| AAK_NAGK-UC |
cd04251 |
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ... |
141-269 |
4.25e-06 |
|
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: 46.98 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 141 GWQMKRDGKYLRRVvaspqprKILDSEAIELLLKEGHVVICSggggvPVTDDGAGSEAVIDKDLAAALLAEQINADGLVI 220
Cdd:cd04251 117 GRKMIIRGGYTGKV-------EKVNSDLIEALLDAGYLPVVS-----PVAYSEEGEPLNVDGDRAAAAIAAALKAERLIL 184
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 446778123 221 LTDADAVYENwgtpqQRAIRHATPDELAPFA-KADGSMGPNV----TAVSGYVR 269
Cdd:cd04251 185 LTDVEGLYLD-----GRVIERITVSDAESLLeKAGGGMKRKLlaaaEAVEGGVR 233
|
|
| AAK_NAGK-C |
cd04250 |
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ... |
165-247 |
9.92e-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: 45.96 E-value: 9.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 165 DSEAIELLLKEGHV-VICSggggVPVTDDGAGSEavIDKDLAAALLAEQINADGLVILTDADAVYENWGTPQQRaIRHAT 243
Cdd:cd04250 147 NPELLETLLEAGYIpVIAP----VGVGEDGETYN--INADTAAGAIAAALKAEKLILLTDVAGVLDDPNDPGSL-ISEIS 219
|
....
gi 446778123 244 PDEL 247
Cdd:cd04250 220 LKEA 223
|
|
| PRK14058 |
PRK14058 |
[LysW]-aminoadipate/[LysW]-glutamate kinase; |
165-257 |
1.73e-05 |
|
[LysW]-aminoadipate/[LysW]-glutamate kinase;
Pssm-ID: 237599 [Multi-domain] Cd Length: 268 Bit Score: 45.28 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 165 DSEAIELLLKEGHVVICSggggvPVTDDGAGSEAVIDKDLAAALLAEQINADGLVILTDADAVYENWGTPqQRAIRHATP 244
Cdd:PRK14058 138 NTDLLKLLLKAGYLPVVA-----PPALSEEGEPLNVDGDRAAAAIAGALKAEALVLLSDVPGLLRDPPDE-GSLIERITP 211
|
90
....*....|....
gi 446778123 245 DEL-APFAKADGSM 257
Cdd:PRK14058 212 EEAeELSKAAGGGM 225
|
|
| PRK00942 |
PRK00942 |
acetylglutamate kinase; Provisional |
165-248 |
1.00e-04 |
|
acetylglutamate kinase; Provisional
Pssm-ID: 234869 [Multi-domain] Cd Length: 283 Bit Score: 43.17 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 165 DSEAIELLLKEGHV-VICSggggVPVTDDGagsEAV-IDKDLAAALLAEQINADGLVILTDADAVYENWGTPqqraIRHA 242
Cdd:PRK00942 151 NPALLEALLEAGYIpVISP----IGVGEDG---ETYnINADTAAGAIAAALGAEKLILLTDVPGVLDDKGQL----ISEL 219
|
....*.
gi 446778123 243 TPDELA 248
Cdd:PRK00942 220 TASEAE 225
|
|
| ArgB |
COG0548 |
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ... |
160-247 |
2.09e-04 |
|
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: 41.94 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 160 PRKIlDSEAIELLLKEGHVVICSggggvPV--TDDGagsEAV-IDKDLAAALLAEQINADGLVILTDADAVYENwgtpQQ 236
Cdd:COG0548 149 VRRV-DPELIRALLDAGYIPVIS-----PIgySPTG---EVYnINADTVAGAIAAALKAEKLILLTDVPGVLDD----PG 215
|
90
....*....|.
gi 446778123 237 RAIRHATPDEL 247
Cdd:COG0548 216 SLISELTAAEA 226
|
|
| AAK_G5K_ProB |
cd04242 |
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ... |
201-228 |
3.30e-04 |
|
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: 41.27 E-value: 3.30e-04
10 20
....*....|....*....|....*...
gi 446778123 201 DKDLAAALLAEQINADGLVILTDADAVY 228
Cdd:cd04242 143 DNDRLSALVAGLVNADLLILLSDVDGLY 170
|
|
| AAK_UMPK-PyrH-Pf |
cd04253 |
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ... |
203-247 |
1.49e-03 |
|
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: 39.15 E-value: 1.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 446778123 203 DLAAALLAEQINADGLVILTDADAVYEnwGTPQQ----RAIRHATPDEL 247
Cdd:cd04253 118 DAVAALLAERLGADLLINATNVDGVYS--KDPRKdpdaKKFDRLSADEL 164
|
|
| AAK_UMPK-PyrH-Ec |
cd04254 |
UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) ... |
173-228 |
2.69e-03 |
|
UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) enzyme that catalyzes UMP phosphorylation and plays a key role in pyrimidine nucleotide biosynthesis; regulation of this process is via feed-back control and via gene repression of carbamoyl phosphate synthetase (the first enzyme of the pyrimidine biosynthesis pathway). The UMP kinase of E. coli (Ec) is known to function as a homohexamer, with GTP and UTP being allosteric effectors. Like other related enzymes (carbamate kinase, aspartokinase, and N-acetylglutamate kinase) the E. coli and most bacterial and chloroplast UMPKs (this CD) have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs appear to lack this residue and the Pyrococcus furiosus structure has an additional Mg ion bound to the ATP molecule which is proposed to function as the catalysis instead. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239787 [Multi-domain] Cd Length: 231 Bit Score: 38.24 E-value: 2.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446778123 173 LKEGHVVICSGGGGVP-VTddgagseavidKDLAAALLAEQINADGLVILTDADAVY 228
Cdd:cd04254 117 LEKGRVVIFAGGTGNPfFT-----------TDTAAALRAIEINADVILKATKVDGVY 162
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| MetL1 |
COG0527 |
Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the ... |
141-228 |
4.20e-03 |
|
Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 440293 [Multi-domain] Cd Length: 407 Bit Score: 38.52 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446778123 141 GWQ--MKRDGKYLRrvvasPQPRKILDSEAIELLLKEGHVVICSGGGGVpvTDDGA-------GSeavidkDLAAALLAE 211
Cdd:COG0527 97 GRQagIITDDNHGK-----ARIDLIETPERIRELLEEGKVVVVAGFQGV--TEDGEittlgrgGS------DTTAVALAA 163
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90
....*....|....*..
gi 446778123 212 QINADGLVILTDADAVY 228
Cdd:COG0527 164 ALKADECEIWTDVDGVY 180
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