|
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: 558.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 1 MKTLVVALGGNALLQRGEALTVENQYRNIDSAVPALARLAQKYRLAIVHGNGPQVGLLSLQNLAYGDVEPYPLDVLVAES 80
Cdd:PRK09411 1 MKTLVVALGGNALLQRGEALTAENQYRNIASAVPALARLARSYRLAIVHGNGPQVGLLALQNLAWKEVEPYPLDVLVAES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 81 QGMIGYMLAQRLAQEALMPPVSTVMTRIAVASNDPAFSAPEKFIGPVYEPELQAQLEAEYGWTMKRDGKYLRRVVPSPTP 160
Cdd:PRK09411 81 QGMIGYMLAQSLSAQPQMPPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAYGWQMKRDGKYLRRVVASPQP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 161 VRIEESESIERLLGEGHAVICCGGGGIPVLECGRGAEAVIDKDLAAALLAEQINADGLVILTDADAVYEHWGTPMQRPIR 240
Cdd:PRK09411 161 RKILDSEAIELLLKEGHVVICSGGGGVPVTEDGAGSEAVIDKDLAAALLAEQINADGLVILTDADAVYENWGTPQQRAIR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 490239592 241 EATPEALAPFARNDGAMGPKIAAVSGYVRRRGKRAWIGALSRIDDTLAGLAGTCIKP 297
Cdd:PRK09411 241 HATPDELAPFAKADGAMGPKVTAVSGYVRSRGKPAWIGALSRIEETLAGEAGTCISL 297
|
|
| ArcC |
COG0549 |
Carbamate kinase [Amino acid transport and metabolism]; |
1-297 |
3.21e-153 |
|
Carbamate kinase [Amino acid transport and metabolism];
Pssm-ID: 440315 Cd Length: 313 Bit Score: 430.65 E-value: 3.21e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 1 MKTLVVALGGNALLQRGEALTVENQYRNIDSAVPALARLAQK-YRLAIVHGNGPQVGLLSLQNLAYGD-VEPYPLDVLVA 78
Cdd:COG0549 2 KKRIVVALGGNALLRRGEPGTAEEQRENVREAAKALADLIEAgHEVVITHGNGPQVGLLLLQNEAAKKkVPPMPLDVCGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 79 ESQGMIGYMLAQ----RLAQEALMPPVSTVMTRIAVASNDPAFSAPEKFIGPVYEPELQAQLEAEYGWTMKRD-GKYLRR 153
Cdd:COG0549 82 MTQGMIGYMLQQalrnELPKRGIDKPVATLVTQVEVDPDDPAFQNPTKPIGPFYTEEEAEELAKEKGWTFKEDaGRGYRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 154 VVPSPTPVRIEESESIERLLGEGHAVICCGGGGIPVL--ECG--RGAEAVIDKDLAAALLAEQINADGLVILTDADAVYE 229
Cdd:COG0549 162 VVPSPKPKRIVEIDAIKALLEAGVIVIAAGGGGIPVVrdEDGglKGVEAVIDKDLASALLAEELDADLLLILTDVDKVYI 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490239592 230 HWGTPMQRPIREATPEALAPFARN----DGAMGPKIAAVSGYVRRRGKRAWIGALSRIDDTLAGLAGTCIKP 297
Cdd:COG0549 242 NFGKPDQRALDEVTVAEAKKYIEEghfaAGSMGPKVEAAIRFVEATGKRAIITSLEKAEEALAGKAGTRIVP 313
|
|
| AAK_CK |
cd04235 |
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ... |
3-295 |
1.16e-146 |
|
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: 413.83 E-value: 1.16e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 3 TLVVALGGNALLQRGEALTVENQYRNIDSAVPALARLAQK-YRLAIVHGNGPQVGLLSLQNLAYGD-VEPYPLDVLVAES 80
Cdd:cd04235 1 RIVVALGGNALLRRGEPGTAEEQRENVKIAAKALADLIKNgHEVVITHGNGPQVGNLLLQNEAAAEkVPAYPLDVCGAMS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 81 QGMIGYMLAQ----RLAQEALMPPVSTVMTRIAVASNDPAFSAPEKFIGPVYEPELQAQLEAEYGWTMKRD-GKYLRRVV 155
Cdd:cd04235 81 QGMIGYMLQQaldnELPKRGIDKPVVTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEKGWTFKEDaGRGYRRVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 156 PSPTPVRIEESESIERLLGEGHAVICCGGGGIPVLECG---RGAEAVIDKDLAAALLAEQINADGLVILTDADAVYEHWG 232
Cdd:cd04235 161 PSPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREGgglKGVEAVIDKDLASALLAEEINADLLVILTDVDNVYINFG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490239592 233 TPMQRPIREATPEALAPFARND----GAMGPKIAAVSGYVRRRGKRAWIGALSRIDDTLAGLAGTCI 295
Cdd:cd04235 241 KPNQKALEQVTVEELEKYIEEGqfapGSMGPKVEAAIRFVESGGKKAIITSLENAEAALEGKAGTVI 307
|
|
| arcC |
TIGR00746 |
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes ... |
2-297 |
7.31e-142 |
|
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: 401.83 E-value: 7.31e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 2 KTLVVALGGNALLQRGEALTVENQYRNIDSAVPALARLA-QKYRLAIVHGNGPQVGLLSLQNLAY-GDVEPYPLDVLVAE 79
Cdd:TIGR00746 1 KRVVVALGGNALLQRGEKGSAEAQRDNVRQTAPQIAKLIkRGYELVITHGNGPQVGNLLLQNQAAdSEVPAMPLDVLGAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 80 SQGMIGYMLAQRLAQE----ALMPPVSTVMTRIAVASNDPAFSAPEKFIGPVYEPELQAQLEAEYGWTMKRD-GKYLRRV 154
Cdd:TIGR00746 81 SQGMIGYMLQQALNNElpkrGMEKPVATVLTQTIVDPKDPAFQNPTKPIGPFYTEEEAKRLAAEKGWIVKEDaGRGWRRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 155 VPSPTPVRIEESESIERLLGEGHAVICCGGGGIPVLECG---RGAEAVIDKDLAAALLAEQINADGLVILTDADAVYEHW 231
Cdd:TIGR00746 161 VPSPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEGaelKGVEAVIDKDLASEKLAEEVNADILVILTDVDAVYINY 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 232 GTPMQRPIREATPEALAPFARN----DGAMGPKIAAVSGYVRRRGKRAWIGALSRIDDTLAGLAGTCIKP 297
Cdd:TIGR00746 241 GKPDEKALREVTVEELEDYYKAghfaAGSMGPKVEAAIEFVESGGKRAIITSLENAVEALEGKAGTRVTK 310
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
2-277 |
5.36e-15 |
|
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: 72.78 E-value: 5.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 2 KTLVVALGGNALLQRGealtvenqyrNIDSAVPALARL-AQKYRLAIVHGNGPQV-GLLSLQNLAYGDVEPYPLDVLVAE 79
Cdd:pfam00696 1 KRVVIKLGGSSLTDKE----------RLKRLADEIAALlEEGRKLVVVHGGGAFAdGLLALLGLSPRFARLTDAETLEVA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 80 SQGMIGyMLAQRLAqEALMppvstvmtriavASNDPAFSAPEKFIgpvyepelqaqleaeygwtmkrdgkYLRRVVPSPT 159
Cdd:pfam00696 71 TMDALG-SLGERLN-AALL------------AAGLPAVGLPAAQL-------------------------LATEAGFIDD 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 160 PVRIEESESIERLLGEGHAVICCGGGGIPVLecgrGAEAVIDKDLAAALLAEQINADGLVILTDADAVYEHWGT--PMQR 237
Cdd:pfam00696 112 VVTRIDTEALEELLEAGVVPVITGFIGIDPE----GELGRGSSDTLAALLAEALGADKLIILTDVDGVYTADPRkvPDAK 187
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 490239592 238 PIREATP-EALAPFARNDGAMG--PKIAAVSGYVRRRGKRAWI 277
Cdd:pfam00696 188 LIPEISYdELLELLASGLATGGmkVKLPAALEAARRGGIPVVI 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: 558.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 1 MKTLVVALGGNALLQRGEALTVENQYRNIDSAVPALARLAQKYRLAIVHGNGPQVGLLSLQNLAYGDVEPYPLDVLVAES 80
Cdd:PRK09411 1 MKTLVVALGGNALLQRGEALTAENQYRNIASAVPALARLARSYRLAIVHGNGPQVGLLALQNLAWKEVEPYPLDVLVAES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 81 QGMIGYMLAQRLAQEALMPPVSTVMTRIAVASNDPAFSAPEKFIGPVYEPELQAQLEAEYGWTMKRDGKYLRRVVPSPTP 160
Cdd:PRK09411 81 QGMIGYMLAQSLSAQPQMPPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAYGWQMKRDGKYLRRVVASPQP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 161 VRIEESESIERLLGEGHAVICCGGGGIPVLECGRGAEAVIDKDLAAALLAEQINADGLVILTDADAVYEHWGTPMQRPIR 240
Cdd:PRK09411 161 RKILDSEAIELLLKEGHVVICSGGGGVPVTEDGAGSEAVIDKDLAAALLAEQINADGLVILTDADAVYENWGTPQQRAIR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 490239592 241 EATPEALAPFARNDGAMGPKIAAVSGYVRRRGKRAWIGALSRIDDTLAGLAGTCIKP 297
Cdd:PRK09411 241 HATPDELAPFAKADGAMGPKVTAVSGYVRSRGKPAWIGALSRIEETLAGEAGTCISL 297
|
|
| PRK12354 |
PRK12354 |
carbamate kinase; Reviewed |
3-297 |
1.48e-156 |
|
carbamate kinase; Reviewed
Pssm-ID: 183466 Cd Length: 307 Bit Score: 438.88 E-value: 1.48e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 3 TLVVALGGNALLQRGEALTVENQYRNIDSAVPALARLAQKYRLAIVHGNGPQVGLLSLQNLAYGDVEPYPLDVLVAESQG 82
Cdd:PRK12354 2 RIVVALGGNALLRRGEPLTAENQRANIRIAAEQIAKIAREHELVIVHGNGPQVGLLALQNAAYKDVTPYPLDVLGAETEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 83 MIGYMLAQRLAQEALMPPVSTVMTRIAVASNDPAFSAPEKFIGPVYEPELQAQLEAEYGWTMKRDGKYLRRVVPSPTPVR 162
Cdd:PRK12354 82 MIGYMLEQELGNLLPERPVATLLTQVEVDANDPAFANPTKPIGPVYDEAEAERLAAEKGWTIKPDGDYFRRVVPSPRPKR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 163 IEESESIERLLGEGHAVICCGGGGIPVL--ECG--RGAEAVIDKDLAAALLAEQINADGLVILTDADAVYEHWGTPMQRP 238
Cdd:PRK12354 162 IVEIRPIRWLLEKGHLVICAGGGGIPVVydADGklHGVEAVIDKDLAAALLAEQLDADLLLILTDVDAVYLDWGKPTQRA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 490239592 239 IREATPEALAPFARNDGAMGPKIAAVSGYVRRRGKRAWIGALSRIDDTLAGLAGTCIKP 297
Cdd:PRK12354 242 IAQATPDELRELGFAAGSMGPKVEAACEFVRATGKIAGIGSLEDIQAILAGEAGTRISP 300
|
|
| ArcC |
COG0549 |
Carbamate kinase [Amino acid transport and metabolism]; |
1-297 |
3.21e-153 |
|
Carbamate kinase [Amino acid transport and metabolism];
Pssm-ID: 440315 Cd Length: 313 Bit Score: 430.65 E-value: 3.21e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 1 MKTLVVALGGNALLQRGEALTVENQYRNIDSAVPALARLAQK-YRLAIVHGNGPQVGLLSLQNLAYGD-VEPYPLDVLVA 78
Cdd:COG0549 2 KKRIVVALGGNALLRRGEPGTAEEQRENVREAAKALADLIEAgHEVVITHGNGPQVGLLLLQNEAAKKkVPPMPLDVCGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 79 ESQGMIGYMLAQ----RLAQEALMPPVSTVMTRIAVASNDPAFSAPEKFIGPVYEPELQAQLEAEYGWTMKRD-GKYLRR 153
Cdd:COG0549 82 MTQGMIGYMLQQalrnELPKRGIDKPVATLVTQVEVDPDDPAFQNPTKPIGPFYTEEEAEELAKEKGWTFKEDaGRGYRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 154 VVPSPTPVRIEESESIERLLGEGHAVICCGGGGIPVL--ECG--RGAEAVIDKDLAAALLAEQINADGLVILTDADAVYE 229
Cdd:COG0549 162 VVPSPKPKRIVEIDAIKALLEAGVIVIAAGGGGIPVVrdEDGglKGVEAVIDKDLASALLAEELDADLLLILTDVDKVYI 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490239592 230 HWGTPMQRPIREATPEALAPFARN----DGAMGPKIAAVSGYVRRRGKRAWIGALSRIDDTLAGLAGTCIKP 297
Cdd:COG0549 242 NFGKPDQRALDEVTVAEAKKYIEEghfaAGSMGPKVEAAIRFVEATGKRAIITSLEKAEEALAGKAGTRIVP 313
|
|
| AAK_CK |
cd04235 |
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ... |
3-295 |
1.16e-146 |
|
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: 413.83 E-value: 1.16e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 3 TLVVALGGNALLQRGEALTVENQYRNIDSAVPALARLAQK-YRLAIVHGNGPQVGLLSLQNLAYGD-VEPYPLDVLVAES 80
Cdd:cd04235 1 RIVVALGGNALLRRGEPGTAEEQRENVKIAAKALADLIKNgHEVVITHGNGPQVGNLLLQNEAAAEkVPAYPLDVCGAMS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 81 QGMIGYMLAQ----RLAQEALMPPVSTVMTRIAVASNDPAFSAPEKFIGPVYEPELQAQLEAEYGWTMKRD-GKYLRRVV 155
Cdd:cd04235 81 QGMIGYMLQQaldnELPKRGIDKPVVTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEKGWTFKEDaGRGYRRVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 156 PSPTPVRIEESESIERLLGEGHAVICCGGGGIPVLECG---RGAEAVIDKDLAAALLAEQINADGLVILTDADAVYEHWG 232
Cdd:cd04235 161 PSPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREGgglKGVEAVIDKDLASALLAEEINADLLVILTDVDNVYINFG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490239592 233 TPMQRPIREATPEALAPFARND----GAMGPKIAAVSGYVRRRGKRAWIGALSRIDDTLAGLAGTCI 295
Cdd:cd04235 241 KPNQKALEQVTVEELEKYIEEGqfapGSMGPKVEAAIRFVESGGKKAIITSLENAEAALEGKAGTVI 307
|
|
| arcC |
TIGR00746 |
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes ... |
2-297 |
7.31e-142 |
|
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: 401.83 E-value: 7.31e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 2 KTLVVALGGNALLQRGEALTVENQYRNIDSAVPALARLA-QKYRLAIVHGNGPQVGLLSLQNLAY-GDVEPYPLDVLVAE 79
Cdd:TIGR00746 1 KRVVVALGGNALLQRGEKGSAEAQRDNVRQTAPQIAKLIkRGYELVITHGNGPQVGNLLLQNQAAdSEVPAMPLDVLGAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 80 SQGMIGYMLAQRLAQE----ALMPPVSTVMTRIAVASNDPAFSAPEKFIGPVYEPELQAQLEAEYGWTMKRD-GKYLRRV 154
Cdd:TIGR00746 81 SQGMIGYMLQQALNNElpkrGMEKPVATVLTQTIVDPKDPAFQNPTKPIGPFYTEEEAKRLAAEKGWIVKEDaGRGWRRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 155 VPSPTPVRIEESESIERLLGEGHAVICCGGGGIPVLECG---RGAEAVIDKDLAAALLAEQINADGLVILTDADAVYEHW 231
Cdd:TIGR00746 161 VPSPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEGaelKGVEAVIDKDLASEKLAEEVNADILVILTDVDAVYINY 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 232 GTPMQRPIREATPEALAPFARN----DGAMGPKIAAVSGYVRRRGKRAWIGALSRIDDTLAGLAGTCIKP 297
Cdd:TIGR00746 241 GKPDEKALREVTVEELEDYYKAghfaAGSMGPKVEAAIEFVESGGKRAIITSLENAVEALEGKAGTRVTK 310
|
|
| PRK12454 |
PRK12454 |
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed |
1-297 |
6.08e-118 |
|
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
Pssm-ID: 183535 Cd Length: 313 Bit Score: 341.21 E-value: 6.08e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 1 MKTLVVALGGNALLQRGEALTVENQYRNIDSAVPALARLAQK-YRLAIVHGNGPQVGLLSLQNLAYGDV--EPYPLDVLV 77
Cdd:PRK12454 2 KKRIVIALGGNALLQPGEKGTAENQMKNVRKTAKQIADLIEEgYEVVITHGNGPQVGNLLLQMDAAKDVgiPPFPLDVAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 78 AESQGMIGYMLAQ----RLAQEALMPPVSTVMTRIAVASNDPAFSAPEKFIGPVYEPELQAQLEAEYGWTMKRD-GKYLR 152
Cdd:PRK12454 82 AMTQGWIGYMIQQalrnELAKRGIEKQVATIVTQVIVDKNDPAFQNPTKPVGPFYDEEEAKKLAKEKGWIVKEDaGRGWR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 153 RVVPSPTPVRIEESESIERLLGEGHAVICCGGGGIPVLECG---RGAEAVIDKDLAAALLAEQINADGLVILTDADAVYE 229
Cdd:PRK12454 162 RVVPSPDPLGIVEIEVIKALVENGFIVIASGGGGIPVIEEDgelKGVEAVIDKDLASELLAEELNADIFIILTDVEKVYL 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490239592 230 HWGTPMQRPIREATPEALAPFARN----DGAMGPKIAAVSGYVRRRGKRAWIGALSRIDDTLAGLAGTCIKP 297
Cdd:PRK12454 242 NYGKPDQKPLDKVTVEEAKKYYEEghfkAGSMGPKILAAIRFVENGGKRAIIASLEKAVEALEGKTGTRIIP 313
|
|
| PRK12353 |
PRK12353 |
putative amino acid kinase; Reviewed |
1-297 |
8.77e-118 |
|
putative amino acid kinase; Reviewed
Pssm-ID: 237071 Cd Length: 314 Bit Score: 340.98 E-value: 8.77e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 1 MKTLVVALGGNALLQRGEalTVENQYRNIDSAVPALARLAQK-YRLAIVHGNGPQVGLLSLQNLAYGDVE----PYPLDV 75
Cdd:PRK12353 2 MKKIVVALGGNALGSTPE--EATAQLEAVKKTAKSLVDLIEEgHEVVITHGNGPQVGNILLAQEAAASEKnkvpAMPLDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 76 LVAESQGMIGYMLAQRLaQEALM-----PPVSTVMTRIAVASNDPAFSAPEKFIGPVYEPELQAQLEAEYGWTMKRD-GK 149
Cdd:PRK12353 80 CGAMSQGYIGYHLQNAL-RNELLkrgidKPVATVVTQVVVDANDPAFKNPTKPIGPFYTEEEAEKLAKEKGYTFKEDaGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 150 YLRRVVPSPTPVRIEESESIERLLGEGHAVICCGGGGIPVLECG---RGAEAVIDKDLAAALLAEQINADGLVILTDADA 226
Cdd:PRK12353 159 GYRRVVPSPKPVDIVEIEAIKTLVDAGQVVIAAGGGGIPVIREGgglKGVEAVIDKDFASAKLAELVDADLLIILTAVDK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490239592 227 VYEHWGTPMQRPIREATPEALAP------FARndGAMGPKIAAVSGYVRRR-GKRAWIGALSRIDDTLAGLAGTCIKP 297
Cdd:PRK12353 239 VYINFGKPNQKKLDEVTVSEAEKyieegqFAP--GSMLPKVEAAISFVESRpGRKAIITSLEKAKEALEGKAGTVIVK 314
|
|
| PRK12686 |
PRK12686 |
carbamate kinase; Reviewed |
1-295 |
6.57e-92 |
|
carbamate kinase; Reviewed
Pssm-ID: 183683 Cd Length: 312 Bit Score: 274.99 E-value: 6.57e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 1 MKTLVVALGGNALLQRGEalTVENQYRNIDSAVPALARL-AQKYRLAIVHGNGPQVGLLSLQ--NLAYGDVEPYPLDVLV 77
Cdd:PRK12686 2 KEKIVIALGGNAILQTEA--TAEAQQTAVREAAQHLVDLiEAGHDIVITHGNGPQVGNLLLQqaESNSNKVPAMPLDTCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 78 AESQGMIGYMLAQ----RLAQEALMPPVSTVMTRIAVASNDPAFSAPEKFIGPVYEPELQAQLEAEYGWTMKRD-GKYLR 152
Cdd:PRK12686 80 AMSQGMIGYWLQNalnnELTERGIDKPVITLVTQVEVDKDDPAFANPTKPIGPFYTEEEAKQQAEQPGSTFKEDaGRGYR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 153 RVVPSPTPVRIEESESIERLLGEGHAVICCGGGGIPVLECG---RGAEAVIDKDLAAALLAEQINADGLVILTDADAVYE 229
Cdd:PRK12686 160 RVVPSPKPQEIIEHDTIRTLVDGGNIVIACGGGGIPVIRDDntlKGVEAVIDKDFASEKLAEQIDADLLIILTGVENVFI 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490239592 230 HWGTPMQRPIREATPEALAPFARND----GAMGPKIAAVSGYVRRR-GKRAWIGALSRIDDTLAGLAGTCI 295
Cdd:PRK12686 240 NFNKPNQQKLDDITVAEAKQYIAEGqfapGSMLPKVEAAIDFVESGeGKKAIITSLEQAKEALAGNAGTHI 310
|
|
| PRK12352 |
PRK12352 |
putative carbamate kinase; Reviewed |
1-295 |
2.30e-69 |
|
putative carbamate kinase; Reviewed
Pssm-ID: 183464 Cd Length: 316 Bit Score: 217.75 E-value: 2.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 1 MKTL-VVALGGNALLQRGEALTVENQYRNIDSAVPALAR-LAQKYRLAIVHGNGPQVGLLSLQNLAYGDVEPYP---LDV 75
Cdd:PRK12352 1 MKELvVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEmLASDYDIVLTHGNGPQVGLDLRRAEIAHEREGLPltpLAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 76 LVAESQGMIGYMLAQRLAQEalMPP-----VSTVMTRIAVASNDPAFSAPEKFIGPVYEPELQAQLEAEY-GWTMKRD-G 148
Cdd:PRK12352 81 CVADTQGGIGYLIQQALNNR--LARhgekkAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDELQKANpDWRFVEDaG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 149 KYLRRVVPSPTPVRIEESESIERLLGEGHAVICCGGGGIPVLECG----RGAEAVIDKDLAAALLAEQINADGLVILTDA 224
Cdd:PRK12352 159 RGYRRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDagdyQSVDAVIDKDLSTALLAREIHADILVITTGV 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490239592 225 DAVYEHWGTPMQRPIREATPEALAPFARND----GAMGPKIAAVSGYVRRRGKRAWIGALSRIDDTLAGLAGTCI 295
Cdd:PRK12352 239 EKVCIHFGKPQQQALDRVDIATMTRYMQEGhfppGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHI 313
|
|
| AAK |
cd02115 |
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ... |
5-264 |
6.38e-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: 75.56 E-value: 6.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 5 VVALGGNaLLQRGEALtvenqyRNIDSAVPALArlAQKYRLAIVHGNGPQVG-----LLSLQNLAYGD-VEPYPLDVLVA 78
Cdd:cd02115 1 VIKFGGS-SVSSEERL------RNLARILVKLA--SEGGRVVVVHGAGPQITdellaHGELLGYARGLrITDRETDALAA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 79 ESQGMIGYMLAQRLAQEalmppvstvmtriavasndpafsapekfigpvyepELQAQLEAEYGWTMKRDGKylrrvvPSP 158
Cdd:cd02115 72 MGEGMSNLLIAAALEQH-----------------------------------GIKAVPLDLTQAGFASPNQ------GHV 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 159 TPVRIEESESIERLLGEGHAVICCGGGGIPvlECGRGAEAVIDKDLAAALLAEQINADGLVILTDADAVY--EHWGTPMQ 236
Cdd:cd02115 111 GKITKVSTDRLKSLLENGILPILSGFGGTD--EKETGTLGRGGSDSTAALLAAALKADRLVILTDVDGVYtaDPRKVPDA 188
|
250 260
....*....|....*....|....*...
gi 490239592 237 RPIREATPEALAPFArNDGAMGPKIAAV 264
Cdd:cd02115 189 KLLSELTYEEAAELA-YAGAMVLKPKAA 215
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
2-277 |
5.36e-15 |
|
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: 72.78 E-value: 5.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 2 KTLVVALGGNALLQRGealtvenqyrNIDSAVPALARL-AQKYRLAIVHGNGPQV-GLLSLQNLAYGDVEPYPLDVLVAE 79
Cdd:pfam00696 1 KRVVIKLGGSSLTDKE----------RLKRLADEIAALlEEGRKLVVVHGGGAFAdGLLALLGLSPRFARLTDAETLEVA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 80 SQGMIGyMLAQRLAqEALMppvstvmtriavASNDPAFSAPEKFIgpvyepelqaqleaeygwtmkrdgkYLRRVVPSPT 159
Cdd:pfam00696 71 TMDALG-SLGERLN-AALL------------AAGLPAVGLPAAQL-------------------------LATEAGFIDD 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 160 PVRIEESESIERLLGEGHAVICCGGGGIPVLecgrGAEAVIDKDLAAALLAEQINADGLVILTDADAVYEHWGT--PMQR 237
Cdd:pfam00696 112 VVTRIDTEALEELLEAGVVPVITGFIGIDPE----GELGRGSSDTLAALLAEALGADKLIILTDVDGVYTADPRkvPDAK 187
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 490239592 238 PIREATP-EALAPFARNDGAMG--PKIAAVSGYVRRRGKRAWI 277
Cdd:pfam00696 188 LIPEISYdELLELLASGLATGGmkVKLPAALEAARRGGIPVVI 230
|
|
| AAK_UMPK-like |
cd04239 |
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ... |
155-228 |
1.53e-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: 1.53e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490239592 155 VPSPTPVR-IEESESIERL---LGEGHAVICCGGGGIPVLECgrgaeavidkDLAAALLAEQINADGLVILTDADAVY 228
Cdd:cd04239 93 VMSAIPMQgVAEPYIRRRAirhLEKGRIVIFGGGTGNPGFTT----------DTAAALRAEEIGADVLLKATNVDGVY 160
|
|
| argB |
TIGR00761 |
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ... |
200-277 |
1.91e-04 |
|
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: 41.88 E-value: 1.91e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490239592 200 IDKDLAAALLAEQINADGLVILTDADAVYEHWGTPMQRPIREATPEALAPFARNDGAMGPKIAAVSGYVRRRGKRAWI 277
Cdd:TIGR00761 154 VNADTAAGALAAALGAEKLVLLTDVPGILNGDGQSLISEIPLDEIEQLIKQGIIKGGMIPKVNAALEALRGGVRSVHI 231
|
|
| AAK_G5K_ProB |
cd04242 |
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ... |
201-263 |
3.15e-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: 3.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490239592 201 DKDLAAALLAEQINADGLVILTDADAVY-----EHWGTPMQRPIREATPE--ALAPFARND---GAMGPKIAA 263
Cdd:cd04242 143 DNDRLSALVAGLVNADLLILLSDVDGLYdknprENPDAKLIPEVEEITDEieAMAGGSGSSvgtGGMRTKLKA 215
|
|
| AAK_NAGK-like |
cd04238 |
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ... |
182-270 |
3.56e-04 |
|
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: 41.34 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 182 CGGGGIPV---LECGRGAEAV-IDKDLAAALLAEQINADGLVILTDADAVYEHWGTpmqrPIREATP---EALAPFARND 254
Cdd:cd04238 135 LEAGYIPViapIAVDEDGETYnVNADTAAGAIAAALKAEKLILLTDVPGVLDDPGS----LISELTPkeaEELIEDGVIS 210
|
90 100
....*....|....*....|
gi 490239592 255 GAMGPK----IAAVSGYVRR 270
Cdd:cd04238 211 GGMIPKveaaLEALEGGVRK 230
|
|
| PRK14058 |
PRK14058 |
[LysW]-aminoadipate/[LysW]-glutamate kinase; |
200-297 |
2.45e-03 |
|
[LysW]-aminoadipate/[LysW]-glutamate kinase;
Pssm-ID: 237599 [Multi-domain] Cd Length: 268 Bit Score: 38.73 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 200 IDKDLAAALLAEQINADGLVILTDADAVYEHWGTPmQRPIREATP---EALAPFARndGAMGPKIAAVSGYVRRRGKRAW 276
Cdd:PRK14058 168 VDGDRAAAAIAGALKAEALVLLSDVPGLLRDPPDE-GSLIERITPeeaEELSKAAG--GGMKKKVLMAAEAVEGGVGRVI 244
|
90 100
....*....|....*....|....
gi 490239592 277 IGALSR---IDDTLAGlAGTCIKP 297
Cdd:PRK14058 245 IADANVddpISAALAG-EGTVIVN 267
|
|
| AAK_NAGK-C |
cd04250 |
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ... |
180-263 |
2.95e-03 |
|
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: 38.64 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 180 ICCGGGGIPV---LECGRGAEAV-IDKDLAAALLAEQINADGLVILTDADAVYEHWGTPmQRPIREATP---EALAPFAR 252
Cdd:cd04250 153 TLLEAGYIPViapVGVGEDGETYnINADTAAGAIAAALKAEKLILLTDVAGVLDDPNDP-GSLISEISLkeaEELIADGI 231
|
90
....*....|.
gi 490239592 253 NDGAMGPKIAA 263
Cdd:cd04250 232 ISGGMIPKVEA 242
|
|
| PRK00942 |
PRK00942 |
acetylglutamate kinase; Provisional |
200-263 |
4.93e-03 |
|
acetylglutamate kinase; Provisional
Pssm-ID: 234869 [Multi-domain] Cd Length: 283 Bit Score: 37.78 E-value: 4.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490239592 200 IDKDLAAALLAEQINADGLVILTDADAVYEHWGTPMQRpIREATPEALAPFARNDGAMGPKIAA 263
Cdd:PRK00942 181 INADTAAGAIAAALGAEKLILLTDVPGVLDDKGQLISE-LTASEAEELIEDGVITGGMIPKVEA 243
|
|
| PRK12314 |
PRK12314 |
gamma-glutamyl kinase; Provisional |
201-263 |
5.12e-03 |
|
gamma-glutamyl kinase; Provisional
Pssm-ID: 183430 [Multi-domain] Cd Length: 266 Bit Score: 37.91 E-value: 5.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490239592 201 DKDLAAALLAEQINADGLVILTDADAVY-----EHWGTPMQRPIREATPEALA-------PFArnDGAMGPKIAA 263
Cdd:PRK12314 155 DNDRLSAIVAKLVKADLLIILSDIDGLYdknprINPDAKLRSEVTEITEEILAlaggagsKFG--TGGMVTKLKA 227
|
|
| AAK_NAGK-UC |
cd04251 |
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ... |
162-295 |
6.13e-03 |
|
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: 37.35 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239592 162 RIEE--SESIERLLGEGHAVICCggggiPVLECGRGAEAVIDKDLAAALLAEQINADGLVILTDADAVYEHwgtpmQRPI 239
Cdd:cd04251 129 KVEKvnSDLIEALLDAGYLPVVS-----PVAYSEEGEPLNVDGDRAAAAIAAALKAERLILLTDVEGLYLD-----GRVI 198
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490239592 240 REATP---EALAPFARndGAMGPKIAAVSGYVRRRGKRAWIG---ALSRIDDTLAGlAGTCI 295
Cdd:cd04251 199 ERITVsdaESLLEKAG--GGMKRKLLAAAEAVEGGVREVVIGdarADSPISSALNG-GGTVI 257
|
|
| |
