|
Name |
Accession |
Description |
Interval |
E-value |
| AAK_CK |
cd04235 |
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ... |
5-312 |
1.14e-171 |
|
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: 477.77 E-value: 1.14e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 5 KIVVALGGNAILSKDA--SAEAQQAALRETAKSLVSLVKENEKLIITHGNGPQVGNLLLQQMIGSTKsNPAMPIDTAVSM 82
Cdd:cd04235 1 RIVVALGGNALLRRGEpgTAEEQRENVKIAAKALADLIKNGHEVVITHGNGPQVGNLLLQNEAAAEK-VPAYPLDVCGAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 83 TEGSIGYWMQNAMDDVLEDEGIDKSAATVVTQVEVDANDSAFQNPSKPIGPFYEKEDINKIRELHpEYIYVEDAGRGYRR 162
Cdd:cd04235 80 SQGMIGYMLQQALDNELPKRGIDKPVVTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEK-GWTFKEDAGRGYRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 163 VVPSPKPVNVREYQVINSLVDNNVIPISVGGGGVPVVREGNHLIGCEAVIDKDFASEKLAELIKADLLIILTAVDNVYIN 242
Cdd:cd04235 159 VVPSPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREGGGLKGVEAVIDKDLASALLAEEINADLLVILTDVDNVYIN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 243 FNKPDQKKLENVTVEELENYINENQFAKGSMLPKVQAAINFVNNGCGEAVVTSLKNINNFLQKGSGTIIT 312
Cdd:cd04235 239 FGKPNQKALEQVTVEELEKYIEEGQFAPGSMGPKVEAAIRFVESGGKKAIITSLENAEAALEGKAGTVIV 308
|
|
| PRK12353 |
PRK12353 |
putative amino acid kinase; Reviewed |
2-313 |
2.59e-167 |
|
putative amino acid kinase; Reviewed
Pssm-ID: 237071 Cd Length: 314 Bit Score: 466.94 E-value: 2.59e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 2 ANRKIVVALGGNAILSKDASAEAQQAALRETAKSLVSLVKENEKLIITHGNGPQVGNLLLQQMIGSTKSN--PAMPIDTA 79
Cdd:PRK12353 1 MMKKIVVALGGNALGSTPEEATAQLEAVKKTAKSLVDLIEEGHEVVITHGNGPQVGNILLAQEAAASEKNkvPAMPLDVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 80 VSMTEGSIGYWMQNAMDDVLEDEGIDKSAATVVTQVEVDANDSAFQNPSKPIGPFYEKEDINKIRElHPEYIYVEDAGRG 159
Cdd:PRK12353 81 GAMSQGYIGYHLQNALRNELLKRGIDKPVATVVTQVVVDANDPAFKNPTKPIGPFYTEEEAEKLAK-EKGYTFKEDAGRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 160 YRRVVPSPKPVNVREYQVINSLVDNNVIPISVGGGGVPVVREGNHLIGCEAVIDKDFASEKLAELIKADLLIILTAVDNV 239
Cdd:PRK12353 160 YRRVVPSPKPVDIVEIEAIKTLVDAGQVVIAAGGGGIPVIREGGGLKGVEAVIDKDFASAKLAELVDADLLIILTAVDKV 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488909732 240 YINFNKPDQKKLENVTVEELENYINENQFAKGSMLPKVQAAINFVNNGCG-EAVVTSLKNINNFLQKGSGTIITK 313
Cdd:PRK12353 240 YINFGKPNQKKLDEVTVSEAEKYIEEGQFAPGSMLPKVEAAISFVESRPGrKAIITSLEKAKEALEGKAGTVIVK 314
|
|
| ArcC |
COG0549 |
Carbamate kinase [Amino acid transport and metabolism]; |
3-313 |
3.93e-165 |
|
Carbamate kinase [Amino acid transport and metabolism];
Pssm-ID: 440315 Cd Length: 313 Bit Score: 461.47 E-value: 3.93e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 3 NRKIVVALGGNAILSKD--ASAEAQQAALRETAKSLVSLVKENEKLIITHGNGPQVGNLLLQQMIGSTKsNPAMPIDTAV 80
Cdd:COG0549 2 KKRIVVALGGNALLRRGepGTAEEQRENVREAAKALADLIEAGHEVVITHGNGPQVGLLLLQNEAAKKK-VPPMPLDVCG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 81 SMTEGSIGYWMQNAMDDVLEDEGIDKSAATVVTQVEVDANDSAFQNPSKPIGPFYEKEDINKIRElHPEYIYVEDAGRGY 160
Cdd:COG0549 81 AMTQGMIGYMLQQALRNELPKRGIDKPVATLVTQVEVDPDDPAFQNPTKPIGPFYTEEEAEELAK-EKGWTFKEDAGRGY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 161 RRVVPSPKPVNVREYQVINSLVDNNV---------IPIsvggggvpVVREGNHLIGCEAVIDKDFASEKLAELIKADLLI 231
Cdd:COG0549 160 RRVVPSPKPKRIVEIDAIKALLEAGViviaaggggIPV--------VRDEDGGLKGVEAVIDKDLASALLAEELDADLLL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 232 ILTAVDNVYINFNKPDQKKLENVTVEELENYINENQFAKGSMLPKVQAAINFVNNGCGEAVVTSLKNINNFLQKGSGTII 311
Cdd:COG0549 232 ILTDVDKVYINFGKPDQRALDEVTVAEAKKYIEEGHFAAGSMGPKVEAAIRFVEATGKRAIITSLEKAEEALAGKAGTRI 311
|
..
gi 488909732 312 TK 313
Cdd:COG0549 312 VP 313
|
|
| arcC |
TIGR00746 |
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes ... |
4-313 |
1.15e-138 |
|
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: 394.52 E-value: 1.15e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 4 RKIVVALGGNAIL--SKDASAEAQQAALRETAKSLVSLVKENEKLIITHGNGPQVGNLLLQQMiGSTKSNPAMPIDTAVS 81
Cdd:TIGR00746 1 KRVVVALGGNALLqrGEKGSAEAQRDNVRQTAPQIAKLIKRGYELVITHGNGPQVGNLLLQNQ-AADSEVPAMPLDVLGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 82 MTEGSIGYWMQNAMDDVLEDEGIDKSAATVVTQVEVDANDSAFQNPSKPIGPFYEKEDiNKIRELHPEYIYVEDAGRGYR 161
Cdd:TIGR00746 80 MSQGMIGYMLQQALNNELPKRGMEKPVATVLTQTIVDPKDPAFQNPTKPIGPFYTEEE-AKRLAAEKGWIVKEDAGRGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 162 RVVPSPKPVNVREYQVINSLVDNNVIPISVGGGGVPVVREGNHLIGCEAVIDKDFASEKLAELIKADLLIILTAVDNVYI 241
Cdd:TIGR00746 159 RVVPSPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEGAELKGVEAVIDKDLASEKLAEEVNADILVILTDVDAVYI 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488909732 242 NFNKPDQKKLENVTVEELENYINENQFAKGSMLPKVQAAINFVNNGCGEAVVTSLKNINNFLQKGSGTIITK 313
Cdd:TIGR00746 239 NYGKPDEKALREVTVEELEDYYKAGHFAAGSMGPKVEAAIEFVESGGKRAIITSLENAVEALEGKAGTRVTK 310
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
4-295 |
6.60e-24 |
|
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: 97.44 E-value: 6.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 4 RKIVVALGGNAILSKDAsaeaqqaaLRETAKSLVSLVKENEKLIITHGNGPQVGNLLLQQMIGSTksnpampidtavsmt 83
Cdd:pfam00696 1 KRVVIKLGGSSLTDKER--------LKRLADEIAALLEEGRKLVVVHGGGAFADGLLALLGLSPR--------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 84 egsigywMQNAMDDVLEDEGIDKSAATVVTQVEVDANDSAFQNpskpigpfyekedinkiRELHPEYIYVEDAGRgyrrv 163
Cdd:pfam00696 58 -------FARLTDAETLEVATMDALGSLGERLNAALLAAGLPA-----------------VGLPAAQLLATEAGF----- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 164 vpSPKPVNVREYQVINSLVDNNVIPISVggggvpvvreGNHLI---GCEAVIDKDFASEKLAELIKADLLIILTAVDNVY 240
Cdd:pfam00696 109 --IDDVVTRIDTEALEELLEAGVVPVIT----------GFIGIdpeGELGRGSSDTLAALLAEALGADKLIILTDVDGVY 176
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 488909732 241 INFNK--PDQKKLENVTVEELENYINeNQFAKGSMLPKVQAAINFVNNGCGEAVVTS 295
Cdd:pfam00696 177 TADPRkvPDAKLIPEISYDELLELLA-SGLATGGMKVKLPAALEAARRGGIPVVIVN 232
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AAK_CK |
cd04235 |
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ... |
5-312 |
1.14e-171 |
|
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: 477.77 E-value: 1.14e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 5 KIVVALGGNAILSKDA--SAEAQQAALRETAKSLVSLVKENEKLIITHGNGPQVGNLLLQQMIGSTKsNPAMPIDTAVSM 82
Cdd:cd04235 1 RIVVALGGNALLRRGEpgTAEEQRENVKIAAKALADLIKNGHEVVITHGNGPQVGNLLLQNEAAAEK-VPAYPLDVCGAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 83 TEGSIGYWMQNAMDDVLEDEGIDKSAATVVTQVEVDANDSAFQNPSKPIGPFYEKEDINKIRELHpEYIYVEDAGRGYRR 162
Cdd:cd04235 80 SQGMIGYMLQQALDNELPKRGIDKPVVTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEK-GWTFKEDAGRGYRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 163 VVPSPKPVNVREYQVINSLVDNNVIPISVGGGGVPVVREGNHLIGCEAVIDKDFASEKLAELIKADLLIILTAVDNVYIN 242
Cdd:cd04235 159 VVPSPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREGGGLKGVEAVIDKDLASALLAEEINADLLVILTDVDNVYIN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 243 FNKPDQKKLENVTVEELENYINENQFAKGSMLPKVQAAINFVNNGCGEAVVTSLKNINNFLQKGSGTIIT 312
Cdd:cd04235 239 FGKPNQKALEQVTVEELEKYIEEGQFAPGSMGPKVEAAIRFVESGGKKAIITSLENAEAALEGKAGTVIV 308
|
|
| PRK12353 |
PRK12353 |
putative amino acid kinase; Reviewed |
2-313 |
2.59e-167 |
|
putative amino acid kinase; Reviewed
Pssm-ID: 237071 Cd Length: 314 Bit Score: 466.94 E-value: 2.59e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 2 ANRKIVVALGGNAILSKDASAEAQQAALRETAKSLVSLVKENEKLIITHGNGPQVGNLLLQQMIGSTKSN--PAMPIDTA 79
Cdd:PRK12353 1 MMKKIVVALGGNALGSTPEEATAQLEAVKKTAKSLVDLIEEGHEVVITHGNGPQVGNILLAQEAAASEKNkvPAMPLDVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 80 VSMTEGSIGYWMQNAMDDVLEDEGIDKSAATVVTQVEVDANDSAFQNPSKPIGPFYEKEDINKIRElHPEYIYVEDAGRG 159
Cdd:PRK12353 81 GAMSQGYIGYHLQNALRNELLKRGIDKPVATVVTQVVVDANDPAFKNPTKPIGPFYTEEEAEKLAK-EKGYTFKEDAGRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 160 YRRVVPSPKPVNVREYQVINSLVDNNVIPISVGGGGVPVVREGNHLIGCEAVIDKDFASEKLAELIKADLLIILTAVDNV 239
Cdd:PRK12353 160 YRRVVPSPKPVDIVEIEAIKTLVDAGQVVIAAGGGGIPVIREGGGLKGVEAVIDKDFASAKLAELVDADLLIILTAVDKV 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488909732 240 YINFNKPDQKKLENVTVEELENYINENQFAKGSMLPKVQAAINFVNNGCG-EAVVTSLKNINNFLQKGSGTIITK 313
Cdd:PRK12353 240 YINFGKPNQKKLDEVTVSEAEKYIEEGQFAPGSMLPKVEAAISFVESRPGrKAIITSLEKAKEALEGKAGTVIVK 314
|
|
| ArcC |
COG0549 |
Carbamate kinase [Amino acid transport and metabolism]; |
3-313 |
3.93e-165 |
|
Carbamate kinase [Amino acid transport and metabolism];
Pssm-ID: 440315 Cd Length: 313 Bit Score: 461.47 E-value: 3.93e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 3 NRKIVVALGGNAILSKD--ASAEAQQAALRETAKSLVSLVKENEKLIITHGNGPQVGNLLLQQMIGSTKsNPAMPIDTAV 80
Cdd:COG0549 2 KKRIVVALGGNALLRRGepGTAEEQRENVREAAKALADLIEAGHEVVITHGNGPQVGLLLLQNEAAKKK-VPPMPLDVCG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 81 SMTEGSIGYWMQNAMDDVLEDEGIDKSAATVVTQVEVDANDSAFQNPSKPIGPFYEKEDINKIRElHPEYIYVEDAGRGY 160
Cdd:COG0549 81 AMTQGMIGYMLQQALRNELPKRGIDKPVATLVTQVEVDPDDPAFQNPTKPIGPFYTEEEAEELAK-EKGWTFKEDAGRGY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 161 RRVVPSPKPVNVREYQVINSLVDNNV---------IPIsvggggvpVVREGNHLIGCEAVIDKDFASEKLAELIKADLLI 231
Cdd:COG0549 160 RRVVPSPKPKRIVEIDAIKALLEAGViviaaggggIPV--------VRDEDGGLKGVEAVIDKDLASALLAEELDADLLL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 232 ILTAVDNVYINFNKPDQKKLENVTVEELENYINENQFAKGSMLPKVQAAINFVNNGCGEAVVTSLKNINNFLQKGSGTII 311
Cdd:COG0549 232 ILTDVDKVYINFGKPDQRALDEVTVAEAKKYIEEGHFAAGSMGPKVEAAIRFVEATGKRAIITSLEKAEEALAGKAGTRI 311
|
..
gi 488909732 312 TK 313
Cdd:COG0549 312 VP 313
|
|
| PRK12686 |
PRK12686 |
carbamate kinase; Reviewed |
4-313 |
5.10e-162 |
|
carbamate kinase; Reviewed
Pssm-ID: 183683 Cd Length: 312 Bit Score: 453.73 E-value: 5.10e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 4 RKIVVALGGNAILSKDASAEAQQAALRETAKSLVSLVKENEKLIITHGNGPQVGNLLLQQMIGSTKSNPAMPIDTAVSMT 83
Cdd:PRK12686 3 EKIVIALGGNAILQTEATAEAQQTAVREAAQHLVDLIEAGHDIVITHGNGPQVGNLLLQQAESNSNKVPAMPLDTCVAMS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 84 EGSIGYWMQNAMDDVLEDEGIDKSAATVVTQVEVDANDSAFQNPSKPIGPFYEKEDINKIRElHPEYIYVEDAGRGYRRV 163
Cdd:PRK12686 83 QGMIGYWLQNALNNELTERGIDKPVITLVTQVEVDKDDPAFANPTKPIGPFYTEEEAKQQAE-QPGSTFKEDAGRGYRRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 164 VPSPKPVNVREYQVINSLVDNNVIPISVGGGGVPVVREGNHLIGCEAVIDKDFASEKLAELIKADLLIILTAVDNVYINF 243
Cdd:PRK12686 162 VPSPKPQEIIEHDTIRTLVDGGNIVIACGGGGIPVIRDDNTLKGVEAVIDKDFASEKLAEQIDADLLIILTGVENVFINF 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488909732 244 NKPDQKKLENVTVEELENYINENQFAKGSMLPKVQAAINFVNNGCG-EAVVTSLKNINNFLQKGSGTIITK 313
Cdd:PRK12686 242 NKPNQQKLDDITVAEAKQYIAEGQFAPGSMLPKVEAAIDFVESGEGkKAIITSLEQAKEALAGNAGTHITL 312
|
|
| arcC |
TIGR00746 |
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes ... |
4-313 |
1.15e-138 |
|
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: 394.52 E-value: 1.15e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 4 RKIVVALGGNAIL--SKDASAEAQQAALRETAKSLVSLVKENEKLIITHGNGPQVGNLLLQQMiGSTKSNPAMPIDTAVS 81
Cdd:TIGR00746 1 KRVVVALGGNALLqrGEKGSAEAQRDNVRQTAPQIAKLIKRGYELVITHGNGPQVGNLLLQNQ-AADSEVPAMPLDVLGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 82 MTEGSIGYWMQNAMDDVLEDEGIDKSAATVVTQVEVDANDSAFQNPSKPIGPFYEKEDiNKIRELHPEYIYVEDAGRGYR 161
Cdd:TIGR00746 80 MSQGMIGYMLQQALNNELPKRGMEKPVATVLTQTIVDPKDPAFQNPTKPIGPFYTEEE-AKRLAAEKGWIVKEDAGRGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 162 RVVPSPKPVNVREYQVINSLVDNNVIPISVGGGGVPVVREGNHLIGCEAVIDKDFASEKLAELIKADLLIILTAVDNVYI 241
Cdd:TIGR00746 159 RVVPSPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEGAELKGVEAVIDKDLASEKLAEEVNADILVILTDVDAVYI 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488909732 242 NFNKPDQKKLENVTVEELENYINENQFAKGSMLPKVQAAINFVNNGCGEAVVTSLKNINNFLQKGSGTIITK 313
Cdd:TIGR00746 239 NYGKPDEKALREVTVEELEDYYKAGHFAAGSMGPKVEAAIEFVESGGKRAIITSLENAVEALEGKAGTRVTK 310
|
|
| PRK12454 |
PRK12454 |
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed |
5-313 |
3.75e-131 |
|
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
Pssm-ID: 183535 Cd Length: 313 Bit Score: 375.49 E-value: 3.75e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 5 KIVVALGGNAILSKD--ASAEAQQAALRETAKSLVSLVKENEKLIITHGNGPQVGNLLLQQMIGSTKSNPAMPIDTAVSM 82
Cdd:PRK12454 4 RIVIALGGNALLQPGekGTAENQMKNVRKTAKQIADLIEEGYEVVITHGNGPQVGNLLLQMDAAKDVGIPPFPLDVAGAM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 83 TEGSIGYWMQNAMDDVLEDEGIDKSAATVVTQVEVDANDSAFQNPSKPIGPFYEKEDINKI-RELHpeYIYVEDAGRGYR 161
Cdd:PRK12454 84 TQGWIGYMIQQALRNELAKRGIEKQVATIVTQVIVDKNDPAFQNPTKPVGPFYDEEEAKKLaKEKG--WIVKEDAGRGWR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 162 RVVPSPKPVNVREYQVINSLVDNNVIPISVGGGGVPVVREGNHLIGCEAVIDKDFASEKLAELIKADLLIILTAVDNVYI 241
Cdd:PRK12454 162 RVVPSPDPLGIVEIEVIKALVENGFIVIASGGGGIPVIEEDGELKGVEAVIDKDLASELLAEELNADIFIILTDVEKVYL 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488909732 242 NFNKPDQKKLENVTVEELENYINENQFAKGSMLPKVQAAINFVNNGCGEAVVTSLKNINNFLQKGSGTIITK 313
Cdd:PRK12454 242 NYGKPDQKPLDKVTVEEAKKYYEEGHFKAGSMGPKILAAIRFVENGGKRAIIASLEKAVEALEGKTGTRIIP 313
|
|
| PRK12352 |
PRK12352 |
putative carbamate kinase; Reviewed |
3-313 |
5.73e-100 |
|
putative carbamate kinase; Reviewed
Pssm-ID: 183464 Cd Length: 316 Bit Score: 296.33 E-value: 5.73e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 3 NRKIVVALGGNAILSKDA--SAEAQQAALRETAKSLVSLVKENEKLIITHGNGPQVGNLLLQQMIGSTKSN-PAMPIDTA 79
Cdd:PRK12352 2 KELVVVAIGGNSIIKDNAsqSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHEREGlPLTPLANC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 80 VSMTEGSIGYWMQNAMDDVLEDEGiDKSAATVVTQVEVDANDSAFQNPSKPIGPFYEKEDINKIRELHPEYIYVEDAGRG 159
Cdd:PRK12352 82 VADTQGGIGYLIQQALNNRLARHG-EKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDELQKANPDWRFVEDAGRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 160 YRRVVPSPKPVNVREYQVINSLVDNNVIPISVGGGGVPVVREGNHLI-GCEAVIDKDFASEKLAELIKADLLIILTAVDN 238
Cdd:PRK12352 161 YRRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDAGDYqSVDAVIDKDLSTALLAREIHADILVITTGVEK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488909732 239 VYINFNKPDQKKLENVTVEELENYINENQFAKGSMLPKVQAAINFVNNGCGEAVVTSLKNINNFLQKGSGTIITK 313
Cdd:PRK12352 241 VCIHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHIIK 315
|
|
| PRK12354 |
PRK12354 |
carbamate kinase; Reviewed |
5-313 |
3.43e-99 |
|
carbamate kinase; Reviewed
Pssm-ID: 183466 Cd Length: 307 Bit Score: 294.05 E-value: 3.43e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 5 KIVVALGGNAILSKD--ASAEAQQAALRETAKSLVSLVKENEkLIITHGNGPQVGNLLLQQMigSTKSNPAMPIDTAVSM 82
Cdd:PRK12354 2 RIVVALGGNALLRRGepLTAENQRANIRIAAEQIAKIAREHE-LVIVHGNGPQVGLLALQNA--AYKDVTPYPLDVLGAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 83 TEGSIGYWMQNAMDDVLEDEGIdksaATVVTQVEVDANDSAFQNPSKPIGPFYEKEDINKIRELHPeYIYVEDaGRGYRR 162
Cdd:PRK12354 79 TEGMIGYMLEQELGNLLPERPV----ATLLTQVEVDANDPAFANPTKPIGPVYDEAEAERLAAEKG-WTIKPD-GDYFRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 163 VVPSPKPVNVREYQVINSLVDNNV---------IPISVggggvpvvREGNHLIGCEAVIDKDFASEKLAELIKADLLIIL 233
Cdd:PRK12354 153 VVPSPRPKRIVEIRPIRWLLEKGHlvicaggggIPVVY--------DADGKLHGVEAVIDKDLAAALLAEQLDADLLLIL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 234 TAVDNVYINFNKPDQKKLENVTVEELENYinenQFAKGSMLPKVQAAINFVNNGCGEAVVTSLKNINNFLQKGSGTIITK 313
Cdd:PRK12354 225 TDVDAVYLDWGKPTQRAIAQATPDELREL----GFAAGSMGPKVEAACEFVRATGKIAGIGSLEDIQAILAGEAGTRISP 300
|
|
| PRK09411 |
PRK09411 |
carbamate kinase; Reviewed |
4-313 |
1.15e-61 |
|
carbamate kinase; Reviewed
Pssm-ID: 181831 Cd Length: 297 Bit Score: 198.10 E-value: 1.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 4 RKIVVALGGNAILSKDA--SAEAQQAALRETAKSLVSLVKEnEKLIITHGNGPQVGNLLLQQMigSTKSNPAMPIDTAVS 81
Cdd:PRK09411 2 KTLVVALGGNALLQRGEalTAENQYRNIASAVPALARLARS-YRLAIVHGNGPQVGLLALQNL--AWKEVEPYPLDVLVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 82 MTEGSIGYWMQNAmddvLEDEGIDKSAATVVTQVEVDANDSAFQNPSKPIGPFYEKEdinKIRELHPEYIYVEDA-GRGY 160
Cdd:PRK09411 79 ESQGMIGYMLAQS----LSAQPQMPPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPE---EQEALEAAYGWQMKRdGKYL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 161 RRVVPSPKPVNVREYQVINSLVDNNVIPISVGGGGVPVVREGNhliGCEAVIDKDFASEKLAELIKADLLIILTAVDNVY 240
Cdd:PRK09411 152 RRVVASPQPRKILDSEAIELLLKEGHVVICSGGGGVPVTEDGA---GSEAVIDKDLAAALLAEQINADGLVILTDADAVY 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488909732 241 INFNKPDQKKLENVTVEELEnyinenQFAK--GSMLPKVQAAINFVNNGCGEAVVTSLKNINNFLQKGSGTIITK 313
Cdd:PRK09411 229 ENWGTPQQRAIRHATPDELA------PFAKadGAMGPKVTAVSGYVRSRGKPAWIGALSRIEETLAGEAGTCISL 297
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
4-295 |
6.60e-24 |
|
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: 97.44 E-value: 6.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 4 RKIVVALGGNAILSKDAsaeaqqaaLRETAKSLVSLVKENEKLIITHGNGPQVGNLLLQQMIGSTksnpampidtavsmt 83
Cdd:pfam00696 1 KRVVIKLGGSSLTDKER--------LKRLADEIAALLEEGRKLVVVHGGGAFADGLLALLGLSPR--------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 84 egsigywMQNAMDDVLEDEGIDKSAATVVTQVEVDANDSAFQNpskpigpfyekedinkiRELHPEYIYVEDAGRgyrrv 163
Cdd:pfam00696 58 -------FARLTDAETLEVATMDALGSLGERLNAALLAAGLPA-----------------VGLPAAQLLATEAGF----- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 164 vpSPKPVNVREYQVINSLVDNNVIPISVggggvpvvreGNHLI---GCEAVIDKDFASEKLAELIKADLLIILTAVDNVY 240
Cdd:pfam00696 109 --IDDVVTRIDTEALEELLEAGVVPVIT----------GFIGIdpeGELGRGSSDTLAALLAEALGADKLIILTDVDGVY 176
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 488909732 241 INFNK--PDQKKLENVTVEELENYINeNQFAKGSMLPKVQAAINFVNNGCGEAVVTS 295
Cdd:pfam00696 177 TADPRkvPDAKLIPEISYDELLELLA-SGLATGGMKVKLPAALEAARRGGIPVVIVN 232
|
|
| AAK |
cd02115 |
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ... |
7-311 |
2.80e-18 |
|
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: 82.49 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 7 VVALGGNAIlskdasaeAQQAALRETAKSLVSLVKENEKLIITHGNGPQVGNLLL----QQMIGSTKSNPAMPIDTAVSM 82
Cdd:cd02115 1 VIKFGGSSV--------SSEERLRNLARILVKLASEGGRVVVVHGAGPQITDELLahgeLLGYARGLRITDRETDALAAM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 83 TEGSIGYWMQNAmddvLEDEGIDksAATVVTQVEVDANDSAFQNpskpigpfyekediNKIRELHPEyiyvedagrgyrr 162
Cdd:cd02115 73 GEGMSNLLIAAA----LEQHGIK--AVPLDLTQAGFASPNQGHV--------------GKITKVSTD------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 163 vvpspkpvnvreyqVINSLVDNNVIPISVGGGGVPvvregNHLIGCEAVIDKDFASEKLAELIKADLLIILTAVDNVYIN 242
Cdd:cd02115 120 --------------RLKSLLENGILPILSGFGGTD-----EKETGTLGRGGSDSTAALLAAALKADRLVILTDVDGVYTA 180
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488909732 243 FNK--PDQKKLENVTVEELENYINenqfaKGSMLPKVQAAINFVNNGCgEAVVTSLKN---INNFLQKGSGTII 311
Cdd:cd02115 181 DPRkvPDAKLLSELTYEEAAELAY-----AGAMVLKPKAADPAARAGI-PVRIANTENpgaLALFTPDGGGTLI 248
|
|
| AAK_NAGK-like |
cd04238 |
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ... |
6-311 |
8.58e-13 |
|
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: 67.15 E-value: 8.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 6 IVVALGGNAILSKDAsaeaqqaaLRETAKSLVSLVKENEKLIITHGNGPQVGNLLLQQMIGSTKSN-------PAMPIdt 78
Cdd:cd04238 1 VVIKYGGSAMKDEEL--------KEAFADDIVLLKQVGINPVIVHGGGPEINELLKRLGIESEFVNglrvtdkETMEI-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 79 aVSMT-EGSIGYWMQNamddvledeGIDKSAATVVTQVEVDANdsafqnpskpigPFYEKEDINKIRELhpeyiyvedag 157
Cdd:cd04238 71 -VEMVlAGKVNKELVS---------LLNRAGGKAVGLSGKDGG------------LIKAEKKEEKDIDL----------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 158 rGYrrvVPSPKPVNVreyQVINSLVDNNVIPIsvggggvpvvregnhlIGCEAV--------IDKDFASEKLAELIKADL 229
Cdd:cd04238 118 -GF---VGEVTEVNP---ELLETLLEAGYIPV----------------IAPIAVdedgetynVNADTAAGAIAAALKAEK 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 230 LIILTAVDNVYINFNKPdqkkLENVTVEELENYINENqFAKGSMLPKVQAAINFVNNGCGEAVVTSLKNINNFLQ----- 304
Cdd:cd04238 175 LILLTDVPGVLDDPGSL----ISELTPKEAEELIEDG-VISGGMIPKVEAALEALEGGVRKVHIIDGRVPHSLLLelftd 249
|
....*..
gi 488909732 305 KGSGTII 311
Cdd:cd04238 250 EGIGTMI 256
|
|
| PRK00942 |
PRK00942 |
acetylglutamate kinase; Provisional |
1-313 |
2.03e-10 |
|
acetylglutamate kinase; Provisional
Pssm-ID: 234869 [Multi-domain] Cd Length: 283 Bit Score: 60.51 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 1 MANRKIVVALGGNAILSKDAsaeaqqaaLRETAKSLVSLVKENEKLIITHGNGPQVGNLLLQQMIGSTKSN-------PA 73
Cdd:PRK00942 21 FMGKTIVIKYGGNAMTDEEL--------KEAFARDIVLLKQVGINPVVVHGGGPQIDELLKKLGIESEFVNglrvtdaET 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 74 MPIdtaVSMtegsigywmqnamddVLedegIDKSAATVVTQvevdANdsafQNPSKPIG------------PFYEKEDIn 141
Cdd:PRK00942 93 MEV---VEM---------------VL----AGKVNKELVSL----IN----KHGGKAVGlsgkdgglitakKLEEDEDL- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 142 kirelhpeyiyvedagrGYrrvVPSPKPVNVreyQVINSLVDNNVIP-ISVGGGGvpvvREGNHLIgceavIDKDFASEK 220
Cdd:PRK00942 142 -----------------GF---VGEVTPVNP---ALLEALLEAGYIPvISPIGVG----EDGETYN-----INADTAAGA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 221 LAELIKADLLIILTAVDNVYinfNKPDQKkLENVTVEELENYINENQFAKGsMLPKVQAAINFVNNGCGEAVVTS----- 295
Cdd:PRK00942 190 IAAALGAEKLILLTDVPGVL---DDKGQL-ISELTASEAEELIEDGVITGG-MIPKVEAALDAARGGVRSVHIIDgrvph 264
|
330 340
....*....|....*....|
gi 488909732 296 --LKNInnFLQKGSGTIITK 313
Cdd:PRK00942 265 alLLEL--FTDEGIGTMIVP 282
|
|
| AAK_NAGK-C |
cd04250 |
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ... |
212-293 |
1.80e-09 |
|
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: 57.52 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 212 IDKDFASEKLAELIKADLLIILTAVDNVYINFNKPDqKKLENVTVEELENYINENQfAKGSMLPKVQAAINFVNNGCGEA 291
Cdd:cd04250 177 INADTAAGAIAAALKAEKLILLTDVAGVLDDPNDPG-SLISEISLKEAEELIADGI-ISGGMIPKVEACIEALEGGVKAA 254
|
..
gi 488909732 292 VV 293
Cdd:cd04250 255 HI 256
|
|
| PRK14058 |
PRK14058 |
[LysW]-aminoadipate/[LysW]-glutamate kinase; |
212-313 |
8.21e-09 |
|
[LysW]-aminoadipate/[LysW]-glutamate kinase;
Pssm-ID: 237599 [Multi-domain] Cd Length: 268 Bit Score: 55.29 E-value: 8.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 212 IDKDFASEKLAELIKADLLIILTAVDNVYINFNKPDqKKLENVTVEELENYineNQFAKGSMLPKVQAAINFVNNGCGEA 291
Cdd:PRK14058 168 VDGDRAAAAIAGALKAEALVLLSDVPGLLRDPPDEG-SLIERITPEEAEEL---SKAAGGGMKKKVLMAAEAVEGGVGRV 243
|
90 100
....*....|....*....|....*
gi 488909732 292 VVTSL---KNINNFLQkGSGTIITK 313
Cdd:PRK14058 244 IIADAnvdDPISAALA-GEGTVIVN 267
|
|
| ArgB |
COG0548 |
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ... |
1-312 |
7.17e-08 |
|
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: 52.73 E-value: 7.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 1 MANRKIVVALGGNAIlskdasaeAQQAALRETAKSLVSLVKENEKLIITHGNGPQVGNLLLQQMIGSTKSN-------PA 73
Cdd:COG0548 21 FRGKTFVIKYGGEAM--------EDEELKAALAQDIALLKSLGIRPVLVHGGGPQINELLKRLGIESEFVNglrvtdeET 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 74 MPIdtaVSMTE-GSIGYWMQNAmddvLEDEGIDKSAATVVtqvevDANdsAFQnpSKPIGPfyekedinkirELHPEYIY 152
Cdd:COG0548 93 LEV---VEMVLaGKVNKEIVAL----LSQGGGNAVGLSGK-----DGN--LIT--ARPLGV-----------GDGVDLGH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 153 VedaGRgyrrvvpsPKPVNVreyQVINSLVDNNVIPisvggggvpvvregnhLIGCEAV--------IDKDFASEKLAEL 224
Cdd:COG0548 146 V---GE--------VRRVDP---ELIRALLDAGYIP----------------VISPIGYsptgevynINADTVAGAIAAA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 225 IKADLLIILTAVDNVYinfnkPDQKKL-ENVTVEELENYINENQFAKGsMLPKVQAAINFVNNGCGEAVVTS-------L 296
Cdd:COG0548 196 LKAEKLILLTDVPGVL-----DDPGSLiSELTAAEAEELIADGVISGG-MIPKLEAALDAVRGGVKRVHIIDgrvphalL 269
|
330
....*....|....*.
gi 488909732 297 KNInnFLQKGSGTIIT 312
Cdd:COG0548 270 LEL--FTDDGIGTMIV 283
|
|
| AAK_P5CS_ProBA |
cd04256 |
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ... |
178-295 |
2.35e-07 |
|
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta 1-pyrroline-5-carboxylate synthetase (P5CS), composed of an N-terminal G5K (ProB) and a C-terminal glutamyl 5- phosphate reductase (G5PR, ProA), the first and second enzyme catalyzing proline (and, in mammals, ornithine) biosynthesis. G5K transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, and is subject to feedback allosteric inhibition by proline or ornithine. In plants, proline plays an important role as an osmoprotectant and, in mammals, ornithine biosynthesis is crucial for proper ammonia detoxification, since a G5K mutation has been shown to cause human hyperammonaemia.
Pssm-ID: 239789 [Multi-domain] Cd Length: 284 Bit Score: 51.28 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 178 INSLVDNNVIPISVGGGGVPVVREGNH-LIGCEAVIDKDFASEKLAELIKADLLIILTAVDNVYI------------NFN 244
Cdd:cd04256 143 LEELLRLNIIPIINTNDAVSPPPEPDEdLQGVISIKDNDSLAARLAVELKADLLILLSDVDGLYDgppgsddaklihTFY 222
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 488909732 245 KPDQKKLEnvtveelenYINENQFAKGSMLPKVQAAINFVNNGCgEAVVTS 295
Cdd:cd04256 223 PGDQQSIT---------FGTKSRVGTGGMEAKVKAALWALQGGT-SVVITN 263
|
|
| PRK12314 |
PRK12314 |
gamma-glutamyl kinase; Provisional |
161-313 |
1.06e-06 |
|
gamma-glutamyl kinase; Provisional
Pssm-ID: 183430 [Multi-domain] Cd Length: 266 Bit Score: 49.08 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 161 RRVVPSPKPV-NVReyQVINSLVDNNVIPIsvggggvpvVREgNHLIGCEAVI----DKDFASEKLAELIKADLLIILTA 235
Cdd:PRK12314 110 RDDFDSPKSRaNVK--NTFESLLELGILPI---------VNE-NDAVATDEIDtkfgDNDRLSAIVAKLVKADLLIILSD 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 236 VDNVY-----INFNKPDQKKLENVTVEELENYINEN-QFAKGSMLPKVQAAINFVNNGCgEAVVTS---LKNINNFLQKG 306
Cdd:PRK12314 178 IDGLYdknprINPDAKLRSEVTEITEEILALAGGAGsKFGTGGMVTKLKAAKFLMEAGI-KMVLANgfnPSDILDFLEGE 256
|
....*...
gi 488909732 307 S-GTIITK 313
Cdd:PRK12314 257 SiGTLFAP 264
|
|
| AAK_NAGK-UC |
cd04251 |
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ... |
212-311 |
5.39e-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: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 212 IDKDFASEKLAELIKADLLIILTAVDNVYInfnkpDQKKLENVTVEELENYINEnqfAKGSMLPKVQAAINFVNNGCGEA 291
Cdd:cd04251 164 VDGDRAAAAIAAALKAERLILLTDVEGLYL-----DGRVIERITVSDAESLLEK---AGGGMKRKLLAAAEAVEGGVREV 235
|
90 100
....*....|....*....|...
gi 488909732 292 VVTS---LKNINNFLQkGSGTII 311
Cdd:cd04251 236 VIGDaraDSPISSALN-GGGTVI 257
|
|
| AAK_G5K_ProB |
cd04242 |
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ... |
171-312 |
7.76e-06 |
|
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, in the first and controlling step of proline (and, in mammals, ornithine) biosynthesis. G5K is subject to feedback allosteric inhibition by proline or ornithine. In microorganisms and plants, proline plays an important role as an osmoprotectant and, in mammals, ornithine biosynthesis is crucial for proper ammonia detoxification, since a G5K mutation has been shown to cause human hyperammonaemia. Microbial G5K generally consists of two domains: a catalytic G5K domain and one PUA (pseudo uridine synthases and archaeosine-specific transglycosylases) domain, and some lack the PUA domain. G5K requires free Mg for activity, it is tetrameric, and it aggregates to higher forms in a proline-dependent way. G5K lacking the PUA domain remains tetrameric, active, and proline-inhibitable, but the Mg requirement and the proline-triggered aggregation are greatly diminished and abolished, respectively, and more proline is needed for inhibition. Although plant and animal G5Ks are part of a bifunctional polypeptide, delta 1-pyrroline-5-carboxylate synthetase (P5CS), composed of an N-terminal G5K (ProB) and a C-terminal glutamyl 5- phosphate reductase (G5PR; ProA); bacterial and yeast G5Ks are monofunctional single-polypeptide enzymes. In this CD, all three domain architectures are present: G5K, G5K+PUA, and G5K+G5PR.
Pssm-ID: 239775 [Multi-domain] Cd Length: 251 Bit Score: 46.28 E-value: 7.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 171 NVReyQVINSLVDNNVIPIsvggggvpvVREgNHLIGCE--AVIDKDFASEKLAELIKADLLIILTAVDNVY-----INf 243
Cdd:cd04242 111 NAR--NTLETLLELGVIPI---------INE-NDTVATEeiRFGDNDRLSALVAGLVNADLLILLSDVDGLYdknprEN- 177
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488909732 244 nkPDQKKLENVTV--EELENYINE--NQFAKGSMLPKVQAAINFVNNGCgEAVVTSLKNINNFLQ----KGSGTIIT 312
Cdd:cd04242 178 --PDAKLIPEVEEitDEIEAMAGGsgSSVGTGGMRTKLKAARIATEAGI-PVVIANGRKPDVLLDilagEAVGTLFL 251
|
|
| PLN02512 |
PLN02512 |
acetylglutamate kinase |
177-312 |
2.01e-05 |
|
acetylglutamate kinase
Pssm-ID: 178128 Cd Length: 309 Bit Score: 45.45 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 177 VINSLVDNNVIPISVGGGGVPVVREGNhligceavIDKDFASEKLAELIKADLLIILTAVDNVYINFNKPDQkKLENVTV 256
Cdd:PLN02512 178 VLRPLVDDGHIPVIATVAADEDGQAYN--------INADTAAGEIAAALGAEKLILLTDVAGVLEDKDDPGS-LVKELDI 248
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488909732 257 EELENYINENQFAkGSMLPKVQAAINFVNNGCGEAVVT------SLknINNFL-QKGSGTIIT 312
Cdd:PLN02512 249 KGVRKLIADGKIA-GGMIPKVECCVRSLAQGVKTAHIIdgrvphSL--LLEILtDEGAGTMIT 308
|
|
| PLN02418 |
PLN02418 |
delta-1-pyrroline-5-carboxylate synthase |
176-305 |
2.09e-04 |
|
delta-1-pyrroline-5-carboxylate synthase
Pssm-ID: 215230 Cd Length: 718 Bit Score: 42.79 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 176 QVINSLVDNNVIPIsVGGGGVPVVREGNHLIGCEAVIDKDFASEKLAELIKADLLIILTAVDNVYIN-FNKPDQKKLENV 254
Cdd:PLN02418 140 ETVESLLDLRVIPI-FNENDAVSTRRAPYEDSSGIFWDNDSLAALLALELKADLLILLSDVEGLYTGpPSDPSSKLIHTY 218
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 488909732 255 TVEELENYI---NENQFAKGSMLPKVQAAINFVNNGCgEAVVTS---LKNINNFLQK 305
Cdd:PLN02418 219 IKEKHQDEItfgEKSRVGRGGMTAKVKAAVNAASAGI-PVVITSgyaLDNIRKVLRG 274
|
|
| AAK_UMPK-PyrH-Pf |
cd04253 |
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ... |
220-312 |
2.95e-04 |
|
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: 41.46 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 220 KLAELIKADLLIILTAVDNVYINFNK--PDQKKLENVTVEELENYINENQFAKGSMLPKVQAAINFVNNGCGEAVVTSLK 297
Cdd:cd04253 123 LLAERLGADLLINATNVDGVYSKDPRkdPDAKKFDRLSADELIDIVGKSSWKAGSNEPFDPLAAKIIERSGIKTIVVDGR 202
|
90
....*....|....*....
gi 488909732 298 NINNFL----QKGSGTIIT 312
Cdd:cd04253 203 DPENLEralkGEFVGTIIE 221
|
|
| P5CS |
TIGR01092 |
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ... |
176-287 |
3.52e-03 |
|
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, EC 2.7.2.11) region followed by a gamma-glutamyl phosphate reductase (ProA, EC 1.2.1.41) region. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130164 [Multi-domain] Cd Length: 715 Bit Score: 39.12 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909732 176 QVINSLVDNNVIPISVGGGGVPVVREGNH-LIGceAVIDKDFASEKLAELIKADLLIILTAVDNVYINFNKPDQKKLENV 254
Cdd:TIGR01092 132 ETVHELLRMNVVPVVNENDAVSTRAAPYSdSQG--IFWDNDSLAALLALELKADLLILLSDVEGLYDGPPSDDDSKLIDT 209
|
90 100 110
....*....|....*....|....*....|....*..
gi 488909732 255 TVEELEN----YINENQFAKGSMLPKVQAAINFVNNG 287
Cdd:TIGR01092 210 FYKEKHQgeitFGTKSRLGRGGMTAKVKAAVWAAYGG 246
|
|
| |
