|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12354 |
PRK12354 |
carbamate kinase; Reviewed |
2-302 |
0e+00 |
|
carbamate kinase; Reviewed
Pssm-ID: 183466 Cd Length: 307 Bit Score: 544.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 2 VVALGGNALLRRTDPMTAEAQRANVKVAAKALAPLAEEYNLVLAHGNGPQVGLLALQAAAYTDVEPYPLDVLGAQTQGMI 81
Cdd:PRK12354 4 VVALGGNALLRRGEPLTAENQRANIRIAAEQIAKIAREHELVIVHGNGPQVGLLALQNAAYKDVTPYPLDVLGAETEGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 82 AYMVEQELGNLLPfEKPLATVLTMTEVDPDDPAFKNPTKFVGPCYSKDDADRLAAKKGWMFKPDGQLWRRVVASPEPRQI 161
Cdd:PRK12354 84 GYMLEQELGNLLP-ERPVATLLTQVEVDANDPAFANPTKPIGPVYDEAEAERLAAEKGWTIKPDGDYFRRVVPSPRPKRI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 162 FELDPIKWLIEKGTVVICAGGGGIPTVYLPDGtrTLVGIEAVIDKDLAAELLARNLGADIFVMATDAEGVCLDWGTTEQR 241
Cdd:PRK12354 163 VEIRPIRWLLEKGHLVICAGGGGIPVVYDADG--KLHGVEAVIDKDLAAALLAEQLDADLLLILTDVDAVYLDWGKPTQR 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309179813 242 VLGTTTPEELDKYEFAAGSMGPKVEAAKRFVRSTGGRAAIGRLEDITLIAAGNAGTTIVPG 302
Cdd:PRK12354 241 AIAQATPDELRELGFAAGSMGPKVEAACEFVRATGKIAGIGSLEDIQAILAGEAGTRISPE 301
|
|
| ArcC |
COG0549 |
Carbamate kinase [Amino acid transport and metabolism]; |
1-301 |
8.28e-179 |
|
Carbamate kinase [Amino acid transport and metabolism];
Pssm-ID: 440315 Cd Length: 313 Bit Score: 495.75 E-value: 8.28e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 1 MVVALGGNALLRRTDPMTAEAQRANVKVAAKALAPLAEE-YNLVLAHGNGPQVGLLALQAAAYTD-VEPYPLDVLGAQTQ 78
Cdd:COG0549 5 IVVALGGNALLRRGEPGTAEEQRENVREAAKALADLIEAgHEVVITHGNGPQVGLLLLQNEAAKKkVPPMPLDVCGAMTQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 79 GMIAYMVEQELGNLLPF---EKPLATVLTMTEVDPDDPAFKNPTKFVGPCYSKDDADRLAAKKGWMFKPD-GQLWRRVVA 154
Cdd:COG0549 85 GMIGYMLQQALRNELPKrgiDKPVATLVTQVEVDPDDPAFQNPTKPIGPFYTEEEAEELAKEKGWTFKEDaGRGYRRVVP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 155 SPEPRQIFELDPIKWLIEKGTVVICAGGGGIPTVYLPDGTrtLVGIEAVIDKDLAAELLARNLGADIFVMATDAEGVCLD 234
Cdd:COG0549 165 SPKPKRIVEIDAIKALLEAGVIVIAAGGGGIPVVRDEDGG--LKGVEAVIDKDLASALLAEELDADLLLILTDVDKVYIN 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309179813 235 WGTTEQRVLGTTTPEELDKY----EFAAGSMGPKVEAAKRFVRSTGGRAAIGRLEDITLIAAGNAGTTIVP 301
Cdd:COG0549 243 FGKPDQRALDEVTVAEAKKYieegHFAAGSMGPKVEAAIRFVEATGKRAIITSLEKAEEALAGKAGTRIVP 313
|
|
| AAK_CK |
cd04235 |
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ... |
1-300 |
1.69e-165 |
|
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: 461.98 E-value: 1.69e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 1 MVVALGGNALLRRTDPMTAEAQRANVKVAAKALAPLAEE-YNLVLAHGNGPQVGLLALQAAAYTD-VEPYPLDVLGAQTQ 78
Cdd:cd04235 2 IVVALGGNALLRRGEPGTAEEQRENVKIAAKALADLIKNgHEVVITHGNGPQVGNLLLQNEAAAEkVPAYPLDVCGAMSQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 79 GMIAYMVEQELGNLLPF---EKPLATVLTMTEVDPDDPAFKNPTKFVGPCYSKDDADRLAAKKGWMFKPD-GQLWRRVVA 154
Cdd:cd04235 82 GMIGYMLQQALDNELPKrgiDKPVVTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEKGWTFKEDaGRGYRRVVP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 155 SPEPRQIFELDPIKWLIEKGTVVICAGGGGIPTVYLPDGtrtLVGIEAVIDKDLAAELLARNLGADIFVMATDAEGVCLD 234
Cdd:cd04235 162 SPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREGGG---LKGVEAVIDKDLASALLAEEINADLLVILTDVDNVYIN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 235 WGTTEQRVLGTTTPEELDKY----EFAAGSMGPKVEAAKRFVRSTGGRAAIGRLEDITLIAAGNAGTTIV 300
Cdd:cd04235 239 FGKPNQKALEQVTVEELEKYieegQFAPGSMGPKVEAAIRFVESGGKKAIITSLENAEAALEGKAGTVIV 308
|
|
| arcC |
TIGR00746 |
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes ... |
1-301 |
1.78e-139 |
|
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes carbamoyl phosphate to convert ADP into ATP. In the pathway in Pyrococcus furiosus, the enzyme acts instead to generate carbamoyl phosphate.The seed alignment for this model includes experimentally confirmed examples from a set of phylogenetically distinct species. In a neighbor-joining tree constructed from an alignment of candidate carbamate kinases and several acetylglutamate kinases, the latter group forms a clear outgroup which roots the tree of carbamate kinase-like proteins. This analysis suggests that in E. coli, the ArcC paralog YqeA may be a second isozyme, while the paralog YahI branches as an outlier and is less likely to be an authentic carbamate kinase. The homolog from Mycoplasma pneumoniae likewise branches outside the set containing known carbamate kinases and also scores below the trusted cutoff. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273248 Cd Length: 310 Bit Score: 396.06 E-value: 1.78e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 1 MVVALGGNALLRRTDPMTAEAQRANVKVAAKALAPLAEE-YNLVLAHGNGPQVGLLALQAAAY-TDVEPYPLDVLGAQTQ 78
Cdd:TIGR00746 3 VVVALGGNALLQRGEKGSAEAQRDNVRQTAPQIAKLIKRgYELVITHGNGPQVGNLLLQNQAAdSEVPAMPLDVLGAMSQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 79 GMIAYMVEQELGNLLP---FEKPLATVLTMTEVDPDDPAFKNPTKFVGPCYSKDDADRLAAKKGWMFKPD-GQLWRRVVA 154
Cdd:TIGR00746 83 GMIGYMLQQALNNELPkrgMEKPVATVLTQTIVDPKDPAFQNPTKPIGPFYTEEEAKRLAAEKGWIVKEDaGRGWRRVVP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 155 SPEPRQIFELDPIKWLIEKGTVVICAGGGGIPTVYLPDGtrtLVGIEAVIDKDLAAELLARNLGADIFVMATDAEGVCLD 234
Cdd:TIGR00746 163 SPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEGAE---LKGVEAVIDKDLASEKLAEEVNADILVILTDVDAVYIN 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309179813 235 WGTTEQRVLGTTTPEELDKY----EFAAGSMGPKVEAAKRFVRSTGGRAAIGRLEDITLIAAGNAGTTIVP 301
Cdd:TIGR00746 240 YGKPDEKALREVTVEELEDYykagHFAAGSMGPKVEAAIEFVESGGKRAIITSLENAVEALEGKAGTRVTK 310
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
2-281 |
9.09e-12 |
|
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: 63.54 E-value: 9.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 2 VVALGGNALlrrtdpmtaeAQRANVKVAAKALAPLAEE-YNLVLAHGNGPQV-GLLALQAAAYTDVEPYPLDVLGAQTQG 79
Cdd:pfam00696 4 VIKLGGSSL----------TDKERLKRLADEIAALLEEgRKLVVVHGGGAFAdGLLALLGLSPRFARLTDAETLEVATMD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 80 MIAYMVEQELGNLLpfekplatvltmtevdpddpafknptkfvgpcyskddADRLAAKKgwmFKPDGQLWRRVVASPEPR 159
Cdd:pfam00696 74 ALGSLGERLNAALL-------------------------------------AAGLPAVG---LPAAQLLATEAGFIDDVV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 160 QIFELDPIKWLIEKGTVVICAGGGGIptvylpdgtrTLVGIEAVIDKDLAAELLARNLGADIFVMATDAEGVCLDWGTTE 239
Cdd:pfam00696 114 TRIDTEALEELLEAGVVPVITGFIGI----------DPEGELGRGSSDTLAALLAEALGADKLIILTDVDGVYTADPRKV 183
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1309179813 240 Q--RVLGTTTPEELDKY---EFAAGSMGPKVEAAKRFVRSTGGRAAI 281
Cdd:pfam00696 184 PdaKLIPEISYDELLELlasGLATGGMKVKLPAALEAARRGGIPVVI 230
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12354 |
PRK12354 |
carbamate kinase; Reviewed |
2-302 |
0e+00 |
|
carbamate kinase; Reviewed
Pssm-ID: 183466 Cd Length: 307 Bit Score: 544.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 2 VVALGGNALLRRTDPMTAEAQRANVKVAAKALAPLAEEYNLVLAHGNGPQVGLLALQAAAYTDVEPYPLDVLGAQTQGMI 81
Cdd:PRK12354 4 VVALGGNALLRRGEPLTAENQRANIRIAAEQIAKIAREHELVIVHGNGPQVGLLALQNAAYKDVTPYPLDVLGAETEGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 82 AYMVEQELGNLLPfEKPLATVLTMTEVDPDDPAFKNPTKFVGPCYSKDDADRLAAKKGWMFKPDGQLWRRVVASPEPRQI 161
Cdd:PRK12354 84 GYMLEQELGNLLP-ERPVATLLTQVEVDANDPAFANPTKPIGPVYDEAEAERLAAEKGWTIKPDGDYFRRVVPSPRPKRI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 162 FELDPIKWLIEKGTVVICAGGGGIPTVYLPDGtrTLVGIEAVIDKDLAAELLARNLGADIFVMATDAEGVCLDWGTTEQR 241
Cdd:PRK12354 163 VEIRPIRWLLEKGHLVICAGGGGIPVVYDADG--KLHGVEAVIDKDLAAALLAEQLDADLLLILTDVDAVYLDWGKPTQR 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309179813 242 VLGTTTPEELDKYEFAAGSMGPKVEAAKRFVRSTGGRAAIGRLEDITLIAAGNAGTTIVPG 302
Cdd:PRK12354 241 AIAQATPDELRELGFAAGSMGPKVEAACEFVRATGKIAGIGSLEDIQAILAGEAGTRISPE 301
|
|
| ArcC |
COG0549 |
Carbamate kinase [Amino acid transport and metabolism]; |
1-301 |
8.28e-179 |
|
Carbamate kinase [Amino acid transport and metabolism];
Pssm-ID: 440315 Cd Length: 313 Bit Score: 495.75 E-value: 8.28e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 1 MVVALGGNALLRRTDPMTAEAQRANVKVAAKALAPLAEE-YNLVLAHGNGPQVGLLALQAAAYTD-VEPYPLDVLGAQTQ 78
Cdd:COG0549 5 IVVALGGNALLRRGEPGTAEEQRENVREAAKALADLIEAgHEVVITHGNGPQVGLLLLQNEAAKKkVPPMPLDVCGAMTQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 79 GMIAYMVEQELGNLLPF---EKPLATVLTMTEVDPDDPAFKNPTKFVGPCYSKDDADRLAAKKGWMFKPD-GQLWRRVVA 154
Cdd:COG0549 85 GMIGYMLQQALRNELPKrgiDKPVATLVTQVEVDPDDPAFQNPTKPIGPFYTEEEAEELAKEKGWTFKEDaGRGYRRVVP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 155 SPEPRQIFELDPIKWLIEKGTVVICAGGGGIPTVYLPDGTrtLVGIEAVIDKDLAAELLARNLGADIFVMATDAEGVCLD 234
Cdd:COG0549 165 SPKPKRIVEIDAIKALLEAGVIVIAAGGGGIPVVRDEDGG--LKGVEAVIDKDLASALLAEELDADLLLILTDVDKVYIN 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309179813 235 WGTTEQRVLGTTTPEELDKY----EFAAGSMGPKVEAAKRFVRSTGGRAAIGRLEDITLIAAGNAGTTIVP 301
Cdd:COG0549 243 FGKPDQRALDEVTVAEAKKYieegHFAAGSMGPKVEAAIRFVEATGKRAIITSLEKAEEALAGKAGTRIVP 313
|
|
| AAK_CK |
cd04235 |
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ... |
1-300 |
1.69e-165 |
|
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: 461.98 E-value: 1.69e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 1 MVVALGGNALLRRTDPMTAEAQRANVKVAAKALAPLAEE-YNLVLAHGNGPQVGLLALQAAAYTD-VEPYPLDVLGAQTQ 78
Cdd:cd04235 2 IVVALGGNALLRRGEPGTAEEQRENVKIAAKALADLIKNgHEVVITHGNGPQVGNLLLQNEAAAEkVPAYPLDVCGAMSQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 79 GMIAYMVEQELGNLLPF---EKPLATVLTMTEVDPDDPAFKNPTKFVGPCYSKDDADRLAAKKGWMFKPD-GQLWRRVVA 154
Cdd:cd04235 82 GMIGYMLQQALDNELPKrgiDKPVVTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEKGWTFKEDaGRGYRRVVP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 155 SPEPRQIFELDPIKWLIEKGTVVICAGGGGIPTVYLPDGtrtLVGIEAVIDKDLAAELLARNLGADIFVMATDAEGVCLD 234
Cdd:cd04235 162 SPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREGGG---LKGVEAVIDKDLASALLAEEINADLLVILTDVDNVYIN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 235 WGTTEQRVLGTTTPEELDKY----EFAAGSMGPKVEAAKRFVRSTGGRAAIGRLEDITLIAAGNAGTTIV 300
Cdd:cd04235 239 FGKPNQKALEQVTVEELEKYieegQFAPGSMGPKVEAAIRFVESGGKKAIITSLENAEAALEGKAGTVIV 308
|
|
| PRK12454 |
PRK12454 |
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed |
2-301 |
1.08e-141 |
|
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
Pssm-ID: 183535 Cd Length: 313 Bit Score: 402.07 E-value: 1.08e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 2 VVALGGNALLRRTDPMTAEAQRANVKVAAKALAPLAEE-YNLVLAHGNGPQVGLLALQAAAYTDV--EPYPLDVLGAQTQ 78
Cdd:PRK12454 6 VIALGGNALLQPGEKGTAENQMKNVRKTAKQIADLIEEgYEVVITHGNGPQVGNLLLQMDAAKDVgiPPFPLDVAGAMTQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 79 GMIAYMVEQELGNLLP---FEKPLATVLTMTEVDPDDPAFKNPTKFVGPCYSKDDADRLAAKKGWMFKPD-GQLWRRVVA 154
Cdd:PRK12454 86 GWIGYMIQQALRNELAkrgIEKQVATIVTQVIVDKNDPAFQNPTKPVGPFYDEEEAKKLAKEKGWIVKEDaGRGWRRVVP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 155 SPEPRQIFELDPIKWLIEKGTVVICAGGGGIPTVylpDGTRTLVGIEAVIDKDLAAELLARNLGADIFVMATDAEGVCLD 234
Cdd:PRK12454 166 SPDPLGIVEIEVIKALVENGFIVIASGGGGIPVI---EEDGELKGVEAVIDKDLASELLAEELNADIFIILTDVEKVYLN 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309179813 235 WGTTEQRVLGTTTPEELDKY----EFAAGSMGPKVEAAKRFVRSTGGRAAIGRLEDITLIAAGNAGTTIVP 301
Cdd:PRK12454 243 YGKPDQKPLDKVTVEEAKKYyeegHFKAGSMGPKILAAIRFVENGGKRAIIASLEKAVEALEGKTGTRIIP 313
|
|
| arcC |
TIGR00746 |
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes ... |
1-301 |
1.78e-139 |
|
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes carbamoyl phosphate to convert ADP into ATP. In the pathway in Pyrococcus furiosus, the enzyme acts instead to generate carbamoyl phosphate.The seed alignment for this model includes experimentally confirmed examples from a set of phylogenetically distinct species. In a neighbor-joining tree constructed from an alignment of candidate carbamate kinases and several acetylglutamate kinases, the latter group forms a clear outgroup which roots the tree of carbamate kinase-like proteins. This analysis suggests that in E. coli, the ArcC paralog YqeA may be a second isozyme, while the paralog YahI branches as an outlier and is less likely to be an authentic carbamate kinase. The homolog from Mycoplasma pneumoniae likewise branches outside the set containing known carbamate kinases and also scores below the trusted cutoff. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273248 Cd Length: 310 Bit Score: 396.06 E-value: 1.78e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 1 MVVALGGNALLRRTDPMTAEAQRANVKVAAKALAPLAEE-YNLVLAHGNGPQVGLLALQAAAY-TDVEPYPLDVLGAQTQ 78
Cdd:TIGR00746 3 VVVALGGNALLQRGEKGSAEAQRDNVRQTAPQIAKLIKRgYELVITHGNGPQVGNLLLQNQAAdSEVPAMPLDVLGAMSQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 79 GMIAYMVEQELGNLLP---FEKPLATVLTMTEVDPDDPAFKNPTKFVGPCYSKDDADRLAAKKGWMFKPD-GQLWRRVVA 154
Cdd:TIGR00746 83 GMIGYMLQQALNNELPkrgMEKPVATVLTQTIVDPKDPAFQNPTKPIGPFYTEEEAKRLAAEKGWIVKEDaGRGWRRVVP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 155 SPEPRQIFELDPIKWLIEKGTVVICAGGGGIPTVYLPDGtrtLVGIEAVIDKDLAAELLARNLGADIFVMATDAEGVCLD 234
Cdd:TIGR00746 163 SPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEGAE---LKGVEAVIDKDLASEKLAEEVNADILVILTDVDAVYIN 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309179813 235 WGTTEQRVLGTTTPEELDKY----EFAAGSMGPKVEAAKRFVRSTGGRAAIGRLEDITLIAAGNAGTTIVP 301
Cdd:TIGR00746 240 YGKPDEKALREVTVEELEDYykagHFAAGSMGPKVEAAIEFVESGGKRAIITSLENAVEALEGKAGTRVTK 310
|
|
| PRK12353 |
PRK12353 |
putative amino acid kinase; Reviewed |
1-301 |
7.03e-137 |
|
putative amino acid kinase; Reviewed
Pssm-ID: 237071 Cd Length: 314 Bit Score: 389.51 E-value: 7.03e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 1 MVVALGGNALLRrtDPMTAEAQRANVKVAAKALAPLAEE-YNLVLAHGNGPQVG--LLALQAAA--YTDVEPYPLDVLGA 75
Cdd:PRK12353 5 IVVALGGNALGS--TPEEATAQLEAVKKTAKSLVDLIEEgHEVVITHGNGPQVGniLLAQEAAAseKNKVPAMPLDVCGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 76 QTQGMIAYMVEQELGNLLP---FEKPLATVLTMTEVDPDDPAFKNPTKFVGPCYSKDDADRLAAKKGWMFKPD-GQLWRR 151
Cdd:PRK12353 83 MSQGYIGYHLQNALRNELLkrgIDKPVATVVTQVVVDANDPAFKNPTKPIGPFYTEEEAEKLAKEKGYTFKEDaGRGYRR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 152 VVASPEPRQIFELDPIKWLIEKGTVVICAGGGGIPTVylpDGTRTLVGIEAVIDKDLAAELLARNLGADIFVMATDAEGV 231
Cdd:PRK12353 163 VVPSPKPVDIVEIEAIKTLVDAGQVVIAAGGGGIPVI---REGGGLKGVEAVIDKDFASAKLAELVDADLLIILTAVDKV 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309179813 232 CLDWGTTEQRVLGTTTPEELDKY----EFAAGSMGPKVEAAKRFVRS-TGGRAAIGRLEDITLIAAGNAGTTIVP 301
Cdd:PRK12353 240 YINFGKPNQKKLDEVTVSEAEKYieegQFAPGSMLPKVEAAISFVESrPGRKAIITSLEKAKEALEGKAGTVIVK 314
|
|
| PRK09411 |
PRK09411 |
carbamate kinase; Reviewed |
1-301 |
4.31e-119 |
|
carbamate kinase; Reviewed
Pssm-ID: 181831 Cd Length: 297 Bit Score: 344.09 E-value: 4.31e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 1 MVVALGGNALLRRTDPMTAEAQRANVKVAAKALAPLAEEYNLVLAHGNGPQVGLLALQAAAYTDVEPYPLDVLGAQTQGM 80
Cdd:PRK09411 4 LVVALGGNALLQRGEALTAENQYRNIASAVPALARLARSYRLAIVHGNGPQVGLLALQNLAWKEVEPYPLDVLVAESQGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 81 IAYMVEQELgNLLPFEKPLATVLTMTEVDPDDPAFKNPTKFVGPCYSKDDADRLAAKKGWMFKPDGQLWRRVVASPEPRQ 160
Cdd:PRK09411 84 IGYMLAQSL-SAQPQMPPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAYGWQMKRDGKYLRRVVASPQPRK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 161 IFELDPIKWLIEKGTVVICAGGGGIPTVYLPDGTrtlvgiEAVIDKDLAAELLARNLGADIFVMATDAEGVCLDWGTTEQ 240
Cdd:PRK09411 163 ILDSEAIELLLKEGHVVICSGGGGVPVTEDGAGS------EAVIDKDLAAALLAEQINADGLVILTDADAVYENWGTPQQ 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309179813 241 RVLGTTTPEELDKYEFAAGSMGPKVEAAKRFVRSTGGRAAIGRLEDITLIAAGNAGTTIVP 301
Cdd:PRK09411 237 RAIRHATPDELAPFAKADGAMGPKVTAVSGYVRSRGKPAWIGALSRIEETLAGEAGTCISL 297
|
|
| PRK12686 |
PRK12686 |
carbamate kinase; Reviewed |
2-300 |
4.06e-114 |
|
carbamate kinase; Reviewed
Pssm-ID: 183683 Cd Length: 312 Bit Score: 332.00 E-value: 4.06e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 2 VVALGGNALLrrTDPMTAEAQRANVKVAAKALAPLAEE-YNLVLAHGNGPQVGLLALQ--AAAYTDVEPYPLDVLGAQTQ 78
Cdd:PRK12686 6 VIALGGNAIL--QTEATAEAQQTAVREAAQHLVDLIEAgHDIVITHGNGPQVGNLLLQqaESNSNKVPAMPLDTCVAMSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 79 GMIAYMVEQELGNLLP---FEKPLATVLTMTEVDPDDPAFKNPTKFVGPCYSKDDADRLAAKKGWMFKPD-GQLWRRVVA 154
Cdd:PRK12686 84 GMIGYWLQNALNNELTergIDKPVITLVTQVEVDKDDPAFANPTKPIGPFYTEEEAKQQAEQPGSTFKEDaGRGYRRVVP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 155 SPEPRQIFELDPIKWLIEKGTVVICAGGGGIPtVYLPDGtrTLVGIEAVIDKDLAAELLARNLGADIFVMATDAEGVCLD 234
Cdd:PRK12686 164 SPKPQEIIEHDTIRTLVDGGNIVIACGGGGIP-VIRDDN--TLKGVEAVIDKDFASEKLAEQIDADLLIILTGVENVFIN 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309179813 235 WGTTEQRVLGTTTPEELDKY----EFAAGSMGPKVEAAKRFVRST-GGRAAIGRLEDITLIAAGNAGTTIV 300
Cdd:PRK12686 241 FNKPNQQKLDDITVAEAKQYiaegQFAPGSMLPKVEAAIDFVESGeGKKAIITSLEQAKEALAGNAGTHIT 311
|
|
| PRK12352 |
PRK12352 |
putative carbamate kinase; Reviewed |
1-300 |
3.24e-87 |
|
putative carbamate kinase; Reviewed
Pssm-ID: 183464 Cd Length: 316 Bit Score: 263.58 E-value: 3.24e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 1 MVVALGGNALLRRTDPMTAEAQRANVK-VAAKALAPLAEEYNLVLAHGNGPQVGLLALQAAAYTDVEPYP---LDVLGAQ 76
Cdd:PRK12352 5 VVVAIGGNSIIKDNASQSIEHQAEAVKaVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHEREGLPltpLANCVAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 77 TQGMIAYMVEQELGNLLPF--EKPLATVLTMTEVDPDDPAFKNPTKFVGPCYSKDDADRL-AAKKGWMFKPD-GQLWRRV 152
Cdd:PRK12352 85 TQGGIGYLIQQALNNRLARhgEKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDELqKANPDWRFVEDaGRGYRRV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 153 VASPEPRQIFELDPIKWLIEKGTVVICAGGGGIPTVYlpDGTRTLVGIEAVIDKDLAAELLARNLGADIFVMATDAEGVC 232
Cdd:PRK12352 165 VASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVR--TDAGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEKVC 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309179813 233 LDWGTTEQRVLGTTTPEELDKY----EFAAGSMGPKVEAAKRFVRSTGGRAAIGRLEDITLIAAGNAGTTIV 300
Cdd:PRK12352 243 IHFGKPQQQALDRVDIATMTRYmqegHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHII 314
|
|
| AAK |
cd02115 |
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ... |
2-299 |
8.48e-13 |
|
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like N-acetylglutamate kinase (NAGK), carbamate kinase (CK), aspartokinase (AK), glutamate-5-kinase (G5K) and UMP kinase (UMPK). The AAK superfamily includes kinases that phosphorylate a variety of amino acid substrates. These kinases catalyze the formation of phosphoric anhydrides, generally with a carboxylate, and use ATP as the source of the phosphoryl group; are involved in amino acid biosynthesis. Some of these kinases control the process via allosteric feed-back inhibition.
Pssm-ID: 239033 [Multi-domain] Cd Length: 248 Bit Score: 66.70 E-value: 8.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 2 VVALGGNALlrrtdpmtaeAQRANVKVAAKALAPLAEE-YNLVLAHGNGPQVG-------LLALQAAAYTdVEPYPLDVL 73
Cdd:cd02115 1 VIKFGGSSV----------SSEERLRNLARILVKLASEgGRVVVVHGAGPQITdellahgELLGYARGLR-ITDRETDAL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 74 GAQTQGMIAYMveqeLGNLLPFEKPLATVLTMTEVDPDDPafknPTKFVGPCYSKDDADrlaakkgwmfkpdgqlwrrvv 153
Cdd:cd02115 70 AAMGEGMSNLL----IAAALEQHGIKAVPLDLTQAGFASP----NQGHVGKITKVSTDR--------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 154 aspeprqifeldpIKWLIEKGTVVICAGGGGiptvylpdGTRTLVGIEAVIDKDLAAELLARNLGADIFVMATDAEGVCL 233
Cdd:cd02115 121 -------------LKSLLENGILPILSGFGG--------TDEKETGTLGRGGSDSTAALLAAALKADRLVILTDVDGVYT 179
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309179813 234 DWGTTEQ--RVLGTTTPEELDKYEfAAGSMGPKVEAAKRFVRStGGRAAIGR---LEDITLIAAGNAGTTI 299
Cdd:cd02115 180 ADPRKVPdaKLLSELTYEEAAELA-YAGAMVLKPKAADPAARA-GIPVRIANtenPGALALFTPDGGGTLI 248
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
2-281 |
9.09e-12 |
|
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: 63.54 E-value: 9.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 2 VVALGGNALlrrtdpmtaeAQRANVKVAAKALAPLAEE-YNLVLAHGNGPQV-GLLALQAAAYTDVEPYPLDVLGAQTQG 79
Cdd:pfam00696 4 VIKLGGSSL----------TDKERLKRLADEIAALLEEgRKLVVVHGGGAFAdGLLALLGLSPRFARLTDAETLEVATMD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 80 MIAYMVEQELGNLLpfekplatvltmtevdpddpafknptkfvgpcyskddADRLAAKKgwmFKPDGQLWRRVVASPEPR 159
Cdd:pfam00696 74 ALGSLGERLNAALL-------------------------------------AAGLPAVG---LPAAQLLATEAGFIDDVV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 160 QIFELDPIKWLIEKGTVVICAGGGGIptvylpdgtrTLVGIEAVIDKDLAAELLARNLGADIFVMATDAEGVCLDWGTTE 239
Cdd:pfam00696 114 TRIDTEALEELLEAGVVPVITGFIGI----------DPEGELGRGSSDTLAALLAEALGADKLIILTDVDGVYTADPRKV 183
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1309179813 240 Q--RVLGTTTPEELDKY---EFAAGSMGPKVEAAKRFVRSTGGRAAI 281
Cdd:pfam00696 184 PdaKLIPEISYDELLELlasGLATGGMKVKLPAALEAARRGGIPVVI 230
|
|
| AAK_NAGK-like |
cd04238 |
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ... |
204-299 |
7.34e-09 |
|
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: 55.21 E-value: 7.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 204 IDKDLAAELLARNLGADIFVMATDAEGVCLDWGTteqrVLGTTTPEELDKY---EFAAGSMGPKVEAAKRFVRSTGGRAA 280
Cdd:cd04238 157 VNADTAAGAIAAALKAEKLILLTDVPGVLDDPGS----LISELTPKEAEELiedGVISGGMIPKVEAALEALEGGVRKVH 232
|
90 100
....*....|....*....|....
gi 1309179813 281 I--GRL-EDITLIAAGN--AGTTI 299
Cdd:cd04238 233 IidGRVpHSLLLELFTDegIGTMI 256
|
|
| PRK00942 |
PRK00942 |
acetylglutamate kinase; Provisional |
204-302 |
7.44e-08 |
|
acetylglutamate kinase; Provisional
Pssm-ID: 234869 [Multi-domain] Cd Length: 283 Bit Score: 52.80 E-value: 7.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 204 IDKDLAAELLARNLGADIFVMATDAEGVCLDWGTteqrVLGTTTPEELDKY---EFAAGSMGPKVEAAKRFVRSTGGRAA 280
Cdd:PRK00942 181 INADTAAGAIAAALGAEKLILLTDVPGVLDDKGQ----LISELTASEAEELiedGVITGGMIPKVEAALDAARGGVRSVH 256
|
90 100
....*....|....*....|....*..
gi 1309179813 281 I--GRLEDITLIA---AGNAGTTIVPG 302
Cdd:PRK00942 257 IidGRVPHALLLElftDEGIGTMIVPD 283
|
|
| AAK_NAGK-UC |
cd04251 |
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ... |
204-300 |
4.73e-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: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 204 IDKDLAAELLARNLGADIFVMATDAEGVCLDwgtteQRVLGTTTPEELDKY-EFAAGSMGPKVEAAKRFVRSTGGRAAIG 282
Cdd:cd04251 164 VDGDRAAAAIAAALKAERLILLTDVEGLYLD-----GRVIERITVSDAESLlEKAGGGMKRKLLAAAEAVEGGVREVVIG 238
|
90
....*....|....*....
gi 1309179813 283 -RLEDITLIAAGNAGTTIV 300
Cdd:cd04251 239 dARADSPISSALNGGGTVI 257
|
|
| AAK_NAGK-C |
cd04250 |
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ... |
204-285 |
1.06e-05 |
|
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: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 204 IDKDLAAELLARNLGADIFVMATDAEGVcLDWGTTEQRVLGTTTPEELDKY---EFAAGSMGPKVEAAKRFVRSTGGRAA 280
Cdd:cd04250 177 INADTAAGAIAAALKAEKLILLTDVAGV-LDDPNDPGSLISEISLKEAEELiadGIISGGMIPKVEACIEALEGGVKAAH 255
|
....*..
gi 1309179813 281 I--GRLE 285
Cdd:cd04250 256 IidGRVP 262
|
|
| AAK_UMPK-like |
cd04239 |
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ... |
172-231 |
3.21e-04 |
|
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: 41.37 E-value: 3.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 172 EKGTVVICAGGGGIPtvylpdGTRTlvgieavidkDLAAELLARNLGADIFVMATDAEGV 231
Cdd:cd04239 116 EKGRIVIFGGGTGNP------GFTT----------DTAAALRAEEIGADVLLKATNVDGV 159
|
|
| ArgB |
COG0548 |
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ... |
207-286 |
6.26e-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: 40.79 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179813 207 DLAAELLARNLGADIFVMATDAEGVcLDwgtTEQRVLGTTTPEELDKY---EFAAGSMGPKVEAAKRFVRSTGGRAAI-- 281
Cdd:COG0548 186 DTVAGAIAAALKAEKLILLTDVPGV-LD---DPGSLISELTAAEAEELiadGVISGGMIPKLEAALDAVRGGVKRVHIid 261
|
....*
gi 1309179813 282 GRLED 286
Cdd:COG0548 262 GRVPH 266
|
|
| |
