|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12353 |
PRK12353 |
putative amino acid kinase; Reviewed |
8-317 |
4.42e-175 |
|
putative amino acid kinase; Reviewed
Pssm-ID: 237071 Cd Length: 314 Bit Score: 486.97 E-value: 4.42e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 8 GKSVVIALGGNALGNTPQE---QLQLVKDTAKNIVDMVEEGTNVIVSHGNGPQVGMINNAFAYASADDGKTPEMPFPEAG 84
Cdd:PRK12353 2 MKKIVVALGGNALGSTPEEataQLEAVKKTAKSLVDLIEEGHEVVITHGNGPQVGNILLAQEAAASEKNKVPAMPLDVCG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 85 AMSQGYIGYQLSQAILNDMKLRGIDRSTACVVTQTVVDPSDPAFRNPTKPVGAFLSEEEAKAKAAETGWTFKEDAGRGWR 164
Cdd:PRK12353 82 AMSQGYIGYHLQNALRNELLKRGIDKPVATVVTQVVVDANDPAFKNPTKPIGPFYTEEEAEKLAKEKGYTFKEDAGRGYR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 165 QVVASPKPVRIVEFDAVKDLMDGGYVVVSTGGGGVPVFEKEGLYEGVPAVIDKDRSSAKLAADFGADMLVILTAVEKVCV 244
Cdd:PRK12353 162 RVVPSPKPVDIVEIEAIKTLVDAGQVVIAAGGGGIPVIREGGGLKGVEAVIDKDFASAKLAELVDADLLIILTAVDKVYI 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496663993 245 NFGKPDQAEIDTMTIAEAEEFIAQGQFAPGSMLPKVEACIEYVRAFPEGKALITSLECAAAGIEGKTGTVITA 317
Cdd:PRK12353 242 NFGKPNQKKLDEVTVSEAEKYIEEGQFAPGSMLPKVEAAISFVESRPGRKAIITSLEKAKEALEGKAGTVIVK 314
|
|
| ArcC |
COG0549 |
Carbamate kinase [Amino acid transport and metabolism]; |
8-317 |
3.69e-161 |
|
Carbamate kinase [Amino acid transport and metabolism];
Pssm-ID: 440315 Cd Length: 313 Bit Score: 451.45 E-value: 3.69e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 8 GKSVVIALGGNALGN-----TPQEQLQLVKDTAKNIVDMVEEGTNVIVSHGNGPQVGMINNAFAYASAddgKTPEMPFPE 82
Cdd:COG0549 2 KKRIVVALGGNALLRrgepgTAEEQRENVREAAKALADLIEAGHEVVITHGNGPQVGLLLLQNEAAKK---KVPPMPLDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 83 AGAMSQGYIGYQLSQAILNDMKLRGIDRSTACVVTQTVVDPSDPAFRNPTKPVGAFLSEEEAKAKAAETGWTFKEDAGRG 162
Cdd:COG0549 79 CGAMTQGMIGYMLQQALRNELPKRGIDKPVATLVTQVEVDPDDPAFQNPTKPIGPFYTEEEAEELAKEKGWTFKEDAGRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 163 WRQVVASPKPVRIVEFDAVKDLMDggyvvvstggggvPVF--------------EKEGLYEGVPAVIDKDRSSAKLAADF 228
Cdd:COG0549 159 YRRVVPSPKPKRIVEIDAIKALLE-------------AGViviaaggggipvvrDEDGGLKGVEAVIDKDLASALLAEEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 229 GADMLVILTAVEKVCVNFGKPDQAEIDTMTIAEAEEFIAQGQFAPGSMLPKVEACIEYVRAfPEGKALITSLECAAAGIE 308
Cdd:COG0549 226 DADLLLILTDVDKVYINFGKPDQRALDEVTVAEAKKYIEEGHFAAGSMGPKVEAAIRFVEA-TGKRAIITSLEKAEEALA 304
|
....*....
gi 496663993 309 GKTGTVITA 317
Cdd:COG0549 305 GKAGTRIVP 313
|
|
| AAK_CK |
cd04235 |
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ... |
11-316 |
8.34e-147 |
|
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: 414.99 E-value: 8.34e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 11 VVIALGGNALGN-----TPQEQLQLVKDTAKNIVDMVEEGTNVIVSHGNGPQVGMINNAFAYAsadDGKTPEMPFPEAGA 85
Cdd:cd04235 2 IVVALGGNALLRrgepgTAEEQRENVKIAAKALADLIKNGHEVVITHGNGPQVGNLLLQNEAA---AEKVPAYPLDVCGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 86 MSQGYIGYQLSQAILNDMKLRGIDRSTACVVTQTVVDPSDPAFRNPTKPVGAFLSEEEAKAKAAETGWTFKEDAGRGWRQ 165
Cdd:cd04235 79 MSQGMIGYMLQQALDNELPKRGIDKPVVTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEKGWTFKEDAGRGYRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 166 VVASPKPVRIVEFDAVKDLMDGGYVVVSTGGGGVPVFEKEGLYEGVPAVIDKDRSSAKLAADFGADMLVILTAVEKVCVN 245
Cdd:cd04235 159 VVPSPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREGGGLKGVEAVIDKDLASALLAEEINADLLVILTDVDNVYIN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496663993 246 FGKPDQAEIDTMTIAEAEEFIAQGQFAPGSMLPKVEACIEYVRAFPeGKALITSLECAAAGIEGKTGTVIT 316
Cdd:cd04235 239 FGKPNQKALEQVTVEELEKYIEEGQFAPGSMGPKVEAAIRFVESGG-KKAIITSLENAEAALEGKAGTVIV 308
|
|
| arcC |
TIGR00746 |
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes ... |
9-316 |
3.30e-107 |
|
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: 314.78 E-value: 3.30e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 9 KSVVIALGGNAL---GN--TPQEQLQLVKDTAKNIVDMVEEGTNVIVSHGNGPQVG--MINNAfayasADDGKTPEMPFP 81
Cdd:TIGR00746 1 KRVVVALGGNALlqrGEkgSAEAQRDNVRQTAPQIAKLIKRGYELVITHGNGPQVGnlLLQNQ-----AADSEVPAMPLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 82 EAGAMSQGYIGYQLSQAILNDMKLRGIDRSTACVVTQTVVDPSDPAFRNPTKPVGAFLSEEEAKAKAAETGWTFKEDAGR 161
Cdd:TIGR00746 76 VLGAMSQGMIGYMLQQALNNELPKRGMEKPVATVLTQTIVDPKDPAFQNPTKPIGPFYTEEEAKRLAAEKGWIVKEDAGR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 162 GWRQVVASPKPVRIVEFDAVKDLMDGGYVVVSTGGGGVPVFEKEGLYEGVPAVIDKDRSSAKLAADFGADMLVILTAVEK 241
Cdd:TIGR00746 156 GWRRVVPSPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEGAELKGVEAVIDKDLASEKLAEEVNADILVILTDVDA 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496663993 242 VCVNFGKPDQAEIDTMTIAEAEEFIAQGQFAPGSMLPKVEACIEYVRAFPEgKALITSLECAAAGIEGKTGTVIT 316
Cdd:TIGR00746 236 VYINYGKPDEKALREVTVEELEDYYKAGHFAAGSMGPKVEAAIEFVESGGK-RAIITSLENAVEALEGKAGTRVT 309
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
9-288 |
1.19e-14 |
|
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: 72.01 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 9 KSVVIALGGNALGNTpqeqlQLVKDTAKNIVDMVEEGTNVIVSHGNGPQVGMINNAFAYASADDGKTPE--MPFPEAGAM 86
Cdd:pfam00696 1 KRVVIKLGGSSLTDK-----ERLKRLADEIAALLEEGRKLVVVHGGGAFADGLLALLGLSPRFARLTDAetLEVATMDAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 87 SQgyIGYQLSQAILND-MKLRGIDRSTACVVTQTVVDpsDPAFRNPTKPVGAFLSeeeakakaaetgwtfkedagrgWRQ 165
Cdd:pfam00696 76 GS--LGERLNAALLAAgLPAVGLPAAQLLATEAGFID--DVVTRIDTEALEELLE----------------------AGV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 166 VvaspkPVrIVEFDAVKDlmdggyvvvstggggvpvfekeglyEGVPAVIDKDRSSAKLAADFGADMLVILTAVEKVCVN 245
Cdd:pfam00696 130 V-----PV-ITGFIGIDP-------------------------EGELGRGSSDTLAALLAEALGADKLIILTDVDGVYTA 178
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 496663993 246 FGK--PDQAEIDTMTIAEAEEFIAqGQFAPGSMLPKVEACIEYVR 288
Cdd:pfam00696 179 DPRkvPDAKLIPEISYDELLELLA-SGLATGGMKVKLPAALEAAR 222
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12353 |
PRK12353 |
putative amino acid kinase; Reviewed |
8-317 |
4.42e-175 |
|
putative amino acid kinase; Reviewed
Pssm-ID: 237071 Cd Length: 314 Bit Score: 486.97 E-value: 4.42e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 8 GKSVVIALGGNALGNTPQE---QLQLVKDTAKNIVDMVEEGTNVIVSHGNGPQVGMINNAFAYASADDGKTPEMPFPEAG 84
Cdd:PRK12353 2 MKKIVVALGGNALGSTPEEataQLEAVKKTAKSLVDLIEEGHEVVITHGNGPQVGNILLAQEAAASEKNKVPAMPLDVCG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 85 AMSQGYIGYQLSQAILNDMKLRGIDRSTACVVTQTVVDPSDPAFRNPTKPVGAFLSEEEAKAKAAETGWTFKEDAGRGWR 164
Cdd:PRK12353 82 AMSQGYIGYHLQNALRNELLKRGIDKPVATVVTQVVVDANDPAFKNPTKPIGPFYTEEEAEKLAKEKGYTFKEDAGRGYR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 165 QVVASPKPVRIVEFDAVKDLMDGGYVVVSTGGGGVPVFEKEGLYEGVPAVIDKDRSSAKLAADFGADMLVILTAVEKVCV 244
Cdd:PRK12353 162 RVVPSPKPVDIVEIEAIKTLVDAGQVVIAAGGGGIPVIREGGGLKGVEAVIDKDFASAKLAELVDADLLIILTAVDKVYI 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496663993 245 NFGKPDQAEIDTMTIAEAEEFIAQGQFAPGSMLPKVEACIEYVRAFPEGKALITSLECAAAGIEGKTGTVITA 317
Cdd:PRK12353 242 NFGKPNQKKLDEVTVSEAEKYIEEGQFAPGSMLPKVEAAISFVESRPGRKAIITSLEKAKEALEGKAGTVIVK 314
|
|
| ArcC |
COG0549 |
Carbamate kinase [Amino acid transport and metabolism]; |
8-317 |
3.69e-161 |
|
Carbamate kinase [Amino acid transport and metabolism];
Pssm-ID: 440315 Cd Length: 313 Bit Score: 451.45 E-value: 3.69e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 8 GKSVVIALGGNALGN-----TPQEQLQLVKDTAKNIVDMVEEGTNVIVSHGNGPQVGMINNAFAYASAddgKTPEMPFPE 82
Cdd:COG0549 2 KKRIVVALGGNALLRrgepgTAEEQRENVREAAKALADLIEAGHEVVITHGNGPQVGLLLLQNEAAKK---KVPPMPLDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 83 AGAMSQGYIGYQLSQAILNDMKLRGIDRSTACVVTQTVVDPSDPAFRNPTKPVGAFLSEEEAKAKAAETGWTFKEDAGRG 162
Cdd:COG0549 79 CGAMTQGMIGYMLQQALRNELPKRGIDKPVATLVTQVEVDPDDPAFQNPTKPIGPFYTEEEAEELAKEKGWTFKEDAGRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 163 WRQVVASPKPVRIVEFDAVKDLMDggyvvvstggggvPVF--------------EKEGLYEGVPAVIDKDRSSAKLAADF 228
Cdd:COG0549 159 YRRVVPSPKPKRIVEIDAIKALLE-------------AGViviaaggggipvvrDEDGGLKGVEAVIDKDLASALLAEEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 229 GADMLVILTAVEKVCVNFGKPDQAEIDTMTIAEAEEFIAQGQFAPGSMLPKVEACIEYVRAfPEGKALITSLECAAAGIE 308
Cdd:COG0549 226 DADLLLILTDVDKVYINFGKPDQRALDEVTVAEAKKYIEEGHFAAGSMGPKVEAAIRFVEA-TGKRAIITSLEKAEEALA 304
|
....*....
gi 496663993 309 GKTGTVITA 317
Cdd:COG0549 305 GKAGTRIVP 313
|
|
| AAK_CK |
cd04235 |
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ... |
11-316 |
8.34e-147 |
|
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: 414.99 E-value: 8.34e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 11 VVIALGGNALGN-----TPQEQLQLVKDTAKNIVDMVEEGTNVIVSHGNGPQVGMINNAFAYAsadDGKTPEMPFPEAGA 85
Cdd:cd04235 2 IVVALGGNALLRrgepgTAEEQRENVKIAAKALADLIKNGHEVVITHGNGPQVGNLLLQNEAA---AEKVPAYPLDVCGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 86 MSQGYIGYQLSQAILNDMKLRGIDRSTACVVTQTVVDPSDPAFRNPTKPVGAFLSEEEAKAKAAETGWTFKEDAGRGWRQ 165
Cdd:cd04235 79 MSQGMIGYMLQQALDNELPKRGIDKPVVTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEKGWTFKEDAGRGYRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 166 VVASPKPVRIVEFDAVKDLMDGGYVVVSTGGGGVPVFEKEGLYEGVPAVIDKDRSSAKLAADFGADMLVILTAVEKVCVN 245
Cdd:cd04235 159 VVPSPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREGGGLKGVEAVIDKDLASALLAEEINADLLVILTDVDNVYIN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496663993 246 FGKPDQAEIDTMTIAEAEEFIAQGQFAPGSMLPKVEACIEYVRAFPeGKALITSLECAAAGIEGKTGTVIT 316
Cdd:cd04235 239 FGKPNQKALEQVTVEELEKYIEEGQFAPGSMGPKVEAAIRFVESGG-KKAIITSLENAEAALEGKAGTVIV 308
|
|
| PRK12686 |
PRK12686 |
carbamate kinase; Reviewed |
7-316 |
5.40e-138 |
|
carbamate kinase; Reviewed
Pssm-ID: 183683 Cd Length: 312 Bit Score: 392.87 E-value: 5.40e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 7 EGKSVVIALGGNALG---NTPQEQLQLVKDTAKNIVDMVEEGTNVIVSHGNGPQVGmiNNAFAYASADDGKTPEMPFPEA 83
Cdd:PRK12686 1 MKEKIVIALGGNAILqteATAEAQQTAVREAAQHLVDLIEAGHDIVITHGNGPQVG--NLLLQQAESNSNKVPAMPLDTC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 84 GAMSQGYIGYQLSQAILNDMKLRGIDRSTACVVTQTVVDPSDPAFRNPTKPVGAFLSEEEAKAKAAETGWTFKEDAGRGW 163
Cdd:PRK12686 79 VAMSQGMIGYWLQNALNNELTERGIDKPVITLVTQVEVDKDDPAFANPTKPIGPFYTEEEAKQQAEQPGSTFKEDAGRGY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 164 RQVVASPKPVRIVEFDAVKDLMDGGYVVVSTGGGGVPVFEKEGLYEGVPAVIDKDRSSAKLAADFGADMLVILTAVEKVC 243
Cdd:PRK12686 159 RRVVPSPKPQEIIEHDTIRTLVDGGNIVIACGGGGIPVIRDDNTLKGVEAVIDKDFASEKLAEQIDADLLIILTGVENVF 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496663993 244 VNFGKPDQAEIDTMTIAEAEEFIAQGQFAPGSMLPKVEACIEYVRAFPEGKALITSLECAAAGIEGKTGTVIT 316
Cdd:PRK12686 239 INFNKPNQQKLDDITVAEAKQYIAEGQFAPGSMLPKVEAAIDFVESGEGKKAIITSLEQAKEALAGNAGTHIT 311
|
|
| PRK12454 |
PRK12454 |
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed |
8-316 |
4.15e-121 |
|
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
Pssm-ID: 183535 Cd Length: 313 Bit Score: 350.07 E-value: 4.15e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 8 GKSVVIALGGNALGN-----TPQEQLQLVKDTAKNIVDMVEEGTNVIVSHGNGPQVGMInnAFAYASADDGKTPEMPFPE 82
Cdd:PRK12454 2 KKRIVIALGGNALLQpgekgTAENQMKNVRKTAKQIADLIEEGYEVVITHGNGPQVGNL--LLQMDAAKDVGIPPFPLDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 83 AGAMSQGYIGYQLSQAILNDMKLRGIDRSTACVVTQTVVDPSDPAFRNPTKPVGAFLSEEEAKAKAAETGWTFKEDAGRG 162
Cdd:PRK12454 80 AGAMTQGWIGYMIQQALRNELAKRGIEKQVATIVTQVIVDKNDPAFQNPTKPVGPFYDEEEAKKLAKEKGWIVKEDAGRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 163 WRQVVASPKPVRIVEFDAVKDLMDGGYVVVSTGGGGVPVFEKEGLYEGVPAVIDKDRSSAKLAADFGADMLVILTAVEKV 242
Cdd:PRK12454 160 WRRVVPSPDPLGIVEIEVIKALVENGFIVIASGGGGIPVIEEDGELKGVEAVIDKDLASELLAEELNADIFIILTDVEKV 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496663993 243 CVNFGKPDQAEIDTMTIAEAEEFIAQGQFAPGSMLPKVEACIEYVRAfPEGKALITSLECAAAGIEGKTGTVIT 316
Cdd:PRK12454 240 YLNYGKPDQKPLDKVTVEEAKKYYEEGHFKAGSMGPKILAAIRFVEN-GGKRAIIASLEKAVEALEGKTGTRII 312
|
|
| arcC |
TIGR00746 |
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes ... |
9-316 |
3.30e-107 |
|
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: 314.78 E-value: 3.30e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 9 KSVVIALGGNAL---GN--TPQEQLQLVKDTAKNIVDMVEEGTNVIVSHGNGPQVG--MINNAfayasADDGKTPEMPFP 81
Cdd:TIGR00746 1 KRVVVALGGNALlqrGEkgSAEAQRDNVRQTAPQIAKLIKRGYELVITHGNGPQVGnlLLQNQ-----AADSEVPAMPLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 82 EAGAMSQGYIGYQLSQAILNDMKLRGIDRSTACVVTQTVVDPSDPAFRNPTKPVGAFLSEEEAKAKAAETGWTFKEDAGR 161
Cdd:TIGR00746 76 VLGAMSQGMIGYMLQQALNNELPKRGMEKPVATVLTQTIVDPKDPAFQNPTKPIGPFYTEEEAKRLAAEKGWIVKEDAGR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 162 GWRQVVASPKPVRIVEFDAVKDLMDGGYVVVSTGGGGVPVFEKEGLYEGVPAVIDKDRSSAKLAADFGADMLVILTAVEK 241
Cdd:TIGR00746 156 GWRRVVPSPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEGAELKGVEAVIDKDLASEKLAEEVNADILVILTDVDA 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496663993 242 VCVNFGKPDQAEIDTMTIAEAEEFIAQGQFAPGSMLPKVEACIEYVRAFPEgKALITSLECAAAGIEGKTGTVIT 316
Cdd:TIGR00746 236 VYINYGKPDEKALREVTVEELEDYYKAGHFAAGSMGPKVEAAIEFVESGGK-RAIITSLENAVEALEGKAGTRVT 309
|
|
| PRK12352 |
PRK12352 |
putative carbamate kinase; Reviewed |
9-316 |
1.24e-99 |
|
putative carbamate kinase; Reviewed
Pssm-ID: 183464 Cd Length: 316 Bit Score: 295.94 E-value: 1.24e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 9 KSVVIALGGNAL-----GNTPQEQLQLVKDTAKNIVDMVEEGTNVIVSHGNGPQVGMINNAFAYASADDGkTPEMPFPEA 83
Cdd:PRK12352 3 ELVVVAIGGNSIikdnaSQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHEREG-LPLTPLANC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 84 GAMSQGYIGYQLSQAILNDMKLRGiDRSTACVVTQTVVDPSDPAFRNPTKPVGAFLSEEEAKA-KAAETGWTFKEDAGRG 162
Cdd:PRK12352 82 VADTQGGIGYLIQQALNNRLARHG-EKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDElQKANPDWRFVEDAGRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 163 WRQVVASPKPVRIVEFDAVKDLMDGGYVVVSTGGGGVPVFEKE-GLYEGVPAVIDKDRSSAKLAADFGADMLVILTAVEK 241
Cdd:PRK12352 161 YRRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDaGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496663993 242 VCVNFGKPDQAEIDTMTIAEAEEFIAQGQFAPGSMLPKVEACIEYVRAfpEGK-ALITSLECAAAGIEGKTGTVIT 316
Cdd:PRK12352 241 VCIHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQ--GGKeVIITTPECLPAALRGETGTHII 314
|
|
| PRK12354 |
PRK12354 |
carbamate kinase; Reviewed |
11-317 |
2.71e-81 |
|
carbamate kinase; Reviewed
Pssm-ID: 183466 Cd Length: 307 Bit Score: 248.59 E-value: 2.71e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 11 VVIALGGNAL---GNTPQEQLQL--VKDTAKNIVDmVEEGTNVIVSHGNGPQVGMInnafAYASADDGKTPEMPFPEAGA 85
Cdd:PRK12354 3 IVVALGGNALlrrGEPLTAENQRanIRIAAEQIAK-IAREHELVIVHGNGPQVGLL----ALQNAAYKDVTPYPLDVLGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 86 MSQGYIGYQLSQAILNDMKlrgiDRSTACVVTQTVVDPSDPAFRNPTKPVGAFLSEEEAKAKAAETGWTFKEDaGRGWRQ 165
Cdd:PRK12354 78 ETEGMIGYMLEQELGNLLP----ERPVATLLTQVEVDANDPAFANPTKPIGPVYDEAEAERLAAEKGWTIKPD-GDYFRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 166 VVASPKPVRIVEFDAVKDLMDGGYVVVSTGGGGV-PVFEKEGLYEGVPAVIDKDRSSAKLAADFGADMLVILTAVEKVCV 244
Cdd:PRK12354 153 VVPSPRPKRIVEIRPIRWLLEKGHLVICAGGGGIpVVYDADGKLHGVEAVIDKDLAAALLAEQLDADLLLILTDVDAVYL 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496663993 245 NFGKPDQAEIDTMTIAEAEEFiaqgQFAPGSMLPKVEACIEYVRAfPEGKALITSLECAAAGIEGKTGTVITA 317
Cdd:PRK12354 233 DWGKPTQRAIAQATPDELREL----GFAAGSMGPKVEAACEFVRA-TGKIAGIGSLEDIQAILAGEAGTRISP 300
|
|
| PRK09411 |
PRK09411 |
carbamate kinase; Reviewed |
9-316 |
4.12e-45 |
|
carbamate kinase; Reviewed
Pssm-ID: 181831 Cd Length: 297 Bit Score: 155.34 E-value: 4.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 9 KSVVIALGGNALGN-----TPQEQLQLVKDTAKNIVDMVEEGTNVIVsHGNGPQVGMInnafAYASADDGKTPEMPFPEA 83
Cdd:PRK09411 2 KTLVVALGGNALLQrgealTAENQYRNIASAVPALARLARSYRLAIV-HGNGPQVGLL----ALQNLAWKEVEPYPLDVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 84 GAMSQGYIGYQLSQAILNDMKLRGIdrstACVVTQTVVDPSDPAFRNPTKPVGAFLSEEEAKAKAAETGWTFKEDaGRGW 163
Cdd:PRK09411 77 VAESQGMIGYMLAQSLSAQPQMPPV----TTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAYGWQMKRD-GKYL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 164 RQVVASPKPVRIVEFDAVKDLMDGGYVVVSTGGGGVPVFEKEglyEGVPAVIDKDRSSAKLAADFGADMLVILTAVEKVC 243
Cdd:PRK09411 152 RRVVASPQPRKILDSEAIELLLKEGHVVICSGGGGVPVTEDG---AGSEAVIDKDLAAALLAEQINADGLVILTDADAVY 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496663993 244 VNFGKPDQAEIDTMTIAEAEEFIAqgqfAPGSMLPKVEACIEYVRAfpEGK-ALITSLECAAAGIEGKTGTVIT 316
Cdd:PRK09411 229 ENWGTPQQRAIRHATPDELAPFAK----ADGAMGPKVTAVSGYVRS--RGKpAWIGALSRIEETLAGEAGTCIS 296
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
9-288 |
1.19e-14 |
|
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: 72.01 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 9 KSVVIALGGNALGNTpqeqlQLVKDTAKNIVDMVEEGTNVIVSHGNGPQVGMINNAFAYASADDGKTPE--MPFPEAGAM 86
Cdd:pfam00696 1 KRVVIKLGGSSLTDK-----ERLKRLADEIAALLEEGRKLVVVHGGGAFADGLLALLGLSPRFARLTDAetLEVATMDAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 87 SQgyIGYQLSQAILND-MKLRGIDRSTACVVTQTVVDpsDPAFRNPTKPVGAFLSeeeakakaaetgwtfkedagrgWRQ 165
Cdd:pfam00696 76 GS--LGERLNAALLAAgLPAVGLPAAQLLATEAGFID--DVVTRIDTEALEELLE----------------------AGV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 166 VvaspkPVrIVEFDAVKDlmdggyvvvstggggvpvfekeglyEGVPAVIDKDRSSAKLAADFGADMLVILTAVEKVCVN 245
Cdd:pfam00696 130 V-----PV-ITGFIGIDP-------------------------EGELGRGSSDTLAALLAEALGADKLIILTDVDGVYTA 178
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 496663993 246 FGK--PDQAEIDTMTIAEAEEFIAqGQFAPGSMLPKVEACIEYVR 288
Cdd:pfam00696 179 DPRkvPDAKLIPEISYDELLELLA-SGLATGGMKVKLPAALEAAR 222
|
|
| AAK_NAGK-like |
cd04238 |
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ... |
215-288 |
1.43e-08 |
|
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the Escherichia coli and Pseudomonas aeruginosa type NAGKs which catalyze the phosphorylation of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in bacteria and photosynthetic organisms using either the acetylated, noncyclic (NC), or non-acetylated, cyclic (C) route of ornithine biosynthesis. Also included in this CD is a distinct group of uncharacterized (UC) bacterial and archeal NAGKs. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239771 [Multi-domain] Cd Length: 256 Bit Score: 54.82 E-value: 1.43e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496663993 215 IDKDRSSAKLAADFGADMLVILTAVEKVCVNFGKPdqaeIDTMTIAEAEEFIAQGQFAPGsMLPKVEACIEYVR 288
Cdd:cd04238 157 VNADTAAGAIAAALKAEKLILLTDVPGVLDDPGSL----ISELTPKEAEELIEDGVISGG-MIPKVEAALEALE 225
|
|
| ArgB |
COG0548 |
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ... |
222-289 |
4.78e-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: 53.11 E-value: 4.78e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496663993 222 AKLAADFGADMLVILTAVEKVcvnfgKPDQAE-IDTMTIAEAEEFIAQGQFAPGsMLPKVEACIEYVRA 289
Cdd:COG0548 190 GAIAAALKAEKLILLTDVPGV-----LDDPGSlISELTAAEAEELIADGVISGG-MIPKLEAALDAVRG 252
|
|
| PRK00942 |
PRK00942 |
acetylglutamate kinase; Provisional |
222-289 |
5.51e-08 |
|
acetylglutamate kinase; Provisional
Pssm-ID: 234869 [Multi-domain] Cd Length: 283 Bit Score: 53.19 E-value: 5.51e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496663993 222 AKLAADFGADMLVILTAVEKVCVNFGKPdqaeIDTMTIAEAEEFIAQGQFAPGsMLPKVEACIEYVRA 289
Cdd:PRK00942 188 GAIAAALGAEKLILLTDVPGVLDDKGQL----ISELTASEAEELIEDGVITGG-MIPKVEAALDAARG 250
|
|
| AAK_NAGK-C |
cd04250 |
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ... |
215-288 |
5.02e-07 |
|
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: 50.20 E-value: 5.02e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496663993 215 IDKDRSSAKLAADFGADMLVILTAVEKVCVNfgKPDQAE-IDTMTIAEAEEFIAQGQFApGSMLPKVEACIEYVR 288
Cdd:cd04250 177 INADTAAGAIAAALKAEKLILLTDVAGVLDD--PNDPGSlISEISLKEAEELIADGIIS-GGMIPKVEACIEALE 248
|
|
| PRK00942 |
PRK00942 |
acetylglutamate kinase; Provisional |
2-59 |
2.35e-06 |
|
acetylglutamate kinase; Provisional
Pssm-ID: 234869 [Multi-domain] Cd Length: 283 Bit Score: 48.18 E-value: 2.35e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 496663993 2 PY-QKGEGKSVVIALGGNALGNTpqeqlQLVKDTAKNIVDMVEEGTNVIVSHGNGPQVG 59
Cdd:PRK00942 16 PYiQRFMGKTIVIKYGGNAMTDE-----ELKEAFARDIVLLKQVGINPVVVHGGGPQID 69
|
|
| PLN02512 |
PLN02512 |
acetylglutamate kinase |
215-284 |
3.47e-06 |
|
acetylglutamate kinase
Pssm-ID: 178128 Cd Length: 309 Bit Score: 47.76 E-value: 3.47e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 215 IDKDRSSAKLAADFGADMLVILTAVEKVCVNFGKPDQAeIDTMTIAEAEEFIAQGQFApGSMLPKVEACI 284
Cdd:PLN02512 205 INADTAAGEIAAALGAEKLILLTDVAGVLEDKDDPGSL-VKELDIKGVRKLIADGKIA-GGMIPKVECCV 272
|
|
| PRK14058 |
PRK14058 |
[LysW]-aminoadipate/[LysW]-glutamate kinase; |
208-287 |
8.69e-06 |
|
[LysW]-aminoadipate/[LysW]-glutamate kinase;
Pssm-ID: 237599 [Multi-domain] Cd Length: 268 Bit Score: 46.43 E-value: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 208 YEGVPAVIDKDRSSAKLAADFGADMLVILTAVEKVCVNFgkPDQAE-IDTMTIAEAEEFIAqgqFAPGSMLPKVEACIEY 286
Cdd:PRK14058 161 EEGEPLNVDGDRAAAAIAGALKAEALVLLSDVPGLLRDP--PDEGSlIERITPEEAEELSK---AAGGGMKKKVLMAAEA 235
|
.
gi 496663993 287 V 287
Cdd:PRK14058 236 V 236
|
|
| AAK |
cd02115 |
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ... |
12-285 |
2.76e-05 |
|
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: 44.74 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 12 VIALGGNALGNTPQeqlqlVKDTAKNIVDMVEEGTNVIVSHGNGPQvgmINNAFAYASADDGKTPEMPFPEA-----GAM 86
Cdd:cd02115 1 VIKFGGSSVSSEER-----LRNLARILVKLASEGGRVVVVHGAGPQ---ITDELLAHGELLGYARGLRITDRetdalAAM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 87 SQGYIGYQLSQAILNdmklRGIdrstaCVVTqtvVDPSDPAFRNPTKPvgaflseeeakakaaETGWTFKEDAGRgWRQV 166
Cdd:cd02115 73 GEGMSNLLIAAALEQ----HGI-----KAVP---LDLTQAGFASPNQG---------------HVGKITKVSTDR-LKSL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 167 VASPKPVRIVEFDAVKDLMdggyvvvstggggvpvfekeglyEGVPAVIDKDRSSAKLAADFGADMLVILTAVEKV--CV 244
Cdd:cd02115 125 LENGILPILSGFGGTDEKE-----------------------TGTLGRGGSDSTAALLAAALKADRLVILTDVDGVytAD 181
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 496663993 245 NFGKPDQAEIDTMTIAEAEEFIAQG--QFAPGSMLPKVEACIE 285
Cdd:cd02115 182 PRKVPDAKLLSELTYEEAAELAYAGamVLKPKAADPAARAGIP 224
|
|
| AAK_NAGK-C |
cd04250 |
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ... |
1-59 |
4.55e-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: 44.42 E-value: 4.55e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 1 MPY-QKGEGKSVVIALGGNALGNTpqeqlQLVKDTAKNIVDMVEEGTNVIVSHGNGPQVG 59
Cdd:cd04250 6 LPYiQKFRGKTVVIKYGGNAMKDE-----ELKESFARDIVLLKYVGINPVVVHGGGPEIN 60
|
|
| AAK_NAGK-UC |
cd04251 |
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ... |
208-287 |
4.85e-04 |
|
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: 40.82 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 208 YEGVPAVIDKDRSSAKLAADFGADMLVILTAVEKVCVNFGKpdqaeIDTMTIAEAEEFIAqgqFAPGSMLPKVEACIEYV 287
Cdd:cd04251 157 EEGEPLNVDGDRAAAAIAAALKAERLILLTDVEGLYLDGRV-----IERITVSDAESLLE---KAGGGMKRKLLAAAEAV 228
|
|
| argB |
CHL00202 |
acetylglutamate kinase; Provisional |
215-284 |
1.84e-03 |
|
acetylglutamate kinase; Provisional
Pssm-ID: 133644 [Multi-domain] Cd Length: 284 Bit Score: 39.39 E-value: 1.84e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 215 IDKDRSSAKLAADFGADMLVILTAVEKVCVNFGKPDQAeIDTMTIAEAEEFIAQGQFApGSMLPKVEACI 284
Cdd:CHL00202 180 INADVVAGEIAAKLNAEKLILLTDTPGILADINDPNSL-ISTLNIKEARNLASTGIIS-GGMIPKVNCCI 247
|
|
| AAK_P5CS_ProBA |
cd04256 |
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ... |
209-284 |
3.75e-03 |
|
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: 38.57 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663993 209 EGVPAVIDKDRSSAKLAADFGADMLVILTAVE------------KVCVNFGKPDQAEIdtmtiaeaeEFIAQGQFAPGSM 276
Cdd:cd04256 172 QGVISIKDNDSLAARLAVELKADLLILLSDVDglydgppgsddaKLIHTFYPGDQQSI---------TFGTKSRVGTGGM 242
|
....*...
gi 496663993 277 LPKVEACI 284
Cdd:cd04256 243 EAKVKAAL 250
|
|
| |
