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Conserved domains on  [gi|488284044|ref|WP_002355252|]
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MULTISPECIES: carbamate kinase [Enterococcus]

Protein Classification

carbamate kinase( domain architecture ID 10793692)

carbamate kinase catalyzes both ATP-phosphorylation of carbamate and carbamoyl phosphate (CP) utilization with the production of ATP from ADP and CP; it is involved in the synthesis of carbamoyl phosphate, an essential precursor of arginine and pyrimidine bases, in the presence of ATP, bicarbonate, and ammonia

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK12686 PRK12686
carbamate kinase; Reviewed
 1-310 0e+00

carbamate kinase; Reviewed


:

Pssm-ID: 183683  Cd Length: 312  Bit Score: 527.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044   1 MSLNVIALGGNAILDTDPTDEGQKAVVNHAAKYIAEFVAKGEQVIVCHGNGPQVGNLLLQQKAGESEKNPALKLDTCVAM 80
Cdd:PRK12686   2 KEKIVIALGGNAILQTEATAEAQQTAVREAAQHLVDLIEAGHDIVITHGNGPQVGNLLLQQAESNSNKVPAMPLDTCVAM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044  81 TQGSIGYWLQNALTNEFEKRNIAKPVISVVTQVRVDKEDPSFKKPSKPIGPFYTKEEADAEAAKDGSTYVEDAGRGYRKV 160
Cdd:PRK12686  82 SQGMIGYWLQNALNNELTERGIDKPVITLVTQVEVDKDDPAFANPTKPIGPFYTEEEAKQQAEQPGSTFKEDAGRGYRRV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 161 VPSPMPKEIVEKEAVRALVEADVLTICSGGGGIPVVAEDGQYVGVEAVNDKDFSARVLAENVDADRLIILTGVDNIYINY 240
Cdd:PRK12686 162 VPSPKPQEIIEHDTIRTLVDGGNIVIACGGGGIPVIRDDNTLKGVEAVIDKDFASEKLAEQIDADLLIILTGVENVFINF 241

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488284044 241 NQPDQKALEQISVAEAEEYIKEGHFAAGSMLPKIEAALDFVKGDDKRKAIITSIENL-ENIDKEAGTVISQ 310
Cdd:PRK12686 242 NKPNQQKLDDITVAEAKQYIAEGQFAPGSMLPKVEAAIDFVESGEGKKAIITSLEQAkEALAGNAGTHITL 312
 
Name Accession Description Interval E-value
PRK12686 PRK12686
carbamate kinase; Reviewed
 1-310 0e+00

carbamate kinase; Reviewed


Pssm-ID: 183683  Cd Length: 312  Bit Score: 527.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044   1 MSLNVIALGGNAILDTDPTDEGQKAVVNHAAKYIAEFVAKGEQVIVCHGNGPQVGNLLLQQKAGESEKNPALKLDTCVAM 80
Cdd:PRK12686   2 KEKIVIALGGNAILQTEATAEAQQTAVREAAQHLVDLIEAGHDIVITHGNGPQVGNLLLQQAESNSNKVPAMPLDTCVAM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044  81 TQGSIGYWLQNALTNEFEKRNIAKPVISVVTQVRVDKEDPSFKKPSKPIGPFYTKEEADAEAAKDGSTYVEDAGRGYRKV 160
Cdd:PRK12686  82 SQGMIGYWLQNALNNELTERGIDKPVITLVTQVEVDKDDPAFANPTKPIGPFYTEEEAKQQAEQPGSTFKEDAGRGYRRV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 161 VPSPMPKEIVEKEAVRALVEADVLTICSGGGGIPVVAEDGQYVGVEAVNDKDFSARVLAENVDADRLIILTGVDNIYINY 240
Cdd:PRK12686 162 VPSPKPQEIIEHDTIRTLVDGGNIVIACGGGGIPVIRDDNTLKGVEAVIDKDFASEKLAEQIDADLLIILTGVENVFINF 241

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488284044 241 NQPDQKALEQISVAEAEEYIKEGHFAAGSMLPKIEAALDFVKGDDKRKAIITSIENL-ENIDKEAGTVISQ 310
Cdd:PRK12686 242 NKPNQQKLDDITVAEAKQYIAEGQFAPGSMLPKVEAAIDFVESGEGKKAIITSLEQAkEALAGNAGTHITL 312
ArcC COG0549
Carbamate kinase [Amino acid transport and metabolism];
1-309 9.89e-179

Carbamate kinase [Amino acid transport and metabolism];


Pssm-ID: 440315  Cd Length: 313  Bit Score: 495.75  E-value: 9.89e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044   1 MSLNVIALGGNAIL--DTDPTDEGQKAVVNHAAKYIAEFVAKGEQVIVCHGNGPQVGNLLLQQKAGeSEKNPALKLDTCV 78
Cdd:COG0549    2 KKRIVVALGGNALLrrGEPGTAEEQRENVREAAKALADLIEAGHEVVITHGNGPQVGLLLLQNEAA-KKKVPPMPLDVCG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044  79 AMTQGSIGYWLQNALTNEFEKRNIAKPVISVVTQVRVDKEDPSFKKPSKPIGPFYTKEEADAEAAKDGSTYVEDAGRGYR 158
Cdd:COG0549   81 AMTQGMIGYMLQQALRNELPKRGIDKPVATLVTQVEVDPDDPAFQNPTKPIGPFYTEEEAEELAKEKGWTFKEDAGRGYR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 159 KVVPSPMPKEIVEKEAVRALVEADVLTICSGGGGIPVVA-EDGQYVGVEAVNDKDFSARVLAENVDADRLIILTGVDNIY 237
Cdd:COG0549  161 RVVPSPKPKRIVEIDAIKALLEAGVIVIAAGGGGIPVVRdEDGGLKGVEAVIDKDLASALLAEELDADLLLILTDVDKVY 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284044 238 INYNQPDQKALEQISVAEAEEYIKEGHFAAGSMLPKIEAALDFVKGDDKRkAIITSIENLEN-IDKEAGTVIS 309
Cdd:COG0549  241 INFGKPDQRALDEVTVAEAKKYIEEGHFAAGSMGPKVEAAIRFVEATGKR-AIITSLEKAEEaLAGKAGTRIV 312
AAK_CK cd04235
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ...
 5-309 8.32e-178

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: 493.18  E-value: 8.32e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044   5 VIALGGNAILDTD--PTDEGQKAVVNHAAKYIAEFVAKGEQVIVCHGNGPQVGNLLLQQKAGeSEKNPALKLDTCVAMTQ 82
Cdd:cd04235    3 VVALGGNALLRRGepGTAEEQRENVKIAAKALADLIKNGHEVVITHGNGPQVGNLLLQNEAA-AEKVPAYPLDVCGAMSQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044  83 GSIGYWLQNALTNEFEKRNIAKPVISVVTQVRVDKEDPSFKKPSKPIGPFYTKEEADAEAAKDGSTYVEDAGRGYRKVVP 162
Cdd:cd04235   82 GMIGYMLQQALDNELPKRGIDKPVVTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEKGWTFKEDAGRGYRRVVP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 163 SPMPKEIVEKEAVRALVEADVLTICSGGGGIPVVAEDGQYVGVEAVNDKDFSARVLAENVDADRLIILTGVDNIYINYNQ 242
Cdd:cd04235  162 SPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREGGGLKGVEAVIDKDLASALLAEEINADLLVILTDVDNVYINFGK 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488284044 243 PDQKALEQISVAEAEEYIKEGHFAAGSMLPKIEAALDFVKGDDKrKAIITSIENLENI-DKEAGTVIS 309
Cdd:cd04235  242 PNQKALEQVTVEELEKYIEEGQFAPGSMGPKVEAAIRFVESGGK-KAIITSLENAEAAlEGKAGTVIV 308
arcC TIGR00746
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes ...
 5-309 3.94e-136

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: 387.97  E-value: 3.94e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044    5 VIALGGNAILD--TDPTDEGQKAVVNHAAKYIAEFVAKGEQVIVCHGNGPQVGNLLLQQKAGESEkNPALKLDTCVAMTQ 82
Cdd:TIGR00746   4 VVALGGNALLQrgEKGSAEAQRDNVRQTAPQIAKLIKRGYELVITHGNGPQVGNLLLQNQAADSE-VPAMPLDVLGAMSQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044   83 GSIGYWLQNALTNEFEKRNIAKPVISVVTQVRVDKEDPSFKKPSKPIGPFYTKEEADAEAAKDGSTYVEDAGRGYRKVVP 162
Cdd:TIGR00746  83 GMIGYMLQQALNNELPKRGMEKPVATVLTQTIVDPKDPAFQNPTKPIGPFYTEEEAKRLAAEKGWIVKEDAGRGWRRVVP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044  163 SPMPKEIVEKEAVRALVEADVLTICSGGGGIPVVAEDGQYVGVEAVNDKDFSARVLAENVDADRLIILTGVDNIYINYNQ 242
Cdd:TIGR00746 163 SPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEGAELKGVEAVIDKDLASEKLAEEVNADILVILTDVDAVYINYGK 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488284044  243 PDQKALEQISVAEAEEYIKEGHFAAGSMLPKIEAALDFVKGDDKRkAIITSIENLENI-DKEAGTVIS 309
Cdd:TIGR00746 243 PDEKALREVTVEELEDYYKAGHFAAGSMGPKVEAAIEFVESGGKR-AIITSLENAVEAlEGKAGTRVT 309
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 5-293 3.89e-22

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: 92.43  E-value: 3.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044    5 VIALGGNAILDTDPtdegqkavVNHAAKYIAEFVAKGEQVIVCHGNGPQVGNLLLQQKAGESEKNPALKLDTCVAMTQ-- 82
Cdd:pfam00696   4 VIKLGGSSLTDKER--------LKRLADEIAALLEEGRKLVVVHGGGAFADGLLALLGLSPRFARLTDAETLEVATMDal 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044   83 GSIG-YWLQNALTNEFEKRNIAKPVISVVTQVRVDKEDpsfkkpskpigpfytkeeadaeaakdgstyvedagrgyrkvv 161
Cdd:pfam00696  76 GSLGeRLNAALLAAGLPAVGLPAAQLLATEAGFIDDVV------------------------------------------ 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044  162 pspmpkEIVEKEAVRALVEADVLTICSGGGGIPVVAEDGqyvgveaVNDKDFSARVLAENVDADRLIILTGVDNIYINYN 241
Cdd:pfam00696 114 ------TRIDTEALEELLEAGVVPVITGFIGIDPEGELG-------RGSSDTLAALLAEALGADKLIILTDVDGVYTADP 180

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 488284044  242 --QPDQKALEQISVAEAEEYIkEGHFAAGSMLPKIEAALDFVKGdDKRKAIITS 293
Cdd:pfam00696 181 rkVPDAKLIPEISYDELLELL-ASGLATGGMKVKLPAALEAARR-GGIPVVIVN 232
 
Name Accession Description Interval E-value
PRK12686 PRK12686
carbamate kinase; Reviewed
 1-310 0e+00

carbamate kinase; Reviewed


Pssm-ID: 183683  Cd Length: 312  Bit Score: 527.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044   1 MSLNVIALGGNAILDTDPTDEGQKAVVNHAAKYIAEFVAKGEQVIVCHGNGPQVGNLLLQQKAGESEKNPALKLDTCVAM 80
Cdd:PRK12686   2 KEKIVIALGGNAILQTEATAEAQQTAVREAAQHLVDLIEAGHDIVITHGNGPQVGNLLLQQAESNSNKVPAMPLDTCVAM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044  81 TQGSIGYWLQNALTNEFEKRNIAKPVISVVTQVRVDKEDPSFKKPSKPIGPFYTKEEADAEAAKDGSTYVEDAGRGYRKV 160
Cdd:PRK12686  82 SQGMIGYWLQNALNNELTERGIDKPVITLVTQVEVDKDDPAFANPTKPIGPFYTEEEAKQQAEQPGSTFKEDAGRGYRRV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 161 VPSPMPKEIVEKEAVRALVEADVLTICSGGGGIPVVAEDGQYVGVEAVNDKDFSARVLAENVDADRLIILTGVDNIYINY 240
Cdd:PRK12686 162 VPSPKPQEIIEHDTIRTLVDGGNIVIACGGGGIPVIRDDNTLKGVEAVIDKDFASEKLAEQIDADLLIILTGVENVFINF 241

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488284044 241 NQPDQKALEQISVAEAEEYIKEGHFAAGSMLPKIEAALDFVKGDDKRKAIITSIENL-ENIDKEAGTVISQ 310
Cdd:PRK12686 242 NKPNQQKLDDITVAEAKQYIAEGQFAPGSMLPKVEAAIDFVESGEGKKAIITSLEQAkEALAGNAGTHITL 312
PRK12353 PRK12353
putative amino acid kinase; Reviewed
 1-308 0e+00

putative amino acid kinase; Reviewed


Pssm-ID: 237071  Cd Length: 314  Bit Score: 503.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044   1 MSLNVIALGGNAILDTDPTDEGQKAVVNHAAKYIAEFVAKGEQVIVCHGNGPQVGNLLLQQKAGESEKN--PALKLDTCV 78
Cdd:PRK12353   2 MKKIVVALGGNALGSTPEEATAQLEAVKKTAKSLVDLIEEGHEVVITHGNGPQVGNILLAQEAAASEKNkvPAMPLDVCG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044  79 AMTQGSIGYWLQNALTNEFEKRNIAKPVISVVTQVRVDKEDPSFKKPSKPIGPFYTKEEADAEAAKDGSTYVEDAGRGYR 158
Cdd:PRK12353  82 AMSQGYIGYHLQNALRNELLKRGIDKPVATVVTQVVVDANDPAFKNPTKPIGPFYTEEEAEKLAKEKGYTFKEDAGRGYR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 159 KVVPSPMPKEIVEKEAVRALVEADVLTICSGGGGIPVVAEDGQYVGVEAVNDKDFSARVLAENVDADRLIILTGVDNIYI 238
Cdd:PRK12353 162 RVVPSPKPVDIVEIEAIKTLVDAGQVVIAAGGGGIPVIREGGGLKGVEAVIDKDFASAKLAELVDADLLIILTAVDKVYI 241

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488284044 239 NYNQPDQKALEQISVAEAEEYIKEGHFAAGSMLPKIEAALDFVKGDDKRKAIITSIENLEN-IDKEAGTVI 308
Cdd:PRK12353 242 NFGKPNQKKLDEVTVSEAEKYIEEGQFAPGSMLPKVEAAISFVESRPGRKAIITSLEKAKEaLEGKAGTVI 312
ArcC COG0549
Carbamate kinase [Amino acid transport and metabolism];
1-309 9.89e-179

Carbamate kinase [Amino acid transport and metabolism];


Pssm-ID: 440315  Cd Length: 313  Bit Score: 495.75  E-value: 9.89e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044   1 MSLNVIALGGNAIL--DTDPTDEGQKAVVNHAAKYIAEFVAKGEQVIVCHGNGPQVGNLLLQQKAGeSEKNPALKLDTCV 78
Cdd:COG0549    2 KKRIVVALGGNALLrrGEPGTAEEQRENVREAAKALADLIEAGHEVVITHGNGPQVGLLLLQNEAA-KKKVPPMPLDVCG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044  79 AMTQGSIGYWLQNALTNEFEKRNIAKPVISVVTQVRVDKEDPSFKKPSKPIGPFYTKEEADAEAAKDGSTYVEDAGRGYR 158
Cdd:COG0549   81 AMTQGMIGYMLQQALRNELPKRGIDKPVATLVTQVEVDPDDPAFQNPTKPIGPFYTEEEAEELAKEKGWTFKEDAGRGYR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 159 KVVPSPMPKEIVEKEAVRALVEADVLTICSGGGGIPVVA-EDGQYVGVEAVNDKDFSARVLAENVDADRLIILTGVDNIY 237
Cdd:COG0549  161 RVVPSPKPKRIVEIDAIKALLEAGVIVIAAGGGGIPVVRdEDGGLKGVEAVIDKDLASALLAEELDADLLLILTDVDKVY 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284044 238 INYNQPDQKALEQISVAEAEEYIKEGHFAAGSMLPKIEAALDFVKGDDKRkAIITSIENLEN-IDKEAGTVIS 309
Cdd:COG0549  241 INFGKPDQRALDEVTVAEAKKYIEEGHFAAGSMGPKVEAAIRFVEATGKR-AIITSLEKAEEaLAGKAGTRIV 312
AAK_CK cd04235
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ...
 5-309 8.32e-178

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: 493.18  E-value: 8.32e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044   5 VIALGGNAILDTD--PTDEGQKAVVNHAAKYIAEFVAKGEQVIVCHGNGPQVGNLLLQQKAGeSEKNPALKLDTCVAMTQ 82
Cdd:cd04235    3 VVALGGNALLRRGepGTAEEQRENVKIAAKALADLIKNGHEVVITHGNGPQVGNLLLQNEAA-AEKVPAYPLDVCGAMSQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044  83 GSIGYWLQNALTNEFEKRNIAKPVISVVTQVRVDKEDPSFKKPSKPIGPFYTKEEADAEAAKDGSTYVEDAGRGYRKVVP 162
Cdd:cd04235   82 GMIGYMLQQALDNELPKRGIDKPVVTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEKGWTFKEDAGRGYRRVVP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 163 SPMPKEIVEKEAVRALVEADVLTICSGGGGIPVVAEDGQYVGVEAVNDKDFSARVLAENVDADRLIILTGVDNIYINYNQ 242
Cdd:cd04235  162 SPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREGGGLKGVEAVIDKDLASALLAEEINADLLVILTDVDNVYINFGK 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488284044 243 PDQKALEQISVAEAEEYIKEGHFAAGSMLPKIEAALDFVKGDDKrKAIITSIENLENI-DKEAGTVIS 309
Cdd:cd04235  242 PNQKALEQVTVEELEKYIEEGQFAPGSMGPKVEAAIRFVESGGK-KAIITSLENAEAAlEGKAGTVIV 308
PRK12454 PRK12454
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
 5-309 4.84e-139

carbamate kinase-like carbamoyl phosphate synthetase; Reviewed


Pssm-ID: 183535  Cd Length: 313  Bit Score: 395.52  E-value: 4.84e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044   5 VIALGGNAIL--DTDPTDEGQKAVVNHAAKYIAEFVAKGEQVIVCHGNGPQVGNLLLQQKAGESEKNPALKLDTCVAMTQ 82
Cdd:PRK12454   6 VIALGGNALLqpGEKGTAENQMKNVRKTAKQIADLIEEGYEVVITHGNGPQVGNLLLQMDAAKDVGIPPFPLDVAGAMTQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044  83 GSIGYWLQNALTNEFEKRNIAKPVISVVTQVRVDKEDPSFKKPSKPIGPFYTKEEADAEAAKDGSTYVEDAGRGYRKVVP 162
Cdd:PRK12454  86 GWIGYMIQQALRNELAKRGIEKQVATIVTQVIVDKNDPAFQNPTKPVGPFYDEEEAKKLAKEKGWIVKEDAGRGWRRVVP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 163 SPMPKEIVEKEAVRALVEADVLTICSGGGGIPVVAEDGQYVGVEAVNDKDFSARVLAENVDADRLIILTGVDNIYINYNQ 242
Cdd:PRK12454 166 SPDPLGIVEIEVIKALVENGFIVIASGGGGIPVIEEDGELKGVEAVIDKDLASELLAEELNADIFIILTDVEKVYLNYGK 245

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488284044 243 PDQKALEQISVAEAEEYIKEGHFAAGSMLPKIEAALDFVKGDDKRkAIITSIENL-ENIDKEAGTVIS 309
Cdd:PRK12454 246 PDQKPLDKVTVEEAKKYYEEGHFKAGSMGPKILAAIRFVENGGKR-AIIASLEKAvEALEGKTGTRII 312
arcC TIGR00746
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes ...
 5-309 3.94e-136

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: 387.97  E-value: 3.94e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044    5 VIALGGNAILD--TDPTDEGQKAVVNHAAKYIAEFVAKGEQVIVCHGNGPQVGNLLLQQKAGESEkNPALKLDTCVAMTQ 82
Cdd:TIGR00746   4 VVALGGNALLQrgEKGSAEAQRDNVRQTAPQIAKLIKRGYELVITHGNGPQVGNLLLQNQAADSE-VPAMPLDVLGAMSQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044   83 GSIGYWLQNALTNEFEKRNIAKPVISVVTQVRVDKEDPSFKKPSKPIGPFYTKEEADAEAAKDGSTYVEDAGRGYRKVVP 162
Cdd:TIGR00746  83 GMIGYMLQQALNNELPKRGMEKPVATVLTQTIVDPKDPAFQNPTKPIGPFYTEEEAKRLAAEKGWIVKEDAGRGWRRVVP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044  163 SPMPKEIVEKEAVRALVEADVLTICSGGGGIPVVAEDGQYVGVEAVNDKDFSARVLAENVDADRLIILTGVDNIYINYNQ 242
Cdd:TIGR00746 163 SPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEGAELKGVEAVIDKDLASEKLAEEVNADILVILTDVDAVYINYGK 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488284044  243 PDQKALEQISVAEAEEYIKEGHFAAGSMLPKIEAALDFVKGDDKRkAIITSIENLENI-DKEAGTVIS 309
Cdd:TIGR00746 243 PDEKALREVTVEELEDYYKAGHFAAGSMGPKVEAAIEFVESGGKR-AIITSLENAVEAlEGKAGTRVT 309
PRK12354 PRK12354
carbamate kinase; Reviewed
 5-312 3.71e-113

carbamate kinase; Reviewed


Pssm-ID: 183466  Cd Length: 307  Bit Score: 329.48  E-value: 3.71e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044   5 VIALGGNAILDTD--PTDEGQKAVVNHAAKYIAEfVAKGEQVIVCHGNGPQVGNLLLQQKAgeSEKNPALKLDTCVAMTQ 82
Cdd:PRK12354   4 VVALGGNALLRRGepLTAENQRANIRIAAEQIAK-IAREHELVIVHGNGPQVGLLALQNAA--YKDVTPYPLDVLGAETE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044  83 GSIGYWLQNALTNEFEKRNIAkpviSVVTQVRVDKEDPSFKKPSKPIGPFYTKEEADAEAAKDGSTYVEDaGRGYRKVVP 162
Cdd:PRK12354  81 GMIGYMLEQELGNLLPERPVA----TLLTQVEVDANDPAFANPTKPIGPVYDEAEAERLAAEKGWTIKPD-GDYFRRVVP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 163 SPMPKEIVEKEAVRALVEADVLTICSGGGGIPVV-AEDGQYVGVEAVNDKDFSARVLAENVDADRLIILTGVDNIYINYN 241
Cdd:PRK12354 156 SPRPKRIVEIRPIRWLLEKGHLVICAGGGGIPVVyDADGKLHGVEAVIDKDLAAALLAEQLDADLLLILTDVDAVYLDWG 235

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284044 242 QPDQKALEQISVAEAEEYikegHFAAGSMLPKIEAALDFVKGDDKRkAIITSIENLENIDK-EAGTVISQKG 312
Cdd:PRK12354 236 KPTQRAIAQATPDELREL----GFAAGSMGPKVEAACEFVRATGKI-AGIGSLEDIQAILAgEAGTRISPET 302
PRK12352 PRK12352
putative carbamate kinase; Reviewed
 3-308 4.33e-111

putative carbamate kinase; Reviewed


Pssm-ID: 183464  Cd Length: 316  Bit Score: 324.83  E-value: 4.33e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044   3 LNVIALGGNAILDTDP--TDEGQKAVVNHAAKYIAEFVAKGEQVIVCHGNGPQVGNLLLQQK-AGESEKNPALKLDTCVA 79
Cdd:PRK12352   4 LVVVAIGGNSIIKDNAsqSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEiAHEREGLPLTPLANCVA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044  80 MTQGSIGYWLQNALTNEFEKRNiAKPVISVVTQVRVDKEDPSFKKPSKPIGPFYTKEEADaEAAKDGSTY--VEDAGRGY 157
Cdd:PRK12352  84 DTQGGIGYLIQQALNNRLARHG-EKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRD-ELQKANPDWrfVEDAGRGY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 158 RKVVPSPMPKEIVEKEAVRALVEADVLTICSGGGGIPVV-AEDGQYVGVEAVNDKDFSARVLAENVDADRLIILTGVDNI 236
Cdd:PRK12352 162 RRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVrTDAGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEKV 241

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284044 237 YINYNQPDQKALEQISVAEAEEYIKEGHFAAGSMLPKIEAALDFVKGDDKRkAIITSIENL-ENIDKEAGTVI 308
Cdd:PRK12352 242 CIHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQGGKE-VIITTPECLpAALRGETGTHI 313
PRK09411 PRK09411
carbamate kinase; Reviewed
 5-309 1.06e-71

carbamate kinase; Reviewed


Pssm-ID: 181831  Cd Length: 297  Bit Score: 223.52  E-value: 1.06e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044   5 VIALGGNAILDTDP--TDEGQKAVVNHAAKYIAEfVAKGEQVIVCHGNGPQVGNLLLQQKAgeSEKNPALKLDTCVAMTQ 82
Cdd:PRK09411   5 VVALGGNALLQRGEalTAENQYRNIASAVPALAR-LARSYRLAIVHGNGPQVGLLALQNLA--WKEVEPYPLDVLVAESQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044  83 GSIGYWLQNALTNEfekrNIAKPVISVVTQVRVDKEDPSFKKPSKPIGPFYTKEEADAEAAKDGSTYVEDaGRGYRKVVP 162
Cdd:PRK09411  82 GMIGYMLAQSLSAQ----PQMPPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAYGWQMKRD-GKYLRRVVA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 163 SPMPKEIVEKEAVRALVEADVLTICSGGGGIPVVAEDGqyvGVEAVNDKDFSARVLAENVDADRLIILTGVDNIYINYNQ 242
Cdd:PRK09411 157 SPQPRKILDSEAIELLLKEGHVVICSGGGGVPVTEDGA---GSEAVIDKDLAAALLAEQINADGLVILTDADAVYENWGT 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488284044 243 PDQKALEQISVAEAEEYIKeghfAAGSMLPKIEAALDFVKGDDKRkAIITSIENLENI-DKEAGTVIS 309
Cdd:PRK09411 234 PQQRAIRHATPDELAPFAK----ADGAMGPKVTAVSGYVRSRGKP-AWIGALSRIEETlAGEAGTCIS 296
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 5-293 3.89e-22

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: 92.43  E-value: 3.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044    5 VIALGGNAILDTDPtdegqkavVNHAAKYIAEFVAKGEQVIVCHGNGPQVGNLLLQQKAGESEKNPALKLDTCVAMTQ-- 82
Cdd:pfam00696   4 VIKLGGSSLTDKER--------LKRLADEIAALLEEGRKLVVVHGGGAFADGLLALLGLSPRFARLTDAETLEVATMDal 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044   83 GSIG-YWLQNALTNEFEKRNIAKPVISVVTQVRVDKEDpsfkkpskpigpfytkeeadaeaakdgstyvedagrgyrkvv 161
Cdd:pfam00696  76 GSLGeRLNAALLAAGLPAVGLPAAQLLATEAGFIDDVV------------------------------------------ 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044  162 pspmpkEIVEKEAVRALVEADVLTICSGGGGIPVVAEDGqyvgveaVNDKDFSARVLAENVDADRLIILTGVDNIYINYN 241
Cdd:pfam00696 114 ------TRIDTEALEELLEAGVVPVITGFIGIDPEGELG-------RGSSDTLAALLAEALGADKLIILTDVDGVYTADP 180

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 488284044  242 --QPDQKALEQISVAEAEEYIkEGHFAAGSMLPKIEAALDFVKGdDKRKAIITS 293
Cdd:pfam00696 181 rkVPDAKLIPEISYDELLELL-ASGLATGGMKVKLPAALEAARR-GGIPVVIVN 232
AAK_NAGK-like cd04238
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ...
 179-308 2.73e-15

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: 74.08  E-value: 2.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 179 VEADVLTICSGGGGIPVVA-----EDGQYVGVEAvndkDFSARVLAENVDADRLIILTGVDNIYINYNQPdqkaLEQISV 253
Cdd:cd04238  126 VNPELLETLLEAGYIPVIApiavdEDGETYNVNA----DTAAGAIAAALKAEKLILLTDVPGVLDDPGSL----ISELTP 197

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 254 AEAEEYIKEGhFAAGSMLPKIEAALDFVKGDDKRKAIIT-----SIENLENIDKEAGTVI 308
Cdd:cd04238  198 KEAEELIEDG-VISGGMIPKVEAALEALEGGVRKVHIIDgrvphSLLLELFTDEGIGTMI 256
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 5-308 3.58e-14

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: 70.93  E-value: 3.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044   5 VIALGGNAILDTDPTDEgqkavvnhAAKYIAEFVAKGEQVIVCHGNGPQVGNLLL-----QQKAGESEKNPALKLDtCVA 79
Cdd:cd02115    1 VIKFGGSSVSSEERLRN--------LARILVKLASEGGRVVVVHGAGPQITDELLahgelLGYARGLRITDRETDA-LAA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044  80 MTQGSIGYWLQNALtnefekrniakpvisvvtqvrvdkedpsfkkpskpigpfytkeeadaeAAKDGSTYVEDAGRGYRK 159
Cdd:cd02115   72 MGEGMSNLLIAAAL------------------------------------------------EQHGIKAVPLDLTQAGFA 103

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 160 VVPSPMPKEI--VEKEAVRALVEADVLTICSGGGGIPVVAedgqyVGVEAVNDKDFSARVLAENVDADRLIILTGVDNIY 237
Cdd:cd02115  104 SPNQGHVGKItkVSTDRLKSLLENGILPILSGFGGTDEKE-----TGTLGRGGSDSTAALLAAALKADRLVILTDVDGVY 178

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488284044 238 INYNQPDQKA--LEQISVAEAEEYIkeghfAAGSMLPKIEAALDFVKGddKRKAIITSIENLENID----KEAGTVI 308
Cdd:cd02115  179 TADPRKVPDAklLSELTYEEAAELA-----YAGAMVLKPKAADPAARA--GIPVRIANTENPGALAlftpDGGGTLI 248
AAK_NAGK-C cd04250
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ...
 179-291 9.90e-13

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: 67.15  E-value: 9.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 179 VEADVLTICSGGGGIPVVA-----EDGQYVGVEAvndkDFSARVLAENVDADRLIILTGVDNIYINYNQPDqKALEQISV 253
Cdd:cd04250  146 VNPELLETLLEAGYIPVIApvgvgEDGETYNINA----DTAAGAIAAALKAEKLILLTDVAGVLDDPNDPG-SLISEISL 220

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 488284044 254 AEAEEYIKEGHFAAGsMLPKIEAALDFVKGDDKRKAII 291
Cdd:cd04250  221 KEAEELIADGIISGG-MIPKVEACIEALEGGVKAAHII 257
PRK00942 PRK00942
acetylglutamate kinase; Provisional
 179-283 8.04e-12

acetylglutamate kinase; Provisional


Pssm-ID: 234869 [Multi-domain]  Cd Length: 283  Bit Score: 64.36  E-value: 8.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 179 VEADVLTICSGGGGIPVVA-----EDGQYVGVEAvndkDFSARVLAENVDADRLIILTGVDNIYINYNQPdqkaLEQISV 253
Cdd:PRK00942 150 VNPALLEALLEAGYIPVISpigvgEDGETYNINA----DTAAGAIAAALGAEKLILLTDVPGVLDDKGQL----ISELTA 221

                         90       100       110
                 ....*....|....*....|....*....|
gi 488284044 254 AEAEEYIKEGHFAAGsMLPKIEAALDFVKG 283
Cdd:PRK00942 222 SEAEELIEDGVITGG-MIPKVEAALDAARG 250
ArgB COG0548
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ...
 5-283 2.16e-09

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: 57.35  E-value: 2.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044   5 VIALGGNAILDtdptDEGQKAVvnhaAKYIAEFVAKGEQVIVCHGNGPQVGNLLlqQKAG-ESEK--------NPALKld 75
Cdd:COG0548   27 VIKYGGEAMED----EELKAAL----AQDIALLKSLGIRPVLVHGGGPQINELL--KRLGiESEFvnglrvtdEETLE-- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044  76 tCVAMTQ-GSIGYWLQNALTnefekRNIAKPV-ISVVTqvrvdkedpsfkkpskpiGPFYTkeeadaeAAKDGSTYVEDA 153
Cdd:COG0548   95 -VVEMVLaGKVNKEIVALLS-----QGGGNAVgLSGKD------------------GNLIT-------ARPLGVGDGVDL 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 154 GR-GyrKVVPspmpkeiVEKEAVRALVEADVlticsggggIPVVA-----EDGQYVGVEAvndkDFSARVLAENVDADRL 227
Cdd:COG0548  144 GHvG--EVRR-------VDPELIRALLDAGY---------IPVISpigysPTGEVYNINA----DTVAGAIAAALKAEKL 201

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488284044 228 IILTGVDNIYinynqPDQKAL-EQISVAEAEEYIKEGHFAAGsMLPKIEAALDFVKG 283
Cdd:COG0548  202 ILLTDVPGVL-----DDPGSLiSELTAAEAEELIADGVISGG-MIPKLEAALDAVRG 252
PLN02512 PLN02512
acetylglutamate kinase
 162-291 1.25e-07

acetylglutamate kinase


Pssm-ID: 178128  Cd Length: 309  Bit Score: 52.38  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 162 PSPMPKEI--------VEKEAVRALVEAdvlticsggGGIPVVA-----EDGQYVGVEAvndkDFSARVLAENVDADRLI 228
Cdd:PLN02512 158 PSPNSADLgfvgevtrVDPTVLRPLVDD---------GHIPVIAtvaadEDGQAYNINA----DTAAGEIAAALGAEKLI 224

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284044 229 ILTGVDNIYINYNQPDQKaLEQISVAEAEEYIKEGHFAAGsMLPKIEAALDFVKGDDKRKAII 291
Cdd:PLN02512 225 LLTDVAGVLEDKDDPGSL-VKELDIKGVRKLIADGKIAGG-MIPKVECCVRSLAQGVKTAHII 285
AAK_NAGK-UC cd04251
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ...
 179-308 6.87e-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: 46.59  E-value: 6.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 179 VEADVLTICSGGGGIPVVAEDGQYVGVEAVN-DKDFSARVLAENVDADRLIILTGVDNIYInynqpDQKALEQISVAEAE 257
Cdd:cd04251  133 VNSDLIEALLDAGYLPVVSPVAYSEEGEPLNvDGDRAAAAIAAALKAERLILLTDVEGLYL-----DGRVIERITVSDAE 207

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488284044 258 EYIKEghfAAGSMLPKIEAALDFVKGdDKRKAIITSIENLENID---KEAGTVI 308
Cdd:cd04251  208 SLLEK---AGGGMKRKLLAAAEAVEG-GVREVVIGDARADSPISsalNGGGTVI 257
PRK12314 PRK12314
gamma-glutamyl kinase; Provisional
 209-312 1.18e-04

gamma-glutamyl kinase; Provisional


Pssm-ID: 183430 [Multi-domain]  Cd Length: 266  Bit Score: 42.92  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 209 NDKdFSARVlAENVDADRLIILTGVDNIY-----INynqPDQKALEQISVAEAEEYIKEG----HFAAGSMLPKIEAAlD 279
Cdd:PRK12314 156 NDR-LSAIV-AKLVKADLLIILSDIDGLYdknprIN---PDAKLRSEVTEITEEILALAGgagsKFGTGGMVTKLKAA-K 229

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 488284044 280 FVKgDDKRKAIITSIENLENI-----DKEAGTVISQKG 312
Cdd:PRK12314 230 FLM-EAGIKMVLANGFNPSDIldfleGESIGTLFAPKK 266
AAK_UMPK-PyrH-Pf cd04253
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ...
 196-308 2.38e-03

AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase (uridylate kinase) enzymes that catalyze UMP phosphorylation and play a key role in pyrimidine nucleotide biosynthesis; regulation of this process is via feed-back control and via gene repression of carbamoyl phosphate synthetase (the first enzyme of the pyrimidine biosynthesis pathway). The UMP kinase of Pyrococcus furiosus (Pf) is known to function as a homohexamer, with GTP and UTP being allosteric effectors. Like other related enzymes (carbamate kinase, aspartokinase, and N-acetylglutamate kinase) the E. coli and most bacterial UMPKs have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs (this CD) appear to lack this residue and the Pyrococcus furiosus structure has an additional Mg ion bound to the ATP molecule which is proposed to function as the catalysis instead. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239786 [Multi-domain]  Cd Length: 221  Bit Score: 38.77  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 196 VAEDGQYV---GVEAVNDKDFSARVLAENVDADRLIILTGVDNIYI---NYNqPDQKALEQISVAEAEEYIKEGHFAAGS 269
Cdd:cd04253   99 AMFTGKIVvmgGTEPGQSTDAVAALLAERLGADLLINATNVDGVYSkdpRKD-PDAKKFDRLSADELIDIVGKSSWKAGS 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 488284044 270 MLPKIEAALDFVKGDDKRKAII--TSIENLENIDK--EAGTVI 308
Cdd:cd04253  178 NEPFDPLAAKIIERSGIKTIVVdgRDPENLERALKgeFVGTII 220
AAK_AKiii-LysC-EC cd04258
AAK_AKiii-LysC-EC: Amino Acid Kinase Superfamily (AAK), AKiii-LysC-EC: this CD includes the ...
 212-275 3.91e-03

AAK_AKiii-LysC-EC: Amino Acid Kinase Superfamily (AAK), AKiii-LysC-EC: this CD includes the N-terminal catalytic aspartokinase (AK) domain of the lysine-sensitive aspartokinase isoenzyme AKIII. AKIII is a monofunctional class enzyme (LysC) found in some bacteria such as E. coli. Aspartokinase is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. In E. coli, LysC is reported to be a homodimer of 50 kD subunits.


Pssm-ID: 239791 [Multi-domain]  Cd Length: 292  Bit Score: 38.50  E-value: 3.91e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 212 DFSARVLAENVDADRLIILTGVDNIYINYNQ--PDQKALEQISVAEAEEYIKEG----HFAagSMLPKIE 275
Cdd:cd04258  204 DYSAALLAEALHAEELQIWTDVAGIYTTDPRicPAARAIKEISFAEAAEMATFGakvlHPA--TLLPAIR 271
AAK_G5K_ProB cd04242
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ...
 209-277 5.51e-03

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: 37.81  E-value: 5.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 209 NDKdFSARVlAENVDADRLIILTGVDNIY-----INynqPDQKALEQISvaEAEEYIKEGHFAAGS------MLPKIEAA 277
Cdd:cd04242  144 NDR-LSALV-AGLVNADLLILLSDVDGLYdknprEN---PDAKLIPEVE--EITDEIEAMAGGSGSsvgtggMRTKLKAA 216
AAK_UMPK-like cd04239
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ...
 161-258 8.46e-03

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: 37.13  E-value: 8.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284044 161 VPSPMP-KEIVE----KEAVRALVEADVLtICSGGGGIPVVAEDgqyvgveAVndkdfsARVLAENVDADRLIILTGVDN 235
Cdd:cd04239   93 VMSAIPmQGVAEpyirRRAIRHLEKGRIV-IFGGGTGNPGFTTD-------TA------AALRAEEIGADVLLKATNVDG 158

                         90       100
                 ....*....|....*....|....*...
gi 488284044 236 IY-----INynqPDQKALEQISVAEAEE 258
Cdd:cd04239  159 VYdadpkKN---PDAKKYDRISYDELLK 183
AAK_AK-HSDH cd04257
AAK_AK-HSDH: Amino Acid Kinase Superfamily (AAK), AK-HSDH; this CD includes the N-terminal ...
 209-273 9.20e-03

AAK_AK-HSDH: Amino Acid Kinase Superfamily (AAK), AK-HSDH; this CD includes the N-terminal catalytic domain of aspartokinase (AK) of the bifunctional enzyme AK - homoserine dehydrogenase (HSDH). These aspartokinases are found in bacteria (E. coli AKI-HSDHI, ThrA and E. coli AKII-HSDHII, MetL) and higher plants (Z. mays AK-HSDH). AK and HSDH are the first and third enzymes in the biosynthetic pathway of the aspartate family of amino acids. AK catalyzes the phosphorylation of Asp to P-aspartyl phosphate. HSDH catalyzes the NADPH-dependent conversion of Asp 3-semialdehyde to homoserine. ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. In E. coli, ThrA is subject to allosteric regulation by the end product L-threonine and the native enzyme is reported to be tetrameric. As with bacteria, plant AK and HSDH are feedback inhibited by pathway end products. Maize AK-HSDH is a Thr-sensitive 180-kD enzyme. Arabidopsis AK-HSDH is an alanine-activated, threonine-sensitive enzyme whose ACT domains, located C-terminal to the AK catalytic domain, were shown to be involved in allosteric activation.


Pssm-ID: 239790 [Multi-domain]  Cd Length: 294  Bit Score: 37.18  E-value: 9.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488284044 209 NDKDFSARVLAENVDADRLIILTGVDNIY-INYNQ-PDQKALEQISVAEAEEYikeGHFAAGSMLPK 273
Cdd:cd04257  203 NGSDYSAAILAALLDADQVEIWTDVDGVYsADPRKvKDARLLPSLSYQEAMEL---SYFGAKVLHPK 266
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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