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Conserved domains on  [gi|487748499|ref|WP_001830533|]
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MULTISPECIES: carbamate kinase [Staphylococcus]

Protein Classification

carbamate kinase( domain architecture ID 10013930)

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

CATH:  3.40.1160.10
EC:  2.7.2.2
Gene Symbol:  arcC
Gene Ontology:  GO:0008804|GO:0019546|GO:0016310|GO:0005524
PubMed:  10211841
SCOP:  4000773

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK12353 PRK12353
putative amino acid kinase; Reviewed
 1-310 0e+00

putative amino acid kinase; Reviewed


:

Pssm-ID: 237071  Cd Length: 314  Bit Score: 532.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499   1 MAKIVVALGGNALGKSPQE---QLELVKNTAKSLVGLITKGHEIVISHGNGPQVGSINLGLNYAAEHDQ-GPAFPFAECG 76
Cdd:PRK12353   2 MKKIVVALGGNALGSTPEEataQLEAVKKTAKSLVDLIEEGHEVVITHGNGPQVGNILLAQEAAASEKNkVPAMPLDVCG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499  77 AMSQAYIGYQLQESLQNELHSMGIDKQVVTLVTQVEVDEGDPAFNSPSKPIGLFYTKEEANRIQQEKGYQFVEDAGRGYR 156
Cdd:PRK12353  82 AMSQGYIGYHLQNALRNELLKRGIDKPVATVVTQVVVDANDPAFKNPTKPIGPFYTEEEAEKLAKEKGYTFKEDAGRGYR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499 157 RVVPSPQPISIIELESIKTLVENDTLVIAAGGGGIPVIREqHDSFKGIDAVIDKDKTSALLGADIHCDQLIILTAIDYVY 236
Cdd:PRK12353 162 RVVPSPKPVDIVEIEAIKTLVDAGQVVIAAGGGGIPVIRE-GGGLKGVEAVIDKDFASAKLAELVDADLLIILTAVDKVY 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487748499 237 INYHTDQQQALKTTNIDTLKTYIEEEQFAKGSMLPKIESAISFIENNPNGSVLITSLNQLDAALEGKIGTLITK 310
Cdd:PRK12353 241 INFGKPNQKKLDEVTVSEAEKYIEEGQFAPGSMLPKVEAAISFVESRPGRKAIITSLEKAKEALEGKAGTVIVK 314
 
Name Accession Description Interval E-value
PRK12353 PRK12353
putative amino acid kinase; Reviewed
 1-310 0e+00

putative amino acid kinase; Reviewed


Pssm-ID: 237071  Cd Length: 314  Bit Score: 532.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499   1 MAKIVVALGGNALGKSPQE---QLELVKNTAKSLVGLITKGHEIVISHGNGPQVGSINLGLNYAAEHDQ-GPAFPFAECG 76
Cdd:PRK12353   2 MKKIVVALGGNALGSTPEEataQLEAVKKTAKSLVDLIEEGHEVVITHGNGPQVGNILLAQEAAASEKNkVPAMPLDVCG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499  77 AMSQAYIGYQLQESLQNELHSMGIDKQVVTLVTQVEVDEGDPAFNSPSKPIGLFYTKEEANRIQQEKGYQFVEDAGRGYR 156
Cdd:PRK12353  82 AMSQGYIGYHLQNALRNELLKRGIDKPVATVVTQVVVDANDPAFKNPTKPIGPFYTEEEAEKLAKEKGYTFKEDAGRGYR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499 157 RVVPSPQPISIIELESIKTLVENDTLVIAAGGGGIPVIREqHDSFKGIDAVIDKDKTSALLGADIHCDQLIILTAIDYVY 236
Cdd:PRK12353 162 RVVPSPKPVDIVEIEAIKTLVDAGQVVIAAGGGGIPVIRE-GGGLKGVEAVIDKDFASAKLAELVDADLLIILTAVDKVY 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487748499 237 INYHTDQQQALKTTNIDTLKTYIEEEQFAKGSMLPKIESAISFIENNPNGSVLITSLNQLDAALEGKIGTLITK 310
Cdd:PRK12353 241 INFGKPNQKKLDEVTVSEAEKYIEEGQFAPGSMLPKVEAAISFVESRPGRKAIITSLEKAKEALEGKAGTVIVK 314
ArcC COG0549
Carbamate kinase [Amino acid transport and metabolism];
1-310 0e+00

Carbamate kinase [Amino acid transport and metabolism];


Pssm-ID: 440315  Cd Length: 313  Bit Score: 508.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499   1 MAKIVVALGGNALGK-----SPQEQLELVKNTAKSLVGLITKGHEIVISHGNGPQVGSINLGLNYAaeHDQGPAFPFAEC 75
Cdd:COG0549    2 KKRIVVALGGNALLRrgepgTAEEQRENVREAAKALADLIEAGHEVVITHGNGPQVGLLLLQNEAA--KKKVPPMPLDVC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499  76 GAMSQAYIGYQLQESLQNELHSMGIDKQVVTLVTQVEVDEGDPAFNSPSKPIGLFYTKEEANRIQQEKGYQFVEDAGRGY 155
Cdd:COG0549   80 GAMTQGMIGYMLQQALRNELPKRGIDKPVATLVTQVEVDPDDPAFQNPTKPIGPFYTEEEAEELAKEKGWTFKEDAGRGY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499 156 RRVVPSPQPISIIELESIKTLVENDTLVIAAGGGGIPVIREQHDSFKGIDAVIDKDKTSALLGADIHCDQLIILTAIDYV 235
Cdd:COG0549  160 RRVVPSPKPKRIVEIDAIKALLEAGVIVIAAGGGGIPVVRDEDGGLKGVEAVIDKDLASALLAEELDADLLLILTDVDKV 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487748499 236 YINYHTDQQQALKTTNIDTLKTYIEEEQFAKGSMLPKIESAISFIEnNPNGSVLITSLNQLDAALEGKIGTLITK 310
Cdd:COG0549  240 YINFGKPDQRALDEVTVAEAKKYIEEGHFAAGSMGPKVEAAIRFVE-ATGKRAIITSLEKAEEALAGKAGTRIVP 313
AAK_CK cd04235
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ...
 3-309 2.51e-171

AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and carbamoyl phosphate (CP) utilization with the production of ATP from ADP and CP. Both CK (this CD) and nonhomologous CP synthetase synthesize carbamoyl phosphate, an essential precursor of arginine and pyrimidine bases, in the presence of ATP, bicarbonate, and ammonia. CK is a homodimer of 33 kDa subunits and is a member of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239768  Cd Length: 308  Bit Score: 477.00  E-value: 2.51e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499   3 KIVVALGGNALGKSPQ-----EQLELVKNTAKSLVGLITKGHEIVISHGNGPQVGSINLGLnyAAEHDQGPAFPFAECGA 77
Cdd:cd04235    1 RIVVALGGNALLRRGEpgtaeEQRENVKIAAKALADLIKNGHEVVITHGNGPQVGNLLLQN--EAAAEKVPAYPLDVCGA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499  78 MSQAYIGYQLQESLQNELHSMGIDKQVVTLVTQVEVDEGDPAFNSPSKPIGLFYTKEEANRIQQEKGYQFVEDAGRGYRR 157
Cdd:cd04235   79 MSQGMIGYMLQQALDNELPKRGIDKPVVTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEKGWTFKEDAGRGYRR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499 158 VVPSPQPISIIELESIKTLVENDTLVIAAGGGGIPVIREQhDSFKGIDAVIDKDKTSALLGADIHCDQLIILTAIDYVYI 237
Cdd:cd04235  159 VVPSPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREG-GGLKGVEAVIDKDLASALLAEEINADLLVILTDVDNVYI 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487748499 238 NYHTDQQQALKTTNIDTLKTYIEEEQFAKGSMLPKIESAISFIENNPnGSVLITSLNQLDAALEGKIGTLIT 309
Cdd:cd04235  238 NFGKPNQKALEQVTVEELEKYIEEGQFAPGSMGPKVEAAIRFVESGG-KKAIITSLENAEAALEGKAGTVIV 308
arcC TIGR00746
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes ...
 3-310 9.94e-126

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: 361.39  E-value: 9.94e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499    3 KIVVALGGNALGK-----SPQEQLELVKNTAKSLVGLITKGHEIVISHGNGPQVGsiNLGLNYAAEHDQGPAFPFAECGA 77
Cdd:TIGR00746   2 RVVVALGGNALLQrgekgSAEAQRDNVRQTAPQIAKLIKRGYELVITHGNGPQVG--NLLLQNQAADSEVPAMPLDVLGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499   78 MSQAYIGYQLQESLQNELHSMGIDKQVVTLVTQVEVDEGDPAFNSPSKPIGLFYTKEEANRIQQEKGYQFVEDAGRGYRR 157
Cdd:TIGR00746  80 MSQGMIGYMLQQALNNELPKRGMEKPVATVLTQTIVDPKDPAFQNPTKPIGPFYTEEEAKRLAAEKGWIVKEDAGRGWRR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499  158 VVPSPQPISIIELESIKTLVENDTLVIAAGGGGIPVIREQhDSFKGIDAVIDKDKTSALLGADIHCDQLIILTAIDYVYI 237
Cdd:TIGR00746 160 VVPSPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEG-AELKGVEAVIDKDLASEKLAEEVNADILVILTDVDAVYI 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487748499  238 NYHTDQQQALKTTNIDTLKTYIEEEQFAKGSMLPKIESAISFIENNPNGSVlITSLNQLDAALEGKIGTLITK 310
Cdd:TIGR00746 239 NYGKPDEKALREVTVEELEDYYKAGHFAAGSMGPKVEAAIEFVESGGKRAI-ITSLENAVEALEGKAGTRVTK 310
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 3-292 4.22e-16

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: 75.87  E-value: 4.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499    3 KIVVALGGNALGKSpqeqlELVKNTAKSLVGLITKGHEIVISHGNGPQVGSINLGLNYAAEHDQGPAFPFAECGAMSQAY 82
Cdd:pfam00696   2 RVVIKLGGSSLTDK-----ERLKRLADEIAALLEEGRKLVVVHGGGAFADGLLALLGLSPRFARLTDAETLEVATMDALG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499   83 IgyqlqeslQNELHSMGIdkqvvtlvtqveVDEGDPAFNSPSKPIGLfytkeeanriqqekgyqfvedagrgyRRVVPSP 162
Cdd:pfam00696  77 S--------LGERLNAAL------------LAAGLPAVGLPAAQLLA--------------------------TEAGFID 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499  163 QPISIIELESIKTLVENDTLVIAAGGGGIPVireqhdsfKGIDAVIDKDKTSALLGADIHCDQLIILTAIDYVYINYHTD 242
Cdd:pfam00696 111 DVVTRIDTEALEELLEAGVVPVITGFIGIDP--------EGELGRGSSDTLAALLAEALGADKLIILTDVDGVYTADPRK 182

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 487748499  243 QQQA--LKTTNIDTLKTYIeEEQFAKGSMLPKIESAISFIENNpNGSVLITS 292
Cdd:pfam00696 183 VPDAklIPEISYDELLELL-ASGLATGGMKVKLPAALEAARRG-GIPVVIVN 232
 
Name Accession Description Interval E-value
PRK12353 PRK12353
putative amino acid kinase; Reviewed
 1-310 0e+00

putative amino acid kinase; Reviewed


Pssm-ID: 237071  Cd Length: 314  Bit Score: 532.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499   1 MAKIVVALGGNALGKSPQE---QLELVKNTAKSLVGLITKGHEIVISHGNGPQVGSINLGLNYAAEHDQ-GPAFPFAECG 76
Cdd:PRK12353   2 MKKIVVALGGNALGSTPEEataQLEAVKKTAKSLVDLIEEGHEVVITHGNGPQVGNILLAQEAAASEKNkVPAMPLDVCG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499  77 AMSQAYIGYQLQESLQNELHSMGIDKQVVTLVTQVEVDEGDPAFNSPSKPIGLFYTKEEANRIQQEKGYQFVEDAGRGYR 156
Cdd:PRK12353  82 AMSQGYIGYHLQNALRNELLKRGIDKPVATVVTQVVVDANDPAFKNPTKPIGPFYTEEEAEKLAKEKGYTFKEDAGRGYR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499 157 RVVPSPQPISIIELESIKTLVENDTLVIAAGGGGIPVIREqHDSFKGIDAVIDKDKTSALLGADIHCDQLIILTAIDYVY 236
Cdd:PRK12353 162 RVVPSPKPVDIVEIEAIKTLVDAGQVVIAAGGGGIPVIRE-GGGLKGVEAVIDKDFASAKLAELVDADLLIILTAVDKVY 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487748499 237 INYHTDQQQALKTTNIDTLKTYIEEEQFAKGSMLPKIESAISFIENNPNGSVLITSLNQLDAALEGKIGTLITK 310
Cdd:PRK12353 241 INFGKPNQKKLDEVTVSEAEKYIEEGQFAPGSMLPKVEAAISFVESRPGRKAIITSLEKAKEALEGKAGTVIVK 314
ArcC COG0549
Carbamate kinase [Amino acid transport and metabolism];
1-310 0e+00

Carbamate kinase [Amino acid transport and metabolism];


Pssm-ID: 440315  Cd Length: 313  Bit Score: 508.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499   1 MAKIVVALGGNALGK-----SPQEQLELVKNTAKSLVGLITKGHEIVISHGNGPQVGSINLGLNYAaeHDQGPAFPFAEC 75
Cdd:COG0549    2 KKRIVVALGGNALLRrgepgTAEEQRENVREAAKALADLIEAGHEVVITHGNGPQVGLLLLQNEAA--KKKVPPMPLDVC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499  76 GAMSQAYIGYQLQESLQNELHSMGIDKQVVTLVTQVEVDEGDPAFNSPSKPIGLFYTKEEANRIQQEKGYQFVEDAGRGY 155
Cdd:COG0549   80 GAMTQGMIGYMLQQALRNELPKRGIDKPVATLVTQVEVDPDDPAFQNPTKPIGPFYTEEEAEELAKEKGWTFKEDAGRGY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499 156 RRVVPSPQPISIIELESIKTLVENDTLVIAAGGGGIPVIREQHDSFKGIDAVIDKDKTSALLGADIHCDQLIILTAIDYV 235
Cdd:COG0549  160 RRVVPSPKPKRIVEIDAIKALLEAGVIVIAAGGGGIPVVRDEDGGLKGVEAVIDKDLASALLAEELDADLLLILTDVDKV 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487748499 236 YINYHTDQQQALKTTNIDTLKTYIEEEQFAKGSMLPKIESAISFIEnNPNGSVLITSLNQLDAALEGKIGTLITK 310
Cdd:COG0549  240 YINFGKPDQRALDEVTVAEAKKYIEEGHFAAGSMGPKVEAAIRFVE-ATGKRAIITSLEKAEEALAGKAGTRIVP 313
AAK_CK cd04235
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ...
 3-309 2.51e-171

AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and carbamoyl phosphate (CP) utilization with the production of ATP from ADP and CP. Both CK (this CD) and nonhomologous CP synthetase synthesize carbamoyl phosphate, an essential precursor of arginine and pyrimidine bases, in the presence of ATP, bicarbonate, and ammonia. CK is a homodimer of 33 kDa subunits and is a member of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239768  Cd Length: 308  Bit Score: 477.00  E-value: 2.51e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499   3 KIVVALGGNALGKSPQ-----EQLELVKNTAKSLVGLITKGHEIVISHGNGPQVGSINLGLnyAAEHDQGPAFPFAECGA 77
Cdd:cd04235    1 RIVVALGGNALLRRGEpgtaeEQRENVKIAAKALADLIKNGHEVVITHGNGPQVGNLLLQN--EAAAEKVPAYPLDVCGA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499  78 MSQAYIGYQLQESLQNELHSMGIDKQVVTLVTQVEVDEGDPAFNSPSKPIGLFYTKEEANRIQQEKGYQFVEDAGRGYRR 157
Cdd:cd04235   79 MSQGMIGYMLQQALDNELPKRGIDKPVVTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEKGWTFKEDAGRGYRR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499 158 VVPSPQPISIIELESIKTLVENDTLVIAAGGGGIPVIREQhDSFKGIDAVIDKDKTSALLGADIHCDQLIILTAIDYVYI 237
Cdd:cd04235  159 VVPSPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREG-GGLKGVEAVIDKDLASALLAEEINADLLVILTDVDNVYI 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487748499 238 NYHTDQQQALKTTNIDTLKTYIEEEQFAKGSMLPKIESAISFIENNPnGSVLITSLNQLDAALEGKIGTLIT 309
Cdd:cd04235  238 NFGKPNQKALEQVTVEELEKYIEEGQFAPGSMGPKVEAAIRFVESGG-KKAIITSLENAEAALEGKAGTVIV 308
PRK12686 PRK12686
carbamate kinase; Reviewed
 1-310 3.01e-151

carbamate kinase; Reviewed


Pssm-ID: 183683  Cd Length: 312  Bit Score: 426.38  E-value: 3.01e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499   1 MAKIVVALGGNALGK---SPQEQLELVKNTAKSLVGLITKGHEIVISHGNGPQVGSINLGLNyAAEHDQGPAFPFAECGA 77
Cdd:PRK12686   2 KEKIVIALGGNAILQteaTAEAQQTAVREAAQHLVDLIEAGHDIVITHGNGPQVGNLLLQQA-ESNSNKVPAMPLDTCVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499  78 MSQAYIGYQLQESLQNELHSMGIDKQVVTLVTQVEVDEGDPAFNSPSKPIGLFYTKEEANRIQQEKGYQFVEDAGRGYRR 157
Cdd:PRK12686  81 MSQGMIGYWLQNALNNELTERGIDKPVITLVTQVEVDKDDPAFANPTKPIGPFYTEEEAKQQAEQPGSTFKEDAGRGYRR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499 158 VVPSPQPISIIELESIKTLVENDTLVIAAGGGGIPVIREQhDSFKGIDAVIDKDKTSALLGADIHCDQLIILTAIDYVYI 237
Cdd:PRK12686 161 VVPSPKPQEIIEHDTIRTLVDGGNIVIACGGGGIPVIRDD-NTLKGVEAVIDKDFASEKLAEQIDADLLIILTGVENVFI 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487748499 238 NYHTDQQQALKTTNIDTLKTYIEEEQFAKGSMLPKIESAISFIENNPNGSVLITSLNQLDAALEGKIGTLITK 310
Cdd:PRK12686 240 NFNKPNQQKLDDITVAEAKQYIAEGQFAPGSMLPKVEAAIDFVESGEGKKAIITSLEQAKEALAGNAGTHITL 312
PRK12454 PRK12454
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
 1-310 4.00e-144

carbamate kinase-like carbamoyl phosphate synthetase; Reviewed


Pssm-ID: 183535  Cd Length: 313  Bit Score: 408.23  E-value: 4.00e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499   1 MAKIVVALGGNALGK-----SPQEQLELVKNTAKSLVGLITKGHEIVISHGNGPQVGSINLGLNyAAEHDQGPAFPFAEC 75
Cdd:PRK12454   2 KKRIVIALGGNALLQpgekgTAENQMKNVRKTAKQIADLIEEGYEVVITHGNGPQVGNLLLQMD-AAKDVGIPPFPLDVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499  76 GAMSQAYIGYQLQESLQNELHSMGIDKQVVTLVTQVEVDEGDPAFNSPSKPIGLFYTKEEANRIQQEKGYQFVEDAGRGY 155
Cdd:PRK12454  81 GAMTQGWIGYMIQQALRNELAKRGIEKQVATIVTQVIVDKNDPAFQNPTKPVGPFYDEEEAKKLAKEKGWIVKEDAGRGW 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499 156 RRVVPSPQPISIIELESIKTLVENDTLVIAAGGGGIPVIREQhDSFKGIDAVIDKDKTSALLGADIHCDQLIILTAIDYV 235
Cdd:PRK12454 161 RRVVPSPDPLGIVEIEVIKALVENGFIVIASGGGGIPVIEED-GELKGVEAVIDKDLASELLAEELNADIFIILTDVEKV 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487748499 236 YINYHTDQQQALKTTNIDTLKTYIEEEQFAKGSMLPKIESAISFIENNpNGSVLITSLNQLDAALEGKIGTLITK 310
Cdd:PRK12454 240 YLNYGKPDQKPLDKVTVEEAKKYYEEGHFKAGSMGPKILAAIRFVENG-GKRAIIASLEKAVEALEGKTGTRIIP 313
arcC TIGR00746
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes ...
 3-310 9.94e-126

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: 361.39  E-value: 9.94e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499    3 KIVVALGGNALGK-----SPQEQLELVKNTAKSLVGLITKGHEIVISHGNGPQVGsiNLGLNYAAEHDQGPAFPFAECGA 77
Cdd:TIGR00746   2 RVVVALGGNALLQrgekgSAEAQRDNVRQTAPQIAKLIKRGYELVITHGNGPQVG--NLLLQNQAADSEVPAMPLDVLGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499   78 MSQAYIGYQLQESLQNELHSMGIDKQVVTLVTQVEVDEGDPAFNSPSKPIGLFYTKEEANRIQQEKGYQFVEDAGRGYRR 157
Cdd:TIGR00746  80 MSQGMIGYMLQQALNNELPKRGMEKPVATVLTQTIVDPKDPAFQNPTKPIGPFYTEEEAKRLAAEKGWIVKEDAGRGWRR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499  158 VVPSPQPISIIELESIKTLVENDTLVIAAGGGGIPVIREQhDSFKGIDAVIDKDKTSALLGADIHCDQLIILTAIDYVYI 237
Cdd:TIGR00746 160 VVPSPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEG-AELKGVEAVIDKDLASEKLAEEVNADILVILTDVDAVYI 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487748499  238 NYHTDQQQALKTTNIDTLKTYIEEEQFAKGSMLPKIESAISFIENNPNGSVlITSLNQLDAALEGKIGTLITK 310
Cdd:TIGR00746 239 NYGKPDEKALREVTVEELEDYYKAGHFAAGSMGPKVEAAIEFVESGGKRAI-ITSLENAVEALEGKAGTRVTK 310
PRK12352 PRK12352
putative carbamate kinase; Reviewed
 4-310 3.09e-117

putative carbamate kinase; Reviewed


Pssm-ID: 183464  Cd Length: 316  Bit Score: 340.24  E-value: 3.09e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499   4 IVVALGGNALGK-----SPQEQLELVKNTAKSLVGLITKGHEIVISHGNGPQVGSINLGLNYAAEHDQGPAFPFAECGAM 78
Cdd:PRK12352   5 VVVAIGGNSIIKdnasqSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHEREGLPLTPLANCVAD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499  79 SQAYIGYQLQESLQNELHSMGiDKQVVTLVTQVEVDEGDPAFNSPSKPIGLFYTKEEANRIQQE-KGYQFVEDAGRGYRR 157
Cdd:PRK12352  85 TQGGIGYLIQQALNNRLARHG-EKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDELQKAnPDWRFVEDAGRGYRR 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499 158 VVPSPQPISIIELESIKTLVENDTLVIAAGGGGIPVIREQHDSFKGIDAVIDKDKTSALLGADIHCDQLIILTAIDYVYI 237
Cdd:PRK12352 164 VVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDAGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEKVCI 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487748499 238 NYHTDQQQALKTTNIDTLKTYIEEEQFAKGSMLPKIESAISFIENNpNGSVLITSLNQLDAALEGKIGTLITK 310
Cdd:PRK12352 244 HFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQG-GKEVIITTPECLPAALRGETGTHIIK 315
PRK12354 PRK12354
carbamate kinase; Reviewed
 3-310 1.18e-112

carbamate kinase; Reviewed


Pssm-ID: 183466  Cd Length: 307  Bit Score: 328.33  E-value: 1.18e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499   3 KIVVALGGNALGK-----SPQEQLELVKNTAKSLVGlITKGHEIVISHGNGPQVGSinLGLNyAAEHDQGPAFPFAECGA 77
Cdd:PRK12354   2 RIVVALGGNALLRrgeplTAENQRANIRIAAEQIAK-IAREHELVIVHGNGPQVGL--LALQ-NAAYKDVTPYPLDVLGA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499  78 MSQAYIGYQLQESLQNELHsmgiDKQVVTLVTQVEVDEGDPAFNSPSKPIGLFYTKEEANRIQQEKGYQFVEDaGRGYRR 157
Cdd:PRK12354  78 ETEGMIGYMLEQELGNLLP----ERPVATLLTQVEVDANDPAFANPTKPIGPVYDEAEAERLAAEKGWTIKPD-GDYFRR 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499 158 VVPSPQPISIIELESIKTLVENDTLVIAAGGGGIPVIREQHDSFKGIDAVIDKDKTSALLGADIHCDQLIILTAIDYVYI 237
Cdd:PRK12354 153 VVPSPRPKRIVEIRPIRWLLEKGHLVICAGGGGIPVVYDADGKLHGVEAVIDKDLAAALLAEQLDADLLLILTDVDAVYL 232

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487748499 238 NYHTDQQQALKTTNIDTLKTYieeeQFAKGSMLPKIESAISFIEnNPNGSVLITSLNQLDAALEGKIGTLITK 310
Cdd:PRK12354 233 DWGKPTQRAIAQATPDELREL----GFAAGSMGPKVEAACEFVR-ATGKIAGIGSLEDIQAILAGEAGTRISP 300
PRK09411 PRK09411
carbamate kinase; Reviewed
 1-310 3.72e-65

carbamate kinase; Reviewed


Pssm-ID: 181831  Cd Length: 297  Bit Score: 206.96  E-value: 3.72e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499   1 MAKIVVALGGNALGK-----SPQEQLELVKNTAKSLVGLiTKGHEIVISHGNGPQVGSinLGLNYAAEHDQgPAFPFAEC 75
Cdd:PRK09411   1 MKTLVVALGGNALLQrgealTAENQYRNIASAVPALARL-ARSYRLAIVHGNGPQVGL--LALQNLAWKEV-EPYPLDVL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499  76 GAMSQAYIGYQLQESLQNELHSmgidKQVVTLVTQVEVDEGDPAFNSPSKPIGLFYTKEEANRIQQEKGYQFVEDaGRGY 155
Cdd:PRK09411  77 VAESQGMIGYMLAQSLSAQPQM----PPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAYGWQMKRD-GKYL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499 156 RRVVPSPQPISIIELESIKTLVENDTLVIAAGGGGIPVIreqhDSFKGIDAVIDKDKTSALLGADIHCDQLIILTAIDYV 235
Cdd:PRK09411 152 RRVVASPQPRKILDSEAIELLLKEGHVVICSGGGGVPVT----EDGAGSEAVIDKDLAAALLAEQINADGLVILTDADAV 227

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487748499 236 YINYHTDQQQALKTTNIDTLKTYIEeeqfAKGSMLPKIESAISFIENNPNgSVLITSLNQLDAALEGKIGTLITK 310
Cdd:PRK09411 228 YENWGTPQQRAIRHATPDELAPFAK----ADGAMGPKVTAVSGYVRSRGK-PAWIGALSRIEETLAGEAGTCISL 297
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 3-292 4.22e-16

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: 75.87  E-value: 4.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499    3 KIVVALGGNALGKSpqeqlELVKNTAKSLVGLITKGHEIVISHGNGPQVGSINLGLNYAAEHDQGPAFPFAECGAMSQAY 82
Cdd:pfam00696   2 RVVIKLGGSSLTDK-----ERLKRLADEIAALLEEGRKLVVVHGGGAFADGLLALLGLSPRFARLTDAETLEVATMDALG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499   83 IgyqlqeslQNELHSMGIdkqvvtlvtqveVDEGDPAFNSPSKPIGLfytkeeanriqqekgyqfvedagrgyRRVVPSP 162
Cdd:pfam00696  77 S--------LGERLNAAL------------LAAGLPAVGLPAAQLLA--------------------------TEAGFID 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499  163 QPISIIELESIKTLVENDTLVIAAGGGGIPVireqhdsfKGIDAVIDKDKTSALLGADIHCDQLIILTAIDYVYINYHTD 242
Cdd:pfam00696 111 DVVTRIDTEALEELLEAGVVPVITGFIGIDP--------EGELGRGSSDTLAALLAEALGADKLIILTDVDGVYTADPRK 182

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 487748499  243 QQQA--LKTTNIDTLKTYIeEEQFAKGSMLPKIESAISFIENNpNGSVLITS 292
Cdd:pfam00696 183 VPDAklIPEISYDELLELL-ASGLATGGMKVKLPAALEAARRG-GIPVVIVN 232
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 5-308 8.19e-16

Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like N-acetylglutamate kinase (NAGK), carbamate kinase (CK), aspartokinase (AK), glutamate-5-kinase (G5K) and UMP kinase (UMPK). The AAK superfamily includes kinases that phosphorylate a variety of amino acid substrates. These kinases catalyze the formation of phosphoric anhydrides, generally with a carboxylate, and use ATP as the source of the phosphoryl group; are involved in amino acid biosynthesis. Some of these kinases control the process via allosteric feed-back inhibition.


Pssm-ID: 239033 [Multi-domain]  Cd Length: 248  Bit Score: 75.56  E-value: 8.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499   5 VVALGGNALgkspqEQLELVKNTAKSLVGLITKGHEIVISHGNGPQVGS----INLGLNYAAeHDQGPAFPFAECGAMSQ 80
Cdd:cd02115    1 VIKFGGSSV-----SSEERLRNLARILVKLASEGGRVVVVHGAGPQITDellaHGELLGYAR-GLRITDRETDALAAMGE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499  81 AYIGYQLQESLQNElhsmGIDKQVVTLvtqvevdegdpafnspskpiglfytkeeanriqqeKGYQFVEDAGRGYRRVVP 160
Cdd:cd02115   75 GMSNLLIAAALEQH----GIKAVPLDL-----------------------------------TQAGFASPNQGHVGKITK 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499 161 spqpisiIELESIKTLVENDTLVIAAGGGGIPVIREqhdsfkGIDAVIDKDKTSALLGADIHCDQLIILTAIDYVYINYH 240
Cdd:cd02115  116 -------VSTDRLKSLLENGILPILSGFGGTDEKET------GTLGRGGSDSTAALLAAALKADRLVILTDVDGVYTADP 182

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487748499 241 TDQQQALKttnIDTLKTYIEEEQFAKGSMLPKIESAISFIENNPngSVLITS---LNQLDAALEGKIGTLI 308
Cdd:cd02115  183 RKVPDAKL---LSELTYEEAAELAYAGAMVLKPKAADPAARAGI--PVRIANtenPGALALFTPDGGGTLI 248
AAK_NAGK-like cd04238
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ...
 4-308 1.03e-06

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: 49.05  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499   4 IVVALGGNALgkspqEQLELVKNTAKSLVGLITKGHEIVISHGNGPQVGSINLGLNYAAEHDQG------PAFPFAEcga 77
Cdd:cd04238    1 VVIKYGGSAM-----KDEELKEAFADDIVLLKQVGINPVIVHGGGPEINELLKRLGIESEFVNGlrvtdkETMEIVE--- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499  78 msQAYIGyQLQESLQNELHSMGIdkqvvtlvtqvevdegdpafnspsKPIGLfyTKEEANRIQQEKGYQFVEDAGRgyrr 157
Cdd:cd04238   73 --MVLAG-KVNKELVSLLNRAGG------------------------KAVGL--SGKDGGLIKAEKKEEKDIDLGF---- 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499 158 vVPSPQPISIielESIKTLVENdtlviaaggGGIPVIreqhdSFKGIDAV-----IDKDKTSALLGADIHCDQLIILTAI 232
Cdd:cd04238  120 -VGEVTEVNP---ELLETLLEA---------GYIPVI-----APIAVDEDgetynVNADTAAGAIAAALKAEKLILLTDV 181

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499 233 DYVYInyhtDQQQALKTTNIDTLKTYIEEEqFAKGSMLPKIESAISFIENNPNGSVLI--TSLNQLDAALEGK--IGTLI 308
Cdd:cd04238  182 PGVLD----DPGSLISELTPKEAEELIEDG-VISGGMIPKVEAALEALEGGVRKVHIIdgRVPHSLLLELFTDegIGTMI 256
AAK_NAGK-C cd04250
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ...
 173-290 6.78e-04

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: 40.57  E-value: 6.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499 173 IKTLVENDTL-VIAAGGGGipvirEQHDSFKgidavIDKDKTSALLGADIHCDQLIILTAIDYVYINYHtDQQQALKTTN 251
Cdd:cd04250  151 LETLLEAGYIpVIAPVGVG-----EDGETYN-----INADTAAGAIAAALKAEKLILLTDVAGVLDDPN-DPGSLISEIS 219

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 487748499 252 IDTLKTYIEEEQfAKGSMLPKIESAISFIENNPNGSVLI 290
Cdd:cd04250  220 LKEAEELIADGI-ISGGMIPKVEACIEALEGGVKAAHII 257
AAK_P5CS_ProBA cd04256
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ...
 191-309 7.08e-04

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: 40.49  E-value: 7.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499 191 IPVI---------REQHDSFKGIDAVIDKDKTSALLGADIHCDQLIILTAIDYVYINYHTDQQQALKTTNI--DTLK-TY 258
Cdd:cd04256  152 IPIIntndavsppPEPDEDLQGVISIKDNDSLAARLAVELKADLLILLSDVDGLYDGPPGSDDAKLIHTFYpgDQQSiTF 231

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 487748499 259 IEEEQFAKGSMLPKIESAISFIENNPngSVLITSLNQLDA---ALEG-KIGTLIT 309
Cdd:cd04256  232 GTKSRVGTGGMEAKVKAALWALQGGT--SVVITNGMAGDVitkILEGkKVGTFFT 284
PRK14058 PRK14058
[LysW]-aminoadipate/[LysW]-glutamate kinase;
187-310 4.81e-03

[LysW]-aminoadipate/[LysW]-glutamate kinase;


Pssm-ID: 237599 [Multi-domain]  Cd Length: 268  Bit Score: 37.96  E-value: 4.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748499 187 GGGGIPVIREQHDSFKGIDAVIDKDKTSALLGADIHCDQLIILTAIDYVYINYhTDQQQALKTTNIDTLKTYIEeeqFAK 266
Cdd:PRK14058 147 KAGYLPVVAPPALSEEGEPLNVDGDRAAAAIAGALKAEALVLLSDVPGLLRDP-PDEGSLIERITPEEAEELSK---AAG 222

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 487748499 267 GSMLPKIESAISFIENNPnGSVLITSLNQ---LDAALEGKiGTLITK 310
Cdd:PRK14058 223 GGMKKKVLMAAEAVEGGV-GRVIIADANVddpISAALAGE-GTVIVN 267
 
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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