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Conserved domains on  [gi|487748489|ref|WP_001830524|]
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carbamate kinase [Staphylococcus epidermidis]

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
 1-308 0e+00

putative amino acid kinase; Reviewed


:

Pssm-ID: 237071  Cd Length: 314  Bit Score: 515.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489   1 MSKIVVALGGNALGQSPKE---QLDLLKSTSKSLVSLIDKGYEIVISHGNGPQVGSINLGLNYAAEHKQ-GPPFPFPECG 76
Cdd:PRK12353   2 MKKIVVALGGNALGSTPEEataQLEAVKKTAKSLVDLIEEGHEVVITHGNGPQVGNILLAQEAAASEKNkVPAMPLDVCG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489  77 AMSQAYIGYQMQESLQNELHSMGIDKQVVTLVTQVQVASDDSAFNNPTKPIGLFYTKEQADKFTKEKGYTFVEDSGRGYR 156
Cdd:PRK12353  82 AMSQGYIGYHLQNALRNELLKRGIDKPVATVVTQVVVDANDPAFKNPTKPIGPFYTEEEAEKLAKEKGYTFKEDAGRGYR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 157 RVVPSPQPISIVELDSIETLITHGTLVIAAGGGGIPVIKENEVYTGVDAVIDKDKTSALLAAHLQSDQLIILTAVDHVYI 236
Cdd:PRK12353 162 RVVPSPKPVDIVEIEAIKTLVDAGQVVIAAGGGGIPVIREGGGLKGVEAVIDKDFASAKLAELVDADLLIILTAVDKVYI 241

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487748489 237 NYGKENQRGLDEVSVDEIKKHISDGQFAKGSMLPKVEAALQFLEKNTKGSVLITSLAGLGDALDGKIGTLIK 308
Cdd:PRK12353 242 NFGKPNQKKLDEVTVSEAEKYIEEGQFAPGSMLPKVEAAISFVESRPGRKAIITSLEKAKEALEGKAGTVIV 313
 
Name Accession Description Interval E-value
PRK12353 PRK12353
putative amino acid kinase; Reviewed
 1-308 0e+00

putative amino acid kinase; Reviewed


Pssm-ID: 237071  Cd Length: 314  Bit Score: 515.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489   1 MSKIVVALGGNALGQSPKE---QLDLLKSTSKSLVSLIDKGYEIVISHGNGPQVGSINLGLNYAAEHKQ-GPPFPFPECG 76
Cdd:PRK12353   2 MKKIVVALGGNALGSTPEEataQLEAVKKTAKSLVDLIEEGHEVVITHGNGPQVGNILLAQEAAASEKNkVPAMPLDVCG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489  77 AMSQAYIGYQMQESLQNELHSMGIDKQVVTLVTQVQVASDDSAFNNPTKPIGLFYTKEQADKFTKEKGYTFVEDSGRGYR 156
Cdd:PRK12353  82 AMSQGYIGYHLQNALRNELLKRGIDKPVATVVTQVVVDANDPAFKNPTKPIGPFYTEEEAEKLAKEKGYTFKEDAGRGYR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 157 RVVPSPQPISIVELDSIETLITHGTLVIAAGGGGIPVIKENEVYTGVDAVIDKDKTSALLAAHLQSDQLIILTAVDHVYI 236
Cdd:PRK12353 162 RVVPSPKPVDIVEIEAIKTLVDAGQVVIAAGGGGIPVIREGGGLKGVEAVIDKDFASAKLAELVDADLLIILTAVDKVYI 241

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487748489 237 NYGKENQRGLDEVSVDEIKKHISDGQFAKGSMLPKVEAALQFLEKNTKGSVLITSLAGLGDALDGKIGTLIK 308
Cdd:PRK12353 242 NFGKPNQKKLDEVTVSEAEKYIEEGQFAPGSMLPKVEAAISFVESRPGRKAIITSLEKAKEALEGKAGTVIV 313
ArcC COG0549
Carbamate kinase [Amino acid transport and metabolism];
1-307 1.69e-170

Carbamate kinase [Amino acid transport and metabolism];


Pssm-ID: 440315  Cd Length: 313  Bit Score: 474.95  E-value: 1.69e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489   1 MSKIVVALGGNALGQ-----SPKEQLDLLKSTSKSLVSLIDKGYEIVISHGNGPQVGSINLGLNYAaeHKQGPPFPFPEC 75
Cdd:COG0549    2 KKRIVVALGGNALLRrgepgTAEEQRENVREAAKALADLIEAGHEVVITHGNGPQVGLLLLQNEAA--KKKVPPMPLDVC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489  76 GAMSQAYIGYQMQESLQNELHSMGIDKQVvtlvtqvqvAS---------DDSAFNNPTKPIGLFYTKEQADKFTKEKGYT 146
Cdd:COG0549   80 GAMTQGMIGYMLQQALRNELPKRGIDKPV---------ATlvtqvevdpDDPAFQNPTKPIGPFYTEEEAEELAKEKGWT 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 147 FVEDSGRGYRRVVPSPQPISIVELDSIETLITHGTLVIAAGGGGIPVI-KENEVYTGVDAVIDKDKTSALLAAHLQSDQL 225
Cdd:COG0549  151 FKEDAGRGYRRVVPSPKPKRIVEIDAIKALLEAGVIVIAAGGGGIPVVrDEDGGLKGVEAVIDKDLASALLAEELDADLL 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 226 IILTAVDHVYINYGKENQRGLDEVSVDEIKKHISDGQFAKGSMLPKVEAALQFLEkNTKGSVLITSLAGLGDALDGKIGT 305
Cdd:COG0549  231 LILTDVDKVYINFGKPDQRALDEVTVAEAKKYIEEGHFAAGSMGPKVEAAIRFVE-ATGKRAIITSLEKAEEALAGKAGT 309


                 ..
gi 487748489 306 LI 307
Cdd:COG0549  310 RI 311
AAK_CK cd04235
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ...
 3-307 1.28e-163

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: 457.36  E-value: 1.28e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489   3 KIVVALGGNALGQ-----SPKEQLDLLKSTSKSLVSLIDKGYEIVISHGNGPQVGSINLGLNYAaeHKQGPPFPFPECGA 77
Cdd:cd04235    1 RIVVALGGNALLRrgepgTAEEQRENVKIAAKALADLIKNGHEVVITHGNGPQVGNLLLQNEAA--AEKVPAYPLDVCGA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489  78 MSQAYIGYQMQESLQNELHSMGIDKQVVTLVTQVQVASDDSAFNNPTKPIGLFYTKEQADKFTKEKGYTFVEDSGRGYRR 157
Cdd:cd04235   79 MSQGMIGYMLQQALDNELPKRGIDKPVVTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEKGWTFKEDAGRGYRR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 158 VVPSPQPISIVELDSIETLITHGTLVIAAGGGGIPVIKENEVYTGVDAVIDKDKTSALLAAHLQSDQLIILTAVDHVYIN 237
Cdd:cd04235  159 VVPSPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREGGGLKGVEAVIDKDLASALLAEEINADLLVILTDVDNVYIN 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 238 YGKENQRGLDEVSVDEIKKHISDGQFAKGSMLPKVEAALQFLEkNTKGSVLITSLAGLGDALDGKIGTLI 307
Cdd:cd04235  239 FGKPNQKALEQVTVEELEKYIEEGQFAPGSMGPKVEAAIRFVE-SGGKKAIITSLENAEAALEGKAGTVI 307
arcC TIGR00746
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes ...
 2-307 1.53e-121

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: 350.99  E-value: 1.53e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489    2 SKIVVALGGNALGQ-----SPKEQLDLLKSTSKSLVSLIDKGYEIVISHGNGPQVGsiNLGLNYAAEHKQGPPFPFPECG 76
Cdd:TIGR00746   1 KRVVVALGGNALLQrgekgSAEAQRDNVRQTAPQIAKLIKRGYELVITHGNGPQVG--NLLLQNQAADSEVPAMPLDVLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489   77 AMSQAYIGYQMQESLQNELHSMGIDKQVVTLVTQVQVASDDSAFNNPTKPIGLFYTKEQADKFTKEKGYTFVEDSGRGYR 156
Cdd:TIGR00746  79 AMSQGMIGYMLQQALNNELPKRGMEKPVATVLTQTIVDPKDPAFQNPTKPIGPFYTEEEAKRLAAEKGWIVKEDAGRGWR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489  157 RVVPSPQPISIVELDSIETLITHGTLVIAAGGGGIPVIKENEVYTGVDAVIDKDKTSALLAAHLQSDQLIILTAVDHVYI 236
Cdd:TIGR00746 159 RVVPSPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEGAELKGVEAVIDKDLASEKLAEEVNADILVILTDVDAVYI 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487748489  237 NYGKENQRGLDEVSVDEIKKHISDGQFAKGSMLPKVEAALQFLEKNTKGSVlITSLAGLGDALDGKIGTLI 307
Cdd:TIGR00746 239 NYGKPDEKALREVTVEELEDYYKAGHFAAGSMGPKVEAAIEFVESGGKRAI-ITSLENAVEALEGKAGTRV 308
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 3-291 1.76e-21

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: 90.89  E-value: 1.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489    3 KIVVALGGNALGQSpkeqlDLLKSTSKSLVSLIDKGYEIVISHGNGPQVGSINLGLNYAAEHKQGPPFPFPECGAMSQAY 82
Cdd:pfam00696   2 RVVIKLGGSSLTDK-----ERLKRLADEIAALLEEGRKLVVVHGGGAFADGLLALLGLSPRFARLTDAETLEVATMDALG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489   83 IgyqMQESLQNELHSMGIDkqvvtlvtqvqvasddsAFNNPTKPIGLFytkeQADKFTKekgytfvedsgrgyrrvvpsp 162
Cdd:pfam00696  77 S---LGERLNAALLAAGLP-----------------AVGLPAAQLLAT----EAGFIDD--------------------- 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489  163 qPISIVELDSIETLITHGTLVIAAGGGGIPVikenevyTGVDAVIDKDKTSALLAAHLQSDQLIILTAVDHVYINYGKEN 242
Cdd:pfam00696 112 -VVTRIDTEALEELLEAGVVPVITGFIGIDP-------EGELGRGSSDTLAALLAEALGADKLIILTDVDGVYTADPRKV 183

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 487748489  243 QRG--LDEVSVDEIKKHISDGqFAKGSMLPKVEAALQFLEKNtKGSVLITS 291
Cdd:pfam00696 184 PDAklIPEISYDELLELLASG-LATGGMKVKLPAALEAARRG-GIPVVIVN 232
 
Name Accession Description Interval E-value
PRK12353 PRK12353
putative amino acid kinase; Reviewed
 1-308 0e+00

putative amino acid kinase; Reviewed


Pssm-ID: 237071  Cd Length: 314  Bit Score: 515.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489   1 MSKIVVALGGNALGQSPKE---QLDLLKSTSKSLVSLIDKGYEIVISHGNGPQVGSINLGLNYAAEHKQ-GPPFPFPECG 76
Cdd:PRK12353   2 MKKIVVALGGNALGSTPEEataQLEAVKKTAKSLVDLIEEGHEVVITHGNGPQVGNILLAQEAAASEKNkVPAMPLDVCG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489  77 AMSQAYIGYQMQESLQNELHSMGIDKQVVTLVTQVQVASDDSAFNNPTKPIGLFYTKEQADKFTKEKGYTFVEDSGRGYR 156
Cdd:PRK12353  82 AMSQGYIGYHLQNALRNELLKRGIDKPVATVVTQVVVDANDPAFKNPTKPIGPFYTEEEAEKLAKEKGYTFKEDAGRGYR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 157 RVVPSPQPISIVELDSIETLITHGTLVIAAGGGGIPVIKENEVYTGVDAVIDKDKTSALLAAHLQSDQLIILTAVDHVYI 236
Cdd:PRK12353 162 RVVPSPKPVDIVEIEAIKTLVDAGQVVIAAGGGGIPVIREGGGLKGVEAVIDKDFASAKLAELVDADLLIILTAVDKVYI 241

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487748489 237 NYGKENQRGLDEVSVDEIKKHISDGQFAKGSMLPKVEAALQFLEKNTKGSVLITSLAGLGDALDGKIGTLIK 308
Cdd:PRK12353 242 NFGKPNQKKLDEVTVSEAEKYIEEGQFAPGSMLPKVEAAISFVESRPGRKAIITSLEKAKEALEGKAGTVIV 313
ArcC COG0549
Carbamate kinase [Amino acid transport and metabolism];
1-307 1.69e-170

Carbamate kinase [Amino acid transport and metabolism];


Pssm-ID: 440315  Cd Length: 313  Bit Score: 474.95  E-value: 1.69e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489   1 MSKIVVALGGNALGQ-----SPKEQLDLLKSTSKSLVSLIDKGYEIVISHGNGPQVGSINLGLNYAaeHKQGPPFPFPEC 75
Cdd:COG0549    2 KKRIVVALGGNALLRrgepgTAEEQRENVREAAKALADLIEAGHEVVITHGNGPQVGLLLLQNEAA--KKKVPPMPLDVC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489  76 GAMSQAYIGYQMQESLQNELHSMGIDKQVvtlvtqvqvAS---------DDSAFNNPTKPIGLFYTKEQADKFTKEKGYT 146
Cdd:COG0549   80 GAMTQGMIGYMLQQALRNELPKRGIDKPV---------ATlvtqvevdpDDPAFQNPTKPIGPFYTEEEAEELAKEKGWT 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 147 FVEDSGRGYRRVVPSPQPISIVELDSIETLITHGTLVIAAGGGGIPVI-KENEVYTGVDAVIDKDKTSALLAAHLQSDQL 225
Cdd:COG0549  151 FKEDAGRGYRRVVPSPKPKRIVEIDAIKALLEAGVIVIAAGGGGIPVVrDEDGGLKGVEAVIDKDLASALLAEELDADLL 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 226 IILTAVDHVYINYGKENQRGLDEVSVDEIKKHISDGQFAKGSMLPKVEAALQFLEkNTKGSVLITSLAGLGDALDGKIGT 305
Cdd:COG0549  231 LILTDVDKVYINFGKPDQRALDEVTVAEAKKYIEEGHFAAGSMGPKVEAAIRFVE-ATGKRAIITSLEKAEEALAGKAGT 309


                 ..
gi 487748489 306 LI 307
Cdd:COG0549  310 RI 311
AAK_CK cd04235
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ...
 3-307 1.28e-163

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: 457.36  E-value: 1.28e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489   3 KIVVALGGNALGQ-----SPKEQLDLLKSTSKSLVSLIDKGYEIVISHGNGPQVGSINLGLNYAaeHKQGPPFPFPECGA 77
Cdd:cd04235    1 RIVVALGGNALLRrgepgTAEEQRENVKIAAKALADLIKNGHEVVITHGNGPQVGNLLLQNEAA--AEKVPAYPLDVCGA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489  78 MSQAYIGYQMQESLQNELHSMGIDKQVVTLVTQVQVASDDSAFNNPTKPIGLFYTKEQADKFTKEKGYTFVEDSGRGYRR 157
Cdd:cd04235   79 MSQGMIGYMLQQALDNELPKRGIDKPVVTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEKGWTFKEDAGRGYRR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 158 VVPSPQPISIVELDSIETLITHGTLVIAAGGGGIPVIKENEVYTGVDAVIDKDKTSALLAAHLQSDQLIILTAVDHVYIN 237
Cdd:cd04235  159 VVPSPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREGGGLKGVEAVIDKDLASALLAEEINADLLVILTDVDNVYIN 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 238 YGKENQRGLDEVSVDEIKKHISDGQFAKGSMLPKVEAALQFLEkNTKGSVLITSLAGLGDALDGKIGTLI 307
Cdd:cd04235  239 FGKPNQKALEQVTVEELEKYIEEGQFAPGSMGPKVEAAIRFVE-SGGKKAIITSLENAEAALEGKAGTVI 307
PRK12686 PRK12686
carbamate kinase; Reviewed
 1-307 7.19e-142

carbamate kinase; Reviewed


Pssm-ID: 183683  Cd Length: 312  Bit Score: 402.50  E-value: 7.19e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489   1 MSKIVVALGGNALGQ---SPKEQLDLLKSTSKSLVSLIDKGYEIVISHGNGPQVGSINLGLNYAAEHKQgPPFPFPECGA 77
Cdd:PRK12686   2 KEKIVIALGGNAILQteaTAEAQQTAVREAAQHLVDLIEAGHDIVITHGNGPQVGNLLLQQAESNSNKV-PAMPLDTCVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489  78 MSQAYIGYQMQESLQNELHSMGIDKQVVTLVTQVQVASDDSAFNNPTKPIGLFYTKEQADKFTKEKGYTFVEDSGRGYRR 157
Cdd:PRK12686  81 MSQGMIGYWLQNALNNELTERGIDKPVITLVTQVEVDKDDPAFANPTKPIGPFYTEEEAKQQAEQPGSTFKEDAGRGYRR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 158 VVPSPQPISIVELDSIETLITHGTLVIAAGGGGIPVIKENEVYTGVDAVIDKDKTSALLAAHLQSDQLIILTAVDHVYIN 237
Cdd:PRK12686 161 VVPSPKPQEIIEHDTIRTLVDGGNIVIACGGGGIPVIRDDNTLKGVEAVIDKDFASEKLAEQIDADLLIILTGVENVFIN 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 238 YGKENQRGLDEVSVDEIKKHISDGQFAKGSMLPKVEAALQFLEKNTKGSVLITSLAGLGDALDGKIGTLI 307
Cdd:PRK12686 241 FNKPNQQKLDDITVAEAKQYIAEGQFAPGSMLPKVEAAIDFVESGEGKKAIITSLEQAKEALAGNAGTHI 310
PRK12454 PRK12454
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
 1-307 4.25e-133

carbamate kinase-like carbamoyl phosphate synthetase; Reviewed


Pssm-ID: 183535  Cd Length: 313  Bit Score: 380.11  E-value: 4.25e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489   1 MSKIVVALGGNAL---GQSP--KEQLDLLKSTSKSLVSLIDKGYEIVISHGNGPQVGSINLGLNyAAEHKQGPPFPFPEC 75
Cdd:PRK12454   2 KKRIVIALGGNALlqpGEKGtaENQMKNVRKTAKQIADLIEEGYEVVITHGNGPQVGNLLLQMD-AAKDVGIPPFPLDVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489  76 GAMSQAYIGYQMQESLQNELHSMGIDKQVVTLVTQVQVASDDSAFNNPTKPIGLFYTKEQADKFTKEKGYTFVEDSGRGY 155
Cdd:PRK12454  81 GAMTQGWIGYMIQQALRNELAKRGIEKQVATIVTQVIVDKNDPAFQNPTKPVGPFYDEEEAKKLAKEKGWIVKEDAGRGW 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 156 RRVVPSPQPISIVELDSIETLITHGTLVIAAGGGGIPVIKENEVYTGVDAVIDKDKTSALLAAHLQSDQLIILTAVDHVY 235
Cdd:PRK12454 161 RRVVPSPDPLGIVEIEVIKALVENGFIVIASGGGGIPVIEEDGELKGVEAVIDKDLASELLAEELNADIFIILTDVEKVY 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487748489 236 INYGKENQRGLDEVSVDEIKKHISDGQFAKGSMLPKVEAALQFLEkNTKGSVLITSLAGLGDALDGKIGTLI 307
Cdd:PRK12454 241 LNYGKPDQKPLDKVTVEEAKKYYEEGHFKAGSMGPKILAAIRFVE-NGGKRAIIASLEKAVEALEGKTGTRI 311
arcC TIGR00746
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes ...
 2-307 1.53e-121

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: 350.99  E-value: 1.53e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489    2 SKIVVALGGNALGQ-----SPKEQLDLLKSTSKSLVSLIDKGYEIVISHGNGPQVGsiNLGLNYAAEHKQGPPFPFPECG 76
Cdd:TIGR00746   1 KRVVVALGGNALLQrgekgSAEAQRDNVRQTAPQIAKLIKRGYELVITHGNGPQVG--NLLLQNQAADSEVPAMPLDVLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489   77 AMSQAYIGYQMQESLQNELHSMGIDKQVVTLVTQVQVASDDSAFNNPTKPIGLFYTKEQADKFTKEKGYTFVEDSGRGYR 156
Cdd:TIGR00746  79 AMSQGMIGYMLQQALNNELPKRGMEKPVATVLTQTIVDPKDPAFQNPTKPIGPFYTEEEAKRLAAEKGWIVKEDAGRGWR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489  157 RVVPSPQPISIVELDSIETLITHGTLVIAAGGGGIPVIKENEVYTGVDAVIDKDKTSALLAAHLQSDQLIILTAVDHVYI 236
Cdd:TIGR00746 159 RVVPSPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEGAELKGVEAVIDKDLASEKLAEEVNADILVILTDVDAVYI 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487748489  237 NYGKENQRGLDEVSVDEIKKHISDGQFAKGSMLPKVEAALQFLEKNTKGSVlITSLAGLGDALDGKIGTLI 307
Cdd:TIGR00746 239 NYGKPDEKALREVTVEELEDYYKAGHFAAGSMGPKVEAAIEFVESGGKRAI-ITSLENAVEALEGKAGTRV 308
PRK12352 PRK12352
putative carbamate kinase; Reviewed
 1-309 1.46e-109

putative carbamate kinase; Reviewed


Pssm-ID: 183464  Cd Length: 316  Bit Score: 320.59  E-value: 1.46e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489   1 MSK-IVVALGGNAL-----GQSPKEQLDLLKSTSKSLVSLIDKGYEIVISHGNGPQVGSINLGLNYAAEHKQGPPFPFPE 74
Cdd:PRK12352   1 MKElVVVAIGGNSIikdnaSQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHEREGLPLTPLAN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489  75 CGAMSQAYIGYQMQESLQNELHSMGiDKQVVTLVTQVQVASDDSAFNNPTKPIGLFYTKEQADKFTKE-KGYTFVEDSGR 153
Cdd:PRK12352  81 CVADTQGGIGYLIQQALNNRLARHG-EKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDELQKAnPDWRFVEDAGR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 154 GYRRVVPSPQPISIVELDSIETLITHGTLVIAAGGGGIPVIKENE-VYTGVDAVIDKDKTSALLAAHLQSDQLIILTAVD 232
Cdd:PRK12352 160 GYRRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDAgDYQSVDAVIDKDLSTALLAREIHADILVITTGVE 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487748489 233 HVYINYGKENQRGLDEVSVDEIKKHISDGQFAKGSMLPKVEAALQFLEKNTKgSVLITSLAGLGDALDGKIGTLIKN 309
Cdd:PRK12352 240 KVCIHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQGGK-EVIITTPECLPAALRGETGTHIIK 315
PRK12354 PRK12354
carbamate kinase; Reviewed
 3-307 2.22e-103

carbamate kinase; Reviewed


Pssm-ID: 183466  Cd Length: 307  Bit Score: 304.45  E-value: 2.22e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489   3 KIVVALGGNAL---GQSPKE--QLDLLKSTSKSLVSlIDKGYEIVISHGNGPQVGSinLGLNyAAEHKQGPPFPFPECGA 77
Cdd:PRK12354   2 RIVVALGGNALlrrGEPLTAenQRANIRIAAEQIAK-IAREHELVIVHGNGPQVGL--LALQ-NAAYKDVTPYPLDVLGA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489  78 MSQAYIGYQMQESLQNELHSMGI---------DKqvvtlvtqvqvasDDSAFNNPTKPIGLFYTKEQADKFTKEKGYTFV 148
Cdd:PRK12354  78 ETEGMIGYMLEQELGNLLPERPVatlltqvevDA-------------NDPAFANPTKPIGPVYDEAEAERLAAEKGWTIK 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 149 EDsGRGYRRVVPSPQPISIVELDSIETLITHGTLVIAAGGGGIPVIKENE-VYTGVDAVIDKDKTSALLAAHLQSDQLII 227
Cdd:PRK12354 145 PD-GDYFRRVVPSPRPKRIVEIRPIRWLLEKGHLVICAGGGGIPVVYDADgKLHGVEAVIDKDLAAALLAEQLDADLLLI 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 228 LTAVDHVYINYGKENQRGLDEVSVDEIKKHisdgQFAKGSMLPKVEAALQFLEkNTKGSVLITSLAGLGDALDGKIGTLI 307
Cdd:PRK12354 224 LTDVDAVYLDWGKPTQRAIAQATPDELREL----GFAAGSMGPKVEAACEFVR-ATGKIAGIGSLEDIQAILAGEAGTRI 298
PRK09411 PRK09411
carbamate kinase; Reviewed
 1-308 2.01e-66

carbamate kinase; Reviewed


Pssm-ID: 181831  Cd Length: 297  Bit Score: 210.04  E-value: 2.01e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489   1 MSKIVVALGGNALGQ-----SPKEQLDLLKSTSKSLVSLIDKgYEIVISHGNGPQVGSinLGLNYAAeHKQGPPFPFPEC 75
Cdd:PRK09411   1 MKTLVVALGGNALLQrgealTAENQYRNIASAVPALARLARS-YRLAIVHGNGPQVGL--LALQNLA-WKEVEPYPLDVL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489  76 GAMSQAYIGYQMQESLQNELHSMGIdkqvVTLVTQVQVASDDSAFNNPTKPIGLFYTKEQADKFTKEKGYTFVEDsGRGY 155
Cdd:PRK09411  77 VAESQGMIGYMLAQSLSAQPQMPPV----TTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAYGWQMKRD-GKYL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 156 RRVVPSPQPISIVELDSIETLITHGTLVIAAGGGGIPVIKENEvytGVDAVIDKDKTSALLAAHLQSDQLIILTAVDHVY 235
Cdd:PRK09411 152 RRVVASPQPRKILDSEAIELLLKEGHVVICSGGGGVPVTEDGA---GSEAVIDKDLAAALLAEQINADGLVILTDADAVY 228

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487748489 236 INYGKENQRGLDEVSVDEIkkhisdGQFAK--GSMLPKVEAALQFLeKNTKGSVLITSLAGLGDALDGKIGTLIK 308
Cdd:PRK09411 229 ENWGTPQQRAIRHATPDEL------APFAKadGAMGPKVTAVSGYV-RSRGKPAWIGALSRIEETLAGEAGTCIS 296
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 3-291 1.76e-21

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: 90.89  E-value: 1.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489    3 KIVVALGGNALGQSpkeqlDLLKSTSKSLVSLIDKGYEIVISHGNGPQVGSINLGLNYAAEHKQGPPFPFPECGAMSQAY 82
Cdd:pfam00696   2 RVVIKLGGSSLTDK-----ERLKRLADEIAALLEEGRKLVVVHGGGAFADGLLALLGLSPRFARLTDAETLEVATMDALG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489   83 IgyqMQESLQNELHSMGIDkqvvtlvtqvqvasddsAFNNPTKPIGLFytkeQADKFTKekgytfvedsgrgyrrvvpsp 162
Cdd:pfam00696  77 S---LGERLNAALLAAGLP-----------------AVGLPAAQLLAT----EAGFIDD--------------------- 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489  163 qPISIVELDSIETLITHGTLVIAAGGGGIPVikenevyTGVDAVIDKDKTSALLAAHLQSDQLIILTAVDHVYINYGKEN 242
Cdd:pfam00696 112 -VVTRIDTEALEELLEAGVVPVITGFIGIDP-------EGELGRGSSDTLAALLAEALGADKLIILTDVDGVYTADPRKV 183

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 487748489  243 QRG--LDEVSVDEIKKHISDGqFAKGSMLPKVEAALQFLEKNtKGSVLITS 291
Cdd:pfam00696 184 PDAklIPEISYDELLELLASG-LATGGMKVKLPAALEAARRG-GIPVVIVN 232
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 5-307 5.53e-17

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: 78.64  E-value: 5.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489   5 VVALGGNALgqspkEQLDLLKSTSKSLVSLIDKGYEIVISHGNGPQVGSINLGLNYAAEHKQGPPFPFPE---CGAMSQA 81
Cdd:cd02115    1 VIKFGGSSV-----SSEERLRNLARILVKLASEGGRVVVVHGAGPQITDELLAHGELLGYARGLRITDREtdaLAAMGEG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489  82 YIGYQMQESLQNELHSMGidkqvvtlvtqvqvasddsafnnptkpiglFYTKEQADkftkekgytFVEDSGRGYRRVVPs 161
Cdd:cd02115   76 MSNLLIAAALEQHGIKAV------------------------------PLDLTQAG---------FASPNQGHVGKITK- 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 162 pqpisiVELDSIETLITHGTLVIAAGGGGIPVIKENEVYtgvdaVIDKDKTSALLAAHLQSDQLIILTAVDHVYINYGKE 241
Cdd:cd02115  116 ------VSTDRLKSLLENGILPILSGFGGTDEKETGTLG-----RGGSDSTAALLAAALKADRLVILTDVDGVYTADPRK 184

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487748489 242 NQRG--LDEVSVDEIKKHIsdgqfAKGSMLPKVEAALQFLEKNTKGSVLITSLAGLGDALDGKI-GTLI 307
Cdd:cd02115  185 VPDAklLSELTYEEAAELA-----YAGAMVLKPKAADPAARAGIPVRIANTENPGALALFTPDGgGTLI 248
AAK_NAGK-like cd04238
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ...
 4-307 8.02e-11

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: 61.37  E-value: 8.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489   4 IVVALGGNALgqspkEQLDLLKSTSKSLVSLIDKGYEIVISHGNGPQVGSINLGLNYAAEHKQGPPFPFPEC-GAMSQAY 82
Cdd:cd04238    1 VVIKYGGSAM-----KDEELKEAFADDIVLLKQVGINPVIVHGGGPEINELLKRLGIESEFVNGLRVTDKETmEIVEMVL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489  83 IGyQMQESLQNELHSMGIdkqvvtlvtqvqvasddsafnnptKPIGLfyTKEQADKFTKEKGYTFVEDSGRgyrrvVPSP 162
Cdd:cd04238   76 AG-KVNKELVSLLNRAGG------------------------KAVGL--SGKDGGLIKAEKKEEKDIDLGF-----VGEV 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 163 QPISIvelDSIETLIthgtlviaaGGGGIPVI------KENEVYTgvdavIDKDKTSALLAAHLQSDQLIILTAVDHVYI 236
Cdd:cd04238  124 TEVNP---ELLETLL---------EAGYIPVIapiavdEDGETYN-----VNADTAAGAIAAALKAEKLILLTDVPGVLD 186

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487748489 237 NYGKenqrGLDEVSVDEIKKHISDGqFAKGSMLPKVEAALQFLEKNTKGSVLIT-----SLAGLGDALDGkIGTLI 307
Cdd:cd04238  187 DPGS----LISELTPKEAEELIEDG-VISGGMIPKVEAALEALEGGVRKVHIIDgrvphSLLLELFTDEG-IGTMI 256
AAK_NAGK-C cd04250
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ...
 173-289 1.65e-09

AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in some bacteria and photosynthetic organisms using the non-acetylated, cyclic route of ornithine biosynthesis. In this pathway, glutamate is first N-acetylated and then phosphorylated by NAGK to give phosphoryl NAG, which is converted to NAG-ornithine. There are two variants of this pathway. In one, typified by the pathway in Thermotoga maritima and Pseudomonas aeruginosa, the acetyl group is recycled by reversible transacetylation from acetylornithine to glutamate. The phosphorylation of NAG by NAGK is feedback inhibited by arginine. In photosynthetic organisms, NAGK is the target of the nitrogen-signaling protein PII. Hexameric formation of NAGK domains appears to be essential to both arginine inhibition and NAGK-PII complex formation. NAGK-C are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239783 [Multi-domain]  Cd Length: 279  Bit Score: 57.52  E-value: 1.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 173 IETLITHGTlviaaggggIPVI------KENEVYTgvdavIDKDKTSALLAAHLQSDQLIILTAVDHVYINYGKENQRgL 246
Cdd:cd04250  151 LETLLEAGY---------IPVIapvgvgEDGETYN-----INADTAAGAIAAALKAEKLILLTDVAGVLDDPNDPGSL-I 215

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 487748489 247 DEVSVDEIKKHISDGQfAKGSMLPKVEAALQFLEKNTKGSVLI 289
Cdd:cd04250  216 SEISLKEAEELIADGI-ISGGMIPKVEACIEALEGGVKAAHII 257
AAK_G5K_ProB cd04242
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ...
 173-307 3.82e-08

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: 53.22  E-value: 3.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 173 IETLITHGTlviaaggggIPVIKENevytgvDAV-------IDKDKTSALLAAHLQSDQLIILTAVDHVY-----INygk 240
Cdd:cd04242  116 LETLLELGV---------IPIINEN------DTVateeirfGDNDRLSALVAGLVNADLLILLSDVDGLYdknprEN--- 177

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487748489 241 ENQRGLDEVSV--DEIKKHISDGQ--FAKGSMLPKVEAALQFLEKNTKgsVLITS---LAGLGDALDGK-IGTLI 307
Cdd:cd04242  178 PDAKLIPEVEEitDEIEAMAGGSGssVGTGGMRTKLKAARIATEAGIP--VVIANgrkPDVLLDILAGEaVGTLF 250
PRK00942 PRK00942
acetylglutamate kinase; Provisional
 1-291 1.97e-07

acetylglutamate kinase; Provisional


Pssm-ID: 234869 [Multi-domain]  Cd Length: 283  Bit Score: 51.26  E-value: 1.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489   1 MSKIVVALGGNALGQSpkeqlDLLKSTSKSLVSLIDKGYEIVISHGNGPQVGSINLGLNYAAEHKQG----PPfpfpecG 76
Cdd:PRK00942  23 GKTIVIKYGGNAMTDE-----ELKEAFARDIVLLKQVGINPVVVHGGGPQIDELLKKLGIESEFVNGlrvtDA------E 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489  77 AM---SQAYIGyQMQESLQNELHSMGIdkqvvtlvtqvqvasddsafnnptKPIGLfYTKE----QADKFTKEKGYTFVE 149
Cdd:PRK00942  92 TMevvEMVLAG-KVNKELVSLINKHGG------------------------KAVGL-SGKDggliTAKKLEEDEDLGFVG 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 150 DsgrgyrrvvpspqpISIVELDSIETLITHGTlviaaggggIPVI------KENEVYtgvdaVIDKDKTSALLAAHLQSD 223
Cdd:PRK00942 146 E--------------VTPVNPALLEALLEAGY---------IPVIspigvgEDGETY-----NINADTAAGAIAAALGAE 197

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487748489 224 QLIILTAVDHVYINYGKEnqrgLDEVSVDEIKKHISDGQFAKGsMLPKVEAALQFLEkNTKGSVLITS 291
Cdd:PRK00942 198 KLILLTDVPGVLDDKGQL----ISELTASEAEELIEDGVITGG-MIPKVEAALDAAR-GGVRSVHIID 259
AAK_P5CS_ProBA cd04256
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ...
 191-306 4.08e-07

AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta 1-pyrroline-5-carboxylate synthetase (P5CS), composed of an N-terminal G5K (ProB) and a C-terminal glutamyl 5- phosphate reductase (G5PR, ProA), the first and second enzyme catalyzing proline (and, in mammals, ornithine) biosynthesis. G5K transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, and is subject to feedback allosteric inhibition by proline or ornithine. In plants, proline plays an important role as an osmoprotectant and, in mammals, ornithine biosynthesis is crucial for proper ammonia detoxification, since a G5K mutation has been shown to cause human hyperammonaemia.


Pssm-ID: 239789 [Multi-domain]  Cd Length: 284  Bit Score: 50.51  E-value: 4.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 191 IPVIKENEVY----------TGVDAVIDKDKTSALLAAHLQSDQLIILTAVDHVYINY-GKENQRGLDEVsvdeIKKHIS 259
Cdd:cd04256  152 IPIINTNDAVspppepdedlQGVISIKDNDSLAARLAVELKADLLILLSDVDGLYDGPpGSDDAKLIHTF----YPGDQQ 227

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 487748489 260 DGQFAK------GSMLPKVEAALQFLEKNTkgSVLITS-LAG--LGDALDG-KIGTL 306
Cdd:cd04256  228 SITFGTksrvgtGGMEAKVKAALWALQGGT--SVVITNgMAGdvITKILEGkKVGTF 282
ArgB COG0548
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ...
 216-289 6.18e-06

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: 46.95  E-value: 6.18e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487748489 216 LAAHLQSDQLIILTAVDHVYinyGKENQRgLDEVSVDEIKKHISDGQFAKGsMLPKVEAALQFLEKNTKGSVLI 289
Cdd:COG0548  192 IAAALKAEKLILLTDVPGVL---DDPGSL-ISELTAAEAEELIADGVISGG-MIPKLEAALDAVRGGVKRVHII 260
PLN02512 PLN02512
acetylglutamate kinase
 189-289 9.93e-06

acetylglutamate kinase


Pssm-ID: 178128  Cd Length: 309  Bit Score: 46.22  E-value: 9.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 189 GGIPVIKENEV-YTGVDAVIDKDKTSALLAAHLQSDQLIILTAVDHVYINYGKENQRgLDEVSVDEIKKHISDGQFAkGS 267
Cdd:PLN02512 186 GHIPVIATVAAdEDGQAYNINADTAAGEIAAALGAEKLILLTDVAGVLEDKDDPGSL-VKELDIKGVRKLIADGKIA-GG 263

                         90       100
                 ....*....|....*....|..
gi 487748489 268 MLPKVEAALQFLEKNTKGSVLI 289
Cdd:PLN02512 264 MIPKVECCVRSLAQGVKTAHII 285
AAK_UMPK-like cd04239
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ...
 159-235 7.27e-05

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: 43.29  E-value: 7.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 159 VPSPQPI-SIVELDSIETLITH---GTLVIAAGGGGIPvikenevYTGVDAVidkdktSALLAAHLQSDQLIILTAVDHV 234
Cdd:cd04239   93 VMSAIPMqGVAEPYIRRRAIRHlekGRIVIFGGGTGNP-------GFTTDTA------AALRAEEIGADVLLKATNVDGV 159


                 .
gi 487748489 235 Y 235
Cdd:cd04239  160 Y 160
AAK_UMPK-PyrH-Pf cd04253
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ...
 165-307 1.49e-04

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


Pssm-ID: 239786 [Multi-domain]  Cd Length: 221  Bit Score: 42.24  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 165 ISIVELDSIETLIT--HGTLVIAAGGGGIPVIKEN-------------EVYTGVDAVIDKDKTSALLAAHLQSDQLIILT 229
Cdd:cd04253   58 ASEAFLDEIGIMATrlNARLLIAALGDAYPPVPTSyeealeamftgkiVVMGGTEPGQSTDAVAALLAERLGADLLINAT 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 230 AVDHVYINYGKE--NQRGLDEVSVDEIKKHISDGQFAKGSMLPKVEAALQFLEKNtKGSVLI---TSLAGLGDALDGK-I 303
Cdd:cd04253  138 NVDGVYSKDPRKdpDAKKFDRLSADELIDIVGKSSWKAGSNEPFDPLAAKIIERS-GIKTIVvdgRDPENLERALKGEfV 216


                 ....
gi 487748489 304 GTLI 307
Cdd:cd04253  217 GTII 220
AAK_NAGK-UC cd04251
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ...
 168-307 7.31e-04

AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar to Escherichia coli and Pseudomonas aeruginosa NAGKs which catalyze the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis. These uncharacterized domain sequences are found in some bacteria (Deinococci and Chloroflexi) and archea and belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239784 [Multi-domain]  Cd Length: 257  Bit Score: 40.43  E-value: 7.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489 168 VELDSIETLITHGTLVIAAggggiPV-IKENEVYTGVDAvidkDKTSALLAAHLQSDQLIILTAVDHVYInygkeNQRGL 246
Cdd:cd04251  133 VNSDLIEALLDAGYLPVVS-----PVaYSEEGEPLNVDG----DRAAAAIAAALKAERLILLTDVEGLYL-----DGRVI 198

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487748489 247 DEVSVDEIKKHIsdgQFAKGSMLPKVEAALQFLEKNTKGSVLITSLAG--LGDALDGKiGTLI 307
Cdd:cd04251  199 ERITVSDAESLL---EKAGGGMKRKLLAAAEAVEGGVREVVIGDARADspISSALNGG-GTVI 257
P5CS TIGR01092
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ...
 191-306 5.02e-03

delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, EC 2.7.2.11) region followed by a gamma-glutamyl phosphate reductase (ProA, EC 1.2.1.41) region. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 130164 [Multi-domain]  Cd Length: 715  Bit Score: 38.35  E-value: 5.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487748489  191 IPVIKENEV-------YTGVDAVI-DKDKTSALLAAHLQSDQLIILTAVDHVYINYGKENQRGLDEVSVDEikKHISDGQ 262
Cdd:TIGR01092 143 VPVVNENDAvstraapYSDSQGIFwDNDSLAALLALELKADLLILLSDVEGLYDGPPSDDDSKLIDTFYKE--KHQGEIT 220

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 487748489  263 F------AKGSMLPKVEAALQFLEKNTkgSVLITS---LAGLGDALDG-KIGTL 306
Cdd:TIGR01092 221 FgtksrlGRGGMTAKVKAAVWAAYGGT--PVIIASgtaPKNITKVVEGkKVGTL 272
AAK_UC cd04240
AAK_UC: Uncharacterized (UC) amino acid kinase-like proteins found mainly in archaea and a few ...
 210-240 6.52e-03

AAK_UC: Uncharacterized (UC) amino acid kinase-like proteins found mainly in archaea and a few bacteria. Sequences in this CD are members of the Amino Acid Kinase (AAK) superfamily.


Pssm-ID: 239773 [Multi-domain]  Cd Length: 203  Bit Score: 36.96  E-value: 6.52e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 487748489 210 DKTSALLAAHLQSDQLIILTAVDHVYINYGK 240
Cdd:cd04240  117 DSIAAWLAKKLGAKRLVIVTDVDGIYEKDGK 147
 
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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