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Conserved domains on  [gi|920779292|gb|ALA37548|]
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uridylate kinase [Mycoplasmoides pneumoniae]

Protein Classification

amino acid kinase family protein( domain architecture ID 663)

amino acid kinase (AAK) family protein catalyzes the phosphorylation of a variety of substrates including amino acids, using ATP as the source of the phosphoryl group

CATH:  3.40.1160.10
EC:  2.7.-.-
Gene Ontology:  GO:0005524|GO:0016310|GO:0016301
PubMed:  12005432
SCOP:  3001310

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAK super family cl00452
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 4-234 4.22e-85

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.


The actual alignment was detected with superfamily member TIGR02075:

Pssm-ID: 444912 [Multi-domain]  Cd Length: 232  Bit Score: 252.55  E-value: 4.22e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292    4 KILIKLSGAGMSADSSEPFSNQFLETVIAQLKQLVPN-YQIGIVIGGGNIMRGKSCSDYNITEIAGHHLGIMATVINGAF 82
Cdd:TIGR02075   3 RVLLKLSGEALAGESQFGIDPDRLNRIANEIKELVKMgIEVGIVIGGGNIFRGVSAAELGIDRVSADYMGMLATVINGLA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292   83 LKAKFDSHKLNSTLLSAVSCPSLAtHIVSQATIDDAFKNHDIVIFAGGTGNPYFSTDTAVALRATQMQADIILIGKNgVD 162
Cdd:TIGR02075  83 LRDALEKLGLKTRVLSAISMPQIC-ESYIRRKAIKHLEKGKVVIFSGGTGNPFFTTDTAAALRAIEINADVILKGTN-VD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 920779292  163 GVYTADPKKDKHAKFLASLTYAEAIKNDLQIMDITAFTMCKENNLKVIIFNINAEHAIIKALSKQGKYTLIE 234
Cdd:TIGR02075 161 GVYTADPKKNKDAKKYDTITYNEALKKNLKVMDLTAFALARDNNLPIVVFNIDKPGALKKVILGKGIGTLVS 232
 
Name Accession Description Interval E-value
pyrH_bact TIGR02075
uridylate kinase; This protein, also called UMP kinase, converts UMP to UDP by adding a ...
 4-234 4.22e-85

uridylate kinase; This protein, also called UMP kinase, converts UMP to UDP by adding a phosphate from ATP. It is the first step in pyrimidine biosynthesis. GTP is an allosteric activator. In a large fraction of all bacterial genomes, the gene tends to be located immediately downstream of elongation factor Ts and upstream of ribosome recycling factor. A related protein family, believed to be equivalent in function and found in the archaea and in spirochetes, is described by a separate model, TIGR02076. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 213681 [Multi-domain]  Cd Length: 232  Bit Score: 252.55  E-value: 4.22e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292    4 KILIKLSGAGMSADSSEPFSNQFLETVIAQLKQLVPN-YQIGIVIGGGNIMRGKSCSDYNITEIAGHHLGIMATVINGAF 82
Cdd:TIGR02075   3 RVLLKLSGEALAGESQFGIDPDRLNRIANEIKELVKMgIEVGIVIGGGNIFRGVSAAELGIDRVSADYMGMLATVINGLA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292   83 LKAKFDSHKLNSTLLSAVSCPSLAtHIVSQATIDDAFKNHDIVIFAGGTGNPYFSTDTAVALRATQMQADIILIGKNgVD 162
Cdd:TIGR02075  83 LRDALEKLGLKTRVLSAISMPQIC-ESYIRRKAIKHLEKGKVVIFSGGTGNPFFTTDTAAALRAIEINADVILKGTN-VD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 920779292  163 GVYTADPKKDKHAKFLASLTYAEAIKNDLQIMDITAFTMCKENNLKVIIFNINAEHAIIKALSKQGKYTLIE 234
Cdd:TIGR02075 161 GVYTADPKKNKDAKKYDTITYNEALKKNLKVMDLTAFALARDNNLPIVVFNIDKPGALKKVILGKGIGTLVS 232
AAK_UMPK-PyrH-Ec cd04254
UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) ...
 4-234 4.60e-81

UMP kinase (UMPK)-Ec, 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 kinase of E. coli (Ec) 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 and chloroplast UMPKs (this CD) 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. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239787 [Multi-domain]  Cd Length: 231  Bit Score: 242.01  E-value: 4.60e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292   4 KILIKLSGAGMSADSSEPFSNQFLETVIAQLKQLVPN-YQIGIVIGGGNIMRGKSCSDYNITEIAGHHLGIMATVINGAF 82
Cdd:cd04254    2 RVLLKLSGEALAGENGFGIDPEVLNRIAREIKEVVDLgVEVAIVVGGGNIFRGASAAEAGMDRATADYMGMLATVINALA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292  83 LKAKFDSHKLNSTLLSAVSCPSLAtHIVSQATIDDAFKNHDIVIFAGGTGNPYFSTDTAVALRATQMQADIILIGKNgVD 162
Cdd:cd04254   82 LQDALESLGVKTRVMSAIPMQGVA-EPYIRRRAIRHLEKGRVVIFAGGTGNPFFTTDTAAALRAIEINADVILKATK-VD 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 920779292 163 GVYTADPKKDKHAKFLASLTYAEAIKNDLQIMDITAFTMCKENNLKVIIFNINAEHAIIKALSKQGKYTLIE 234
Cdd:cd04254  160 GVYDADPKKNPNAKRYDHLTYDEVLSKGLKVMDATAFTLCRDNNLPIVVFNINEPGNLLKAVKGEGVGTLIS 231
PyrH COG0528
Uridylate kinase [Nucleotide transport and metabolism]; Uridylate kinase is part of the ...
 5-235 4.99e-77

Uridylate kinase [Nucleotide transport and metabolism]; Uridylate kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440294 [Multi-domain]  Cd Length: 238  Bit Score: 232.21  E-value: 4.99e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292   5 ILIKLSGAGMSADSSEPFSNQFLETVIAQLKQLVP------------NYqigivigggniMRGKSCSDYNITEIAGHHLG 72
Cdd:COG0528    9 VLLKLSGEALAGEGGFGIDPEVLDRIAEEIKEVVDlgvevaivigggNI-----------FRGASGAAKGMDRATADYMG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292  73 IMATVINGAFLKAKFDSHKLNSTLLSAVSCPSLA-THIVSQAtiDDAFKNHDIVIFAGGTGNPYFSTDTAVALRATQMQA 151
Cdd:COG0528   78 MLATVMNALALQDALEKLGVPTRVQSAIEMPQVAePYIRRRA--IRHLEKGRVVIFAAGTGNPYFTTDTAAALRAIEIGA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292 152 DIILIGKNgVDGVYTADPKKDKHAKFLASLTYAEAIKNDLQIMDITAFTMCKENNLKVIIFNINAEHAIIKALSKQGKYT 231
Cdd:COG0528  156 DVLLKATK-VDGVYDADPKKNPDAKKYDRLTYDEVLAKGLKVMDATAFSLCRDNNLPIIVFNMNKPGNLLRAVLGEKIGT 234


                 ....
gi 920779292 232 LIEK 235
Cdd:COG0528  235 LVSG 238
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 71-213 6.28e-20

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: 84.73  E-value: 6.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292   71 LGIMATVINGAFLKAKFDSHKLNSTLLSAVSCPSLATHI--VSQATIDDAFKNHDIVIFAGGTGNP------YFSTDTAV 142
Cdd:pfam00696  75 LGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVtrIDTEALEELLEAGVVPVITGFIGIDpegelgRGSSDTLA 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 920779292  143 ALRATQMQADIILIGKNgVDGVYTADPKKDKHAKFLASLTYAEAIKNDLQ--------IMDITAFTMCKENNLKVIIFN 213
Cdd:pfam00696 155 ALLAEALGADKLIILTD-VDGVYTADPRKVPDAKLIPEISYDELLELLASglatggmkVKLPAALEAARRGGIPVVIVN 232
IPPK_Arch NF040647
isopentenyl phosphate kinase;
120-233 1.84e-05

isopentenyl phosphate kinase;


Pssm-ID: 468614 [Multi-domain]  Cd Length: 258  Bit Score: 44.51  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292 120 KNHDIVIFAGgtgnpyfstDTAVALRATQMQADIILIGKNgVDGVYTADPKKDKHAKFLASLTYAEAIKN--DLQIMDIT 197
Cdd:NF040647 144 NNIKYGILSG---------DQIIPYLAKKLKPDRVILGSD-VDGVYDKNPKKYPDAKLIDKVNSLDDLESleGTNNVDVT 213

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 920779292 198 A-----FTMC---KENNLKVIIFNINAEHAIIKALSKQ-GKYTLI 233
Cdd:NF040647 214 GgmygkVKELlklAELGIESYIINGNKPENIYKALGGEkVIGTVI 258
PRK06635 PRK06635
aspartate kinase; Reviewed
 115-185 3.08e-05

aspartate kinase; Reviewed


Pssm-ID: 235843 [Multi-domain]  Cd Length: 404  Bit Score: 44.34  E-value: 3.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292 115 IDDAFKNHDIVIFAG-------------GTGNpyfSTDTAVALrATQMQADIILIGKNgVDGVYTADPKKDKHAKFLASL 181
Cdd:PRK06635 121 IREALDEGDVVVVAGfqgvdedgeittlGRGG---SDTTAVAL-AAALKADECEIYTD-VDGVYTTDPRIVPKARKLDKI 195


                 ....
gi 920779292 182 TYAE 185
Cdd:PRK06635 196 SYEE 199
 
Name Accession Description Interval E-value
pyrH_bact TIGR02075
uridylate kinase; This protein, also called UMP kinase, converts UMP to UDP by adding a ...
 4-234 4.22e-85

uridylate kinase; This protein, also called UMP kinase, converts UMP to UDP by adding a phosphate from ATP. It is the first step in pyrimidine biosynthesis. GTP is an allosteric activator. In a large fraction of all bacterial genomes, the gene tends to be located immediately downstream of elongation factor Ts and upstream of ribosome recycling factor. A related protein family, believed to be equivalent in function and found in the archaea and in spirochetes, is described by a separate model, TIGR02076. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 213681 [Multi-domain]  Cd Length: 232  Bit Score: 252.55  E-value: 4.22e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292    4 KILIKLSGAGMSADSSEPFSNQFLETVIAQLKQLVPN-YQIGIVIGGGNIMRGKSCSDYNITEIAGHHLGIMATVINGAF 82
Cdd:TIGR02075   3 RVLLKLSGEALAGESQFGIDPDRLNRIANEIKELVKMgIEVGIVIGGGNIFRGVSAAELGIDRVSADYMGMLATVINGLA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292   83 LKAKFDSHKLNSTLLSAVSCPSLAtHIVSQATIDDAFKNHDIVIFAGGTGNPYFSTDTAVALRATQMQADIILIGKNgVD 162
Cdd:TIGR02075  83 LRDALEKLGLKTRVLSAISMPQIC-ESYIRRKAIKHLEKGKVVIFSGGTGNPFFTTDTAAALRAIEINADVILKGTN-VD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 920779292  163 GVYTADPKKDKHAKFLASLTYAEAIKNDLQIMDITAFTMCKENNLKVIIFNINAEHAIIKALSKQGKYTLIE 234
Cdd:TIGR02075 161 GVYTADPKKNKDAKKYDTITYNEALKKNLKVMDLTAFALARDNNLPIVVFNIDKPGALKKVILGKGIGTLVS 232
AAK_UMPK-PyrH-Ec cd04254
UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) ...
 4-234 4.60e-81

UMP kinase (UMPK)-Ec, 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 kinase of E. coli (Ec) 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 and chloroplast UMPKs (this CD) 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. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239787 [Multi-domain]  Cd Length: 231  Bit Score: 242.01  E-value: 4.60e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292   4 KILIKLSGAGMSADSSEPFSNQFLETVIAQLKQLVPN-YQIGIVIGGGNIMRGKSCSDYNITEIAGHHLGIMATVINGAF 82
Cdd:cd04254    2 RVLLKLSGEALAGENGFGIDPEVLNRIAREIKEVVDLgVEVAIVVGGGNIFRGASAAEAGMDRATADYMGMLATVINALA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292  83 LKAKFDSHKLNSTLLSAVSCPSLAtHIVSQATIDDAFKNHDIVIFAGGTGNPYFSTDTAVALRATQMQADIILIGKNgVD 162
Cdd:cd04254   82 LQDALESLGVKTRVMSAIPMQGVA-EPYIRRRAIRHLEKGRVVIFAGGTGNPFFTTDTAAALRAIEINADVILKATK-VD 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 920779292 163 GVYTADPKKDKHAKFLASLTYAEAIKNDLQIMDITAFTMCKENNLKVIIFNINAEHAIIKALSKQGKYTLIE 234
Cdd:cd04254  160 GVYDADPKKNPNAKRYDHLTYDEVLSKGLKVMDATAFTLCRDNNLPIVVFNINEPGNLLKAVKGEGVGTLIS 231
PyrH COG0528
Uridylate kinase [Nucleotide transport and metabolism]; Uridylate kinase is part of the ...
 5-235 4.99e-77

Uridylate kinase [Nucleotide transport and metabolism]; Uridylate kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440294 [Multi-domain]  Cd Length: 238  Bit Score: 232.21  E-value: 4.99e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292   5 ILIKLSGAGMSADSSEPFSNQFLETVIAQLKQLVP------------NYqigivigggniMRGKSCSDYNITEIAGHHLG 72
Cdd:COG0528    9 VLLKLSGEALAGEGGFGIDPEVLDRIAEEIKEVVDlgvevaivigggNI-----------FRGASGAAKGMDRATADYMG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292  73 IMATVINGAFLKAKFDSHKLNSTLLSAVSCPSLA-THIVSQAtiDDAFKNHDIVIFAGGTGNPYFSTDTAVALRATQMQA 151
Cdd:COG0528   78 MLATVMNALALQDALEKLGVPTRVQSAIEMPQVAePYIRRRA--IRHLEKGRVVIFAAGTGNPYFTTDTAAALRAIEIGA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292 152 DIILIGKNgVDGVYTADPKKDKHAKFLASLTYAEAIKNDLQIMDITAFTMCKENNLKVIIFNINAEHAIIKALSKQGKYT 231
Cdd:COG0528  156 DVLLKATK-VDGVYDADPKKNPDAKKYDRLTYDEVLAKGLKVMDATAFSLCRDNNLPIIVFNMNKPGNLLRAVLGEKIGT 234


                 ....
gi 920779292 232 LIEK 235
Cdd:COG0528  235 LVSG 238
AAK_UMPK-like cd04239
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ...
 4-234 4.50e-71

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: 216.63  E-value: 4.50e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292   4 KILIKLSGAGMSADSSEpFSNQFLETVIAQLKQLVPN-YQIGIVIGGGNIMRGKSCSDYNITEIAGHHLGIMATVINGAF 82
Cdd:cd04239    1 RIVLKLSGEALAGEGGG-IDPEVLKEIAREIKEVVDLgVEVAIVVGGGNIARGYIAAARGMPRATADYIGMLATVMNALA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292  83 LKAKFDSHKLNSTLLSAVSCPSLATHIVSQATIDdAFKNHDIVIFAGGTGNPYFSTDTAVALRATQMQADIILIGKNgVD 162
Cdd:cd04239   80 LQDALEKLGVKTRVMSAIPMQGVAEPYIRRRAIR-HLEKGRIVIFGGGTGNPGFTTDTAAALRAEEIGADVLLKATN-VD 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 920779292 163 GVYTADPKKDKHAKFLASLTYAEAIKNDLQIMDITAFTMCKENNLKVIIFNINAEHAIIKALSKQGKYTLIE 234
Cdd:cd04239  158 GVYDADPKKNPDAKKYDRISYDELLKKGLKVMDATALTLCRRNKIPIIVFNGLKPGNLLRALKGEHVGTLIE 229
AAK_UMPK-PyrH-Pf cd04253
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ...
 60-234 4.10e-21

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: 87.69  E-value: 4.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292  60 DYNITEIAGHHLGIMATVINGAFLKAkfdshklnstLLSAVSCPSLATHivsQATIDDAFKnHDIVIfAGGTgNPYFSTD 139
Cdd:cd04253   55 KLGASEAFLDEIGIMATRLNARLLIA----------ALGDAYPPVPTSY---EEALEAMFT-GKIVV-MGGT-EPGQSTD 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292 140 TAVALRATQMQADIILIGKNgVDGVYTADPKKDKHAKFLASLTYAEAIK----NDLQ-----IMDITAFTMCKENNLKVI 210
Cdd:cd04253  119 AVAALLAERLGADLLINATN-VDGVYSKDPRKDPDAKKFDRLSADELIDivgkSSWKagsnePFDPLAAKIIERSGIKTI 197

                        170       180
                 ....*....|....*....|....
gi 920779292 211 IFNINAEHAIIKALSKQGKYTLIE 234
Cdd:cd04253  198 VVDGRDPENLERALKGEFVGTIIE 221
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 71-213 6.28e-20

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: 84.73  E-value: 6.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292   71 LGIMATVINGAFLKAKFDSHKLNSTLLSAVSCPSLATHI--VSQATIDDAFKNHDIVIFAGGTGNP------YFSTDTAV 142
Cdd:pfam00696  75 LGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVtrIDTEALEELLEAGVVPVITGFIGIDpegelgRGSSDTLA 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 920779292  143 ALRATQMQADIILIGKNgVDGVYTADPKKDKHAKFLASLTYAEAIKNDLQ--------IMDITAFTMCKENNLKVIIFN 213
Cdd:pfam00696 155 ALLAEALGADKLIILTD-VDGVYTADPRKVPDAKLIPEISYDELLELLASglatggmkVKLPAALEAARRGGIPVVIVN 232
pyrH_arch TIGR02076
uridylate kinase, putative; This family consists of the archaeal and spirochete proteins most ...
 71-234 1.41e-16

uridylate kinase, putative; This family consists of the archaeal and spirochete proteins most closely related to bacterial uridylate kinases (TIGR02075), an enzyme involved in pyrimidine biosynthesis. Members are likely, but not known, to be functionally equivalent to their bacterial counterparts. However, substantial sequence differences suggest that regulatory mechanisms may be different; the bacterial form is allosterically regulated by GTP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 273956 [Multi-domain]  Cd Length: 221  Bit Score: 75.42  E-value: 1.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292   71 LGIMATvingaflkakfdshKLNSTLLSAVSCPSLATHIVSqaTIDDAFK---NHDIVIfAGGTgNPYFSTDTAVALRAT 147
Cdd:TIGR02076  65 IGIDAT--------------RLNAMLLIAALGDDAYPKVPE--NFEEALEamsLGKIVV-MGGT-HPGHTTDAVAALLAE 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292  148 QMQADIILIGKNgVDGVYTADPKKDKHAKFLASLTYAEAIK----NDLQ-----IMDITAFTMCKENNLKVIIFNINAEH 218
Cdd:TIGR02076 127 FSKADLLINATN-VDGVYDKDPKKDPDAKKFDKLTPEELVEivgsSSVKagsneVVDPLAAKIIERSKIRTIVVNGRDPE 205

                         170
                  ....*....|....*.
gi 920779292  219 AIIKALSKQGKYTLIE 234
Cdd:TIGR02076 206 NLEKVLKGEHVGTIIE 221
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 60-233 1.95e-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: 1.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292  60 DYNITEIAGHHLGIMATVINGAFLKAKFDSHKLNSTLLSAVSCPSLATHI--------VSQATIDDAFKNHDIVIFAGGT 131
Cdd:cd02115   58 GLRITDRETDALAAMGEGMSNLLIAAALEQHGIKAVPLDLTQAGFASPNQghvgkitkVSTDRLKSLLENGILPILSGFG 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292 132 G--------NPYFSTDTAVALRATQMQADIILIGKNgVDGVYTADPKKDKHAKFLASLTYAEA--IKNDL-QIMDITAFT 200
Cdd:cd02115  138 GtdeketgtLGRGGSDSTAALLAAALKADRLVILTD-VDGVYTADPRKVPDAKLLSELTYEEAaeLAYAGaMVLKPKAAD 216

                        170       180       190
                 ....*....|....*....|....*....|....
gi 920779292 201 MCKENNLKVIIfnINAEHAIIKAL-SKQGKYTLI 233
Cdd:cd02115  217 PAARAGIPVRI--ANTENPGALALfTPDGGGTLI 248
AAK_AK-DapG-like cd04246
AAK_AK-DapG-like: Amino Acid Kinase Superfamily (AAK), AK-DapG-like; this CD includes the ...
 66-185 1.87e-09

AAK_AK-DapG-like: Amino Acid Kinase Superfamily (AAK), AK-DapG-like; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the diaminopimelate-sensitive aspartokinase isoenzyme AKI (DapG), a monofunctional enzymes found in Bacilli (Bacillus subtilis 168), Clostridia, and Actinobacteria bacterial species, as well as, the catalytic AK domain of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis 168, the lysine plus threonine-sensitive aspartokinase of Corynebacterium glutamicum, and related isoenzymes. In Bacillus subtilis, the regulation of the diaminopimelate-lysine biosynthetic pathway involves dual control by diaminopimelate and lysine, effected through separate diaminopimelate- and lysine-sensitive aspartokinase isoenzymes. The role of the AKI isoenzyme is most likely to provide a constant level of aspartyl-beta-phosphate for the biosynthesis of diaminopimelate for peptidoglycan synthesis and dipicolinate during sporulation. The B. subtilis 168 AKII is induced by methionine, and repressed and inhibited by lysine. In Corynebacterium glutamicum and other various Gram-positive bacteria, the DAP-lysine pathway is feedback regulated by the concerted action of lysine and threonine. Also included in this CD are the aspartokinases of the extreme thermophile, Thermus thermophilus HB27, the Gram-negative obligate methylotroph, Methylophilus methylotrophus AS1, and those single aspartokinase isoenzyme types found in Pseudomonas, C. glutamicum, and Amycolatopsis lactamdurans. The B. subtilis AKI is tetrameric consisting of two alpha and two beta subunits; the alpha (43 kD) and beta (17 kD) subunit formed by two in-phase overlapping genes. The alpha subunit contains the AK catalytic domain and two ACT domains. The beta subunit contains two ACT domains. The B. subtilis 168 AKII aspartokinase is also described as tetrameric consisting of two alpha and two beta subunits. Some archeal aspartokinases in this group lack recognizable ACT domains.


Pssm-ID: 239779 [Multi-domain]  Cd Length: 239  Bit Score: 55.96  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292  66 IAGHHLGIMATVINGAFLKAKFDSHKLNSTLLSavscpslathiVSQATIDDAFKNHDIVIFAG-------------GTG 132
Cdd:cd04246   81 MALNRLGIKAISLTGWQAGILTDDHHGNARIID-----------IDPKRILEALEEGDVVVVAGfqgvnedgeittlGRG 149

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 920779292 133 NpyfSTDTAVALrATQMQADIILIGKNgVDGVYTADPKKDKHAKFLASLTYAE 185
Cdd:cd04246  150 G---SDTTAVAL-AAALKADRCEIYTD-VDGVYTADPRIVPKARKLDVISYDE 197
AAK_AKii-LysC-BS cd04261
AAK_AKii-LysC-BS: Amino Acid Kinase Superfamily (AAK), AKii; this CD includes the N-terminal ...
 66-187 2.99e-09

AAK_AKii-LysC-BS: Amino Acid Kinase Superfamily (AAK), AKii; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis 168, and the lysine plus threonine-sensitive aspartokinase of Corynebacterium glutamicum, and related sequences. In B. subtilis 168, the regulation of the diaminopimelate (Dap)-lysine biosynthetic pathway involves dual control by Dap and lysine, effected through separate Dap- and lysine-sensitive aspartokinase isoenzymes. The B. subtilis 168 AKII is induced by methionine, and repressed and inhibited by lysine. Although Corynebacterium glutamicum is known to contain a single aspartokinase isoenzyme type, both the succinylase and dehydrogenase variant pathways of DAP-lysine synthesis operate simultaneously in this organism. In this organism and other various Gram-positive bacteria, the DAP-lysine pathway is feedback regulated by the concerted action of lysine and theronine. Also included in this CD are the aspartokinases of the extreme thermophile, Thermus thermophilus HB27, the Gram-negative obligate methylotroph, Methylophilus methylotrophus AS1, and those single aspartokinases found in Pseudomons, C. glutamicum, and Amycolatopsis lactamdurans. B. subtilis 168 AKII, and the C. glutamicum, Streptomyces clavuligerus and A. lactamdurans aspartokinases are described as tetramers consisting of two alpha and two beta subunits; the alpha (44 kD) and beta (18 kD) subunits formed by two in-phase overlapping polypeptides.


Pssm-ID: 239794 [Multi-domain]  Cd Length: 239  Bit Score: 55.61  E-value: 2.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292  66 IAGHHLGIMATVINGAFLKAKFDSHKLNSTLLSavscpslathiVSQATIDDAFKNHDIVIFAG-------------GTG 132
Cdd:cd04261   81 MALNRLGIKAISLTGWQAGILTDGHHGKARIID-----------IDPDRIRELLEEGDVVIVAGfqginedgdittlGRG 149

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 920779292 133 NpyfSTDTAVALrATQMQADIILIGKNgVDGVYTADPKKDKHAKFLASLTYAEAI 187
Cdd:cd04261  150 G---SDTSAVAL-AAALGADRCEIYTD-VDGVYTADPRIVPKARKLDEISYDEML 199
AAK_AK cd04234
AAK_AK: Amino Acid Kinase Superfamily (AAK), Aspartokinase (AK); this CD includes the ...
 73-186 1.25e-07

AAK_AK: Amino Acid Kinase Superfamily (AAK), Aspartokinase (AK); this CD includes the N-terminal catalytic domain of aspartokinase (4-L-aspartate-4-phosphotransferase;). AK is the first enzyme in the biosynthetic pathway of the aspartate family of amino acids (lysine, threonine, methionine, and isoleucine) and the bacterial cell wall component, meso-diaminopimelate. It also catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. One mechanism for the regulation of this pathway is by the production of several isoenzymes of aspartokinase with different repressors and allosteric inhibitors. Pairs of ACT domains are proposed to specifically bind amino acids leading to allosteric regulation of the enzyme. In Escherichia coli, three different aspartokinase isoenzymes are regulated specifically by lysine, methionine, and threonine. AK-HSDHI (ThrA) and AK-HSDHII (MetL) are bifunctional enzymes that consist of an N-terminal AK and a C-terminal homoserine dehydrogenase (HSDH). ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. The third isoenzyme, AKIII (LysC), is monofunctional and is involved in lysine synthesis. The three Bacillus subtilis isoenzymes, AKI (DapG), AKII (LysC), and AKIII (YclM), are feedback-inhibited by meso-diaminopimelate, lysine, and lysine plus threonine, respectively. The E. coli lysine-sensitive AK is described as a homodimer, whereas, the B. subtilis lysine-sensitive AK is described as a heterodimeric complex of alpha- and beta- subunits that are formed from two in-frame overlapping genes. A single AK enzyme type has been described in Pseudomonas, Amycolatopsis, and Corynebacterium. The fungal aspartate pathway is regulated at the AK step, with L-Thr being an allosteric inhibitor of the Saccharomyces cerevisiae AK (Hom3). At least two distinct AK isoenzymes can occur in higher plants, one is a monofunctional lysine-sensitive isoenzyme, which is involved in the overall regulation of the pathway and can be synergistically inhibited by S-adenosylmethionine. The other isoenzyme is a bifunctional, threonine-sensitive AK-HSDH protein. Also included in this CD is the catalytic domain of the Methylomicrobium alcaliphilum ectoine AK, the first enzyme of the ectoine biosynthetic pathway, found in this bacterium, and several other halophilic/halotolerant bacteria.


Pssm-ID: 239767 [Multi-domain]  Cd Length: 227  Bit Score: 50.55  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292  73 IMATVINGAFLKAK-FDSHKLnstLLSAVSCPSLATHI-VSQATIDDAFKNHDIVI----FAGGTGNPYFST------D- 139
Cdd:cd04234   64 LLAAALRDRGIKARsLDARQA---GITTDDNHGAARIIeISYERLKELLAEIGKVPvvtgFIGRNEDGEITTlgrggsDy 140

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 920779292 140 TAVALrATQMQADIILIGKNgVDGVYTADPKKDKHAKFLASLTYAEA 186
Cdd:cd04234  141 SAAAL-AAALGADEVEIWTD-VDGIYTADPRIVPEARLIPEISYDEA 185
MetL1 COG0527
Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the ...
 108-186 6.74e-07

Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440293 [Multi-domain]  Cd Length: 407  Bit Score: 49.31  E-value: 6.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292 108 HIVSQATIDDAFKNHDIVIFAGGTG-NPYFST--------D-TAVALrATQMQADIILIGKNgVDGVYTADPKKDKHAKF 177
Cdd:COG0527  115 LIETPERIRELLEEGKVVVVAGFQGvTEDGEIttlgrggsDtTAVAL-AAALKADECEIWTD-VDGVYTADPRIVPDARK 192


                 ....*....
gi 920779292 178 LASLTYAEA 186
Cdd:COG0527  193 LPEISYEEM 201
AAK_UMPK-MosAB cd04255
AAK_UMPK-MosAB: This CD includes the alpha and beta subunits of the Mo storage protein (MosA ...
 134-191 1.53e-06

AAK_UMPK-MosAB: This CD includes the alpha and beta subunits of the Mo storage protein (MosA and MosB) which are related to uridine monophosphate kinase (UMPK) enzymes that catalyze the phosphorylation of UMP by ATP, yielding UDP, and playing a key role in pyrimidine nucleotide biosynthesis. The Mo storage protein from the nitrogen-fixing bacterium, Azotobacter vinelandii, is characterized as an alpha4-beta4 octamer containing a polynuclear molybdenum-oxide cluster which is ATP-dependent to bind Mo and pH-dependent to release Mo. These and related bacterial sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239788 [Multi-domain]  Cd Length: 262  Bit Score: 47.77  E-value: 1.53e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 920779292 134 PYFSTDTAVALRATQMQADIILIGKNgVDGVYTADPKKDKHAKFLASLTYAEAIKNDL 191
Cdd:cd04255  159 PPHRTDVGAFLLAEVIGARNLIFVKD-EDGLYTADPKKNKKAEFIPEISAAELLKKDL 215
asp_kinases TIGR00657
aspartate kinase; Aspartate kinase catalyzes a first step in the biosynthesis from Asp of Lys ...
 124-227 2.65e-06

aspartate kinase; Aspartate kinase catalyzes a first step in the biosynthesis from Asp of Lys (and its precursor diaminopimelate), Met, and Thr. In E. coli, a distinct isozyme is inhibited by each of the three amino acid products. The Met-sensitive (I) and Thr-sensitive (II) forms are bifunctional enzymes fused to homoserine dehydrogenases and form homotetramers, while the Lys-sensitive form (III) is a monofunctional homodimer.The Lys-sensitive enzyme of Bacillus subtilis resembles the E. coli form but is an alpha 2/beta 2 heterotetramer, where the beta subunit is translated from an in-phase alternative initiator at Met-246. This may be a feature of a number of closely related forms, including a paralog from B. subtilis. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273201 [Multi-domain]  Cd Length: 441  Bit Score: 47.35  E-value: 2.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292  124 IVIFAG---GTGNPYFST------DTAVALRATQMQADIILIGKNgVDGVYTADPKKDKHAKFLASLTYAEAIknDL--- 191
Cdd:TIGR00657 170 IPVVAGfqgATEKGETTTlgrggsDYTAALLAAALKADECEIYTD-VDGIYTTDPRIVPDARRIDEISYEEML--ELasf 246

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 920779292  192 --QIMDITAFTMCKENNLKVII---FNINAEHAIIKALSKQ 227
Cdd:TIGR00657 247 gaKVLHPRTLEPAMRAKIPIVVkstFNPEAPGTLIVASTKE 287
AAK_AK-HSDH-like cd04243
AAK_AK-HSDH-like: Amino Acid Kinase Superfamily (AAK), AK-HSDH-like; this family includes the ...
 141-186 5.18e-06

AAK_AK-HSDH-like: Amino Acid Kinase Superfamily (AAK), AK-HSDH-like; this family includes the N-terminal catalytic domain of aspartokinase (AK) of the bifunctional enzyme AK- homoserine dehydrogenase (HSDH). These aspartokinases are found in such bacteria as E. coli (AKI-HSDHI, ThrA and AKII-HSDHII, MetL) and in higher plants (Z. mays AK-HSDH). AK and HSDH are the first and third enzymes in the biosynthetic pathway of the aspartate family of amino acids. AK catalyzes the phosphorylation of Asp to P-aspartyl phosphate. HSDH catalyzes the NADPH-dependent conversion of Asp 3-semialdehyde to homoserine. ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. In E. coli, ThrA is subject to allosteric regulation by the end product L-threonine and the native enzyme is reported to be tetrameric. As with bacteria, plant AK and HSDH are feedback inhibited by pathway end products. Maize AK-HSDH is a Thr-sensitive 180-kD enzyme. Arabidopsis AK-HSDH is an alanine-activated, threonine-sensitive enzyme whose ACT domains, located C-terminal to the AK catalytic domain, were shown to be involved in allosteric activation. Also included in this CD is the catalytic domain of the aspartokinase (AK) of the lysine-sensitive aspartokinase isoenzyme AKIII, a monofunctional class enzyme (LysC) found in some bacteria such as E. coli. In E. coli, LysC is reported to be a homodimer of 50 kD subunits. Also included in this CD is the catalytic domain of aspartokinase (AK) of the bifunctional enzyme AK - DAP decarboxylase (DapDC) found in some bacteria. DapDC, which is the lysA gene product, catalyzes the decarboxylation of DAP to lysine.


Pssm-ID: 239776 [Multi-domain]  Cd Length: 293  Bit Score: 46.39  E-value: 5.18e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 920779292 141 AVALRATQMQ--ADiiligkngVDGVYTADPKKDKHAKFLASLTYAEA 186
Cdd:cd04243  212 AALLDAEEVEiwTD--------VDGVYTADPRKVPDARLLKELSYDEA 251
AAK_AK-HSDH cd04257
AAK_AK-HSDH: Amino Acid Kinase Superfamily (AAK), AK-HSDH; this CD includes the N-terminal ...
 161-187 1.56e-05

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


Pssm-ID: 239790 [Multi-domain]  Cd Length: 294  Bit Score: 44.88  E-value: 1.56e-05
                         10        20
                 ....*....|....*....|....*..
gi 920779292 161 VDGVYTADPKKDKHAKFLASLTYAEAI 187
Cdd:cd04257  227 VDGVYSADPRKVKDARLLPSLSYQEAM 253
IPPK_Arch NF040647
isopentenyl phosphate kinase;
120-233 1.84e-05

isopentenyl phosphate kinase;


Pssm-ID: 468614 [Multi-domain]  Cd Length: 258  Bit Score: 44.51  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292 120 KNHDIVIFAGgtgnpyfstDTAVALRATQMQADIILIGKNgVDGVYTADPKKDKHAKFLASLTYAEAIKN--DLQIMDIT 197
Cdd:NF040647 144 NNIKYGILSG---------DQIIPYLAKKLKPDRVILGSD-VDGVYDKNPKKYPDAKLIDKVNSLDDLESleGTNNVDVT 213

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 920779292 198 A-----FTMC---KENNLKVIIFNINAEHAIIKALSKQ-GKYTLI 233
Cdd:NF040647 214 GgmygkVKELlklAELGIESYIINGNKPENIYKALGGEkVIGTVI 258
PRK06635 PRK06635
aspartate kinase; Reviewed
 115-185 3.08e-05

aspartate kinase; Reviewed


Pssm-ID: 235843 [Multi-domain]  Cd Length: 404  Bit Score: 44.34  E-value: 3.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292 115 IDDAFKNHDIVIFAG-------------GTGNpyfSTDTAVALrATQMQADIILIGKNgVDGVYTADPKKDKHAKFLASL 181
Cdd:PRK06635 121 IREALDEGDVVVVAGfqgvdedgeittlGRGG---SDTTAVAL-AAALKADECEIYTD-VDGVYTTDPRIVPKARKLDKI 195


                 ....
gi 920779292 182 TYAE 185
Cdd:PRK06635 196 SYEE 199
thrA PRK09436
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional
 161-187 3.83e-05

bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional


Pssm-ID: 181856 [Multi-domain]  Cd Length: 819  Bit Score: 44.38  E-value: 3.83e-05
                         10        20
                 ....*....|....*....|....*..
gi 920779292 161 VDGVYTADPKKDKHAKFLASLTYAEAI 187
Cdd:PRK09436 229 VDGVYTADPRVVPDARLLKSLSYQEAM 255
AAK_G5K_ProB cd04242
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ...
 139-233 4.54e-05

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: 43.20  E-value: 4.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292 139 DTAVALRATQMQAD--IILigkNGVDGVYTADPKKDKHAKFlasLTYAEAIKNDLQIMD---------------ITAFTM 201
Cdd:cd04242  145 DRLSALVAGLVNADllILL---SDVDGLYDKNPRENPDAKL---IPEVEEITDEIEAMAggsgssvgtggmrtkLKAARI 218

                         90       100       110
                 ....*....|....*....|....*....|..
gi 920779292 202 CKENNLKVIIFNINAEHAIIKALSKQGKYTLI 233
Cdd:cd04242  219 ATEAGIPVVIANGRKPDVLLDILAGEAVGTLF 250
PRK08210 PRK08210
aspartate kinase I; Reviewed
 115-185 5.98e-05

aspartate kinase I; Reviewed


Pssm-ID: 236188 [Multi-domain]  Cd Length: 403  Bit Score: 43.30  E-value: 5.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292 115 IDDAFKNHDIVI---FAGGTGNPYFST------DTAVALRATQMQADIILIGKNgVDGVYTADPKKDKHAKFLASLTYAE 185
Cdd:PRK08210 126 ILEALEEGDVVVvagFQGVTENGDITTlgrggsDTTAAALGVALKAEYVDIYTD-VDGIMTADPRIVEDARLLDVVSYNE 204
AAK_AK-Hom3 cd04247
AAK_AK-Hom3: Amino Acid Kinase Superfamily (AAK), AK-Hom3; this CD includes the N-terminal ...
 129-186 7.92e-05

AAK_AK-Hom3: Amino Acid Kinase Superfamily (AAK), AK-Hom3; this CD includes the N-terminal catalytic domain of the aspartokinase HOM3, a monofunctional class enzyme found in Saccharomyces cerevisiae and other related AK domains. Aspartokinase, the first enzyme in the aspartate metabolic pathway, catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP, and in fungi, is responsible for the production of threonine, isoleucine and methionine. S. cerevisiae has a single aspartokinase isoenzyme type, which is regulated by feedback, allosteric inhibition by L-threonine. Recent studies show that the allosteric transition triggered by binding of threonine to AK involves a large change in the conformation of the native hexameric enzyme that is converted to an inactive one of different shape and substantially smaller hydrodynamic size.


Pssm-ID: 239780 [Multi-domain]  Cd Length: 306  Bit Score: 42.81  E-value: 7.92e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 920779292 129 GGTGNPYfsTDTAVALRATQMQADIILIGKNgVDGVYTADPKKDKHAKFLASLTYAEA 186
Cdd:cd04247  208 SQIGRGY--TDLCAALCAVGLNADELQIWKE-VDGIFTADPRKVPTARLLPSITPEEA 262
PRK06291 PRK06291
aspartate kinase; Provisional
 127-186 1.20e-04

aspartate kinase; Provisional


Pssm-ID: 235773 [Multi-domain]  Cd Length: 465  Bit Score: 42.61  E-value: 1.20e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 920779292 127 FAGGTGNPYFST------DTAVALRATQMQADIILIGKNgVDGVYTADPKKDKHAKFLASLTYAEA 186
Cdd:PRK06291 196 FIGETEEGIITTlgrggsDYSAAIIGAALDADEIWIWTD-VDGVMTTDPRIVPEARVIPKISYIEA 260
AAK_AKi-DapG-BS cd04260
AAK_AKi-DapG-BS: Amino Acid Kinase Superfamily (AAK), AKi-DapG; this CD includes the ...
 110-185 2.39e-04

AAK_AKi-DapG-BS: Amino Acid Kinase Superfamily (AAK), AKi-DapG; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the diaminopimelate-sensitive aspartokinase isoenzyme AKI (DapG), a monofunctional class enzyme found in Bacilli (Bacillus subtilis 168), Clostridia, and Actinobacteria bacterial species. In Bacillus subtilis, the regulation of the diaminopimelate-lysine biosynthetic pathway involves dual control by diaminopimelate and lysine, effected through separate diaminopimelate- and lysine-sensitive aspartokinase isoenzymes. AKI activity is invariant during the exponential and stationary phases of growth and is not altered by addition of amino acids to the growth medium. The role of this isoenzyme is most likely to provide a constant level of aspartyl-beta-phosphate for the biosynthesis of diaminopimelate for peptidoglycan synthesis and dipicolinate during sporulation. The B. subtilis AKI is tetrameric consisting of two alpha and two beta subunits; the alpha (43 kD) and beta (17 kD) subunit formed by two in-phase overlapping genes. The alpha subunit contains the AK catalytic domain and two ACT domains. The beta subunit contains two ACT domains.


Pssm-ID: 239793 [Multi-domain]  Cd Length: 244  Bit Score: 41.22  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292 110 VSQATIDDAFKNHDIVI---FAGGTGNPYFST------DTAVALRATQMQADIILIGKNgVDGVYTADPKKDKHAKFLAS 180
Cdd:cd04260  119 VNPKKILSALKEGDVVVvagFQGVTEDGEVTTlgrggsDTTAAALGAALNAEYVEIYTD-VDGIMTADPRVVPNARILDV 197


                 ....*
gi 920779292 181 LTYAE 185
Cdd:cd04260  198 VSYNE 202
ProB COG0263
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ...
 139-194 5.86e-04

Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440033 [Multi-domain]  Cd Length: 371  Bit Score: 40.41  E-value: 5.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 920779292 139 DTAVALRATQMQAD--IILigkNGVDGVYTADPKKDKHAKFLAsltYAEAIKNDLQIM 194
Cdd:COG0263  153 DRLAALVANLVEADllVLL---TDVDGLYDADPRKDPDAKLIP---EVEEITPEIEAM 204
AAK_AK-DapDC cd04259
AAK_AK-DapDC: Amino Acid Kinase Superfamily (AAK), AK-DapDC; this CD includes the N-terminal ...
 73-186 1.37e-03

AAK_AK-DapDC: Amino Acid Kinase Superfamily (AAK), AK-DapDC; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the bifunctional enzyme AK - DAP decarboxylase (DapDC) found in some bacteria. Aspartokinase is the first enzyme in the aspartate metabolic pathway, catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. DapDC, which is the lysA gene product, catalyzes the decarboxylation of DAP to lysine.


Pssm-ID: 239792 [Multi-domain]  Cd Length: 295  Bit Score: 39.06  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292  73 IMATVINGAFLKAK------FDSHKLnstlLSAVSCPSLATHIVSQATI----DDA-----FKNHDIVIFAGG--TGNPY 135
Cdd:cd04259  120 LMSTRLGAAYLEAQglkvkwLDAREL----LTATPTLGGETMNYLSARCeseyADAllqkrLADGAQLIITQGfiARNAH 195

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 920779292 136 FST--------DTAVALRATQMQADIILIGKNgVDGVYTADPKKDKHAKFLASLTYAEA 186
Cdd:cd04259  196 GETvllgrggsDTSAAYFAAKLQAARCEIWTD-VPGLFTANPHEVPHARLLKRLDYDEA 253
AAK_AK-LysC-like cd04244
AAK_AK-LysC-like: Amino Acid Kinase Superfamily (AAK), AK-LysC-like; this CD includes the ...
 138-186 2.05e-03

AAK_AK-LysC-like: Amino Acid Kinase Superfamily (AAK), AK-LysC-like; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the lysine-sensitive AK isoenzyme found in higher plants. The lysine-sensitive AK isoenzyme is a monofunctional protein. It is involved in the overall regulation of the aspartate pathway and can be synergistically inhibited by S-adenosylmethionine. Also included in this CD is an uncharacterized LysC-like AK found in Euryarchaeota and some bacteria. AK catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP.


Pssm-ID: 239777 [Multi-domain]  Cd Length: 298  Bit Score: 38.51  E-value: 2.05e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 920779292 138 TDTAVALRATQMQADIILIGKNgVDGVYTADPKKDKHAKFLASLTYAEA 186
Cdd:cd04244  209 SDYSATIIGAALDADEIWIWKD-VDGVMTADPRIVPEARTIPRLSYAEA 256
AAK_P5CS_ProBA cd04256
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ...
 139-224 3.24e-03

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


Pssm-ID: 239789 [Multi-domain]  Cd Length: 284  Bit Score: 37.80  E-value: 3.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292 139 DTAVALRATQMQADIiLIGKNGVDGVYTADPKKDKhAKFL--------ASLTYAEAIKNDLQIMD--ITAFTMCKENNLK 208
Cdd:cd04256  181 DSLAARLAVELKADL-LILLSDVDGLYDGPPGSDD-AKLIhtfypgdqQSITFGTKSRVGTGGMEakVKAALWALQGGTS 258

                         90
                 ....*....|....*.
gi 920779292 209 VIIFNINAEHAIIKAL 224
Cdd:cd04256  259 VVITNGMAGDVITKIL 274
metL PRK09466
bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional
 149-186 4.62e-03

bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional


Pssm-ID: 236530 [Multi-domain]  Cd Length: 810  Bit Score: 37.98  E-value: 4.62e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 920779292 149 MQADIILIGKNG----------------------VDGVYTADPKKDKHAKFLASLTYAEA 186
Cdd:PRK09466 198 EAGETVLLGRNGsdysatligalagvervtiwsdVAGVYSADPRKVKDACLLPLLRLDEA 257
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
138-186 7.29e-03

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 37.37  E-value: 7.29e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 920779292 138 TDTAVALRATQMQADIILIGKNgVDGVYTADPKKDKHAKFLASLTYAEA 186
Cdd:PRK08961 215 SDTSAAYFAAKLGASRVEIWTD-VPGMFSANPKEVPDARLLTRLDYDEA 262
 
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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