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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394766842  16 RRVLLKLSGEVF-GGGAVGLDPDVVSDAARQIAEAVATGVQVAVVVGGGNFFRGAELSQSGMARDRADYMGMLGTVMNAL 94
Cdd:cd04254    1 KRVLLKLSGEALaGENGFGIDPEVLNRIAREIKEVVDLGVEVAIVVGGGNIFRGASAAEAGMDRATADYMGMLATVINAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394766842  95 ALQDFIEKAGVPARVQSAIAMTQVAEPYIPLRAIRHLEKGRVVVFGAGAGLPYFSTDTVSAQRALETRCDELLVGKNgVD 174
Cdd:cd04254   81 ALQDALESLGVKTRVMSAIPMQGVAEPYIRRRAIRHLEKGRVVIFAGGTGNPFFTTDTAAALRAIEINADVILKATK-VD 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 394766842 175 GVYTADPRKDPTARLLSRLTYERALADGLKVVDASAFALCRDNSLTMRVFGMGEGGNITRALLGEQIGTLVT 246
Cdd:cd04254  160 GVYDADPKKNPNAKRYDHLTYDEVLSKGLKVMDATAFTLCRDNNLPIVVFNINEPGNLLKAVKGEGVGTLIS 231

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394766842   16 RRVLLKLSGEVFGggavglDPDVVSDAARQIAEAVATGVQVAVVVGGGNFFRGaELSQSGMARDRA-------------D 82
Cdd:pfam00696   1 KRVVIKLGGSSLT------DKERLKRLADEIAALLEEGRKLVVVHGGGAFADG-LLALLGLSPRFArltdaetlevatmD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394766842   83 YMGMLGTVMNALALQDFIEKAGVPARVQSAIAMTQVAEPY--IPLRAIRH-LEKGRVVVFGAGAGLP------YFSTDTV 153
Cdd:pfam00696  74 ALGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVtrIDTEALEElLEAGVVPVITGFIGIDpegelgRGSSDTL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 394766842  154 SAQRALETRCDELLVGKNgVDGVYTADPRKDPTARLLSRLTYERAL--------ADGLKVVDASAFALCRDNSLTMRVF 224
Cdd:pfam00696 154 AALLAEALGADKLIILTD-VDGVYTADPRKVPDAKLIPEISYDELLellasglaTGGMKVKLPAALEAARRGGIPVVIV 231

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394766842  16 RRVLLKLSGEVF-GGGAVGLDPDVVSDAARQIAEAVATGVQVAVVVGGGNFFRGAELSQSGMARDRADYMGMLGTVMNAL 94
Cdd:cd04254    1 KRVLLKLSGEALaGENGFGIDPEVLNRIAREIKEVVDLGVEVAIVVGGGNIFRGASAAEAGMDRATADYMGMLATVINAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394766842  95 ALQDFIEKAGVPARVQSAIAMTQVAEPYIPLRAIRHLEKGRVVVFGAGAGLPYFSTDTVSAQRALETRCDELLVGKNgVD 174
Cdd:cd04254   81 ALQDALESLGVKTRVMSAIPMQGVAEPYIRRRAIRHLEKGRVVIFAGGTGNPFFTTDTAAALRAIEINADVILKATK-VD 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 394766842 175 GVYTADPRKDPTARLLSRLTYERALADGLKVVDASAFALCRDNSLTMRVFGMGEGGNITRALLGEQIGTLVT 246
Cdd:cd04254  160 GVYDADPKKNPNAKRYDHLTYDEVLSKGLKVMDATAFTLCRDNNLPIVVFNINEPGNLLKAVKGEGVGTLIS 231

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394766842  17 RVLLKLSGEVFGGGAVGLDPDVVSDAARQIAEAVATGVQVAVVVGGGNFFRGAELSQSGMARDRADYMGMLGTVMNALAL 96
Cdd:cd04239    1 RIVLKLSGEALAGEGGGIDPEVLKEIAREIKEVVDLGVEVAIVVGGGNIARGYIAAARGMPRATADYIGMLATVMNALAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394766842  97 QDFIEKAGVPARVQSAIAMTQVAEPYIPLRAIRHLEKGRVVVFGAGAGLPYFSTDTVSAQRALETRCDELLVGKNgVDGV 176
Cdd:cd04239   81 QDALEKLGVKTRVMSAIPMQGVAEPYIRRRAIRHLEKGRIVIFGGGTGNPGFTTDTAAALRAEEIGADVLLKATN-VDGV 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394766842 177 YTADPRKDPTARLLSRLTYERALADGLKVVDASAFALCRDNSLTMRVFGMGEGGNITRALLGEQIGTLVT 246
Cdd:cd04239  160 YDADPKKNPDAKKYDRISYDELLKKGLKVMDATALTLCRRNKIPIIVFNGLKPGNLLRALKGEHVGTLIE 229

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394766842  82 DYMGMLGTVMNALALQDFIEKA--GVPARVQSAIAMtqvaepyiplrairhLEKGRVVVfgAGAGLPYFSTDTVSAQRAL 159
Cdd:cd04253   64 DEIGIMATRLNARLLIAALGDAypPVPTSYEEALEA---------------MFTGKIVV--MGGTEPGQSTDAVAALLAE 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394766842 160 ETRCDELLVGKNgVDGVYTADPRKDPTARLLSRLTYERAL---------ADGLKVVDASAFALCRDNSLTMRVFGMGEGG 230
Cdd:cd04253  127 RLGADLLINATN-VDGVYSKDPRKDPDAKKFDRLSADELIdivgksswkAGSNEPFDPLAAKIIERSGIKTIVVDGRDPE 205

                        170
                 ....*....|....*.
gi 394766842 231 NITRALLGEQIGTLVT 246
Cdd:cd04253  206 NLERALKGEFVGTIIE 221

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394766842  81 ADYMGMLGTVMNALALQDFIEKAGVPARVQSAIAMTQVAEPYIPLRAIRH---------LEKGRVVVFGAGAG------- 144
Cdd:cd02115   66 TDALAAMGEGMSNLLIAAALEQHGIKAVPLDLTQAGFASPNQGHVGKITKvstdrlkslLENGILPILSGFGGtdeketg 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394766842 145 -LPYFSTDTVSAQRALETRCDELLVGKNgVDGVYTADPRKDPTARLLSRLTYERAL---ADGLKVVDASAFALCRDNSLT 220
Cdd:cd02115  146 tLGRGGSDSTAALLAAALKADRLVILTD-VDGVYTADPRKVPDAKLLSELTYEEAAelaYAGAMVLKPKAADPAARAGIP 224

                        170       180
                 ....*....|....*....|....*
gi 394766842 221 MRVFGMGEGGNItRALLGEQIGTLV 245
Cdd:cd02115  225 VRIANTENPGAL-ALFTPDGGGTLI 248

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 394766842 150 TDTVSAQRALETRCDELLVGKNgVDGVYTADPRKDPTARLLSRLTYERA 198
Cdd:cd04247  215 TDLCAALCAVGLNADELQIWKE-VDGIFTADPRKVPTARLLPSITPEEA 262

aspartate kinase; Reviewed

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 394766842 173 VDGVYTADPRKDPTARLLSRLTYERAL---ADGLKVVDASAFALCRDNSLTMRVfgmgeggnitRALLGEQIGTLVTQE 248
Cdd:PRK06635 175 VDGVYTTDPRIVPKARKLDKISYEEMLelaSLGAKVLHPRSVEYAKKYNVPLRV----------RSSFSDNPGTLITGE 243

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 394766842 173 VDGVYTADPRKDPTARLLSRLTYERAL---ADGLKVVDASAFALCRDNSLTMRVfgmgeggnitRALLGEQIGTLVT 246
Cdd:cd04246  173 VDGVYTADPRIVPKARKLDVISYDEMLemaSLGAKVLHPRSVELAKKYNVPLRV----------RSSFSENPGTLIT 239

bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional

                         10        20
                 ....*....|....*....|....*.
gi 394766842 173 VDGVYTADPRKDPTARLLSRLTYERA 198
Cdd:PRK09436 229 VDGVYTADPRVVPDARLLKSLSYQEA 254

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.

                         10        20
                 ....*....|....*....|....*.
gi 394766842 173 VDGVYTADPRKDPTARLLSRLTYERA 198
Cdd:cd04243  226 VDGVYTADPRKVPDARLLKELSYDEA 251

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394766842 124 PLRAIRHLEKGRVVVFGAGAG---------LPYFSTDTVSAQRALETRCDELLVGKNgVDGVYTADPRKDPTARLLSRLT 194
Cdd:cd04260  121 PKKILSALKEGDVVVVAGFQGvtedgevttLGRGGSDTTAAALGAALNAEYVEIYTD-VDGIMTADPRVVPNARILDVVS 199

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 394766842 195 YERA--LAD-GLKVVDASAFALCRDNSLTMRVfgmgeggnitRALLGEQIGTLVT 246
Cdd:cd04260  200 YNEVfqMAHqGAKVIHPRAVEIAMQANIPIRI----------RSTMSENPGTLIT 244

aspartate kinase I; Reviewed

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 394766842 173 VDGVYTADPRKDPTARLLSRLTYERA--LAD-GLKVVDASAFALCRDNSLTMRVfgmgeggnitRALLGEQIGTLVTQ 247
Cdd:PRK08210 180 VDGIMTADPRIVEDARLLDVVSYNEVfqMAYqGAKVIHPRAVEIAMQANIPLRI----------RSTYSDSPGTLITS 247

bifunctional aspartate kinase/diaminopimelate decarboxylase;

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 394766842 173 VDGVYTADPRKDPTARLLSRLTYERA--LAD-GLKVVDASAFALCRDNSLTMRV 223
Cdd:PRK08961 237 VPGMFSANPKEVPDARLLTRLDYDEAqeIATtGAKVLHPRSIKPCRDAGIPMAI 290

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394766842 173 VDGVYTADPRKDPTARLLSRLT----YERALADGL-----------KVvdaSAFALCRDNSLTMRVFGMGEGGNITRALL 237
Cdd:COG0263  174 VDGLYDADPRKDPDAKLIPEVEeitpEIEAMAGGAgsglgtggmatKL---EAARIATRAGIPTVIASGREPNVLLRILA 250

                 ....*..
gi 394766842 238 GEQIGTL 244
Cdd:COG0263  251 GERVGTL 257

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.

                         10        20        30
                 ....*....|....*....|....*....|....*
gi 394766842 164 DELLVGKNgVDGVYTADPRKDPTARLLSRLTYERA 198
Cdd:cd04244  223 DEIWIWKD-VDGVMTADPRIVPEARTIPRLSYAEA 256

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 394766842 151 DTVSAQRALETRCDeLLVGKNGVDGVYTADPRKDPTARLLS 191
Cdd:cd04242  145 DRLSALVAGLVNAD-LLILLSDVDGLYDKNPRENPDAKLIP 184

aspartate kinase; Validated

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 394766842 173 VDGVYTADPRKDPTARLLSRLTYE--RALAD-GLKVVDASAFALCRDNSLTMRV---FGMGEG 229
Cdd:PRK08841 175 VDGVYTCDPRVVKNARKLDVIDFPsmEAMARkGAKVLHLPSVQHAWKHSVPLRVlssFEVGEG 237