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Conserved domains on  [gi|1691016300|ref|WP_139688851|]
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MULTISPECIES: UMP kinase [Sutterella]

Protein Classification

uridine monophosphate kinase( domain architecture ID 10001676)

uridine monophosphate kinase catalyzing the conversion of UMP to UTP in pyrimidine nucleotide biosynthesis

EC:  2.7.4.22
Gene Ontology:  GO:0005524|GO:0033862|GO:0044210|GO:0016310
PubMed:  18945668
SCOP:  4003224

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PyrH COG0528
Uridylate kinase [Nucleotide transport and metabolism]; Uridylate kinase is part of the ...
 8-243 1.37e-161

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: 446.38  E-value: 1.37e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300   8 KPVYKRILLKLSGEALMGDDAFGINRQVLQHMIEEIRSVLDLGVQIGIVVGGGNIFRGVALGATGMDRATGDYMGMLATV 87
Cdd:COG0528     3 KPKYKRVLLKLSGEALAGEGGFGIDPEVLDRIAEEIKEVVDLGVEVAIVIGGGNIFRGASGAAKGMDRATADYMGMLATV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  88 MNAMALQDCCRNNGIEARVQSALHIEQVAEPYIRGKALRHLRLGRVVIFAAGTGNPFMTTDTTAALRGAEVGADIVLKAT 167
Cdd:COG0528    83 MNALALQDALEKLGVPTRVQSAIEMPQVAEPYIRRRAIRHLEKGRVVIFAAGTGNPYFTTDTAAALRAIEIGADVLLKAT 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1691016300 168 KVDGIYTADPKKDPTATMYDEITFDHALRTNLKVMDATAFALCREQGLPIKVFNINKKGALRRVVLGEKEGTLVHS 243
Cdd:COG0528   163 KVDGVYDADPKKNPDAKKYDRLTYDEVLAKGLKVMDATAFSLCRDNNLPIIVFNMNKPGNLLRAVLGEKIGTLVSG 238
 
Name Accession Description Interval E-value
PyrH COG0528
Uridylate kinase [Nucleotide transport and metabolism]; Uridylate kinase is part of the ...
 8-243 1.37e-161

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: 446.38  E-value: 1.37e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300   8 KPVYKRILLKLSGEALMGDDAFGINRQVLQHMIEEIRSVLDLGVQIGIVVGGGNIFRGVALGATGMDRATGDYMGMLATV 87
Cdd:COG0528     3 KPKYKRVLLKLSGEALAGEGGFGIDPEVLDRIAEEIKEVVDLGVEVAIVIGGGNIFRGASGAAKGMDRATADYMGMLATV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  88 MNAMALQDCCRNNGIEARVQSALHIEQVAEPYIRGKALRHLRLGRVVIFAAGTGNPFMTTDTTAALRGAEVGADIVLKAT 167
Cdd:COG0528    83 MNALALQDALEKLGVPTRVQSAIEMPQVAEPYIRRRAIRHLEKGRVVIFAAGTGNPYFTTDTAAALRAIEIGADVLLKAT 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1691016300 168 KVDGIYTADPKKDPTATMYDEITFDHALRTNLKVMDATAFALCREQGLPIKVFNINKKGALRRVVLGEKEGTLVHS 243
Cdd:COG0528   163 KVDGVYDADPKKNPDAKKYDRLTYDEVLAKGLKVMDATAFSLCRDNNLPIIVFNMNKPGNLLRAVLGEKIGTLVSG 238
AAK_UMPK-PyrH-Ec cd04254
UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) ...
 12-242 4.00e-142

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: 397.25  E-value: 4.00e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  12 KRILLKLSGEALMGDDAFGINRQVLQHMIEEIRSVLDLGVQIGIVVGGGNIFRGVALGATGMDRATGDYMGMLATVMNAM 91
Cdd:cd04254     1 KRVLLKLSGEALAGENGFGIDPEVLNRIAREIKEVVDLGVEVAIVVGGGNIFRGASAAEAGMDRATADYMGMLATVINAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  92 ALQDCCRNNGIEARVQSALHIEQVAEPYIRGKALRHLRLGRVVIFAAGTGNPFMTTDTTAALRGAEVGADIVLKATKVDG 171
Cdd:cd04254    81 ALQDALESLGVKTRVMSAIPMQGVAEPYIRRRAIRHLEKGRVVIFAGGTGNPFFTTDTAAALRAIEINADVILKATKVDG 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1691016300 172 IYTADPKKDPTATMYDEITFDHALRTNLKVMDATAFALCREQGLPIKVFNINKKGALRRVVLGEKEGTLVH 242
Cdd:cd04254   161 VYDADPKKNPNAKRYDHLTYDEVLSKGLKVMDATAFTLCRDNNLPIVVFNINEPGNLLKAVKGEGVGTLIS 231
pyrH_bact TIGR02075
uridylate kinase; This protein, also called UMP kinase, converts UMP to UDP by adding a ...
 11-242 2.26e-130

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: 367.34  E-value: 2.26e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  11 YKRILLKLSGEALMGDDAFGINRQVLQHMIEEIRSVLDLGVQIGIVVGGGNIFRGVALGATGMDRATGDYMGMLATVMNA 90
Cdd:TIGR02075   1 YKRVLLKLSGEALAGESQFGIDPDRLNRIANEIKELVKMGIEVGIVIGGGNIFRGVSAAELGIDRVSADYMGMLATVING 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  91 MALQDCCRNNGIEARVQSALHIEQVAEPYIRGKALRHLRLGRVVIFAAGTGNPFMTTDTTAALRGAEVGADIVLKATKVD 170
Cdd:TIGR02075  81 LALRDALEKLGLKTRVLSAISMPQICESYIRRKAIKHLEKGKVVIFSGGTGNPFFTTDTAAALRAIEINADVILKGTNVD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1691016300 171 GIYTADPKKDPTATMYDEITFDHALRTNLKVMDATAFALCREQGLPIKVFNINKKGALRRVVLGEKEGTLVH 242
Cdd:TIGR02075 161 GVYTADPKKNKDAKKYDTITYNEALKKNLKVMDLTAFALARDNNLPIVVFNIDKPGALKKVILGKGIGTLVS 232
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 12-221 2.15e-28

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: 107.45  E-value: 2.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  12 KRILLKLSGEALmgDDAfginrQVLQHMIEEIRSVLDLGVQIGIVVGGGNIFRGVA------------LGATGMDRATGD 79
Cdd:pfam00696   1 KRVVIKLGGSSL--TDK-----ERLKRLADEIAALLEEGRKLVVVHGGGAFADGLLallglsprfarlTDAETLEVATMD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  80 YMGMLATVMNAMALQDCCRNNGIEAR---VQSALHIEQVAEPYIRGKALRHLRLGRVVIFAAGTGNP------FMTTDTT 150
Cdd:pfam00696  74 ALGSLGERLNAALLAAGLPAVGLPAAqllATEAGFIDDVVTRIDTEALEELLEAGVVPVITGFIGIDpegelgRGSSDTL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1691016300 151 AALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFDHALRTN--------LKVMDATAFALCREQGLPIKVFN 221
Cdd:pfam00696 154 AALLAEALGADKLIILTDVDGVYTADPRKVPDAKLIPEISYDELLELLasglatggMKVKLPAALEAARRGGIPVVIVN 232
PRK06635 PRK06635
aspartate kinase; Reviewed
 81-243 5.01e-08

aspartate kinase; Reviewed


Pssm-ID: 235843 [Multi-domain]  Cd Length: 404  Bit Score: 52.81  E-value: 5.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  81 MGMLAtvmnaMALQDCcrnnGIEAR-------------VQSALHIEQvaepyIRGKALRH-LRLGRVVIFA-----AGTG 141
Cdd:PRK06635   78 VALLA-----MALQSL----GVKARsftgwqagiitdsAHGKARITD-----IDPSRIREaLDEGDVVVVAgfqgvDEDG 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 142 NpfMTT------DTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFDHALrtNL-----KVMDATAFALC 210
Cdd:PRK06635  144 E--ITTlgrggsDTTAVALAAALKADECEIYTDVDGVYTTDPRIVPKARKLDKISYEEML--ELaslgaKVLHPRSVEYA 219

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1691016300 211 REQGLPIKVfninkkgalrRVVLGEKEGTLVHS 243
Cdd:PRK06635  220 KKYNVPLRV----------RSSFSDNPGTLITG 242
IPPK_Arch NF040647
isopentenyl phosphate kinase;
160-241 1.15e-06

isopentenyl phosphate kinase;


Pssm-ID: 468614 [Multi-domain]  Cd Length: 258  Bit Score: 48.36  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 160 ADIVLKATKVDGIYTADPKKDPTATMYDEITFDHALRT-------------NLKVMDATafaLCREQGLPIKVFNINKKG 226
Cdd:NF040647  166 PDRVILGSDVDGVYDKNPKKYPDAKLIDKVNSLDDLESlegtnnvdvtggmYGKVKELL---KLAELGIESYIINGNKPE 242

                          90
                  ....*....|....*.
gi 1691016300 227 ALRRVVLGEK-EGTLV 241
Cdd:NF040647  243 NIYKALGGEKvIGTVI 258
 
Name Accession Description Interval E-value
PyrH COG0528
Uridylate kinase [Nucleotide transport and metabolism]; Uridylate kinase is part of the ...
 8-243 1.37e-161

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: 446.38  E-value: 1.37e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300   8 KPVYKRILLKLSGEALMGDDAFGINRQVLQHMIEEIRSVLDLGVQIGIVVGGGNIFRGVALGATGMDRATGDYMGMLATV 87
Cdd:COG0528     3 KPKYKRVLLKLSGEALAGEGGFGIDPEVLDRIAEEIKEVVDLGVEVAIVIGGGNIFRGASGAAKGMDRATADYMGMLATV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  88 MNAMALQDCCRNNGIEARVQSALHIEQVAEPYIRGKALRHLRLGRVVIFAAGTGNPFMTTDTTAALRGAEVGADIVLKAT 167
Cdd:COG0528    83 MNALALQDALEKLGVPTRVQSAIEMPQVAEPYIRRRAIRHLEKGRVVIFAAGTGNPYFTTDTAAALRAIEIGADVLLKAT 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1691016300 168 KVDGIYTADPKKDPTATMYDEITFDHALRTNLKVMDATAFALCREQGLPIKVFNINKKGALRRVVLGEKEGTLVHS 243
Cdd:COG0528   163 KVDGVYDADPKKNPDAKKYDRLTYDEVLAKGLKVMDATAFSLCRDNNLPIIVFNMNKPGNLLRAVLGEKIGTLVSG 238
AAK_UMPK-PyrH-Ec cd04254
UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) ...
 12-242 4.00e-142

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: 397.25  E-value: 4.00e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  12 KRILLKLSGEALMGDDAFGINRQVLQHMIEEIRSVLDLGVQIGIVVGGGNIFRGVALGATGMDRATGDYMGMLATVMNAM 91
Cdd:cd04254     1 KRVLLKLSGEALAGENGFGIDPEVLNRIAREIKEVVDLGVEVAIVVGGGNIFRGASAAEAGMDRATADYMGMLATVINAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  92 ALQDCCRNNGIEARVQSALHIEQVAEPYIRGKALRHLRLGRVVIFAAGTGNPFMTTDTTAALRGAEVGADIVLKATKVDG 171
Cdd:cd04254    81 ALQDALESLGVKTRVMSAIPMQGVAEPYIRRRAIRHLEKGRVVIFAGGTGNPFFTTDTAAALRAIEINADVILKATKVDG 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1691016300 172 IYTADPKKDPTATMYDEITFDHALRTNLKVMDATAFALCREQGLPIKVFNINKKGALRRVVLGEKEGTLVH 242
Cdd:cd04254   161 VYDADPKKNPNAKRYDHLTYDEVLSKGLKVMDATAFTLCRDNNLPIVVFNINEPGNLLKAVKGEGVGTLIS 231
pyrH_bact TIGR02075
uridylate kinase; This protein, also called UMP kinase, converts UMP to UDP by adding a ...
 11-242 2.26e-130

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: 367.34  E-value: 2.26e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  11 YKRILLKLSGEALMGDDAFGINRQVLQHMIEEIRSVLDLGVQIGIVVGGGNIFRGVALGATGMDRATGDYMGMLATVMNA 90
Cdd:TIGR02075   1 YKRVLLKLSGEALAGESQFGIDPDRLNRIANEIKELVKMGIEVGIVIGGGNIFRGVSAAELGIDRVSADYMGMLATVING 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  91 MALQDCCRNNGIEARVQSALHIEQVAEPYIRGKALRHLRLGRVVIFAAGTGNPFMTTDTTAALRGAEVGADIVLKATKVD 170
Cdd:TIGR02075  81 LALRDALEKLGLKTRVLSAISMPQICESYIRRKAIKHLEKGKVVIFSGGTGNPFFTTDTAAALRAIEINADVILKGTNVD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1691016300 171 GIYTADPKKDPTATMYDEITFDHALRTNLKVMDATAFALCREQGLPIKVFNINKKGALRRVVLGEKEGTLVH 242
Cdd:TIGR02075 161 GVYTADPKKNKDAKKYDTITYNEALKKNLKVMDLTAFALARDNNLPIVVFNIDKPGALKKVILGKGIGTLVS 232
AAK_UMPK-like cd04239
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ...
 13-242 2.51e-119

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: 339.51  E-value: 2.51e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  13 RILLKLSGEALMGDDAfGINRQVLQHMIEEIRSVLDLGVQIGIVVGGGNIFRGVALGATGMDRATGDYMGMLATVMNAMA 92
Cdd:cd04239     1 RIVLKLSGEALAGEGG-GIDPEVLKEIAREIKEVVDLGVEVAIVVGGGNIARGYIAAARGMPRATADYIGMLATVMNALA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  93 LQDCCRNNGIEARVQSALHIEQVAEPYIRGKALRHLRLGRVVIFAAGTGNPFMTTDTTAALRGAEVGADIVLKATKVDGI 172
Cdd:cd04239    80 LQDALEKLGVKTRVMSAIPMQGVAEPYIRRRAIRHLEKGRIVIFGGGTGNPGFTTDTAAALRAEEIGADVLLKATNVDGV 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 173 YTADPKKDPTATMYDEITFDHALRTNLKVMDATAFALCREQGLPIKVFNINKKGALRRVVLGEKEGTLVH 242
Cdd:cd04239   160 YDADPKKNPDAKKYDRISYDELLKKGLKVMDATALTLCRRNKIPIIVFNGLKPGNLLRALKGEHVGTLIE 229
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 12-221 2.15e-28

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: 107.45  E-value: 2.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  12 KRILLKLSGEALmgDDAfginrQVLQHMIEEIRSVLDLGVQIGIVVGGGNIFRGVA------------LGATGMDRATGD 79
Cdd:pfam00696   1 KRVVIKLGGSSL--TDK-----ERLKRLADEIAALLEEGRKLVVVHGGGAFADGLLallglsprfarlTDAETLEVATMD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  80 YMGMLATVMNAMALQDCCRNNGIEAR---VQSALHIEQVAEPYIRGKALRHLRLGRVVIFAAGTGNP------FMTTDTT 150
Cdd:pfam00696  74 ALGSLGERLNAALLAAGLPAVGLPAAqllATEAGFIDDVVTRIDTEALEELLEAGVVPVITGFIGIDpegelgRGSSDTL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1691016300 151 AALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFDHALRTN--------LKVMDATAFALCREQGLPIKVFN 221
Cdd:pfam00696 154 AALLAEALGADKLIILTDVDGVYTADPRKVPDAKLIPEISYDELLELLasglatggMKVKLPAALEAARRGGIPVVIVN 232
AAK_UMPK-PyrH-Pf cd04253
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ...
 13-241 2.94e-26

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: 101.56  E-value: 2.94e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  13 RILLKLSGEALMGDdafgINRQVLQHMIEEIRSVLDlGVQIGIVVGGGNIFR---GVA--LGAtgmDRATGDYMGMLATV 87
Cdd:cd04253     1 RIVISLGGSVLAPE----KDADFIKEYANVLRKISD-GHKVAVVVGGGRLAReyiSVArkLGA---SEAFLDEIGIMATR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  88 MNAMALqdccrnngIEARVQSALHIEQVAEPyirgkALRHLRLGRVVIfAAGTgNPFMTTDTTAALRGAEVGADIVLKAT 167
Cdd:cd04253    73 LNARLL--------IAALGDAYPPVPTSYEE-----ALEAMFTGKIVV-MGGT-EPGQSTDAVAALLAERLGADLLINAT 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 168 KVDGIYTADPKKDPTATMYDEITFDHALR----------TNLkVMDATAFALCREQGLPIKVFNINKKGALRRVVLGEKE 237
Cdd:cd04253   138 NVDGVYSKDPRKDPDAKKFDRLSADELIDivgksswkagSNE-PFDPLAAKIIERSGIKTIVVDGRDPENLERALKGEFV 216


                  ....
gi 1691016300 238 GTLV 241
Cdd:cd04253   217 GTII 220
pyrH_arch TIGR02076
uridylate kinase, putative; This family consists of the archaeal and spirochete proteins most ...
 14-241 8.43e-24

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: 95.07  E-value: 8.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  14 ILLKLSGEALMGDdafgINRQVLQHMIEEIRSVLDlGVQIGIVVGGGNIFR---GVA--LGAtgmDRATGDYMGMLATVM 88
Cdd:TIGR02076   1 IVISLGGSVLSPE----IDAEFIKEFANILRKLSD-EHKVGVVVGGGKTARryiGVAreLGA---SETFLDEIGIDATRL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  89 NAMALqdccrnngIEARVQSALHIeqVAEPYIrgKALRHLRLGRVVIfAAGTgNPFMTTDTTAALRGAEVGADIVLKATK 168
Cdd:TIGR02076  73 NAMLL--------IAALGDDAYPK--VPENFE--EALEAMSLGKIVV-MGGT-HPGHTTDAVAALLAEFSKADLLINATN 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 169 VDGIYTADPKKDPTATMYDEITF----DHALRTNLK-----VMDATAFALCREQGLPIKVFNINKKGALRRVVLGEKEGT 239
Cdd:TIGR02076 139 VDGVYDKDPKKDPDAKKFDKLTPeelvEIVGSSSVKagsneVVDPLAAKIIERSKIRTIVVNGRDPENLEKVLKGEHVGT 218


                  ..
gi 1691016300 240 LV 241
Cdd:TIGR02076 219 II 220
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 15-241 1.99e-23

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: 94.82  E-value: 1.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  15 LLKLSGEALMGDDAFGINRQVLQHMIEEirsvldlGVQIGIVVGGGNIFRGVALGAT---------GMDRATGDYMGMLA 85
Cdd:cd02115     1 VIKFGGSSVSSEERLRNLARILVKLASE-------GGRVVVVHGAGPQITDELLAHGellgyarglRITDRETDALAAMG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  86 TVMNAMALQDCCRNNGIEARVQSA---------LHIEQVAEPYIRGKALRHLRLGRVVIFAAGTG--------NPFMTTD 148
Cdd:cd02115    74 EGMSNLLIAAALEQHGIKAVPLDLtqagfaspnQGHVGKITKVSTDRLKSLLENGILPILSGFGGtdeketgtLGRGGSD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 149 TTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFDHALRT---NLKVMDATAFALCREQGLPIKVFNINKK 225
Cdd:cd02115   154 STAALLAAALKADRLVILTDVDGVYTADPRKVPDAKLLSELTYEEAAELayaGAMVLKPKAADPAARAGIPVRIANTENP 233

                         250
                  ....*....|....*.
gi 1691016300 226 GALrRVVLGEKEGTLV 241
Cdd:cd02115   234 GAL-ALFTPDGGGTLI 248
AAK_AK cd04234
AAK_AK: Amino Acid Kinase Superfamily (AAK), Aspartokinase (AK); this CD includes the ...
 83-241 2.41e-15

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: 72.51  E-value: 2.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  83 MLATVMNAMALQDccrnNGIEAR---------VQSALHIEQVAEPYIRGKALRHL-RLGRVVI---FAAGTGNPFMTT-- 147
Cdd:cd04234    59 RLSARLLAAALRD----RGIKARsldarqagiTTDDNHGAARIIEISYERLKELLaEIGKVPVvtgFIGRNEDGEITTlg 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 148 ----DTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFDHALR-TNL--KVMDATAFALCREQGLPIKVF 220
Cdd:cd04234   135 rggsDYSAAALAAALGADEVEIWTDVDGIYTADPRIVPEARLIPEISYDEALElAYFgaKVLHPRAVEPARKANIPIRVK 214

                         170       180
                  ....*....|....*....|.
gi 1691016300 221 NINKKgalrrvvlgEKEGTLV 241
Cdd:cd04234   215 NTFNP---------EAPGTLI 226
asp_kinases TIGR00657
aspartate kinase; Aspartate kinase catalyzes a first step in the biosynthesis from Asp of Lys ...
 120-221 1.76e-13

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: 68.92  E-value: 1.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 120 IRGKALRHLRLGRVVIFA---AGTGNPFMTT------DTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEIT 190
Cdd:TIGR00657 157 LTERLEPLLEEGIIPVVAgfqGATEKGETTTlgrggsDYTAALLAAALKADECEIYTDVDGIYTTDPRIVPDARRIDEIS 236

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1691016300 191 FDHAL---RTNLKVMDATAFALCREQGLPIKVFN 221
Cdd:TIGR00657 237 YEEMLelaSFGAKVLHPRTLEPAMRAKIPIVVKS 270
MetL1 COG0527
Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the ...
 90-243 5.24e-11

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: 61.64  E-value: 5.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  90 AMALQDccrnNGIEARVQSA--LHIE--------QVAEPYIRGKALRHLRLGRVVIFA---AGTGNPFMTT------DTT 150
Cdd:COG0527    82 AMALQE----LGVPAVSLDGrqAGIItddnhgkaRIDLIETPERIRELLEEGKVVVVAgfqGVTEDGEITTlgrggsDTT 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 151 AALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFDHALrtNL-----KVMDATAFALCREQGLPIKV---FNi 222
Cdd:COG0527   158 AVALAAALKADECEIWTDVDGVYTADPRIVPDARKLPEISYEEML--ELaylgaKVLHPRAVEPAMKYNIPLRVrstFN- 234

                         170       180
                  ....*....|....*....|.
gi 1691016300 223 nkkgalrrvvlGEKEGTLVHS 243
Cdd:COG0527   235 -----------PDAPGTLITA 244
AAK_AK-DapG-like cd04246
AAK_AK-DapG-like: Amino Acid Kinase Superfamily (AAK), AK-DapG-like; this CD includes the ...
 125-242 4.17e-10

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: 57.89  E-value: 4.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 125 LRHLRLGRVVIfAAG----TGNPFMTT------DTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFDHA 194
Cdd:cd04246   120 LEALEEGDVVV-VAGfqgvNEDGEITTlgrggsDTTAVALAAALKADRCEIYTDVDGVYTADPRIVPKARKLDVISYDEM 198

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1691016300 195 LR-TNL--KVMDATAFALCREQGLPIKVfninkkgalrRVVLGEKEGTLVH 242
Cdd:cd04246   199 LEmASLgaKVLHPRSVELAKKYNVPLRV----------RSSFSENPGTLIT 239
AAK_AKii-LysC-BS cd04261
AAK_AKii-LysC-BS: Amino Acid Kinase Superfamily (AAK), AKii; this CD includes the N-terminal ...
 126-241 8.34e-10

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: 57.16  E-value: 8.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 126 RHLRLGRVVIFA-----AGTGNpfMTT------DTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFDHA 194
Cdd:cd04261   121 ELLEEGDVVIVAgfqgiNEDGD--ITTlgrggsDTSAVALAAALGADRCEIYTDVDGVYTADPRIVPKARKLDEISYDEM 198

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1691016300 195 LR-TNL--KVMDATAFALCREQGLPIKVfninkkgalrRVVLGEKEGTLV 241
Cdd:cd04261   199 LEmASLgaKVLHPRSVELAKKYGVPLRV----------LSSFSEEPGTLI 238
AAK_UMPK-MosAB cd04255
AAK_UMPK-MosAB: This CD includes the alpha and beta subunits of the Mo storage protein (MosA ...
 33-242 1.46e-09

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: 56.63  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  33 RQVLQHMIEEIRSVLdLGVQIGIVVGGGNifRGVALGATGMDratgdyMGMLATVMNAMALQDCCRNNGIEARVQSALHI 112
Cdd:cd04255    47 AEAVLPLVEEIVALR-PEHKLLILTGGGT--RARHVYSIGLD------LGMPTGVLAKLGASVSEQNAEMLATLLAKHGG 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 113 EQVAEPYIRGKALrHLRLGRVVIFA-----------AGTGN-PFMTTDTTAALRGAEVGADIVLKATKVDGIYTADPKKD 180
Cdd:cd04255   118 SKVGHGDLLQLPT-FLKAGRAPVISgmppyglwehpAEEGRiPPHRTDVGAFLLAEVIGARNLIFVKDEDGLYTADPKKN 196

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1691016300 181 PTATMYDEITFDHALRTNL-------KVMDATAFALCREQglpIKVFNINKKGALRRVVLGEKEGTLVH 242
Cdd:cd04255   197 KKAEFIPEISAAELLKKDLddlvlerPVLDLLQNARHVKE---VQIVNGLVPGNLTRALRGEHVGTIIR 262
PRK06635 PRK06635
aspartate kinase; Reviewed
 81-243 5.01e-08

aspartate kinase; Reviewed


Pssm-ID: 235843 [Multi-domain]  Cd Length: 404  Bit Score: 52.81  E-value: 5.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300  81 MGMLAtvmnaMALQDCcrnnGIEAR-------------VQSALHIEQvaepyIRGKALRH-LRLGRVVIFA-----AGTG 141
Cdd:PRK06635   78 VALLA-----MALQSL----GVKARsftgwqagiitdsAHGKARITD-----IDPSRIREaLDEGDVVVVAgfqgvDEDG 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 142 NpfMTT------DTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFDHALrtNL-----KVMDATAFALC 210
Cdd:PRK06635  144 E--ITTlgrggsDTTAVALAAALKADECEIYTDVDGVYTTDPRIVPKARKLDKISYEEML--ELaslgaKVLHPRSVEYA 219

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1691016300 211 REQGLPIKVfninkkgalrRVVLGEKEGTLVHS 243
Cdd:PRK06635  220 KKYNVPLRV----------RSSFSDNPGTLITG 242
AAK_AK-HSDH-like cd04243
AAK_AK-HSDH-like: Amino Acid Kinase Superfamily (AAK), AK-HSDH-like; this family includes the ...
 148-242 5.42e-08

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: 52.17  E-value: 5.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 148 DTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFDHAlrTNL-----KVMDATAFALCREQGLPIKVFNI 222
Cdd:cd04243   205 DYSAALLAALLDAEEVEIWTDVDGVYTADPRKVPDARLLKELSYDEA--MELayfgaKVLHPRTIQPAIRKNIPIFIKNT 282

                          90       100
                  ....*....|....*....|
gi 1691016300 223 NKkgalrrvvlGEKEGTLVH 242
Cdd:cd04243   283 FN---------PEAPGTLIS 293
PRK08210 PRK08210
aspartate kinase I; Reviewed
 125-192 2.61e-07

aspartate kinase I; Reviewed


Pssm-ID: 236188 [Multi-domain]  Cd Length: 403  Bit Score: 50.62  E-value: 2.61e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1691016300 125 LRHLRLGRVVI---FAAGTGNPFMTT------DTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFD 192
Cdd:PRK08210  127 LEALEEGDVVVvagFQGVTENGDITTlgrggsDTTAAALGVALKAEYVDIYTDVDGIMTADPRIVEDARLLDVVSYN 203
AAK_AK-LysC-like cd04244
AAK_AK-LysC-like: Amino Acid Kinase Superfamily (AAK), AK-LysC-like; this CD includes the ...
 147-221 6.89e-07

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: 48.91  E-value: 6.89e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1691016300 147 TDTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFDHALRT---NLKVMDATAFALCREQGLPIKVFN 221
Cdd:cd04244   209 SDYSATIIGAALDADEIWIWKDVDGVMTADPRIVPEARTIPRLSYAEAMELayfGAKVLHPRTVEPAMEKGIPVRVKN 286
PRK07431 PRK07431
aspartate kinase; Provisional
 126-243 8.13e-07

aspartate kinase; Provisional


Pssm-ID: 236018 [Multi-domain]  Cd Length: 587  Bit Score: 49.53  E-value: 8.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 126 RHLRLGRVVIfAAG------TGNPFMTT------DTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFDH 193
Cdd:PRK07431  123 RHLDAGKVVV-VAGfqgislSSNLEITTlgrggsDTSAVALAAALGADACEIYTDVPGVLTTDPRLVPEAQLMDEISCDE 201

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1691016300 194 ALR-TNL--KVMDATAFALCREQGLPIKVfninkkgalrRVVLGEKEGTLVHS 243
Cdd:PRK07431  202 MLElASLgaSVLHPRAVEIARNYGVPLVV----------RSSWSDAPGTLVTS 244
AAK_AKi-DapG-BS cd04260
AAK_AKi-DapG-BS: Amino Acid Kinase Superfamily (AAK), AKi-DapG; this CD includes the ...
 123-242 9.70e-07

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: 48.15  E-value: 9.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 123 KALRHLRLGRVVI---FAAGTGNPFMTT------DTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFD- 192
Cdd:cd04260   123 KILSALKEGDVVVvagFQGVTEDGEVTTlgrggsDTTAAALGAALNAEYVEIYTDVDGIMTADPRVVPNARILDVVSYNe 202

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1691016300 193 --HALRTNLKVMDATAFALCREQGLPIKVfninkkgalrRVVLGEKEGTLVH 242
Cdd:cd04260   203 vfQMAHQGAKVIHPRAVEIAMQANIPIRI----------RSTMSENPGTLIT 244
IPPK_Arch NF040647
isopentenyl phosphate kinase;
160-241 1.15e-06

isopentenyl phosphate kinase;


Pssm-ID: 468614 [Multi-domain]  Cd Length: 258  Bit Score: 48.36  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 160 ADIVLKATKVDGIYTADPKKDPTATMYDEITFDHALRT-------------NLKVMDATafaLCREQGLPIKVFNINKKG 226
Cdd:NF040647  166 PDRVILGSDVDGVYDKNPKKYPDAKLIDKVNSLDDLESlegtnnvdvtggmYGKVKELL---KLAELGIESYIINGNKPE 242

                          90
                  ....*....|....*.
gi 1691016300 227 ALRRVVLGEK-EGTLV 241
Cdd:NF040647  243 NIYKALGGEKvIGTVI 258
PRK06291 PRK06291
aspartate kinase; Provisional
 136-221 1.42e-06

aspartate kinase; Provisional


Pssm-ID: 235773 [Multi-domain]  Cd Length: 465  Bit Score: 48.38  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 136 FAAGTGNPFMTT------DTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFDHALRTNL---KVMDATA 206
Cdd:PRK06291  196 FIGETEEGIITTlgrggsDYSAAIIGAALDADEIWIWTDVDGVMTTDPRIVPEARVIPKISYIEAMELSYfgaKVLHPRT 275

                          90
                  ....*....|....*
gi 1691016300 207 FALCREQGLPIKVFN 221
Cdd:PRK06291  276 IEPAMEKGIPVRVKN 290
PRK09084 PRK09084
aspartate kinase III; Validated
 148-194 2.76e-06

aspartate kinase III; Validated


Pssm-ID: 236376 [Multi-domain]  Cd Length: 448  Bit Score: 47.51  E-value: 2.76e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1691016300 148 DTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFDHA 194
Cdd:PRK09084  200 DYSAALLAEALNASRVEIWTDVPGIYTTDPRIVPAAKRIDEISFEEA 246
AAK_P5CS_ProBA cd04256
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ...
 148-242 5.76e-06

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: 46.27  E-value: 5.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 148 DTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMY-------DEITFDHALRTNLKVMDA--TAFALCREQGLPIK 218
Cdd:cd04256   181 DSLAARLAVELKADLLILLSDVDGLYDGPPGSDDAKLIHtfypgdqQSITFGTKSRVGTGGMEAkvKAALWALQGGTSVV 260

                          90       100
                  ....*....|....*....|....
gi 1691016300 219 VFNINKKGALRRVVLGEKEGTLVH 242
Cdd:cd04256   261 ITNGMAGDVITKILEGKKVGTFFT 284
AAK_G5K_ProB cd04242
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ...
 148-190 9.46e-06

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: 45.51  E-value: 9.46e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1691016300 148 DTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEIT 190
Cdd:cd04242   145 DRLSALVAGLVNADLLILLSDVDGLYDKNPRENPDAKLIPEVE 187
PLN02418 PLN02418
delta-1-pyrroline-5-carboxylate synthase
 144-242 1.18e-05

delta-1-pyrroline-5-carboxylate synthase


Pssm-ID: 215230  Cd Length: 718  Bit Score: 45.87  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 144 FMTTDTTAALRGAEVGADIVLKATKVDGIYTAdPKKDPTATM---------YDEITFDHALRTNLKVMDA--TAFALCRE 212
Cdd:PLN02418  174 FWDNDSLAALLALELKADLLILLSDVEGLYTG-PPSDPSSKLihtyikekhQDEITFGEKSRVGRGGMTAkvKAAVNAAS 252

                          90       100       110
                  ....*....|....*....|....*....|
gi 1691016300 213 QGLPIKVFNINKKGALRRVVLGEKEGTLVH 242
Cdd:PLN02418  253 AGIPVVITSGYALDNIRKVLRGERVGTLFH 282
AAK_AK-HSDH cd04257
AAK_AK-HSDH: Amino Acid Kinase Superfamily (AAK), AK-HSDH; this CD includes the N-terminal ...
 123-242 1.79e-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: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 123 KALRHLRLGRVVI--FAAGTGNPFMTT------DTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFDHA 194
Cdd:cd04257   173 KAWFSSNGKVIVVtgFIASNPQGETTTlgrngsDYSAAILAALLDADQVEIWTDVDGVYSADPRKVKDARLLPSLSYQEA 252

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1691016300 195 L---RTNLKVMDATAFALCREQGLPIKVFNINKkgalrrvvlGEKEGTLVH 242
Cdd:cd04257   253 MelsYFGAKVLHPKTIQPVAKKNIPILIKNTFN---------PEAPGTLIS 294
AAK_AK-Hom3 cd04247
AAK_AK-Hom3: Amino Acid Kinase Superfamily (AAK), AK-Hom3; this CD includes the N-terminal ...
 147-194 2.15e-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: 44.73  E-value: 2.15e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1691016300 147 TDTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFDHA 194
Cdd:cd04247   215 TDLCAALCAVGLNADELQIWKEVDGIFTADPRKVPTARLLPSITPEEA 262
AAK_AKiii-LysC-EC cd04258
AAK_AKiii-LysC-EC: Amino Acid Kinase Superfamily (AAK), AKiii-LysC-EC: this CD includes the ...
 147-194 2.25e-05

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


Pssm-ID: 239791 [Multi-domain]  Cd Length: 292  Bit Score: 44.66  E-value: 2.25e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1691016300 147 TDTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFDHA 194
Cdd:cd04258   203 SDYSAALLAEALHAEELQIWTDVAGIYTTDPRICPAARAIKEISFAEA 250
AAK_AK-DapDC cd04259
AAK_AK-DapDC: Amino Acid Kinase Superfamily (AAK), AK-DapDC; this CD includes the N-terminal ...
 147-219 3.97e-05

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: 43.68  E-value: 3.97e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1691016300 147 TDTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFDHALR---TNLKVMDATAFALCREQGLPIKV 219
Cdd:cd04259   206 SDTSAAYFAAKLQAARCEIWTDVPGLFTANPHEVPHARLLKRLDYDEAQEiatMGAKVLHPRCIPPARRANIPMVV 281
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
147-219 4.26e-05

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 44.30  E-value: 4.26e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1691016300 147 TDTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFDHALR---TNLKVMDATAFALCREQGLPIKV 219
Cdd:PRK08961  215 SDTSAAYFAAKLGASRVEIWTDVPGMFSANPKEVPDARLLTRLDYDEAQEiatTGAKVLHPRSIKPCRDAGIPMAI 290
AAK_FomA-like cd04241
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ...
 157-241 1.72e-04

AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar proteins found in a wide range of organisms. Together, the fomA and fomB genes in the fosfomycin biosynthetic gene cluster of Streptomyces wedmorensis confer high-level fosfomycin resistance. FomA and FomB proteins converted fosfomycin to fosfomycin monophosphate and fosfomycin diphosphate in the presence of ATP and a magnesium ion, indicating that FomA and FomB catalyzed phosphorylations of fosfomycin and fosfomycin monophosphate, respectively. FomA and related sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239774 [Multi-domain]  Cd Length: 252  Bit Score: 41.86  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 157 EVGADIVLKATKVDGIYTADPkkdPTATMYDEITFD--HALRTNLKVM--DAT--------AFALCREQGLPIKVFNINK 224
Cdd:cd04241   159 ALKPERVIFLTDVDGVYDKPP---PDAKLIPEIDVGslEDILAALGSAgtDVTggmagkieELLELARRGIEVYIFNGDK 235

                          90
                  ....*....|....*..
gi 1691016300 225 KGALRRVVLGEKEGTLV 241
Cdd:cd04241   236 PENLYRALLGNFIGTRI 252
PRK08373 PRK08373
aspartate kinase; Validated
 122-195 1.97e-04

aspartate kinase; Validated


Pssm-ID: 236250 [Multi-domain]  Cd Length: 341  Bit Score: 41.96  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 122 GKALRHLRLGRVVIFAAGTG--NPFMTT------DTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFDH 193
Cdd:PRK08373  158 KILYELLERGRVPVVPGFIGnlNGFRATlgrggsDYSAVALGVLLNAKAVLIMSDVEGIYTADPKLVPSARLIPYLSYDE 237


                  ..
gi 1691016300 194 AL 195
Cdd:PRK08373  238 AL 239
ProB COG0263
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ...
 148-190 2.29e-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: 41.56  E-value: 2.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1691016300 148 DTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEIT 190
Cdd:COG0263   153 DRLAALVANLVEADLLVLLTDVDGLYDADPRKDPDAKLIPEVE 195
thrA PRK09436
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional
 148-194 3.43e-04

bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional


Pssm-ID: 181856 [Multi-domain]  Cd Length: 819  Bit Score: 41.30  E-value: 3.43e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1691016300 148 DTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFDHA 194
Cdd:PRK09436  208 DYSAAILAACLDADCCEIWTDVDGVYTADPRVVPDARLLKSLSYQEA 254
PRK05925 PRK05925
aspartate kinase; Provisional
 147-226 1.89e-03

aspartate kinase; Provisional


Pssm-ID: 235646 [Multi-domain]  Cd Length: 440  Bit Score: 39.03  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 147 TDTTAALRGAEVGADIVLKATKVDGIYTADPKKDPTATMYDEITFDHAlrTNL-----KVMDATAFALCREQGLPIKV-- 219
Cdd:PRK05925  190 SDFSASLIAELCKAREVRIYTDVNGIYTMDPKIIKDAQLIPELSFEEM--QNLasfgaKVLHPPMLKPCVRAGIPIFVts 267


                  ....*...
gi 1691016300 220 -FNINKKG 226
Cdd:PRK05925  268 tFDVTKGG 275
P5CS TIGR01092
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ...
 144-242 3.57e-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: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691016300 144 FMTTDTTAALRGAEVGADIVLKATKVDGIYTAdPKKDPTATMYD---------EITFDHALRTNLKVMDA--TAFALCRE 212
Cdd:TIGR01092 166 FWDNDSLAALLALELKADLLILLSDVEGLYDG-PPSDDDSKLIDtfykekhqgEITFGTKSRLGRGGMTAkvKAAVWAAY 244

                          90       100       110
                  ....*....|....*....|....*....|
gi 1691016300 213 QGLPIKVFNINKKGALRRVVLGEKEGTLVH 242
Cdd:TIGR01092 245 GGTPVIIASGTAPKNITKVVEGKKVGTLFH 274
PRK08841 PRK08841
aspartate kinase; Validated
 131-193 6.74e-03

aspartate kinase; Validated


Pssm-ID: 181563 [Multi-domain]  Cd Length: 392  Bit Score: 37.04  E-value: 6.74e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1691016300 131 GRVVIFAAGTG---NPFMTT------DTTA-ALRGAeVGADIVLKATKVDGIYTADPKKDPTATMYDEITFDH 193
Cdd:PRK08841  128 DQIVIVAGFQGrneNGDITTlgrggsDTTAvALAGA-LNADECQIFTDVDGVYTCDPRVVKNARKLDVIDFPS 199
 
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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