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Conserved domains on  [gi|748714066|ref|WP_039972186|]
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MULTISPECIES: UMP kinase [Pseudoalteromonas]

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 ...
 6-241 3.85e-153

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: 425.58  E-value: 3.85e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066   6 KPIFRRVLLKLSGEALMGDEGFGIDPKVLDRMAQEIKELVELDVEVGLVIGGGNFLRGGSLAEAGMNRVVGDHMGMLATV 85
Cdd:COG0528    3 KPKYKRVLLKLSGEALAGEGGFGIDPEVLDRIAEEIKEVVDLGVEVAIVIGGGNIFRGASGAAKGMDRATADYMGMLATV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066  86 MNGLAMRDALHRAFVNCRLMSAIPLNGVCDAYNWAEAISLLKSGRVVIFAAGTGNPFFTTDSAACLRGIEIEADTVIKAT 165
Cdd:COG0528   83 MNALALQDALEKLGVPTRVQSAIEMPQVAEPYIRRRAIRHLEKGRVVIFAAGTGNPYFTTDTAAALRAIEIGADVLLKAT 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 748714066 166 KVDGVFSDDPVKNPEATLYRHLSYNEIIDKELKVMDLAAFTLARDHNMPLSVFNMNKSGALKRVIMGEEEGTLISS 241
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 ...
 6-241 3.85e-153

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: 425.58  E-value: 3.85e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066   6 KPIFRRVLLKLSGEALMGDEGFGIDPKVLDRMAQEIKELVELDVEVGLVIGGGNFLRGGSLAEAGMNRVVGDHMGMLATV 85
Cdd:COG0528    3 KPKYKRVLLKLSGEALAGEGGFGIDPEVLDRIAEEIKEVVDLGVEVAIVIGGGNIFRGASGAAKGMDRATADYMGMLATV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066  86 MNGLAMRDALHRAFVNCRLMSAIPLNGVCDAYNWAEAISLLKSGRVVIFAAGTGNPFFTTDSAACLRGIEIEADTVIKAT 165
Cdd:COG0528   83 MNALALQDALEKLGVPTRVQSAIEMPQVAEPYIRRRAIRHLEKGRVVIFAAGTGNPYFTTDTAAALRAIEIGADVLLKAT 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 748714066 166 KVDGVFSDDPVKNPEATLYRHLSYNEIIDKELKVMDLAAFTLARDHNMPLSVFNMNKSGALKRVIMGEEEGTLISS 241
Cdd:COG0528  163 KVDGVYDADPKKNPDAKKYDRLTYDEVLAKGLKVMDATAFSLCRDNNLPIIVFNMNKPGNLLRAVLGEKIGTLVSG 238
AAK_UMPK-PyrH-Ec cd04254
UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) ...
 10-240 1.54e-141

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: 395.71  E-value: 1.54e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066  10 RRVLLKLSGEALMGDEGFGIDPKVLDRMAQEIKELVELDVEVGLVIGGGNFLRGGSLAEAGMNRVVGDHMGMLATVMNGL 89
Cdd:cd04254    1 KRVLLKLSGEALAGENGFGIDPEVLNRIAREIKEVVDLGVEVAIVVGGGNIFRGASAAEAGMDRATADYMGMLATVINAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066  90 AMRDALHRAFVNCRLMSAIPLNGVCDAYNWAEAISLLKSGRVVIFAAGTGNPFFTTDSAACLRGIEIEADTVIKATKVDG 169
Cdd:cd04254   81 ALQDALESLGVKTRVMSAIPMQGVAEPYIRRRAIRHLEKGRVVIFAGGTGNPFFTTDTAAALRAIEINADVILKATKVDG 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 748714066 170 VFSDDPVKNPEATLYRHLSYNEIIDKELKVMDLAAFTLARDHNMPLSVFNMNKSGALKRVIMGEEEGTLIS 240
Cdd:cd04254  161 VYDADPKKNPNAKRYDHLTYDEVLSKGLKVMDATAFTLCRDNNLPIVVFNINEPGNLLKAVKGEGVGTLIS 231
pyrH_bact TIGR02075
uridylate kinase; This protein, also called UMP kinase, converts UMP to UDP by adding a ...
 9-240 9.01e-137

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: 383.90  E-value: 9.01e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066    9 FRRVLLKLSGEALMGDEGFGIDPKVLDRMAQEIKELVELDVEVGLVIGGGNFLRGGSLAEAGMNRVVGDHMGMLATVMNG 88
Cdd:TIGR02075   1 YKRVLLKLSGEALAGESQFGIDPDRLNRIANEIKELVKMGIEVGIVIGGGNIFRGVSAAELGIDRVSADYMGMLATVING 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066   89 LAMRDALHRAFVNCRLMSAIPLNGVCDAYNWAEAISLLKSGRVVIFAAGTGNPFFTTDSAACLRGIEIEADTVIKATKVD 168
Cdd:TIGR02075  81 LALRDALEKLGLKTRVLSAISMPQICESYIRRKAIKHLEKGKVVIFSGGTGNPFFTTDTAAALRAIEINADVILKGTNVD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 748714066  169 GVFSDDPVKNPEATLYRHLSYNEIIDKELKVMDLAAFTLARDHNMPLSVFNMNKSGALKRVIMGEEEGTLIS 240
Cdd:TIGR02075 161 GVYTADPKKNKDAKKYDTITYNEALKKNLKVMDLTAFALARDNNLPIVVFNIDKPGALKKVILGKGIGTLVS 232
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 10-219 4.79e-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: 106.68  E-value: 4.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066   10 RRVLLKLSGEALMgdegfgiDPKVLDRMAQEIKELVELDVEVGLVIGGGNFLRG------------GSLAEAGMNRVVGD 77
Cdd:pfam00696   1 KRVVIKLGGSSLT-------DKERLKRLADEIAALLEEGRKLVVVHGGGAFADGllallglsprfaRLTDAETLEVATMD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066   78 HMGMLATVMNGLAMRDALHRAFVNCRLMSAIP---LNGVCDAYNWAEAISLLKSGRVVIFAAGTGNP------FFTTDSA 148
Cdd:pfam00696  74 ALGSLGERLNAALLAAGLPAVGLPAAQLLATEagfIDDVVTRIDTEALEELLEAGVVPVITGFIGIDpegelgRGSSDTL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 748714066  149 ACLRGIEIEADTVIKATKVDGVFSDDPVKNPEATLYRHLSYNEIIDKE--------LKVMDLAAFTLARDHNMPLSVFN 219
Cdd:pfam00696 154 AALLAEALGADKLIILTDVDGVYTADPRKVPDAKLIPEISYDELLELLasglatggMKVKLPAALEAARRGGIPVVIVN 232
PRK06291 PRK06291
aspartate kinase; Provisional
 125-249 2.17e-06

aspartate kinase; Provisional


Pssm-ID: 235773 [Multi-domain]  Cd Length: 465  Bit Score: 48.00  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066 125 LLKSGRV-VI--FAAGTGNPFFTT------DSAACLRGIEIEADTVIKATKVDGVFSDDPVKNPEATLYRHLSYNEIIdk 195
Cdd:PRK06291 184 LLKEGVIpVVtgFIGETEEGIITTlgrggsDYSAAIIGAALDADEIWIWTDVDGVMTTDPRIVPEARVIPKISYIEAM-- 261

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 748714066 196 EL-----KVMDLAAFTLARDHNMPLSVFNMNKSgalkrvimgEEEGTLISSQA--SDEVIK 249
Cdd:PRK06291 262 ELsyfgaKVLHPRTIEPAMEKGIPVRVKNTFNP---------EFPGTLITSDSesSKRVVK 313
 
Name Accession Description Interval E-value
PyrH COG0528
Uridylate kinase [Nucleotide transport and metabolism]; Uridylate kinase is part of the ...
 6-241 3.85e-153

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: 425.58  E-value: 3.85e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066   6 KPIFRRVLLKLSGEALMGDEGFGIDPKVLDRMAQEIKELVELDVEVGLVIGGGNFLRGGSLAEAGMNRVVGDHMGMLATV 85
Cdd:COG0528    3 KPKYKRVLLKLSGEALAGEGGFGIDPEVLDRIAEEIKEVVDLGVEVAIVIGGGNIFRGASGAAKGMDRATADYMGMLATV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066  86 MNGLAMRDALHRAFVNCRLMSAIPLNGVCDAYNWAEAISLLKSGRVVIFAAGTGNPFFTTDSAACLRGIEIEADTVIKAT 165
Cdd:COG0528   83 MNALALQDALEKLGVPTRVQSAIEMPQVAEPYIRRRAIRHLEKGRVVIFAAGTGNPYFTTDTAAALRAIEIGADVLLKAT 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 748714066 166 KVDGVFSDDPVKNPEATLYRHLSYNEIIDKELKVMDLAAFTLARDHNMPLSVFNMNKSGALKRVIMGEEEGTLISS 241
Cdd:COG0528  163 KVDGVYDADPKKNPDAKKYDRLTYDEVLAKGLKVMDATAFSLCRDNNLPIIVFNMNKPGNLLRAVLGEKIGTLVSG 238
AAK_UMPK-PyrH-Ec cd04254
UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) ...
 10-240 1.54e-141

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: 395.71  E-value: 1.54e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066  10 RRVLLKLSGEALMGDEGFGIDPKVLDRMAQEIKELVELDVEVGLVIGGGNFLRGGSLAEAGMNRVVGDHMGMLATVMNGL 89
Cdd:cd04254    1 KRVLLKLSGEALAGENGFGIDPEVLNRIAREIKEVVDLGVEVAIVVGGGNIFRGASAAEAGMDRATADYMGMLATVINAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066  90 AMRDALHRAFVNCRLMSAIPLNGVCDAYNWAEAISLLKSGRVVIFAAGTGNPFFTTDSAACLRGIEIEADTVIKATKVDG 169
Cdd:cd04254   81 ALQDALESLGVKTRVMSAIPMQGVAEPYIRRRAIRHLEKGRVVIFAGGTGNPFFTTDTAAALRAIEINADVILKATKVDG 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 748714066 170 VFSDDPVKNPEATLYRHLSYNEIIDKELKVMDLAAFTLARDHNMPLSVFNMNKSGALKRVIMGEEEGTLIS 240
Cdd:cd04254  161 VYDADPKKNPNAKRYDHLTYDEVLSKGLKVMDATAFTLCRDNNLPIVVFNINEPGNLLKAVKGEGVGTLIS 231
pyrH_bact TIGR02075
uridylate kinase; This protein, also called UMP kinase, converts UMP to UDP by adding a ...
 9-240 9.01e-137

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: 383.90  E-value: 9.01e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066    9 FRRVLLKLSGEALMGDEGFGIDPKVLDRMAQEIKELVELDVEVGLVIGGGNFLRGGSLAEAGMNRVVGDHMGMLATVMNG 88
Cdd:TIGR02075   1 YKRVLLKLSGEALAGESQFGIDPDRLNRIANEIKELVKMGIEVGIVIGGGNIFRGVSAAELGIDRVSADYMGMLATVING 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066   89 LAMRDALHRAFVNCRLMSAIPLNGVCDAYNWAEAISLLKSGRVVIFAAGTGNPFFTTDSAACLRGIEIEADTVIKATKVD 168
Cdd:TIGR02075  81 LALRDALEKLGLKTRVLSAISMPQICESYIRRKAIKHLEKGKVVIFSGGTGNPFFTTDTAAALRAIEINADVILKGTNVD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 748714066  169 GVFSDDPVKNPEATLYRHLSYNEIIDKELKVMDLAAFTLARDHNMPLSVFNMNKSGALKRVIMGEEEGTLIS 240
Cdd:TIGR02075 161 GVYTADPKKNKDAKKYDTITYNEALKKNLKVMDLTAFALARDNNLPIVVFNIDKPGALKKVILGKGIGTLVS 232
AAK_UMPK-like cd04239
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ...
 11-240 2.22e-120

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: 342.21  E-value: 2.22e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066  11 RVLLKLSGEALMGDEGfGIDPKVLDRMAQEIKELVELDVEVGLVIGGGNFLRGGSLAEAGMNRVVGDHMGMLATVMNGLA 90
Cdd:cd04239    1 RIVLKLSGEALAGEGG-GIDPEVLKEIAREIKEVVDLGVEVAIVVGGGNIARGYIAAARGMPRATADYIGMLATVMNALA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066  91 MRDALHRAFVNCRLMSAIPLNGVCDAYNWAEAISLLKSGRVVIFAAGTGNPFFTTDSAACLRGIEIEADTVIKATKVDGV 170
Cdd:cd04239   80 LQDALEKLGVKTRVMSAIPMQGVAEPYIRRRAIRHLEKGRIVIFGGGTGNPGFTTDTAAALRAEEIGADVLLKATNVDGV 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066 171 FSDDPVKNPEATLYRHLSYNEIIDKELKVMDLAAFTLARDHNMPLSVFNMNKSGALKRVIMGEEEGTLIS 240
Cdd:cd04239  160 YDADPKKNPDAKKYDRISYDELLKKGLKVMDATALTLCRRNKIPIIVFNGLKPGNLLRALKGEHVGTLIE 229
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 13-239 9.44e-36

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: 127.17  E-value: 9.44e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066  13 LLKLSGEaLMGDEGFgidpkvLDRMAQEIKELVELDVEVGLVIGGGNFLR---------GGSLAEAGMNRVVGDHMGMLA 83
Cdd:cd02115    1 VIKFGGS-SVSSEER------LRNLARILVKLASEGGRVVVVHGAGPQITdellahgelLGYARGLRITDRETDALAAMG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066  84 TVMNGLAMRDALHRAFVNCRLMSAIPL---------NGVCDAYNWAEAISLLKSGRVVIFAAGTG--------NPFFTTD 146
Cdd:cd02115   74 EGMSNLLIAAALEQHGIKAVPLDLTQAgfaspnqghVGKITKVSTDRLKSLLENGILPILSGFGGtdeketgtLGRGGSD 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066 147 SAACLRGIEIEADTVIKATKVDGVFSDDPVKNPEATLYRHLSY---NEIIDKELKVMDLAAFTLARDHNMPLSVFNMNKS 223
Cdd:cd02115  154 STAALLAAALKADRLVILTDVDGVYTADPRKVPDAKLLSELTYeeaAELAYAGAMVLKPKAADPAARAGIPVRIANTENP 233

                        250
                 ....*....|....*.
gi 748714066 224 GALkRVIMGEEEGTLI 239
Cdd:cd02115  234 GAL-ALFTPDGGGTLI 248
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 10-219 4.79e-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: 106.68  E-value: 4.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066   10 RRVLLKLSGEALMgdegfgiDPKVLDRMAQEIKELVELDVEVGLVIGGGNFLRG------------GSLAEAGMNRVVGD 77
Cdd:pfam00696   1 KRVVIKLGGSSLT-------DKERLKRLADEIAALLEEGRKLVVVHGGGAFADGllallglsprfaRLTDAETLEVATMD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066   78 HMGMLATVMNGLAMRDALHRAFVNCRLMSAIP---LNGVCDAYNWAEAISLLKSGRVVIFAAGTGNP------FFTTDSA 148
Cdd:pfam00696  74 ALGSLGERLNAALLAAGLPAVGLPAAQLLATEagfIDDVVTRIDTEALEELLEAGVVPVITGFIGIDpegelgRGSSDTL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 748714066  149 ACLRGIEIEADTVIKATKVDGVFSDDPVKNPEATLYRHLSYNEIIDKE--------LKVMDLAAFTLARDHNMPLSVFN 219
Cdd:pfam00696 154 AALLAEALGADKLIILTDVDGVYTADPRKVPDAKLIPEISYDELLELLasglatggMKVKLPAALEAARRGGIPVVIVN 232
AAK_UMPK-PyrH-Pf cd04253
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ...
 11-239 2.72e-27

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: 104.25  E-value: 2.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066  11 RVLLKLSGEALMGDegfgIDPKVLDRMAQEIKELVElDVEVGLVIGGGNFLRG--GSLAEAGMNRVVGDHMGMLATVMNG 88
Cdd:cd04253    1 RIVISLGGSVLAPE----KDADFIKEYANVLRKISD-GHKVAVVVGGGRLAREyiSVARKLGASEAFLDEIGIMATRLNA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066  89 LAMRDALHRAFvncrlmSAIPLNgvcdaYNwaEAISLLKSGRVVIfAAGTgNPFFTTDSAACLRGIEIEADTVIKATKVD 168
Cdd:cd04253   76 RLLIAALGDAY------PPVPTS-----YE--EALEAMFTGKIVV-MGGT-EPGQSTDAVAALLAERLGADLLINATNVD 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066 169 GVFSDDPVKNPEATLYRHLSYNE----IIDKELK-----VMDLAAFTLARDHNMPLSVFNMNKSGALKRVIMGEEEGTLI 239
Cdd:cd04253  141 GVYSKDPRKDPDAKKFDRLSADElidiVGKSSWKagsnePFDPLAAKIIERSGIKTIVVDGRDPENLERALKGEFVGTII 220
pyrH_arch TIGR02076
uridylate kinase, putative; This family consists of the archaeal and spirochete proteins most ...
 12-239 6.24e-25

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: 98.15  E-value: 6.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066   12 VLLKLSGEALMGDegfgIDPKVLDRMAQEIKELVElDVEVGLVIGGGNFLRG--GSLAEAGMNRVVGDHMGMLATVMNGL 89
Cdd:TIGR02076   1 IVISLGGSVLSPE----IDAEFIKEFANILRKLSD-EHKVGVVVGGGKTARRyiGVARELGASETFLDEIGIDATRLNAM 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066   90 AmrdalhrafvncrLMSAIPLngvcDAY-----NWAEAISLLKSGRVVIfaAGTGNPFFTTDSAACLRGIEIEADTVIKA 164
Cdd:TIGR02076  76 L-------------LIAALGD----DAYpkvpeNFEEALEAMSLGKIVV--MGGTHPGHTTDAVAALLAEFSKADLLINA 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066  165 TKVDGVFSDDPVKNPEATLYRHLSYNEIID----KELK-----VMDLAAFTLARDHNMPLSVFNMNKSGALKRVIMGEEE 235
Cdd:TIGR02076 137 TNVDGVYDKDPKKDPDAKKFDKLTPEELVEivgsSSVKagsneVVDPLAAKIIERSKIRTIVVNGRDPENLEKVLKGEHV 216


                  ....
gi 748714066  236 GTLI 239
Cdd:TIGR02076 217 GTII 220
AAK_UMPK-MosAB cd04255
AAK_UMPK-MosAB: This CD includes the alpha and beta subunits of the Mo storage protein (MosA ...
 41-239 1.76e-08

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: 53.55  E-value: 1.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066  41 IKELVELDVEVGLVIGGGNFLRGGSLAEAGMNrvvgdhMGMLATVMNGLAMRDALHRAFVNCRLMSAIPLNGVCDAYNWA 120
Cdd:cd04255   54 VEEIVALRPEHKLLILTGGGTRARHVYSIGLD------LGMPTGVLAKLGASVSEQNAEMLATLLAKHGGSKVGHGDLLQ 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066 121 EAISLlKSGRVVIFA-----------AGTGN-PFFTTDSAACLRGIEIEADTVIKATKVDGVFSDDPVKNPEATLYRHLS 188
Cdd:cd04255  128 LPTFL-KAGRAPVISgmppyglwehpAEEGRiPPHRTDVGAFLLAEVIGARNLIFVKDEDGLYTADPKKNKKAEFIPEIS 206

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 748714066 189 YNEIIDKELK--VMDLAAFTLARD--HNMPLSVFNMNKSGALKRVIMGEEEGTLI 239
Cdd:cd04255  207 AAELLKKDLDdlVLERPVLDLLQNarHVKEVQIVNGLVPGNLTRALRGEHVGTII 261
AAK_AK cd04234
AAK_AK: Amino Acid Kinase Superfamily (AAK), Aspartokinase (AK); this CD includes the ...
 94-240 1.77e-08

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: 53.25  E-value: 1.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066  94 ALHRAFVNCRLMSA---------IPLNGVCDAYNWAEAISLLKS-GRVVI---FAAGTGNPFFTT------D-SAACLrG 153
Cdd:cd04234   68 ALRDRGIKARSLDArqagittddNHGAARIIEISYERLKELLAEiGKVPVvtgFIGRNEDGEITTlgrggsDySAAAL-A 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066 154 IEIEADTVIKATKVDGVFSDDPVKNPEATLYRHLSYNEIIdkEL-----KVMDLAAFTLARDHNMPLSVFNMNKSgalkr 228
Cdd:cd04234  147 AALGADEVEIWTDVDGIYTADPRIVPEARLIPEISYDEAL--ELayfgaKVLHPRAVEPARKANIPIRVKNTFNP----- 219

                        170
                 ....*....|..
gi 748714066 229 vimgEEEGTLIS 240
Cdd:cd04234  220 ----EAPGTLIT 227
AAK_AKi-DapG-BS cd04260
AAK_AKi-DapG-BS: Amino Acid Kinase Superfamily (AAK), AKi-DapG; this CD includes the ...
 124-239 1.06e-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: 51.23  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066 124 SLLKSGRVVI---FAAGTGNPFFTT------DSAACLRGIEIEADTVIKATKVDGVFSDDPVKNPEATLYRHLSYNEII- 193
Cdd:cd04260  126 SALKEGDVVVvagFQGVTEDGEVTTlgrggsDTTAAALGAALNAEYVEIYTDVDGIMTADPRVVPNARILDVVSYNEVFq 205

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 748714066 194 --DKELKVMDLAAFTLARDHNMPLSVfnmnksgalkRVIMGEEEGTLI 239
Cdd:cd04260  206 maHQGAKVIHPRAVEIAMQANIPIRI----------RSTMSENPGTLI 243
AAK_AK-DapG-like cd04246
AAK_AK-DapG-like: Amino Acid Kinase Superfamily (AAK), AK-DapG-like; this CD includes the ...
 123-239 1.58e-07

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: 50.57  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066 123 ISLLKSGRVVIfAAG----TGNPFFTT------DSAACLRGIEIEADTVIKATKVDGVFSDDPVKNPEATLYRHLSYNEI 192
Cdd:cd04246  120 LEALEEGDVVV-VAGfqgvNEDGEITTlgrggsDTTAVALAAALKADRCEIYTDVDGVYTADPRIVPKARKLDVISYDEM 198

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 748714066 193 IdkEL-----KVMDLAAFTLARDHNMPLSVfnmnksgalkRVIMGEEEGTLI 239
Cdd:cd04246  199 L--EMaslgaKVLHPRSVELAKKYNVPLRV----------RSSFSENPGTLI 238
MetL1 COG0527
Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the ...
 124-246 2.10e-06

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: 48.15  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066 124 SLLKSGRVVIFA---AGTGNPFFTT------D-SAACLrGIEIEADTVIKATKVDGVFSDDPVKNPEATLYRHLSYNEII 193
Cdd:COG0527  124 ELLEEGKVVVVAgfqGVTEDGEITTlgrggsDtTAVAL-AAALKADECEIWTDVDGVYTADPRIVPDARKLPEISYEEML 202

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 748714066 194 dkEL-----KVMDLAAFTLARDHNMPLSV---FNmnksgalkrvimGEEEGTLISSQASDE 246
Cdd:COG0527  203 --ELaylgaKVLHPRAVEPAMKYNIPLRVrstFN------------PDAPGTLITAEDEME 249
PRK06291 PRK06291
aspartate kinase; Provisional
 125-249 2.17e-06

aspartate kinase; Provisional


Pssm-ID: 235773 [Multi-domain]  Cd Length: 465  Bit Score: 48.00  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066 125 LLKSGRV-VI--FAAGTGNPFFTT------DSAACLRGIEIEADTVIKATKVDGVFSDDPVKNPEATLYRHLSYNEIIdk 195
Cdd:PRK06291 184 LLKEGVIpVVtgFIGETEEGIITTlgrggsDYSAAIIGAALDADEIWIWTDVDGVMTTDPRIVPEARVIPKISYIEAM-- 261

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 748714066 196 EL-----KVMDLAAFTLARDHNMPLSVFNMNKSgalkrvimgEEEGTLISSQA--SDEVIK 249
Cdd:PRK06291 262 ELsyfgaKVLHPRTIEPAMEKGIPVRVKNTFNP---------EFPGTLITSDSesSKRVVK 313
AAK_FomA-like cd04241
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ...
 11-239 3.11e-06

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: 46.87  E-value: 3.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066  11 RVLLKLSGEALM-GDEGFGIDPKVLDRMAQEIKELVELDVEvgLVIGGGNF-----------LRGGSLAEAGMNRVvgdH 78
Cdd:cd04241    1 MIILKLGGSVITdKDRPETIREENLERIARELAEAIDEKLV--LVHGGGSFghpkakeyglpDGDGSFSAEGVAET---H 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066  79 MGMLAtvmngLAMR--DALHRAFVncrlmSAIPL---------NGVCDAYNWAEAISLLKSGRV------VIFAAGTGNP 141
Cdd:cd04241   76 EAMLE-----LNSIvvDALLEAGV-----PAVSVppssffvteNGRIVSFDLEVIKELLDRGFVpvlhgdVVLDEGGGIT 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066 142 FFTTDSAACLRGIEIEADTVIKATKVDGVFSDDPvknPEATLYRHLSYNEI--IDKELKVMD-----------LAAFTLA 208
Cdd:cd04241  146 ILSGDDIVVELAKALKPERVIFLTDVDGVYDKPP---PDAKLIPEIDVGSLedILAALGSAGtdvtggmagkiEELLELA 222

                        250       260       270
                 ....*....|....*....|....*....|.
gi 748714066 209 RdHNMPLSVFNMNKSGALKRVIMGEEEGTLI 239
Cdd:cd04241  223 R-RGIEVYIFNGDKPENLYRALLGNFIGTRI 252
AAK_AKii-LysC-BS cd04261
AAK_AKii-LysC-BS: Amino Acid Kinase Superfamily (AAK), AKii; this CD includes the N-terminal ...
 123-239 1.17e-05

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: 45.21  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066 123 ISLLKSGRVVIFA-----AGTGNpfFTT------DS-----AACLRgieieADTVIKATKVDGVFSDDPVKNPEATLYRH 186
Cdd:cd04261  120 RELLEEGDVVIVAgfqgiNEDGD--ITTlgrggsDTsavalAAALG-----ADRCEIYTDVDGVYTADPRIVPKARKLDE 192

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 748714066 187 LSYNEIIdkEL-----KVMDLAAFTLARDHNMPLSVfnmnksgalkRVIMGEEEGTLI 239
Cdd:cd04261  193 ISYDEML--EMaslgaKVLHPRSVELAKKYGVPLRV----------LSSFSEEPGTLI 238
AAK_AK-HSDH-like cd04243
AAK_AK-HSDH-like: Amino Acid Kinase Superfamily (AAK), AK-HSDH-like; this family includes the ...
 148-240 2.20e-05

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: 44.47  E-value: 2.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066 148 AACL--RGIEIEADtvikatkVDGVFSDDPVKNPEATLYRHLSYNEiidkelkVMDLAAF--------TL--ARDHNMPL 215
Cdd:cd04243  212 AALLdaEEVEIWTD-------VDGVYTADPRKVPDARLLKELSYDE-------AMELAYFgakvlhprTIqpAIRKNIPI 277

                         90       100
                 ....*....|....*....|....*.
gi 748714066 216 SVFN-MNksgalkrvimGEEEGTLIS 240
Cdd:cd04243  278 FIKNtFN----------PEAPGTLIS 293
PRK08210 PRK08210
aspartate kinase I; Reviewed
 123-246 2.29e-05

aspartate kinase I; Reviewed


Pssm-ID: 236188 [Multi-domain]  Cd Length: 403  Bit Score: 44.84  E-value: 2.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066 123 ISLLKSGRVVI---FAAGTGNPFFTT------DSAACLRGIEIEADTVIKATKVDGVFSDDPVKNPEATLYRHLSYNEII 193
Cdd:PRK08210 127 LEALEEGDVVVvagFQGVTENGDITTlgrggsDTTAAALGVALKAEYVDIYTDVDGIMTADPRIVEDARLLDVVSYNEVF 206

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 748714066 194 ---DKELKVMDLAAFTLARDHNMPLSVfnmnksgalkRVIMGEEEGTLISSQASDE 246
Cdd:PRK08210 207 qmaYQGAKVIHPRAVEIAMQANIPLRI----------RSTYSDSPGTLITSLGDAK 252
AAK_G5K_ProB cd04242
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ...
 155-239 2.91e-05

AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, in the first and controlling step of proline (and, in mammals, ornithine) biosynthesis. G5K is subject to feedback allosteric inhibition by proline or ornithine. In microorganisms and plants, proline plays an important role as an osmoprotectant and, in mammals, ornithine biosynthesis is crucial for proper ammonia detoxification, since a G5K mutation has been shown to cause human hyperammonaemia. Microbial G5K generally consists of two domains: a catalytic G5K domain and one PUA (pseudo uridine synthases and archaeosine-specific transglycosylases) domain, and some lack the PUA domain. G5K requires free Mg for activity, it is tetrameric, and it aggregates to higher forms in a proline-dependent way. G5K lacking the PUA domain remains tetrameric, active, and proline-inhibitable, but the Mg requirement and the proline-triggered aggregation are greatly diminished and abolished, respectively, and more proline is needed for inhibition. Although plant and animal G5Ks are part of a bifunctional polypeptide, delta 1-pyrroline-5-carboxylate synthetase (P5CS), composed of an N-terminal G5K (ProB) and a C-terminal glutamyl 5- phosphate reductase (G5PR; ProA); bacterial and yeast G5Ks are monofunctional single-polypeptide enzymes. In this CD, all three domain architectures are present: G5K, G5K+PUA, and G5K+G5PR.


Pssm-ID: 239775 [Multi-domain]  Cd Length: 251  Bit Score: 43.97  E-value: 2.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066 155 EIEADTVIKATKVDGVFSDDPVKNPEATLYRHLsynEIIDKELKVMD---------------LAAFTLARDHNMPLSVFN 219
Cdd:cd04242  154 LVNADLLILLSDVDGLYDKNPRENPDAKLIPEV---EEITDEIEAMAggsgssvgtggmrtkLKAARIATEAGIPVVIAN 230

                         90       100
                 ....*....|....*....|
gi 748714066 220 MNKSGALKRVIMGEEEGTLI 239
Cdd:cd04242  231 GRKPDVLLDILAGEAVGTLF 250
AAK_AK-DapDC cd04259
AAK_AK-DapDC: Amino Acid Kinase Superfamily (AAK), AK-DapDC; this CD includes the N-terminal ...
 145-240 1.80e-04

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: 41.75  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066 145 TDSAACLRGIEIEADTVIKATKVDGVFSDDPVKNPEATLYRHLSYN---EIIDKELKVMDLAAFTLARDHNMPLSVfnmn 221
Cdd:cd04259  206 SDTSAAYFAAKLQAARCEIWTDVPGLFTANPHEVPHARLLKRLDYDeaqEIATMGAKVLHPRCIPPARRANIPMVV---- 281

                         90
                 ....*....|....*....
gi 748714066 222 ksgalKRVIMGEEEGTLIS 240
Cdd:cd04259  282 -----RSTERPELSGTLIT 295
PRK06635 PRK06635
aspartate kinase; Reviewed
 148-247 2.72e-04

aspartate kinase; Reviewed


Pssm-ID: 235843 [Multi-domain]  Cd Length: 404  Bit Score: 41.64  E-value: 2.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066 148 AACLRgieieADTVIKATKVDGVFSDDPVKNPEATLYRHLSYNEIIdkEL-----KVMDLAAFTLARDHNMPLSVfnmnk 222
Cdd:PRK06635 161 AAALK-----ADECEIYTDVDGVYTTDPRIVPKARKLDKISYEEML--ELaslgaKVLHPRSVEYAKKYNVPLRV----- 228

                         90       100
                 ....*....|....*....|....*
gi 748714066 223 sgalkRVIMGEEEGTLISSQASDEV 247
Cdd:PRK06635 229 -----RSSFSDNPGTLITGEEEEIM 248
AAK_AK-HSDH cd04257
AAK_AK-HSDH: Amino Acid Kinase Superfamily (AAK), AK-HSDH; this CD includes the N-terminal ...
 148-240 6.15e-04

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: 40.26  E-value: 6.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066 148 AACLrgieiEADTVIKATKVDGVFSDDPVKNPEATLYRHLSYNEiidkelkVMDLAAF--------TL--ARDHNMPLSV 217
Cdd:cd04257  213 AALL-----DADQVEIWTDVDGVYSADPRKVKDARLLPSLSYQE-------AMELSYFgakvlhpkTIqpVAKKNIPILI 280

                         90       100
                 ....*....|....*....|...
gi 748714066 218 FNMNKSgalkrvimgEEEGTLIS 240
Cdd:cd04257  281 KNTFNP---------EAPGTLIS 294
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
145-245 7.27e-04

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 40.45  E-value: 7.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066 145 TDSAACLRGIEIEADTVIKATKVDGVFSDDPVKNPEATLYRHLSYNEIidKEL-----KVMDLAAFTLARDHNMPLSVfn 219
Cdd:PRK08961 215 SDTSAAYFAAKLGASRVEIWTDVPGMFSANPKEVPDARLLTRLDYDEA--QEIattgaKVLHPRSIKPCRDAGIPMAI-- 290

                         90       100
                 ....*....|....*....|....*.
gi 748714066 220 mnksgalKRVIMGEEEGTLISSQASD 245
Cdd:PRK08961 291 -------LDTERPDLSGTSIDGDAEP 309
ProB COG0263
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ...
 156-244 2.02e-03

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: 38.86  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066 156 IEADTVIKATKVDGVFSDDPVKNPEATLYRHLSYneiIDKELKVM---------------DLAAFTLARDHNMPLSVFNM 220
Cdd:COG0263  163 VEADLLVLLTDVDGLYDADPRKDPDAKLIPEVEE---ITPEIEAMaggagsglgtggmatKLEAARIATRAGIPTVIASG 239

                         90       100
                 ....*....|....*....|....
gi 748714066 221 NKSGALKRVIMGEEEGTLISSQAS 244
Cdd:COG0263  240 REPNVLLRILAGERVGTLFLPSGE 263
thrA PRK09436
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional
 148-246 4.17e-03

bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional


Pssm-ID: 181856 [Multi-domain]  Cd Length: 819  Bit Score: 38.21  E-value: 4.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066 148 AACLRgieieADTVIKATKVDGVFSDDPVKNPEATLYRHLSYNEiidkelkVMDLAAF--------TL--ARDHNMPLSV 217
Cdd:PRK09436 215 AACLD-----ADCCEIWTDVDGVYTADPRVVPDARLLKSLSYQE-------AMELSYFgakvlhprTIapIAQFQIPCLI 282

                         90       100
                 ....*....|....*....|....*....
gi 748714066 218 FNMNKSGAlkrvimgeeEGTLISSQASDE 246
Cdd:PRK09436 283 KNTFNPQA---------PGTLIGAESDED 302
PRK07431 PRK07431
aspartate kinase; Provisional
 124-244 4.36e-03

aspartate kinase; Provisional


Pssm-ID: 236018 [Multi-domain]  Cd Length: 587  Bit Score: 37.98  E-value: 4.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066 124 SLLKSGRVVIfAAG------TGNPFFTT------DSAACLRGIEIEADTVIKATKVDGVFSDDPVKNPEATLYRHLSYNE 191
Cdd:PRK07431 123 RHLDAGKVVV-VAGfqgislSSNLEITTlgrggsDTSAVALAAALGADACEIYTDVPGVLTTDPRLVPEAQLMDEISCDE 201

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 748714066 192 IIdkEL-----KVMDLAAFTLARDHNMPLSVfnmnksgalkRVIMGEEEGTLISSQAS 244
Cdd:PRK07431 202 ML--ELaslgaSVLHPRAVEIARNYGVPLVV----------RSSWSDAPGTLVTSPPP 247
AAK_AK-LysC-like cd04244
AAK_AK-LysC-like: Amino Acid Kinase Superfamily (AAK), AK-LysC-like; this CD includes the ...
 145-219 7.71e-03

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


Pssm-ID: 239777 [Multi-domain]  Cd Length: 298  Bit Score: 36.97  E-value: 7.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748714066 145 TDSAACLRGIEIEADTVIKATKVDGVFSDDPVKNPEATLYRHLSYNEIIdkEL-----KVMDLAAFTLARDHNMPLSVFN 219
Cdd:cd04244  209 SDYSATIIGAALDADEIWIWKDVDGVMTADPRIVPEARTIPRLSYAEAM--ELayfgaKVLHPRTVEPAMEKGIPVRVKN 286
 
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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