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Conserved domains on  [gi|2270920631|ref|WP_254272404|]
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UMP kinase [Halomicroarcula marina]

Protein Classification

amino acid kinase family protein( domain architecture ID 663)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAK super family cl00452
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 12-225 3.24e-89

Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like N-acetylglutamate kinase (NAGK), carbamate kinase (CK), aspartokinase (AK), glutamate-5-kinase (G5K) and UMP kinase (UMPK). The AAK superfamily includes kinases that phosphorylate a variety of amino acid substrates. These kinases catalyze the formation of phosphoric anhydrides, generally with a carboxylate, and use ATP as the source of the phosphoryl group; are involved in amino acid biosynthesis. Some of these kinases control the process via allosteric feed-back inhibition.


The actual alignment was detected with superfamily member TIGR02076:

Pssm-ID: 444912 [Multi-domain]  Cd Length: 221  Bit Score: 262.25  E-value: 3.24e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  12 LAPDLEPDRVADYAAAVQSLDEAgHTLGAVVGGGPTAREYIGTARELGANEIELDQLGIAVTRLNARLLIAALGGRAASP 91
Cdd:TIGR02076  10 LSPEIDAEFIKEFANILRKLSDE-HKVGVVVGGGKTARRYIGVARELGASETFLDEIGIDATRLNAMLLIAALGDDAYPK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  92 PAESYDEGRQAIRRGDIPVLGGIVAAQTTDAVAAAFAEYVDADLLVYATSVDGVYDADPKQDGDATRFDQLPAGELVDII 171
Cdd:TIGR02076  89 VPENFEEALEAMSLGKIVVMGGTHPGHTTDAVAALLAEFSKADLLINATNVDGVYDKDPKKDPDAKKFDKLTPEELVEIV 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2270920631 172 ADMEMDAGSNAPVDLLAAKVIQRSGIRTVVLDGTDPNRLVRAVeDGEFDGTEIT 225
Cdd:TIGR02076 169 GSSSVKAGSNEVVDPLAAKIIERSKIRTIVVNGRDPENLEKVL-KGEHVGTIIE 221
 
Name Accession Description Interval E-value
pyrH_arch TIGR02076
uridylate kinase, putative; This family consists of the archaeal and spirochete proteins most ...
 12-225 3.24e-89

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: 262.25  E-value: 3.24e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  12 LAPDLEPDRVADYAAAVQSLDEAgHTLGAVVGGGPTAREYIGTARELGANEIELDQLGIAVTRLNARLLIAALGGRAASP 91
Cdd:TIGR02076  10 LSPEIDAEFIKEFANILRKLSDE-HKVGVVVGGGKTARRYIGVARELGASETFLDEIGIDATRLNAMLLIAALGDDAYPK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  92 PAESYDEGRQAIRRGDIPVLGGIVAAQTTDAVAAAFAEYVDADLLVYATSVDGVYDADPKQDGDATRFDQLPAGELVDII 171
Cdd:TIGR02076  89 VPENFEEALEAMSLGKIVVMGGTHPGHTTDAVAALLAEFSKADLLINATNVDGVYDKDPKKDPDAKKFDKLTPEELVEIV 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2270920631 172 ADMEMDAGSNAPVDLLAAKVIQRSGIRTVVLDGTDPNRLVRAVeDGEFDGTEIT 225
Cdd:TIGR02076 169 GSSSVKAGSNEVVDPLAAKIIERSKIRTIVVNGRDPENLEKVL-KGEHVGTIIE 221
AAK_UMPK-PyrH-Pf cd04253
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ...
 12-225 8.82e-87

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: 256.02  E-value: 8.82e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  12 LAPDLEPDRVADYAAAVQSLDEaGHTLGAVVGGGPTAREYIGTARELGANEIELDQLGIAVTRLNARLLIAALGGRAASP 91
Cdd:cd04253    11 LAPEKDADFIKEYANVLRKISD-GHKVAVVVGGGRLAREYISVARKLGASEAFLDEIGIMATRLNARLLIAALGDAYPPV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  92 PaESYDEGRQAIRRGDIPVLGGIVAAQTTDAVAAAFAEYVDADLLVYATSVDGVYDADPKQDGDATRFDQLPAGELVDII 171
Cdd:cd04253    90 P-TSYEEALEAMFTGKIVVMGGTEPGQSTDAVAALLAERLGADLLINATNVDGVYSKDPRKDPDAKKFDRLSADELIDIV 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2270920631 172 ADMEMDAGSNAPVDLLAAKVIQRSGIRTVVLDGTDPNRLVRAVeDGEFDGTEIT 225
Cdd:cd04253   169 GKSSWKAGSNEPFDPLAAKIIERSGIKTIVVDGRDPENLERAL-KGEFVGTIIE 221
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 17-203 4.15e-26

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: 100.90  E-value: 4.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  17 EPDRVADYAAAVQSLDEAGHTLGAVVGGGPTAREYIgTARELGANEI-----------ELDQLGIAVTRLNARLLIAALG 85
Cdd:pfam00696  14 DKERLKRLADEIAALLEEGRKLVVVHGGGAFADGLL-ALLGLSPRFArltdaetlevaTMDALGSLGERLNAALLAAGLP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  86 GRAASPPA---------------ESYDEGRQAIRRGDIPVLGGIVAA--------QTTDAVAAAFAEYVDADLLVYATSV 142
Cdd:pfam00696  93 AVGLPAAQllateagfiddvvtrIDTEALEELLEAGVVPVITGFIGIdpegelgrGSSDTLAALLAEALGADKLIILTDV 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2270920631 143 DGVYDADPKQDGDATRFDQLPAGELVDIIADmEMDAGSNAPVDLLAAKVIQRSGIRTVVLD 203
Cdd:pfam00696 173 DGVYTADPRKVPDAKLIPEISYDELLELLAS-GLATGGMKVKLPAALEAARRGGIPVVIVN 232
COG1608 COG1608
Isopentenyl phosphate kinase [Lipid transport and metabolism];
41-224 5.07e-13

Isopentenyl phosphate kinase [Lipid transport and metabolism];


Pssm-ID: 441216 [Multi-domain]  Cd Length: 254  Bit Score: 66.01  E-value: 5.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  41 VVGGG----PTAREY-----IGTARELGANEIELdqlgiAVTRLNaRLLIAAL---GGRAASPPAES---YDEGR----- 100
Cdd:COG1608    43 VHGGGsfghPVAKKYglhgtLGTEDAEGVSETHR-----AMRELN-RIVVDALleaGVPAVSVPPSSfavRDNGRilsfd 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631 101 -----QAIRRGDIPVLGGIVAAQT--------TDAVAAAFAEYVDADLLVYATSVDGVYDADPKqdgdatrfdqlpaGEL 167
Cdd:COG1608   117 tepikEMLEEGFVPVLHGDVVFDAergftilsGDEIVVYLAKELKPERVGLATDVDGVYDDDPK-------------GKL 183

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631 168 VDIIADMEMDA-----GSNAPVDL---LAAKV-----IQRSGIRTVVLDGTDPNRLVRAVEDGEFDGTEI 224
Cdd:COG1608   184 IPEITRSNFDEvldalGGSAGTDVtggMAGKVeelleLAKPGVEVYIFNGNKPGNLSAALRGEEVRGTRI 253
IPPK_Arch NF040647
isopentenyl phosphate kinase;
41-224 1.37e-12

isopentenyl phosphate kinase;


Pssm-ID: 468614 [Multi-domain]  Cd Length: 258  Bit Score: 64.93  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  41 VVGGG----PTAREY-IGTA--------RELGANEIELDqlgiaVTRLNArLLIAAL---GGRAASPPAESYDEGRQA-- 102
Cdd:NF040647   43 VHGGGsfghPKAKKYgIGEGingeeferKRKGFWETQNA-----MRRLNN-LVCDALieyGIPAVSIQPSSFIRTGNKri 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631 103 -----------IRRGDIPVLGGIVAAQTT--------DAVAAAFAEYVDADLLVYATSVDGVYDADPKQDGDATRFDQlp 163
Cdd:NF040647  117 lhfdldlikkyLELGFVPVLYGDVVLDNNikygilsgDQIIPYLAKKLKPDRVILGSDVDGVYDKNPKKYPDAKLIDK-- 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2270920631 164 agelVDIIADMEMDAGSNaPVDL---LAAKV-----IQRSGIRTVVLDGTDPNRLVRAVEDGEFDGTEI 224
Cdd:NF040647  195 ----VNSLDDLESLEGTN-NVDVtggMYGKVkellkLAELGIESYIINGNKPENIYKALGGEKVIGTVI 258
PRK12314 PRK12314
gamma-glutamyl kinase; Provisional
 121-228 4.82e-09

gamma-glutamyl kinase; Provisional


Pssm-ID: 183430 [Multi-domain]  Cd Length: 266  Bit Score: 54.86  E-value: 4.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631 121 DAVAAAFAEYVDADLLVYATSVDGVYDADPKQDGDATRFdqlpagELVDIIAD--MEMDAGSNAPV-------DLLAAKV 191
Cdd:PRK12314  157 DRLSAIVAKLVKADLLIILSDIDGLYDKNPRINPDAKLR------SEVTEITEeiLALAGGAGSKFgtggmvtKLKAAKF 230

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2270920631 192 IQRSGIRTVVLDGTDPnRLVRAVEDGEFDGTEITPEG 228
Cdd:PRK12314  231 LMEAGIKMVLANGFNP-SDILDFLEGESIGTLFAPKK 266
 
Name Accession Description Interval E-value
pyrH_arch TIGR02076
uridylate kinase, putative; This family consists of the archaeal and spirochete proteins most ...
 12-225 3.24e-89

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: 262.25  E-value: 3.24e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  12 LAPDLEPDRVADYAAAVQSLDEAgHTLGAVVGGGPTAREYIGTARELGANEIELDQLGIAVTRLNARLLIAALGGRAASP 91
Cdd:TIGR02076  10 LSPEIDAEFIKEFANILRKLSDE-HKVGVVVGGGKTARRYIGVARELGASETFLDEIGIDATRLNAMLLIAALGDDAYPK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  92 PAESYDEGRQAIRRGDIPVLGGIVAAQTTDAVAAAFAEYVDADLLVYATSVDGVYDADPKQDGDATRFDQLPAGELVDII 171
Cdd:TIGR02076  89 VPENFEEALEAMSLGKIVVMGGTHPGHTTDAVAALLAEFSKADLLINATNVDGVYDKDPKKDPDAKKFDKLTPEELVEIV 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2270920631 172 ADMEMDAGSNAPVDLLAAKVIQRSGIRTVVLDGTDPNRLVRAVeDGEFDGTEIT 225
Cdd:TIGR02076 169 GSSSVKAGSNEVVDPLAAKIIERSKIRTIVVNGRDPENLEKVL-KGEHVGTIIE 221
AAK_UMPK-PyrH-Pf cd04253
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ...
 12-225 8.82e-87

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: 256.02  E-value: 8.82e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  12 LAPDLEPDRVADYAAAVQSLDEaGHTLGAVVGGGPTAREYIGTARELGANEIELDQLGIAVTRLNARLLIAALGGRAASP 91
Cdd:cd04253    11 LAPEKDADFIKEYANVLRKISD-GHKVAVVVGGGRLAREYISVARKLGASEAFLDEIGIMATRLNARLLIAALGDAYPPV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  92 PaESYDEGRQAIRRGDIPVLGGIVAAQTTDAVAAAFAEYVDADLLVYATSVDGVYDADPKQDGDATRFDQLPAGELVDII 171
Cdd:cd04253    90 P-TSYEEALEAMFTGKIVVMGGTEPGQSTDAVAALLAERLGADLLINATNVDGVYSKDPRKDPDAKKFDRLSADELIDIV 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2270920631 172 ADMEMDAGSNAPVDLLAAKVIQRSGIRTVVLDGTDPNRLVRAVeDGEFDGTEIT 225
Cdd:cd04253   169 GKSSWKAGSNEPFDPLAAKIIERSGIKTIVVDGRDPENLERAL-KGEFVGTIIE 221
AAK_UMPK-like cd04239
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ...
 14-225 1.18e-54

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: 174.65  E-value: 1.18e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  14 PDLEPDRVADYAAAVQSLDEAGHTLGAVVGGGPTAREYIGTARelGANEIELDQLGIAVTRLNARLLIAALGG-----RA 88
Cdd:cd04239    16 GGIDPEVLKEIAREIKEVVDLGVEVAIVVGGGNIARGYIAAAR--GMPRATADYIGMLATVMNALALQDALEKlgvktRV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  89 ASP-----PAESYDEgRQAIR---RGDIPVLGGIVA--AQTTDAVAAAFAEYVDADLLVYATSVDGVYDADPKQDGDATR 158
Cdd:cd04239    94 MSAipmqgVAEPYIR-RRAIRhleKGRIVIFGGGTGnpGFTTDTAAALRAEEIGADVLLKATNVDGVYDADPKKNPDAKK 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2270920631 159 FDQLPAGELVDIIAdmemdagsnAPVDLLAAKVIQRSGIRTVVLDGTDPNRLVRAVEdGEFDGTEIT 225
Cdd:cd04239   173 YDRISYDELLKKGL---------KVMDATALTLCRRNKIPIIVFNGLKPGNLLRALK-GEHVGTLIE 229
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 17-203 4.15e-26

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: 100.90  E-value: 4.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  17 EPDRVADYAAAVQSLDEAGHTLGAVVGGGPTAREYIgTARELGANEI-----------ELDQLGIAVTRLNARLLIAALG 85
Cdd:pfam00696  14 DKERLKRLADEIAALLEEGRKLVVVHGGGAFADGLL-ALLGLSPRFArltdaetlevaTMDALGSLGERLNAALLAAGLP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  86 GRAASPPA---------------ESYDEGRQAIRRGDIPVLGGIVAA--------QTTDAVAAAFAEYVDADLLVYATSV 142
Cdd:pfam00696  93 AVGLPAAQllateagfiddvvtrIDTEALEELLEAGVVPVITGFIGIdpegelgrGSSDTLAALLAEALGADKLIILTDV 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2270920631 143 DGVYDADPKQDGDATRFDQLPAGELVDIIADmEMDAGSNAPVDLLAAKVIQRSGIRTVVLD 203
Cdd:pfam00696 173 DGVYTADPRKVPDAKLIPEISYDELLELLAS-GLATGGMKVKLPAALEAARRGGIPVVIVN 232
pyrH_bact TIGR02075
uridylate kinase; This protein, also called UMP kinase, converts UMP to UDP by adding a ...
 18-225 5.50e-18

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: 79.59  E-value: 5.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  18 PDRVADYAAAVQSLDEAGHTLGAVVGGGPTAReyiG-TARELGANEIELDQLGIAVTRLNARLLIAAL-----GGRAASP 91
Cdd:TIGR02075  23 PDRLNRIANEIKELVKMGIEVGIVIGGGNIFR---GvSAAELGIDRVSADYMGMLATVINGLALRDALeklglKTRVLSA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  92 -----PAESYDEGR--QAIRRGDIPVLGGIVAAQ--TTDAVAAAFAEYVDADLLVYATSVDGVYDADPKQDGDATRFDQL 162
Cdd:TIGR02075 100 ismpqICESYIRRKaiKHLEKGKVVIFSGGTGNPffTTDTAAALRAIEINADVILKGTNVDGVYTADPKKNKDAKKYDTI 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2270920631 163 PAGE-LVDIIADMemdagsnapvDLLAAKVIQRSGIRTVVLDGTDPNRLVRAVEdGEFDGTEIT 225
Cdd:TIGR02075 180 TYNEaLKKNLKVM----------DLTAFALARDNNLPIVVFNIDKPGALKKVIL-GKGIGTLVS 232
AAK_UMPK-PyrH-Ec cd04254
UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) ...
 18-225 4.92e-17

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: 76.76  E-value: 4.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  18 PDRVADYAAAVQSLDEAGHTLGAVVGGGPTAREYigTARELGANEIELDQLGIAVTRLNARLLIAALGG-----RAAS-- 90
Cdd:cd04254    22 PEVLNRIAREIKEVVDLGVEVAIVVGGGNIFRGA--SAAEAGMDRATADYMGMLATVINALALQDALESlgvktRVMSai 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  91 ---PPAESYDEgRQAIR---RGDIPVLGGIVAAQ--TTDAVAAAFAEYVDADLLVYATSVDGVYDADPKQDGDATRFDQL 162
Cdd:cd04254   100 pmqGVAEPYIR-RRAIRhleKGRVVIFAGGTGNPffTTDTAAALRAIEINADVILKATKVDGVYDADPKKNPNAKRYDHL 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2270920631 163 PAGELvdIIADME-MDAGsnapvdllAAKVIQRSGIRTVVLDGTDPNRLVRAVEdGEFDGTEIT 225
Cdd:cd04254   179 TYDEV--LSKGLKvMDAT--------AFTLCRDNNLPIVVFNINEPGNLLKAVK-GEGVGTLIS 231
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 19-224 2.34e-16

Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like N-acetylglutamate kinase (NAGK), carbamate kinase (CK), aspartokinase (AK), glutamate-5-kinase (G5K) and UMP kinase (UMPK). The AAK superfamily includes kinases that phosphorylate a variety of amino acid substrates. These kinases catalyze the formation of phosphoric anhydrides, generally with a carboxylate, and use ATP as the source of the phosphoryl group; are involved in amino acid biosynthesis. Some of these kinases control the process via allosteric feed-back inhibition.


Pssm-ID: 239033 [Multi-domain]  Cd Length: 248  Bit Score: 75.17  E-value: 2.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  19 DRVADYAAAVQSLDEAGHTLGAVVGGGPTAREYI-------GTARELGANEIELDQLGIAVTRLNARLLIAAL---GGRA 88
Cdd:cd02115    13 ERLRNLARILVKLASEGGRVVVVHGAGPQITDELlahgellGYARGLRITDRETDALAAMGEGMSNLLIAAALeqhGIKA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  89 ------------------ASPPAESYDEGRQAIRRGDIPVLGGI----------VAAQTTDAVAAAFAEYVDADLLVYAT 140
Cdd:cd02115    93 vpldltqagfaspnqghvGKITKVSTDRLKSLLENGILPILSGFggtdeketgtLGRGGSDSTAALLAAALKADRLVILT 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631 141 SVDGVYDADPKQDGDATRFDQLPAGELVDIIADMEMdagsnaPVDLLAAKVIQRSGIRTVVLDGTDPNRLVRAVEDGEfd 220
Cdd:cd02115   173 DVDGVYTADPRKVPDAKLLSELTYEEAAELAYAGAM------VLKPKAADPAARAGIPVRIANTENPGALALFTPDGG-- 244


                  ....
gi 2270920631 221 GTEI 224
Cdd:cd02115   245 GTLI 248
AAK_G5K_ProB cd04242
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ...
 121-222 6.79e-14

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: 68.62  E-value: 6.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631 121 DAVAAAFAEYVDADLLVYATSVDGVYDADPKQDGDATRFDqlpagELVDIIADME-MDAGSNAPVD-------LLAAKVI 192
Cdd:cd04242   145 DRLSALVAGLVNADLLILLSDVDGLYDKNPRENPDAKLIP-----EVEEITDEIEaMAGGSGSSVGtggmrtkLKAARIA 219

                          90       100       110
                  ....*....|....*....|....*....|
gi 2270920631 193 QRSGIRTVVLDGTDPNRLVRAVEdGEFDGT 222
Cdd:cd04242   220 TEAGIPVVIANGRKPDVLLDILA-GEAVGT 248
COG1608 COG1608
Isopentenyl phosphate kinase [Lipid transport and metabolism];
41-224 5.07e-13

Isopentenyl phosphate kinase [Lipid transport and metabolism];


Pssm-ID: 441216 [Multi-domain]  Cd Length: 254  Bit Score: 66.01  E-value: 5.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  41 VVGGG----PTAREY-----IGTARELGANEIELdqlgiAVTRLNaRLLIAAL---GGRAASPPAES---YDEGR----- 100
Cdd:COG1608    43 VHGGGsfghPVAKKYglhgtLGTEDAEGVSETHR-----AMRELN-RIVVDALleaGVPAVSVPPSSfavRDNGRilsfd 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631 101 -----QAIRRGDIPVLGGIVAAQT--------TDAVAAAFAEYVDADLLVYATSVDGVYDADPKqdgdatrfdqlpaGEL 167
Cdd:COG1608   117 tepikEMLEEGFVPVLHGDVVFDAergftilsGDEIVVYLAKELKPERVGLATDVDGVYDDDPK-------------GKL 183

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631 168 VDIIADMEMDA-----GSNAPVDL---LAAKV-----IQRSGIRTVVLDGTDPNRLVRAVEDGEFDGTEI 224
Cdd:COG1608   184 IPEITRSNFDEvldalGGSAGTDVtggMAGKVeelleLAKPGVEVYIFNGNKPGNLSAALRGEEVRGTRI 253
ProB COG0263
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ...
 121-228 6.66e-13

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: 66.60  E-value: 6.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631 121 DAVAAAFAEYVDADLLVYATSVDGVYDADPKQDGDATRFDQLPAGElvDIIADMEMDAGSNapV-------DLLAAKVIQ 193
Cdd:COG0263   153 DRLAALVANLVEADLLVLLTDVDGLYDADPRKDPDAKLIPEVEEIT--PEIEAMAGGAGSG--LgtggmatKLEAARIAT 228

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2270920631 194 RSGIRTVVLDGTDPNRLVRAVeDGEFDGTEITPEG 228
Cdd:COG0263   229 RAGIPTVIASGREPNVLLRIL-AGERVGTLFLPSG 262
IPPK_Arch NF040647
isopentenyl phosphate kinase;
41-224 1.37e-12

isopentenyl phosphate kinase;


Pssm-ID: 468614 [Multi-domain]  Cd Length: 258  Bit Score: 64.93  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  41 VVGGG----PTAREY-IGTA--------RELGANEIELDqlgiaVTRLNArLLIAAL---GGRAASPPAESYDEGRQA-- 102
Cdd:NF040647   43 VHGGGsfghPKAKKYgIGEGingeeferKRKGFWETQNA-----MRRLNN-LVCDALieyGIPAVSIQPSSFIRTGNKri 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631 103 -----------IRRGDIPVLGGIVAAQTT--------DAVAAAFAEYVDADLLVYATSVDGVYDADPKQDGDATRFDQlp 163
Cdd:NF040647  117 lhfdldlikkyLELGFVPVLYGDVVLDNNikygilsgDQIIPYLAKKLKPDRVILGSDVDGVYDKNPKKYPDAKLIDK-- 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2270920631 164 agelVDIIADMEMDAGSNaPVDL---LAAKV-----IQRSGIRTVVLDGTDPNRLVRAVEDGEFDGTEI 224
Cdd:NF040647  195 ----VNSLDDLESLEGTN-NVDVtggMYGKVkellkLAELGIESYIINGNKPENIYKALGGEKVIGTVI 258
PyrH COG0528
Uridylate kinase [Nucleotide transport and metabolism]; Uridylate kinase is part of the ...
 18-226 1.38e-12

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: 64.65  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  18 PDRVADYAAAVQSLDEAGHTLGAVVGGGPTAReyiG-TARELGANEIELDQLGIAVTRLNARLLIAAL---GGRAA---- 89
Cdd:COG0528    28 PEVLDRIAEEIKEVVDLGVEVAIVIGGGNIFR---GaSGAAKGMDRATADYMGMLATVMNALALQDALeklGVPTRvqsa 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  90 ---SPPAESYDEgRQAIR---RGDIpVlggIVAAQT------TDAVAAAFAEYVDADLLVYATSVDGVYDADPKQDGDAT 157
Cdd:COG0528   105 iemPQVAEPYIR-RRAIRhleKGRV-V---IFAAGTgnpyftTDTAAALRAIEIGADVLLKATKVDGVYDADPKKNPDAK 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2270920631 158 RFDQLPAGElvdIIAD----MEMDAGSnapvdlLAakviQRSGIRTVVLDGTDPNRLVRAVEdGEFDGTEITP 226
Cdd:COG0528   180 KYDRLTYDE---VLAKglkvMDATAFS------LC----RDNNLPIIVFNMNKPGNLLRAVL-GEKIGTLVSG 238
AAK_FomA-like cd04241
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ...
 41-224 3.12e-09

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: 55.34  E-value: 3.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  41 VVGGG----PTAREY-----IGTARELGANEIELdqlgiAVTRLNARL------------------LIAALGGRAASPPA 93
Cdd:cd04241    43 VHGGGsfghPKAKEYglpdgDGSFSAEGVAETHE-----AMLELNSIVvdalleagvpavsvppssFFVTENGRIVSFDL 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  94 ESYDEgrqAIRRGDIPVLGGIVAAQTT--------DAVAAAFAEYVDADLLVYATSVDGVYDADPkqdGDATRFDQLPAG 165
Cdd:cd04241   118 EVIKE---LLDRGFVPVLHGDVVLDEGggitilsgDDIVVELAKALKPERVIFLTDVDGVYDKPP---PDAKLIPEIDVG 191

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2270920631 166 ELVDIIADMEMDAgsnapVD--------LLAAKVIQRSGIRTVVLDGTDPNRLVRAVeDGEFDGTEI 224
Cdd:cd04241   192 SLEDILAALGSAG-----TDvtggmagkIEELLELARRGIEVYIFNGDKPENLYRAL-LGNFIGTRI 252
PRK12314 PRK12314
gamma-glutamyl kinase; Provisional
 121-228 4.82e-09

gamma-glutamyl kinase; Provisional


Pssm-ID: 183430 [Multi-domain]  Cd Length: 266  Bit Score: 54.86  E-value: 4.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631 121 DAVAAAFAEYVDADLLVYATSVDGVYDADPKQDGDATRFdqlpagELVDIIAD--MEMDAGSNAPV-------DLLAAKV 191
Cdd:PRK12314  157 DRLSAIVAKLVKADLLIILSDIDGLYDKNPRINPDAKLR------SEVTEITEeiLALAGGAGSKFgtggmvtKLKAAKF 230

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2270920631 192 IQRSGIRTVVLDGTDPnRLVRAVEDGEFDGTEITPEG 228
Cdd:PRK12314  231 LMEAGIKMVLANGFNP-SDILDFLEGESIGTLFAPKK 266
AAK_UMPK-MosAB cd04255
AAK_UMPK-MosAB: This CD includes the alpha and beta subunits of the Mo storage protein (MosA ...
 36-225 2.62e-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: 52.78  E-value: 2.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  36 HTLGAVVGGGPTAREYIGTARELGANEIELDQLGIAVTRLNARLLIAAL---GGRAASPP-----AESYDEGRQAIRRG- 106
Cdd:cd04255    64 HKLLILTGGGTRARHVYSIGLDLGMPTGVLAKLGASVSEQNAEMLATLLakhGGSKVGHGdllqlPTFLKAGRAPVISGm 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631 107 ------DIPVLGGIVAAQTTDAVAAAFAEYVDADLLVYATSVDGVYDADPKQDGDATRFDQLPAGELvdiiADMEMDags 180
Cdd:cd04255   144 ppyglwEHPAEEGRIPPHRTDVGAFLLAEVIGARNLIFVKDEDGLYTADPKKNKKAEFIPEISAAEL----LKKDLD--- 216

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2270920631 181 NAPVDLLAAKVIQRS-GIRTV-VLDGTDPNRLVRAVEdGEFDGTEIT 225
Cdd:cd04255   217 DLVLERPVLDLLQNArHVKEVqIVNGLVPGNLTRALR-GEHVGTIIR 262
AAK_AK-HSDH-like cd04243
AAK_AK-HSDH-like: Amino Acid Kinase Superfamily (AAK), AK-HSDH-like; this family includes the ...
 65-166 2.79e-06

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


Pssm-ID: 239776 [Multi-domain]  Cd Length: 293  Bit Score: 47.16  E-value: 2.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  65 LDQLGIAVTRLNARLLIAALGGraASPPAESYDEGRQAIRR-----GDIPVLGGIVAA----QTT-------DAVAAAFA 128
Cdd:cd04243   135 LQEQGLPAAWLDARELLLTDDG--FLNAVVDLKLSKERLAQllaehGKVVVTQGFIASnedgETTtlgrggsDYSAALLA 212

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2270920631 129 EYVDADLLVYATSVDGVYDADPKQDGDATRFDQLPAGE 166
Cdd:cd04243   213 ALLDAEEVEIWTDVDGVYTADPRKVPDARLLKELSYDE 250
AAK_AK-HSDH cd04257
AAK_AK-HSDH: Amino Acid Kinase Superfamily (AAK), AK-HSDH; this CD includes the N-terminal ...
 65-166 6.00e-06

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: 46.03  E-value: 6.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  65 LDQLGIAVTRLNARLLIAALGGraASPPAESYDEGRQAIRR-----GDIPVLGGIVAAQ-----TT------DAVAAAFA 128
Cdd:cd04257   136 LNQQGLDAAWIDARELIVTDGG--YLNAVVDIELSKERIKAwfssnGKVIVVTGFIASNpqgetTTlgrngsDYSAAILA 213

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2270920631 129 EYVDADLLVYATSVDGVYDADPKQDGDATRFDQLPAGE 166
Cdd:cd04257   214 ALLDADQVEIWTDVDGVYSADPRKVKDARLLPSLSYQE 251
AAK_UC cd04240
AAK_UC: Uncharacterized (UC) amino acid kinase-like proteins found mainly in archaea and a few ...
 79-224 1.24e-05

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


Pssm-ID: 239773 [Multi-domain]  Cd Length: 203  Bit Score: 44.66  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  79 LLIAALGGRAAsppAESYDEGRQAIRRGDIPVL--GGIVAAQ---------TTDAVAAAFAEYVDADLLVYATSVDGVYD 147
Cdd:cd04240    67 YLLADLEPRLV---ARTLAELTDVLERGKIAILlpYRLLLDTdplphswevTSDSIAAWLAKKLGAKRLVIVTDVDGIYE 143

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2270920631 148 adpkqdgdatrfdqlPAGELVDIIADMEMDAGSNapVDLLAAKVIQRSGIRTVVLDGTDPNRLVRAVEDGEFDGTEI 224
Cdd:cd04240   144 ---------------KDGKLVNEIAAAELLGETS--VDPAFPRLLTKYGIRCYVVNGDDPERVLAALRGREGVGTRI 203
asp_kinases TIGR00657
aspartate kinase; Aspartate kinase catalyzes a first step in the biosynthesis from Asp of Lys ...
 86-227 4.41e-05

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: 43.88  E-value: 4.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  86 GRAASPPAESYDEGRQAIRRGDIPVLGGIVAAQ-----TT------DAVAAAFAEYVDADLLVYATSVDGVYDADPKQDG 154
Cdd:TIGR00657 148 GRARVIIEILTERLEPLLEEGIIPVVAGFQGATekgetTTlgrggsDYTAALLAAALKADECEIYTDVDGIYTTDPRIVP 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631 155 DATRFDQLPAGELvdiiadMEMDAgsnapvdlLAAKVIQ--------RSGIRTVVLDGTDPnrlvravedgEFDGTEITP 226
Cdd:TIGR00657 228 DARRIDEISYEEM------LELAS--------FGAKVLHprtlepamRAKIPIVVKSTFNP----------EAPGTLIVA 283


                  .
gi 2270920631 227 E 227
Cdd:TIGR00657 284 S 284
AAK_P5CS_ProBA cd04256
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ...
 88-154 8.95e-05

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: 42.42  E-value: 8.95e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2270920631  88 AASPPAESYDEgrqairrgdipvLGGIVAAQTTDAVAAAFAEYVDADLLVYATSVDGVYDADPKQDG 154
Cdd:cd04256   160 AVSPPPEPDED------------LQGVISIKDNDSLAARLAVELKADLLILLSDVDGLYDGPPGSDD 214
AAK_AK cd04234
AAK_AK: Amino Acid Kinase Superfamily (AAK), Aspartokinase (AK); this CD includes the ...
 65-225 1.51e-04

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: 41.69  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  65 LDQLGIAVTRLNARLLIAALGGRAASPPAESYDEGR---QAIRRGDIPVLGGIVAAQ-----TT------DAVAAAFAEY 130
Cdd:cd04234    69 LRDRGIKARSLDARQAGITTDDNHGAARIIEISYERlkeLLAEIGKVPVVTGFIGRNedgeiTTlgrggsDYSAAALAAA 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631 131 VDADLLVYATSVDGVYDADPKQDGDATRFDQLPAGELvdiiadMEM-DAGsnapvdllaAKVIQRsgiRTVV-LDGTDPN 208
Cdd:cd04234   149 LGADEVEIWTDVDGIYTADPRIVPEARLIPEISYDEA------LELaYFG---------AKVLHP---RAVEpARKANIP 210

                         170
                  ....*....|....*..
gi 2270920631 209 RLVRAVEDGEFDGTEIT 225
Cdd:cd04234   211 IRVKNTFNPEAPGTLIT 227
ArgB COG0548
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ...
 100-225 2.48e-04

N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440314 [Multi-domain]  Cd Length: 283  Bit Score: 41.17  E-value: 2.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631 100 RQAIRRGDIPVLGGI----------VAAqttDAVAAAFAEYVDADLLVYATSVDGVYDAdpkqdgDATRFDQLPAGELVD 169
Cdd:COG0548   158 RALLDAGYIPVISPIgysptgevynINA---DTVAGAIAAALKAEKLILLTDVPGVLDD------PGSLISELTAAEAEE 228

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2270920631 170 IIADMEMDAGsnapvdlLAAKV---IQ--RSGI-RTVVLDGTDPNRLVRAVEDGEFDGTEIT 225
Cdd:COG0548   229 LIADGVISGG-------MIPKLeaaLDavRGGVkRVHIIDGRVPHALLLELFTDDGIGTMIV 283
PRK12454 PRK12454
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
 106-226 4.18e-04

carbamate kinase-like carbamoyl phosphate synthetase; Reviewed


Pssm-ID: 183535  Cd Length: 313  Bit Score: 40.37  E-value: 4.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631 106 GDIPV------LGGIVAAQTTDAVAAAFAEYVDADLLVYATSVDGVYDADPKQDGDAtrFDQLPAGELVDIIADMEMDAG 179
Cdd:PRK12454  194 GGIPVieedgeLKGVEAVIDKDLASELLAEELNADIFIILTDVEKVYLNYGKPDQKP--LDKVTVEEAKKYYEEGHFKAG 271

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2270920631 180 SNAPVDLLAAKVIQRSGIRTVVldgTDPNRLVRAVEdGEfDGTEITP 226
Cdd:PRK12454  272 SMGPKILAAIRFVENGGKRAII---ASLEKAVEALE-GK-TGTRIIP 313
thrA PRK09436
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional
 65-162 4.82e-04

bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional


Pssm-ID: 181856 [Multi-domain]  Cd Length: 819  Bit Score: 40.91  E-value: 4.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631  65 LDQLGIAVTRLNARLLIAALGGraaspPAES---YDEGRQAIRR-----GDIPVLGGIVAAQ-----TT------DAVAA 125
Cdd:PRK09436  138 LEARGHDVTVIDPRELLLADGH-----YLEStvdIAESTRRIAAsfipaDHVILMPGFTAGNekgelVTlgrngsDYSAA 212

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2270920631 126 AFAEYVDADLLVYATSVDGVYDADPKQDGDATRFDQL 162
Cdd:PRK09436  213 ILAACLDADCCEIWTDVDGVYTADPRVVPDARLLKSL 249
PRK00942 PRK00942
acetylglutamate kinase; Provisional
 121-227 1.51e-03

acetylglutamate kinase; Provisional


Pssm-ID: 234869 [Multi-domain]  Cd Length: 283  Bit Score: 38.94  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631 121 DAVAAAFAEYVDADLLVYATSVDGVYdadpkqDGDATRFDQLPAGELVDIIADMEMDAGSNapVDLLAAKVIQRSGIRTV 200
Cdd:PRK00942  184 DTAAGAIAAALGAEKLILLTDVPGVL------DDKGQLISELTASEAEELIEDGVITGGMI--PKVEAALDAARGGVRSV 255

                          90       100
                  ....*....|....*....|....*...
gi 2270920631 201 -VLDGTDPNRLVRAVEDGEFDGTEITPE 227
Cdd:PRK00942  256 hIIDGRVPHALLLELFTDEGIGTMIVPD 283
AAK_NAGK-like cd04238
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ...
 121-224 3.20e-03

AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the Escherichia coli and Pseudomonas aeruginosa type NAGKs which catalyze the phosphorylation of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in bacteria and photosynthetic organisms using either the acetylated, noncyclic (NC), or non-acetylated, cyclic (C) route of ornithine biosynthesis. Also included in this CD is a distinct group of uncharacterized (UC) bacterial and archeal NAGKs. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239771 [Multi-domain]  Cd Length: 256  Bit Score: 37.87  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631 121 DAVAAAFAEYVDADLLVYATSVDGVYDAdpkqdgDATRFDQLPAGELVDIIADMEMDAGSNAPVDlLAAKVIQRSGIRTV 200
Cdd:cd04238   160 DTAAGAIAAALKAEKLILLTDVPGVLDD------PGSLISELTPKEAEELIEDGVISGGMIPKVE-AALEALEGGVRKVH 232

                          90       100
                  ....*....|....*....|....
gi 2270920631 201 VLDGTDPNRLVRAVEDGEFDGTEI 224
Cdd:cd04238   233 IIDGRVPHSLLLELFTDEGIGTMI 256
AAK_AKii-LysC-BS cd04261
AAK_AKii-LysC-BS: Amino Acid Kinase Superfamily (AAK), AKii; this CD includes the N-terminal ...
 100-195 5.62e-03

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: 36.74  E-value: 5.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270920631 100 RQAIRRGDIPVLGGI--VAAQ---TT------DAVAAAFAEYVDADLLVYATSVDGVYDADPKQDGDATRFDQLPAGELv 168
Cdd:cd04261   120 RELLEEGDVVIVAGFqgINEDgdiTTlgrggsDTSAVALAAALGADRCEIYTDVDGVYTADPRIVPKARKLDEISYDEM- 198

                          90       100
                  ....*....|....*....|....*...
gi 2270920631 169 diiadMEMDAgsnapvdlLAAKVIQ-RS 195
Cdd:cd04261   199 -----LEMAS--------LGAKVLHpRS 213
 
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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