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Conserved domains on  [gi|10639249|emb|CAC11251|]
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gamma-glutamyl kinase related protein [Thermoplasma acidophilum]

Protein Classification

COG1608 family protein( domain architecture ID 10004056)

COG1608 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IPPK_Arch NF040647
isopentenyl phosphate kinase;
2-244 1.70e-100

isopentenyl phosphate kinase;


:

Pssm-ID: 468614 [Multi-domain]  Cd Length: 258  Bit Score: 292.97  E-value: 1.70e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249    2 MILKIGGSVITDKSAYRTARTYAIRSIVKVLSGI--EDLVCVVHGGGSFGHIKAMEFGLP----GPKNPRSSIGYSIVHR 75
Cdd:NF040647   1 IILKLGGSVITDKDIYPKIDWDNLERIAKEISNAldEDKLIIVHGGGSFGHPKAKKYGIGeginGEEFERKRKGFWETQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249   76 DMENLDLMVIDAMIEMGMRPISVPISALRYDGR-----FDYTPLIRYIDAGFVPVSYGDVYIKDEHSYGIYSGDDIMADM 150
Cdd:NF040647  81 AMRRLNNLVCDALIEYGIPAVSIQPSSFIRTGNkrilhFDLDLIKKYLELGFVPVLYGDVVLDNNIKYGILSGDQIIPYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249  151 AELLKPDVAVFLTDVDGIYSKDPKRNPDAVLLRDIDTNI---TFDRVQN-DVTGGIGKKFESMVKMkSSVKNGVYLINGN 226
Cdd:NF040647 161 AKKLKPDRVILGSDVDGVYDKNPKKYPDAKLIDKVNSLDdleSLEGTNNvDVTGGMYGKVKELLKL-AELGIESYIINGN 239

                        250
                 ....*....|....*....
gi 10639249  227 HPERIG-DIGKESFIGTVI 244
Cdd:NF040647 240 KPENIYkALGGEKVIGTVI 258
 
Name Accession Description Interval E-value
IPPK_Arch NF040647
isopentenyl phosphate kinase;
2-244 1.70e-100

isopentenyl phosphate kinase;


Pssm-ID: 468614 [Multi-domain]  Cd Length: 258  Bit Score: 292.97  E-value: 1.70e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249    2 MILKIGGSVITDKSAYRTARTYAIRSIVKVLSGI--EDLVCVVHGGGSFGHIKAMEFGLP----GPKNPRSSIGYSIVHR 75
Cdd:NF040647   1 IILKLGGSVITDKDIYPKIDWDNLERIAKEISNAldEDKLIIVHGGGSFGHPKAKKYGIGeginGEEFERKRKGFWETQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249   76 DMENLDLMVIDAMIEMGMRPISVPISALRYDGR-----FDYTPLIRYIDAGFVPVSYGDVYIKDEHSYGIYSGDDIMADM 150
Cdd:NF040647  81 AMRRLNNLVCDALIEYGIPAVSIQPSSFIRTGNkrilhFDLDLIKKYLELGFVPVLYGDVVLDNNIKYGILSGDQIIPYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249  151 AELLKPDVAVFLTDVDGIYSKDPKRNPDAVLLRDIDTNI---TFDRVQN-DVTGGIGKKFESMVKMkSSVKNGVYLINGN 226
Cdd:NF040647 161 AKKLKPDRVILGSDVDGVYDKNPKKYPDAKLIDKVNSLDdleSLEGTNNvDVTGGMYGKVKELLKL-AELGIESYIINGN 239

                        250
                 ....*....|....*....
gi 10639249  227 HPERIG-DIGKESFIGTVI 244
Cdd:NF040647 240 KPENIYkALGGEKVIGTVI 258
AAK_FomA-like cd04241
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ...
 1-244 3.48e-92

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: 271.44  E-value: 3.48e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249   1 MMILKIGGSVITDKSAYRTARTYAIRSIVKVLSG-IEDLVCVVHGGGSFGHIKAMEFGLPGPKNPRSSIGYSIVHRDMEN 79
Cdd:cd04241   1 MIILKLGGSVITDKDRPETIREENLERIARELAEaIDEKLVLVHGGGSFGHPKAKEYGLPDGDGSFSAEGVAETHEAMLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249  80 LDLMVIDAMIEMGMRPISVPISAL-----RYDGRFDYTPLIRYIDAGFVPVSYGDVYIKDEHSYGIYSGDDIMADMAELL 154
Cdd:cd04241  81 LNSIVVDALLEAGVPAVSVPPSSFfvtenGRIVSFDLEVIKELLDRGFVPVLHGDVVLDEGGGITILSGDDIVVELAKAL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249 155 KPDVAVFLTDVDGIYSKDPkrnPDAVLLRDIDT-NITFDRV-----QNDVTGGIGKKFESMVKMKSSvKNGVYLINGNHP 228
Cdd:cd04241 161 KPERVIFLTDVDGVYDKPP---PDAKLIPEIDVgSLEDILAalgsaGTDVTGGMAGKIEELLELARR-GIEVYIFNGDKP 236

                       250
                ....*....|....*.
gi 10639249 229 ERIGDIGKESFIGTVI 244
Cdd:cd04241 237 ENLYRALLGNFIGTRI 252
COG1608 COG1608
Isopentenyl phosphate kinase [Lipid transport and metabolism];
1-245 9.06e-92

Isopentenyl phosphate kinase [Lipid transport and metabolism];


Pssm-ID: 441216 [Multi-domain]  Cd Length: 254  Bit Score: 270.55  E-value: 9.06e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249   1 MMILKIGGSVITDKSAYRTARTYAIRSIVKVLSGIEDL-VCVVHGGGSFGHIKAMEFGLPGPKNPRSSIGYSIVHRDMEN 79
Cdd:COG1608   1 MIVLKLGGSVITDKDKPETVRRDALERIAREIAAALDLdLVIVHGGGSFGHPVAKKYGLHGTLGTEDAEGVSETHRAMRE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249  80 LDLMVIDAMIEMGMRPISVPISAL--RYDGR---FDYTPLIRYIDAGFVPVSYGDVYIKDEHSYGIYSGDDIMADMAELL 154
Cdd:COG1608  81 LNRIVVDALLEAGVPAVSVPPSSFavRDNGRilsFDTEPIKEMLEEGFVPVLHGDVVFDAERGFTILSGDEIVVYLAKEL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249 155 KPDVAVFLTDVDGIYSKDPKrnpdAVLLRDIDTNiTFDRV--------QNDVTGGIGKKFESMVKMKSSVKNgVYLINGN 226
Cdd:COG1608 161 KPERVGLATDVDGVYDDDPK----GKLIPEITRS-NFDEVldalggsaGTDVTGGMAGKVEELLELAKPGVE-VYIFNGN 234

                       250       260
                ....*....|....*....|
gi 10639249 227 HPERIGDIGK-ESFIGTVIR 245
Cdd:COG1608 235 KPGNLSAALRgEEVRGTRIR 254
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 3-233 1.93e-27

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: 105.14  E-value: 1.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249     3 ILKIGGSVITDKSAYRtartyAIRSIVKVLSGIEDLVCVVHGGGSFGHIKAMEFGLPgpknPRSSIGYSIVHRDMENLDL 82
Cdd:pfam00696   4 VIKLGGSSLTDKERLK-----RLADEIAALLEEGRKLVVVHGGGAFADGLLALLGLS----PRFARLTDAETLEVATMDA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249    83 MVI------DAMIEMGMRPISVPISAL---------RYDGRFDYTPLIRYIDAGFVPVSYGDVYIKDEHSYGIYSGDDIM 147
Cdd:pfam00696  75 LGSlgerlnAALLAAGLPAVGLPAAQLlateagfidDVVTRIDTEALEELLEAGVVPVITGFIGIDPEGELGRGSSDTLA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249   148 ADMAELLKPDVAVFLTDVDGIYSKDPKRNPDAVLLRDIDTNITFDRVQN-DVTGGIGKKFESMVKMkssvkngvyLINGN 226
Cdd:pfam00696 155 ALLAEALGADKLIILTDVDGVYTADPRKVPDAKLIPEISYDELLELLASgLATGGMKVKLPAALEA---------ARRGG 225


                  ....*..
gi 10639249   227 HPERIGD 233
Cdd:pfam00696 226 IPVVIVN 232
pyrH_arch TIGR02076
uridylate kinase, putative; This family consists of the archaeal and spirochete proteins most ...
 3-244 3.27e-10

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: 58.09  E-value: 3.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249     3 ILKIGGSVITDKSAYRTARTYAirSIVKVLSGiEDLVCVVHGGGsfghikamefglpgpKNPRSSIGysiVHRDM---EN 79
Cdd:TIGR02076   2 VISLGGSVLSPEIDAEFIKEFA--NILRKLSD-EHKVGVVVGGG---------------KTARRYIG---VARELgasET 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249    80 -LDLMVIDA--MIEMGMrpisvpISALRYDGR----FDYTPLIRYIDAGFVPVSYGdvyIKDEHSygiysGDDIMADMAE 152
Cdd:TIGR02076  61 fLDEIGIDAtrLNAMLL------IAALGDDAYpkvpENFEEALEAMSLGKIVVMGG---THPGHT-----TDAVAALLAE 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249   153 LLKPDVAVFLTDVDGIYSKDPKRNPDAVLLRDidtnITFDRVQNDVTGGIGKKFESMV------KMKSSVKNGVYLINGN 226
Cdd:TIGR02076 127 FSKADLLINATNVDGVYDKDPKKDPDAKKFDK----LTPEELVEIVGSSSVKAGSNEVvdplaaKIIERSKIRTIVVNGR 202

                         250
                  ....*....|....*...
gi 10639249   227 HPERIGDIGKESFIGTVI 244
Cdd:TIGR02076 203 DPENLEKVLKGEHVGTII 220
PRK12314 PRK12314
gamma-glutamyl kinase; Provisional
 151-242 9.57e-07

gamma-glutamyl kinase; Provisional


Pssm-ID: 183430 [Multi-domain]  Cd Length: 266  Bit Score: 48.70  E-value: 9.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249  151 AELLKPDVAVFLTDVDGIYSKDPKRNPDAVLLRDIdTNITFDRVQndVTGGIGKKFES--MV-KMKSS---VKNG--VYL 222
Cdd:PRK12314 164 AKLVKADLLIILSDIDGLYDKNPRINPDAKLRSEV-TEITEEILA--LAGGAGSKFGTggMVtKLKAAkflMEAGikMVL 240

                         90       100
                 ....*....|....*....|
gi 10639249  223 INGNHPERIGDIGKESFIGT 242
Cdd:PRK12314 241 ANGFNPSDILDFLEGESIGT 260
 
Name Accession Description Interval E-value
IPPK_Arch NF040647
isopentenyl phosphate kinase;
2-244 1.70e-100

isopentenyl phosphate kinase;


Pssm-ID: 468614 [Multi-domain]  Cd Length: 258  Bit Score: 292.97  E-value: 1.70e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249    2 MILKIGGSVITDKSAYRTARTYAIRSIVKVLSGI--EDLVCVVHGGGSFGHIKAMEFGLP----GPKNPRSSIGYSIVHR 75
Cdd:NF040647   1 IILKLGGSVITDKDIYPKIDWDNLERIAKEISNAldEDKLIIVHGGGSFGHPKAKKYGIGeginGEEFERKRKGFWETQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249   76 DMENLDLMVIDAMIEMGMRPISVPISALRYDGR-----FDYTPLIRYIDAGFVPVSYGDVYIKDEHSYGIYSGDDIMADM 150
Cdd:NF040647  81 AMRRLNNLVCDALIEYGIPAVSIQPSSFIRTGNkrilhFDLDLIKKYLELGFVPVLYGDVVLDNNIKYGILSGDQIIPYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249  151 AELLKPDVAVFLTDVDGIYSKDPKRNPDAVLLRDIDTNI---TFDRVQN-DVTGGIGKKFESMVKMkSSVKNGVYLINGN 226
Cdd:NF040647 161 AKKLKPDRVILGSDVDGVYDKNPKKYPDAKLIDKVNSLDdleSLEGTNNvDVTGGMYGKVKELLKL-AELGIESYIINGN 239

                        250
                 ....*....|....*....
gi 10639249  227 HPERIG-DIGKESFIGTVI 244
Cdd:NF040647 240 KPENIYkALGGEKVIGTVI 258
AAK_FomA-like cd04241
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ...
 1-244 3.48e-92

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: 271.44  E-value: 3.48e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249   1 MMILKIGGSVITDKSAYRTARTYAIRSIVKVLSG-IEDLVCVVHGGGSFGHIKAMEFGLPGPKNPRSSIGYSIVHRDMEN 79
Cdd:cd04241   1 MIILKLGGSVITDKDRPETIREENLERIARELAEaIDEKLVLVHGGGSFGHPKAKEYGLPDGDGSFSAEGVAETHEAMLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249  80 LDLMVIDAMIEMGMRPISVPISAL-----RYDGRFDYTPLIRYIDAGFVPVSYGDVYIKDEHSYGIYSGDDIMADMAELL 154
Cdd:cd04241  81 LNSIVVDALLEAGVPAVSVPPSSFfvtenGRIVSFDLEVIKELLDRGFVPVLHGDVVLDEGGGITILSGDDIVVELAKAL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249 155 KPDVAVFLTDVDGIYSKDPkrnPDAVLLRDIDT-NITFDRV-----QNDVTGGIGKKFESMVKMKSSvKNGVYLINGNHP 228
Cdd:cd04241 161 KPERVIFLTDVDGVYDKPP---PDAKLIPEIDVgSLEDILAalgsaGTDVTGGMAGKIEELLELARR-GIEVYIFNGDKP 236

                       250
                ....*....|....*.
gi 10639249 229 ERIGDIGKESFIGTVI 244
Cdd:cd04241 237 ENLYRALLGNFIGTRI 252
COG1608 COG1608
Isopentenyl phosphate kinase [Lipid transport and metabolism];
1-245 9.06e-92

Isopentenyl phosphate kinase [Lipid transport and metabolism];


Pssm-ID: 441216 [Multi-domain]  Cd Length: 254  Bit Score: 270.55  E-value: 9.06e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249   1 MMILKIGGSVITDKSAYRTARTYAIRSIVKVLSGIEDL-VCVVHGGGSFGHIKAMEFGLPGPKNPRSSIGYSIVHRDMEN 79
Cdd:COG1608   1 MIVLKLGGSVITDKDKPETVRRDALERIAREIAAALDLdLVIVHGGGSFGHPVAKKYGLHGTLGTEDAEGVSETHRAMRE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249  80 LDLMVIDAMIEMGMRPISVPISAL--RYDGR---FDYTPLIRYIDAGFVPVSYGDVYIKDEHSYGIYSGDDIMADMAELL 154
Cdd:COG1608  81 LNRIVVDALLEAGVPAVSVPPSSFavRDNGRilsFDTEPIKEMLEEGFVPVLHGDVVFDAERGFTILSGDEIVVYLAKEL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249 155 KPDVAVFLTDVDGIYSKDPKrnpdAVLLRDIDTNiTFDRV--------QNDVTGGIGKKFESMVKMKSSVKNgVYLINGN 226
Cdd:COG1608 161 KPERVGLATDVDGVYDDDPK----GKLIPEITRS-NFDEVldalggsaGTDVTGGMAGKVEELLELAKPGVE-VYIFNGN 234

                       250       260
                ....*....|....*....|
gi 10639249 227 HPERIGDIGK-ESFIGTVIR 245
Cdd:COG1608 235 KPGNLSAALRgEEVRGTRIR 254
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 3-233 1.93e-27

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: 105.14  E-value: 1.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249     3 ILKIGGSVITDKSAYRtartyAIRSIVKVLSGIEDLVCVVHGGGSFGHIKAMEFGLPgpknPRSSIGYSIVHRDMENLDL 82
Cdd:pfam00696   4 VIKLGGSSLTDKERLK-----RLADEIAALLEEGRKLVVVHGGGAFADGLLALLGLS----PRFARLTDAETLEVATMDA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249    83 MVI------DAMIEMGMRPISVPISAL---------RYDGRFDYTPLIRYIDAGFVPVSYGDVYIKDEHSYGIYSGDDIM 147
Cdd:pfam00696  75 LGSlgerlnAALLAAGLPAVGLPAAQLlateagfidDVVTRIDTEALEELLEAGVVPVITGFIGIDPEGELGRGSSDTLA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249   148 ADMAELLKPDVAVFLTDVDGIYSKDPKRNPDAVLLRDIDTNITFDRVQN-DVTGGIGKKFESMVKMkssvkngvyLINGN 226
Cdd:pfam00696 155 ALLAEALGADKLIILTDVDGVYTADPRKVPDAKLIPEISYDELLELLASgLATGGMKVKLPAALEA---------ARRGG 225


                  ....*..
gi 10639249   227 HPERIGD 233
Cdd:pfam00696 226 IPVVIVN 232
AAK_UMPK-like cd04239
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ...
 3-245 1.50e-15

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: 72.96  E-value: 1.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249   3 ILKIGGSVITDKSayRTARTYAIRSIVKVLSGIEDL---VCVVHGGGS-FGHIKAMEFGLPgpKNPRSSIGYSIVhrdME 78
Cdd:cd04239   3 VLKLSGEALAGEG--GGIDPEVLKEIAREIKEVVDLgveVAIVVGGGNiARGYIAAARGMP--RATADYIGMLAT---VM 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249  79 NlDLMVIDAMIEMGMrpISVPISALRYDG---RFDYTPLIRYIDAGFVPVSYGDVYIKdehsygIYSGDDIMADMAELLK 155
Cdd:cd04239  76 N-ALALQDALEKLGV--KTRVMSAIPMQGvaePYIRRRAIRHLEKGRIVIFGGGTGNP------GFTTDTAAALRAEEIG 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249 156 PDVAVFLTDVDGIYSKDPKRNPDAVLLrdidTNITFDRVQNdvtggIGKKFESMVKMKSSVKNG--VYLINGNHPERIGD 233
Cdd:cd04239 147 ADVLLKATNVDGVYDADPKKNPDAKKY----DRISYDELLK-----KGLKVMDATALTLCRRNKipIIVFNGLKPGNLLR 217

                       250
                ....*....|..
gi 10639249 234 IGKESFIGTVIR 245
Cdd:cd04239 218 ALKGEHVGTLIE 229
AAK_UMPK-PyrH-Pf cd04253
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ...
 123-244 2.87e-11

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: 61.11  E-value: 2.87e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249 123 VPVSYGDVyIKDEHSYGI---------YSGDDIMADMAELLKPDVAVFLTDVDGIYSKDPKRNPDAVLLRdidtNITFDR 193
Cdd:cd04253  89 VPTSYEEA-LEAMFTGKIvvmggtepgQSTDAVAALLAERLGADLLINATNVDGVYSKDPRKDPDAKKFD----RLSADE 163

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 10639249 194 VQNDVTGGI----GKKFESMVKMKSSVKNG--VYLINGNHPERIGDIGKESFIGTVI 244
Cdd:cd04253 164 LIDIVGKSSwkagSNEPFDPLAAKIIERSGikTIVVDGRDPENLERALKGEFVGTII 220
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 3-244 1.24e-10

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: 59.76  E-value: 1.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249   3 ILKIGGSVITDKSAYRTartyaIRSIVKVLSGIEDLVCVVHGGGSFGHikamEFGLPGPKNPRSSIGYSIVHRDMENL-- 80
Cdd:cd02115   1 VIKFGGSSVSSEERLRN-----LARILVKLASEGGRVVVVHGAGPQIT----DELLAHGELLGYARGLRITDRETDALaa 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249  81 --DLMVIDAMIEM--------------GMRPISVPISALRYDGRFDYTPLIRYIDAGFVPV-SYGDVYIKDEHS--YGIY 141
Cdd:cd02115  72 mgEGMSNLLIAAAleqhgikavpldltQAGFASPNQGHVGKITKVSTDRLKSLLENGILPIlSGFGGTDEKETGtlGRGG 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249 142 SgDDIMADMAELLKPDVAVFLTDVDGIYSKDPKRNPDAVLLRdidtNITFDRVQNDVTGGIG----KKFESMVKMKSSvk 217
Cdd:cd02115 152 S-DSTAALLAAALKADRLVILTDVDGVYTADPRKVPDAKLLS----ELTYEEAAELAYAGAMvlkpKAADPAARAGIP-- 224

                       250       260
                ....*....|....*....|....*..
gi 10639249 218 ngVYLINGNHPERIGDIGKESfIGTVI 244
Cdd:cd02115 225 --VRIANTENPGALALFTPDG-GGTLI 248
pyrH_arch TIGR02076
uridylate kinase, putative; This family consists of the archaeal and spirochete proteins most ...
 3-244 3.27e-10

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: 58.09  E-value: 3.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249     3 ILKIGGSVITDKSAYRTARTYAirSIVKVLSGiEDLVCVVHGGGsfghikamefglpgpKNPRSSIGysiVHRDM---EN 79
Cdd:TIGR02076   2 VISLGGSVLSPEIDAEFIKEFA--NILRKLSD-EHKVGVVVGGG---------------KTARRYIG---VARELgasET 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249    80 -LDLMVIDA--MIEMGMrpisvpISALRYDGR----FDYTPLIRYIDAGFVPVSYGdvyIKDEHSygiysGDDIMADMAE 152
Cdd:TIGR02076  61 fLDEIGIDAtrLNAMLL------IAALGDDAYpkvpENFEEALEAMSLGKIVVMGG---THPGHT-----TDAVAALLAE 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249   153 LLKPDVAVFLTDVDGIYSKDPKRNPDAVLLRDidtnITFDRVQNDVTGGIGKKFESMV------KMKSSVKNGVYLINGN 226
Cdd:TIGR02076 127 FSKADLLINATNVDGVYDKDPKKDPDAKKFDK----LTPEELVEIVGSSSVKAGSNEVvdplaaKIIERSKIRTIVVNGR 202

                         250
                  ....*....|....*...
gi 10639249   227 HPERIGDIGKESFIGTVI 244
Cdd:TIGR02076 203 DPENLEKVLKGEHVGTII 220
AAK_G5K_ProB cd04242
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ...
 151-245 4.13e-10

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: 58.22  E-value: 4.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249 151 AELLKPDVAVFLTDVDGIYSKDPKRNPDAVLLRDIDTNItfDRVQNDV--------TGGIGKKFESMVKMKSSVKNgVYL 222
Cdd:cd04242 152 AGLVNADLLILLSDVDGLYDKNPRENPDAKLIPEVEEIT--DEIEAMAggsgssvgTGGMRTKLKAARIATEAGIP-VVI 228

                        90       100
                ....*....|....*....|...
gi 10639249 223 INGNHPERIGDIGKESFIGTVIR 245
Cdd:cd04242 229 ANGRKPDVLLDILAGEAVGTLFL 251
proB TIGR01027
glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ...
 144-244 2.41e-07

glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ProB-like domain of delta 1-pyrroline-5-carboxylate synthetase does not hit the C-terminal 100 residues of this model. The noise cutoff is set low enough to hit delta 1-pyrroline-5-carboxylate synthetase and other partial matches to this family. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 162163 [Multi-domain]  Cd Length: 363  Bit Score: 50.77  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249   144 DDIMADMAELLKPDVAVFLTDVDGIYSKDPKRNPDAVLLRDI-DTNITFDRVQNDV-----TGGIGKKFES-MVKMKSSV 216
Cdd:TIGR01027 146 DTLSALVAILVGADLLVLLTDVDGLYDADPRTNPDAKLIPVVeEITDLLLGVAGDSgssvgTGGMRTKLQAaDLATRAGV 225

                          90       100
                  ....*....|....*....|....*...
gi 10639249   217 KngVYLINGNHPERIGDIGKESFIGTVI 244
Cdd:TIGR01027 226 P--VIIASGSKPEKIADALEGAPVGTLF 251
PRK12314 PRK12314
gamma-glutamyl kinase; Provisional
 151-242 9.57e-07

gamma-glutamyl kinase; Provisional


Pssm-ID: 183430 [Multi-domain]  Cd Length: 266  Bit Score: 48.70  E-value: 9.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249  151 AELLKPDVAVFLTDVDGIYSKDPKRNPDAVLLRDIdTNITFDRVQndVTGGIGKKFES--MV-KMKSS---VKNG--VYL 222
Cdd:PRK12314 164 AKLVKADLLIILSDIDGLYDKNPRINPDAKLRSEV-TEITEEILA--LAGGAGSKFGTggMVtKLKAAkflMEAGikMVL 240

                         90       100
                 ....*....|....*....|
gi 10639249  223 INGNHPERIGDIGKESFIGT 242
Cdd:PRK12314 241 ANGFNPSDILDFLEGESIGT 260
AAK_UMPK-MosAB cd04255
AAK_UMPK-MosAB: This CD includes the alpha and beta subunits of the Mo storage protein (MosA ...
 3-245 1.92e-06

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


Pssm-ID: 239788 [Multi-domain]  Cd Length: 262  Bit Score: 47.77  E-value: 1.92e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249   3 ILKIGGSVITDKSAYrtartyAIRSIVKVLSGI--EDLVCVVHGGGSFG-HIKAMEFGLPGPKNPRSSIGYSIVHRDMEN 79
Cdd:cd04255  34 VVKIGGQSIIDRGAE------AVLPLVEEIVALrpEHKLLILTGGGTRArHVYSIGLDLGMPTGVLAKLGASVSEQNAEM 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249  80 LDLMvidamiemgMRPISVPisalrYDGRFDYTPLIRYIDAGFVPVSYG-DVYIKDEH--SYG---IYSGDDIMADMAEL 153
Cdd:cd04255 108 LATL---------LAKHGGS-----KVGHGDLLQLPTFLKAGRAPVISGmPPYGLWEHpaEEGripPHRTDVGAFLLAEV 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249 154 LKPDVAVFLTDVDGIYSKDPKRNPDAVLLRDIDTNITFDRVQNDVTggIGKKFESMVKMKSSVKNgVYLINGNHPERIGD 233
Cdd:cd04255 174 IGARNLIFVKDEDGLYTADPKKNKKAEFIPEISAAELLKKDLDDLV--LERPVLDLLQNARHVKE-VQIVNGLVPGNLTR 250

                       250
                ....*....|..
gi 10639249 234 IGKESFIGTVIR 245
Cdd:cd04255 251 ALRGEHVGTIIR 262
ProB COG0263
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ...
 151-186 2.91e-06

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: 47.34  E-value: 2.91e-06
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 10639249 151 AELLKPDVAVFLTDVDGIYSKDPKRNPDAVLLRDID 186
Cdd:COG0263 160 ANLVEADLLVLLTDVDGLYDADPRKDPDAKLIPEVE 195
PyrH COG0528
Uridylate kinase [Nucleotide transport and metabolism]; Uridylate kinase is part of the ...
 163-194 2.29e-05

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: 44.23  E-value: 2.29e-05
                        10        20        30
                ....*....|....*....|....*....|..
gi 10639249 163 TDVDGIYSKDPKRNPDAVLLrdidTNITFDRV 194
Cdd:COG0528 162 TKVDGVYDADPKKNPDAKKY----DRLTYDEV 189
AAK_P5CS_ProBA cd04256
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ...
 133-245 2.82e-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: 44.35  E-value: 2.82e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249 133 KDEHSYGIYS---GDDIMADMAELLKPDVAVFLTDVDGIYSKDPkRNPDAVLlrdIDTNITFDrvQNDVTGGIGKKFeSM 209
Cdd:cd04256 167 PDEDLQGVISikdNDSLAARLAVELKADLLILLSDVDGLYDGPP-GSDDAKL---IHTFYPGD--QQSITFGTKSRV-GT 239

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 10639249 210 VKMKSSVKNGVYLINGNHPERIGDIGKESFIGTVIR 245
Cdd:cd04256 240 GGMEAKVKAALWALQGGTSVVITNGMAGDVITKILE 275
AAK_UC cd04240
AAK_UC: Uncharacterized (UC) amino acid kinase-like proteins found mainly in archaea and a few ...
 3-244 3.04e-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: 43.50  E-value: 3.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249   3 ILKIGGSVITD-KSAYRTARTYAIRSIVkvlsgiedlvcVVHGGGSFGhikamefglpgpknprssigySIVHRDMENLD 81
Cdd:cd04240   1 VVKIGGSLIREaVRLLRWLKTLSGGGVV-----------IVPGGGPFA---------------------DVVRRYQERKG 48

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249  82 L-------MVIDAMIEMG--MRPISVPISAlrydgrFDYTPLIRYIDAGFVPV--SYGDVYIKDE--HSYGIYSgDDIMA 148
Cdd:cd04240  49 LsdaaahwMAILAMEQYGylLADLEPRLVA------RTLAELTDVLERGKIAIllPYRLLLDTDPlpHSWEVTS-DSIAA 121

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249 149 DMAELLKPDVAVFLTDVDGIYSKDPKrnpdavLLRDIDTNitfdrvqndVTGGIGKKFESMVKMKSSVKNGVYLINGNHP 228
Cdd:cd04240 122 WLAKKLGAKRLVIVTDVDGIYEKDGK------LVNEIAAA---------ELLGETSVDPAFPRLLTKYGIRCYVVNGDDP 186

                       250
                ....*....|....*...
gi 10639249 229 ERIGDI--GKEsFIGTVI 244
Cdd:cd04240 187 ERVLAAlrGRE-GVGTRI 203
P5CS TIGR01092
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ...
 135-242 7.54e-05

delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, EC 2.7.2.11) region followed by a gamma-glutamyl phosphate reductase (ProA, EC 1.2.1.41) region. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 130164 [Multi-domain]  Cd Length: 715  Bit Score: 43.36  E-value: 7.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249   135 EHSYGIYSGDDIMADMAEL-LKPDVAVFLTDVDGIYSKDPKrNPDAVLlrdIDTNITFDRvQNDVTGGIGKKFeSMVKMK 213
Cdd:TIGR01092 160 SDSQGIFWDNDSLAALLALeLKADLLILLSDVEGLYDGPPS-DDDSKL---IDTFYKEKH-QGEITFGTKSRL-GRGGMT 233

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 10639249   214 SSVKNGVY---------LINGNHPERIGDIGKESFIGT 242
Cdd:TIGR01092 234 AKVKAAVWaayggtpviIASGTAPKNITKVVEGKKVGT 271
pyrH_bact TIGR02075
uridylate kinase; This protein, also called UMP kinase, converts UMP to UDP by adding a ...
 154-197 1.00e-04

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: 42.23  E-value: 1.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 10639249   154 LKPDVAVFLTDVDGIYSKDPKRNPDAVLLRdidtNITFDRVQND 197
Cdd:TIGR02075 148 INADVILKGTNVDGVYTADPKKNKDAKKYD----TITYNEALKK 187
AAK_NAGK-like cd04238
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ...
 118-244 1.07e-04

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: 42.50  E-value: 1.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249 118 IDAGFVPV----SYGDvyikDEHSYGIySGDDIMADMAELLKPDVAVFLTDVDGIYskdpkRNPDAVL----LRDIDTNI 189
Cdd:cd04238 135 LEAGYIPViapiAVDE----DGETYNV-NADTAAGAIAAALKAEKLILLTDVPGVL-----DDPGSLIseltPKEAEELI 204

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 10639249 190 TfdrvQNDVTGGIGKKFESMVKmksSVKNGV---YLINGNHPERI-GDIGKESFIGTVI 244
Cdd:cd04238 205 E----DGVISGGMIPKVEAALE---ALEGGVrkvHIIDGRVPHSLlLELFTDEGIGTMI 256
AAK_UMPK-PyrH-Ec cd04254
UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) ...
 163-196 1.68e-04

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: 41.71  E-value: 1.68e-04
                        10        20        30
                ....*....|....*....|....*....|....
gi 10639249 163 TDVDGIYSKDPKRNPDAVLLrdidTNITFDRVQN 196
Cdd:cd04254 156 TKVDGVYDADPKKNPNAKRY----DHLTYDEVLS 185
asp_kinases TIGR00657
aspartate kinase; Aspartate kinase catalyzes a first step in the biosynthesis from Asp of Lys ...
 143-244 3.78e-04

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: 41.19  E-value: 3.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249   143 GDDIMAD-MAELLKPDVAVFLTDVDGIYSKDPKRNPDAvllRDIDTnITFDRVQNDVTGGIGKKFESMVKmkssvkngvY 221
Cdd:TIGR00657 192 GSDYTAAlLAAALKADECEIYTDVDGIYTTDPRIVPDA---RRIDE-ISYEEMLELASFGAKVLHPRTLE---------P 258

                          90       100
                  ....*....|....*....|...
gi 10639249   222 LINGNHPERIGDIGKESFIGTVI 244
Cdd:TIGR00657 259 AMRAKIPIVVKSTFNPEAPGTLI 281
PLN02418 PLN02418
delta-1-pyrroline-5-carboxylate synthase
 135-205 4.67e-04

delta-1-pyrroline-5-carboxylate synthase


Pssm-ID: 215230  Cd Length: 718  Bit Score: 40.86  E-value: 4.67e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10639249  135 EHSYGIYSGDDIMADMAEL-LKPDVAVFLTDVDGIYSKDPKrNPDAVLLRdidtniTFDRVQNDVTGGIGKK 205
Cdd:PLN02418 168 EDSSGIFWDNDSLAALLALeLKADLLILLSDVEGLYTGPPS-DPSSKLIH------TYIKEKHQDEITFGEK 232
AAK_AK-HSDH cd04257
AAK_AK-HSDH: Amino Acid Kinase Superfamily (AAK), AK-HSDH; this CD includes the N-terminal ...
 163-182 1.01e-03

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: 39.49  E-value: 1.01e-03
                        10        20
                ....*....|....*....|
gi 10639249 163 TDVDGIYSKDPKRNPDAVLL 182
Cdd:cd04257 225 TDVDGVYSADPRKVKDARLL 244
AAK_AK-HSDH-like cd04243
AAK_AK-HSDH-like: Amino Acid Kinase Superfamily (AAK), AK-HSDH-like; this family includes the ...
 163-186 1.05e-03

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: 39.46  E-value: 1.05e-03
                        10        20
                ....*....|....*....|....
gi 10639249 163 TDVDGIYSKDPKRNPDAVLLRDID 186
Cdd:cd04243 224 TDVDGVYTADPRKVPDARLLKELS 247
AAK_AK cd04234
AAK_AK: Amino Acid Kinase Superfamily (AAK), Aspartokinase (AK); this CD includes the ...
 143-192 1.13e-03

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: 38.99  E-value: 1.13e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 10639249 143 GDDIMA-DMAELLKPDVAVFLTDVDGIYSKDPKRNPDAVLLRdidtNITFD 192
Cdd:cd04234 137 GSDYSAaALAAALGADEVEIWTDVDGIYTADPRIVPEARLIP----EISYD 183
thrA PRK09436
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional
 163-182 1.58e-03

bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional


Pssm-ID: 181856 [Multi-domain]  Cd Length: 819  Bit Score: 39.37  E-value: 1.58e-03
                         10        20
                 ....*....|....*....|
gi 10639249  163 TDVDGIYSKDPKRNPDAVLL 182
Cdd:PRK09436 227 TDVDGVYTADPRVVPDARLL 246
AAK_NAGK-UC cd04251
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ...
 3-244 1.68e-03

AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar to Escherichia coli and Pseudomonas aeruginosa NAGKs which catalyze the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis. These uncharacterized domain sequences are found in some bacteria (Deinococci and Chloroflexi) and archea and belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239784 [Multi-domain]  Cd Length: 257  Bit Score: 38.89  E-value: 1.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249   3 ILKIGGSVITDKSAyrtartyairsIVKVLSGIEDLVCVVHGGGSFGHIKAMEFGLP-----GPKNPRSS---------- 67
Cdd:cd04251   2 VVKIGGSVVSDLDK-----------VIDDIANFGERLIVVHGGGNYVNEYLKRLGVEpkfvtSPSGIRSRytdketlevf 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249  68 ------IGYSIVHRdMENLDLMV-----IDAMIEMGMRPISVPIS------ALRYD-----GRFDYTPLIRYIDAGFVPV 125
Cdd:cd04251  71 vmvmglINKKIVAR-LHSLGVKAvgltgLDGRLLEAKRKEIVRVNergrkmIIRGGytgkvEKVNSDLIEALLDAGYLPV 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249 126 sYGDVYIKDEHSYGIYSGDDIMADMAELLKPDVAVFLTDVDGIYSkdpkrnpDAVLLRDIDTNiTFDRVQNDVTGGIGKK 205
Cdd:cd04251 150 -VSPVAYSEEGEPLNVDGDRAAAAIAAALKAERLILLTDVEGLYL-------DGRVIERITVS-DAESLLEKAGGGMKRK 220

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 10639249 206 FESMVKMKSSVKNGVYLINGNHPERIGDIGKESfiGTVI 244
Cdd:cd04251 221 LLAAAEAVEGGVREVVIGDARADSPISSALNGG--GTVI 257
ArgB COG0548
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ...
 108-245 8.67e-03

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: 36.55  E-value: 8.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249 108 RFDYTPLIRYIDAGFVPV----SYGDvyikDEHSYGIySGDDIMADMAELLKPDVAVFLTDVDGIYSKDpkrnpdavllR 183
Cdd:COG0548 151 RVDPELIRALLDAGYIPVispiGYSP----TGEVYNI-NADTVAGAIAAALKAEKLILLTDVPGVLDDP----------G 215

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10639249 184 DIDTNITFDRVQ-----NDVTGGIGKKFESMVKmksSVKNGV---YLINGNHPeriGDIGKESF----IGTVIR 245
Cdd:COG0548 216 SLISELTAAEAEeliadGVISGGMIPKLEAALD---AVRGGVkrvHIIDGRVP---HALLLELFtddgIGTMIV 283
MetL1 COG0527
Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the ...
 163-192 8.69e-03

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: 36.98  E-value: 8.69e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 10639249 163 TDVDGIYSKDPKRNPDAVLLRdidtNITFD 192
Cdd:COG0527 174 TDVDGVYTADPRIVPDARKLP----EISYE 199
PRK00942 PRK00942
acetylglutamate kinase; Provisional
 118-245 8.76e-03

acetylglutamate kinase; Provisional


Pssm-ID: 234869 [Multi-domain]  Cd Length: 283  Bit Score: 36.62  E-value: 8.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10639249  118 IDAGFVPV----SYGDvyikDEHSYGIySGDDIMADMAELLKPDVAVFLTDVDGIYsKDPKRnpdavLLRDIDTNiTFDR 193
Cdd:PRK00942 159 LEAGYIPVispiGVGE----DGETYNI-NADTAAGAIAAALGAEKLILLTDVPGVL-DDKGQ-----LISELTAS-EAEE 226

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10639249  194 VQND--VTGGigkkfesM-VKMKS---SVKNGV---YLINGNHPERI-GDIGKESFIGTVIR 245
Cdd:PRK00942 227 LIEDgvITGG-------MiPKVEAaldAARGGVrsvHIIDGRVPHALlLELFTDEGIGTMIV 281
 
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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