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Conserved domains on  [gi|757131282|ref|WP_042685552|]
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isopentenyl phosphate kinase [Methermicoccus shengliensis]

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
COG1608 COG1608
Isopentenyl phosphate kinase [Lipid transport and metabolism];
1-248 9.83e-95

Isopentenyl phosphate kinase [Lipid transport and metabolism];


:

Pssm-ID: 441216 [Multi-domain]  Cd Length: 254  Bit Score: 278.26  E-value: 9.83e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282   1 MKVLKIGGSVLTEKHTEEKkVRMEVLDRIASEIAP-RADGLILVHGAGSFGHPEAIRHGVG---RRFSTEGVLKTHQSVC 76
Cdd:COG1608    1 MIVLKLGGSVITDKDKPET-VRRDALERIAREIAAaLDLDLVIVHGGGSFGHPVAKKYGLHgtlGTEDAEGVSETHRAMR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282  77 LLNRIVVSALVRGGVPAVPVSPLGCAIADGGRLVSMEMTPILHMVERGLVPVLHGDVVMDRTLGAAVVSGDALVAHIAKG 156
Cdd:COG1608   80 ELNRIVVDALLEAGVPAVSVPPSSFAVRDNGRILSFDTEPIKEMLEEGFVPVLHGDVVFDAERGFTILSGDEIVVYLAKE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282 157 LGAHHVGMGTSAQGVLDA--HGRTIPEVTEHNIEQVRQWVRPSGGGDATGGMVGKVEELWRLAGEGIESWVFSALDEGAV 234
Cdd:COG1608  160 LKPERVGLATDVDGVYDDdpKGKLIPEITRSNFDEVLDALGGSAGTDVTGGMAGKVEELLELAKPGVEVYIFNGNKPGNL 239

                        250
                 ....*....|....*
gi 757131282 235 AAFLDGHPV-GTRVR 248
Cdd:COG1608  240 SAALRGEEVrGTRIR 254
 
Name Accession Description Interval E-value
COG1608 COG1608
Isopentenyl phosphate kinase [Lipid transport and metabolism];
1-248 9.83e-95

Isopentenyl phosphate kinase [Lipid transport and metabolism];


Pssm-ID: 441216 [Multi-domain]  Cd Length: 254  Bit Score: 278.26  E-value: 9.83e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282   1 MKVLKIGGSVLTEKHTEEKkVRMEVLDRIASEIAP-RADGLILVHGAGSFGHPEAIRHGVG---RRFSTEGVLKTHQSVC 76
Cdd:COG1608    1 MIVLKLGGSVITDKDKPET-VRRDALERIAREIAAaLDLDLVIVHGGGSFGHPVAKKYGLHgtlGTEDAEGVSETHRAMR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282  77 LLNRIVVSALVRGGVPAVPVSPLGCAIADGGRLVSMEMTPILHMVERGLVPVLHGDVVMDRTLGAAVVSGDALVAHIAKG 156
Cdd:COG1608   80 ELNRIVVDALLEAGVPAVSVPPSSFAVRDNGRILSFDTEPIKEMLEEGFVPVLHGDVVFDAERGFTILSGDEIVVYLAKE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282 157 LGAHHVGMGTSAQGVLDA--HGRTIPEVTEHNIEQVRQWVRPSGGGDATGGMVGKVEELWRLAGEGIESWVFSALDEGAV 234
Cdd:COG1608  160 LKPERVGLATDVDGVYDDdpKGKLIPEITRSNFDEVLDALGGSAGTDVTGGMAGKVEELLELAKPGVEVYIFNGNKPGNL 239

                        250
                 ....*....|....*
gi 757131282 235 AAFLDGHPV-GTRVR 248
Cdd:COG1608  240 SAALRGEEVrGTRIR 254
AAK_FomA-like cd04241
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ...
 1-247 8.89e-83

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: 247.94  E-value: 8.89e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282   1 MKVLKIGGSVLTEKhTEEKKVRMEVLDRIASEIAPRADG-LILVHGAGSFGHPEAIRHGVGR---RFSTEGVLKTHQSVC 76
Cdd:cd04241    1 MIILKLGGSVITDK-DRPETIREENLERIARELAEAIDEkLVLVHGGGSFGHPKAKEYGLPDgdgSFSAEGVAETHEAML 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282  77 LLNRIVVSALVRGGVPAVPVSPLGCAIADGGRLVSMEMTPILHMVERGLVPVLHGDVVMDRTLGAAVVSGDALVAHIAKG 156
Cdd:cd04241   80 ELNSIVVDALLEAGVPAVSVPPSSFFVTENGRIVSFDLEVIKELLDRGFVPVLHGDVVLDEGGGITILSGDDIVVELAKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282 157 LGAHHVGMGTSAQGVLDAH---GRTIPEVTEHNIEQVRQWVRpSGGGDATGGMVGKVEELWRLAGEGIESWVFSALDEGA 233
Cdd:cd04241  160 LKPERVIFLTDVDGVYDKPppdAKLIPEIDVGSLEDILAALG-SAGTDVTGGMAGKIEELLELARRGIEVYIFNGDKPEN 238

                        250
                 ....*....|....
gi 757131282 234 VAAFLDGHPVGTRV 247
Cdd:cd04241  239 LYRALLGNFIGTRI 252
IPPK_Arch NF040647
isopentenyl phosphate kinase;
3-247 7.32e-61

isopentenyl phosphate kinase;


Pssm-ID: 468614 [Multi-domain]  Cd Length: 258  Bit Score: 192.43  E-value: 7.32e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282   3 VLKIGGSVLTEKhTEEKKVRMEVLDRIASEI--APRADGLILVHGAGSFGHPEAIRHGVGRRFSTE-------GVLKTHQ 73
Cdd:NF040647   2 ILKLGGSVITDK-DIYPKIDWDNLERIAKEIsnALDEDKLIIVHGGGSFGHPKAKKYGIGEGINGEeferkrkGFWETQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282  74 SVCLLNRIVVSALVRGGVPAVPVSPLGCAIADGGRLVSMEMTPILHMVERGLVPVLHGDVVMDRTLGAAVVSGDALVAHI 153
Cdd:NF040647  81 AMRRLNNLVCDALIEYGIPAVSIQPSSFIRTGNKRILHFDLDLIKKYLELGFVPVLYGDVVLDNNIKYGILSGDQIIPYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282 154 AKGLGAHHVGMGTSAQGVLDAHGRTIPE---VTEHNIEQVRQWVRPSGGGDATGGMVGKVEELWRLAGEGIESWVFSALD 230
Cdd:NF040647 161 AKKLKPDRVILGSDVDGVYDKNPKKYPDaklIDKVNSLDDLESLEGTNNVDVTGGMYGKVKELLKLAELGIESYIINGNK 240

                        250
                 ....*....|....*...
gi 757131282 231 EGAVAAFLDGHPV-GTRV 247
Cdd:NF040647 241 PENIYKALGGEKViGTVI 258
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 1-227 4.22e-32

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: 117.47  E-value: 4.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282    1 MKVLKIGGSVLTEKhteekkvrmEVLDRIASEIAP-RADG--LILVHGAGSFGHPEAIRHGVGRRFST-----EGVLKTH 72
Cdd:pfam00696   2 RVVIKLGGSSLTDK---------ERLKRLADEIAAlLEEGrkLVVVHGGGAFADGLLALLGLSPRFARltdaeTLEVATM 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282   73 QSVCLLNRIVVSALVRGGVPAVPVSPLGCAIADGGRLV----SMEMTPILHMVERGLVPVLHGDVVMDRTLGAAVVSGDA 148
Cdd:pfam00696  73 DALGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDdvvtRIDTEALEELLEAGVVPVITGFIGIDPEGELGRGSSDT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282  149 LVAHIAKGLGAHHVGMGTSAQGVLDAHGRTIPEVTEHNIEQVRQWVRPSGGGDATGGMVGKVEELWRLAGEG-IESWVFS 227
Cdd:pfam00696 153 LAALLAEALGADKLIILTDVDGVYTADPRKVPDAKLIPEISYDELLELLASGLATGGMKVKLPAALEAARRGgIPVVIVN 232
PRK14058 PRK14058
[LysW]-aminoadipate/[LysW]-glutamate kinase;
1-249 5.82e-05

[LysW]-aminoadipate/[LysW]-glutamate kinase;


Pssm-ID: 237599 [Multi-domain]  Cd Length: 268  Bit Score: 43.35  E-value: 5.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282   1 MKVLKIGGSVLTEKhteekkvrMEVLDRIASeIAPRADGLILVHGAGS--------FGH-PEAIRH--GVGRRFSTEGVL 69
Cdd:PRK14058   1 MIVVKIGGSVGIDP--------EDALIDVAS-LWADGERVVLVHGGSDevnellerLGIePRFVTSpsGVTSRYTDRETL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282  70 KTHQSV-CLLNRIVVSALVRGGVPAVPVSPLGCAIADG----------------------GRLVSMEMTPILHMVERGLV 126
Cdd:PRK14058  72 EVFIMAmALINKQLVERLQSLGVNAVGLSGLDGGLLEGkrkkavrvveegkkkiirgdytGKIEEVNTDLLKLLLKAGYL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282 127 PVLhgDVVMDRTLGAAV-VSGDALVAHIAKGLGAHHVGMGTSAQGVL---DAHGRTIPEVTEHNIEQVRQWVRpsgggda 202
Cdd:PRK14058 152 PVV--APPALSEEGEPLnVDGDRAAAAIAGALKAEALVLLSDVPGLLrdpPDEGSLIERITPEEAEELSKAAG------- 222

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 757131282 203 tGGMVGKVEelwrLAGEGIESWVF-----SALDEGAVAAFLDGHpvGTRVRN 249
Cdd:PRK14058 223 -GGMKKKVL----MAAEAVEGGVGrviiaDANVDDPISAALAGE--GTVIVN 267
 
Name Accession Description Interval E-value
COG1608 COG1608
Isopentenyl phosphate kinase [Lipid transport and metabolism];
1-248 9.83e-95

Isopentenyl phosphate kinase [Lipid transport and metabolism];


Pssm-ID: 441216 [Multi-domain]  Cd Length: 254  Bit Score: 278.26  E-value: 9.83e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282   1 MKVLKIGGSVLTEKHTEEKkVRMEVLDRIASEIAP-RADGLILVHGAGSFGHPEAIRHGVG---RRFSTEGVLKTHQSVC 76
Cdd:COG1608    1 MIVLKLGGSVITDKDKPET-VRRDALERIAREIAAaLDLDLVIVHGGGSFGHPVAKKYGLHgtlGTEDAEGVSETHRAMR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282  77 LLNRIVVSALVRGGVPAVPVSPLGCAIADGGRLVSMEMTPILHMVERGLVPVLHGDVVMDRTLGAAVVSGDALVAHIAKG 156
Cdd:COG1608   80 ELNRIVVDALLEAGVPAVSVPPSSFAVRDNGRILSFDTEPIKEMLEEGFVPVLHGDVVFDAERGFTILSGDEIVVYLAKE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282 157 LGAHHVGMGTSAQGVLDA--HGRTIPEVTEHNIEQVRQWVRPSGGGDATGGMVGKVEELWRLAGEGIESWVFSALDEGAV 234
Cdd:COG1608  160 LKPERVGLATDVDGVYDDdpKGKLIPEITRSNFDEVLDALGGSAGTDVTGGMAGKVEELLELAKPGVEVYIFNGNKPGNL 239

                        250
                 ....*....|....*
gi 757131282 235 AAFLDGHPV-GTRVR 248
Cdd:COG1608  240 SAALRGEEVrGTRIR 254
AAK_FomA-like cd04241
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ...
 1-247 8.89e-83

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: 247.94  E-value: 8.89e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282   1 MKVLKIGGSVLTEKhTEEKKVRMEVLDRIASEIAPRADG-LILVHGAGSFGHPEAIRHGVGR---RFSTEGVLKTHQSVC 76
Cdd:cd04241    1 MIILKLGGSVITDK-DRPETIREENLERIARELAEAIDEkLVLVHGGGSFGHPKAKEYGLPDgdgSFSAEGVAETHEAML 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282  77 LLNRIVVSALVRGGVPAVPVSPLGCAIADGGRLVSMEMTPILHMVERGLVPVLHGDVVMDRTLGAAVVSGDALVAHIAKG 156
Cdd:cd04241   80 ELNSIVVDALLEAGVPAVSVPPSSFFVTENGRIVSFDLEVIKELLDRGFVPVLHGDVVLDEGGGITILSGDDIVVELAKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282 157 LGAHHVGMGTSAQGVLDAH---GRTIPEVTEHNIEQVRQWVRpSGGGDATGGMVGKVEELWRLAGEGIESWVFSALDEGA 233
Cdd:cd04241  160 LKPERVIFLTDVDGVYDKPppdAKLIPEIDVGSLEDILAALG-SAGTDVTGGMAGKIEELLELARRGIEVYIFNGDKPEN 238

                        250
                 ....*....|....
gi 757131282 234 VAAFLDGHPVGTRV 247
Cdd:cd04241  239 LYRALLGNFIGTRI 252
IPPK_Arch NF040647
isopentenyl phosphate kinase;
3-247 7.32e-61

isopentenyl phosphate kinase;


Pssm-ID: 468614 [Multi-domain]  Cd Length: 258  Bit Score: 192.43  E-value: 7.32e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282   3 VLKIGGSVLTEKhTEEKKVRMEVLDRIASEI--APRADGLILVHGAGSFGHPEAIRHGVGRRFSTE-------GVLKTHQ 73
Cdd:NF040647   2 ILKLGGSVITDK-DIYPKIDWDNLERIAKEIsnALDEDKLIIVHGGGSFGHPKAKKYGIGEGINGEeferkrkGFWETQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282  74 SVCLLNRIVVSALVRGGVPAVPVSPLGCAIADGGRLVSMEMTPILHMVERGLVPVLHGDVVMDRTLGAAVVSGDALVAHI 153
Cdd:NF040647  81 AMRRLNNLVCDALIEYGIPAVSIQPSSFIRTGNKRILHFDLDLIKKYLELGFVPVLYGDVVLDNNIKYGILSGDQIIPYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282 154 AKGLGAHHVGMGTSAQGVLDAHGRTIPE---VTEHNIEQVRQWVRPSGGGDATGGMVGKVEELWRLAGEGIESWVFSALD 230
Cdd:NF040647 161 AKKLKPDRVILGSDVDGVYDKNPKKYPDaklIDKVNSLDDLESLEGTNNVDVTGGMYGKVKELLKLAELGIESYIINGNK 240

                        250
                 ....*....|....*...
gi 757131282 231 EGAVAAFLDGHPV-GTRV 247
Cdd:NF040647 241 PENIYKALGGEKViGTVI 258
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 1-227 4.22e-32

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: 117.47  E-value: 4.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282    1 MKVLKIGGSVLTEKhteekkvrmEVLDRIASEIAP-RADG--LILVHGAGSFGHPEAIRHGVGRRFST-----EGVLKTH 72
Cdd:pfam00696   2 RVVIKLGGSSLTDK---------ERLKRLADEIAAlLEEGrkLVVVHGGGAFADGLLALLGLSPRFARltdaeTLEVATM 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282   73 QSVCLLNRIVVSALVRGGVPAVPVSPLGCAIADGGRLV----SMEMTPILHMVERGLVPVLHGDVVMDRTLGAAVVSGDA 148
Cdd:pfam00696  73 DALGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDdvvtRIDTEALEELLEAGVVPVITGFIGIDPEGELGRGSSDT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282  149 LVAHIAKGLGAHHVGMGTSAQGVLDAHGRTIPEVTEHNIEQVRQWVRPSGGGDATGGMVGKVEELWRLAGEG-IESWVFS 227
Cdd:pfam00696 153 LAALLAEALGADKLIILTDVDGVYTADPRKVPDAKLIPEISYDELLELLASGLATGGMKVKLPAALEAARRGgIPVVIVN 232
AAK_NAGK-like cd04238
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ...
 3-211 4.74e-09

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: 55.21  E-value: 4.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282   3 VLKIGGSVLTEKhteekkvrmEVLDRIASEIA-PRADG--LILVHGAG--------SFGHPEAIRHgvGRRFSTEGVLKT 71
Cdd:cd04238    2 VIKYGGSAMKDE---------ELKEAFADDIVlLKQVGinPVIVHGGGpeinellkRLGIESEFVN--GLRVTDKETMEI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282  72 HQSV--CLLNRIVVSALVRGGVPAVPVS----------PLGCAIADG---GRLVSMEMTPILHMVERGLVPVLhGDVVMD 136
Cdd:cd04238   71 VEMVlaGKVNKELVSLLNRAGGKAVGLSgkdgglikaeKKEEKDIDLgfvGEVTEVNPELLETLLEAGYIPVI-APIAVD 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757131282 137 RTLGAAVVSGDALVAHIAKGLGAHHVGMGTSAQGVLDAHGRTIPEVTEHNIEQVRQwvrpsgGGDATGGMVGKVE 211
Cdd:cd04238  150 EDGETYNVNADTAAGAIAAALKAEKLILLTDVPGVLDDPGSLISELTPKEAEELIE------DGVISGGMIPKVE 218
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 3-247 5.11e-08

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: 52.44  E-value: 5.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282   3 VLKIGGSVLTEKHteekkvRMEVLDRIASEIAPRADGLILVHGAGSFGHPEAIRHGVGRRFSTE-GVLKTHQSVCL---- 77
Cdd:cd02115    1 VIKFGGSSVSSEE------RLRNLARILVKLASEGGRVVVVHGAGPQITDELLAHGELLGYARGlRITDRETDALAamge 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282  78 --LNRIVVSALVRGGVPAVPVSPLGCAIADGGRLVSMEMTPI----LHM-VERGLVPVLHGDVVMDRTLGA--AVVSGDA 148
Cdd:cd02115   75 gmSNLLIAAALEQHGIKAVPLDLTQAGFASPNQGHVGKITKVstdrLKSlLENGILPILSGFGGTDEKETGtlGRGGSDS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282 149 LVAHIAKGLGAHHVGMGTSAQGVLDAHGRTIPE---VTEHNIEQVRQWVrpsgggdATGGMVGKVEELWRLAGEGIESWV 225
Cdd:cd02115  155 TAALLAAALKADRLVILTDVDGVYTADPRKVPDaklLSELTYEEAAELA-------YAGAMVLKPKAADPAARAGIPVRI 227

                        250       260
                 ....*....|....*....|..
gi 757131282 226 FSALDEGAVAAFLDGHPvGTRV 247
Cdd:cd02115  228 ANTENPGALALFTPDGG-GTLI 248
AAK_NAGK-UC cd04251
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ...
 2-196 1.16e-07

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: 51.22  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282   2 KVLKIGGSVLTEkhteekkvrmevLDRIASEIAPRADGLILVHGAG--------SFGH-PEAIRH--GVGRRFSTEGVLK 70
Cdd:cd04251    1 IVVKIGGSVVSD------------LDKVIDDIANFGERLIVVHGGGnyvneylkRLGVePKFVTSpsGIRSRYTDKETLE 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282  71 THQSVC-LLNRIVVSALVRGGVPAVPVSPLGCAIA----------------------DGGRLVSMEMTPILHMVERGLVP 127
Cdd:cd04251   69 VFVMVMgLINKKIVARLHSLGVKAVGLTGLDGRLLeakrkeivrvnergrkmiirggYTGKVEKVNSDLIEALLDAGYLP 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757131282 128 VLhGDVVMDRTLGAAVVSGDALVAHIAKGLGAHHVGMGTSAQGVLdAHGRTIPEVTEHNIEQVRQWVRP 196
Cdd:cd04251  149 VV-SPVAYSEEGEPLNVDGDRAAAAIAAALKAERLILLTDVEGLY-LDGRVIERITVSDAESLLEKAGG 215
AAK_NAGK-NC cd04249
AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation ...
 3-247 3.12e-05

AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis using the acetylated, noncyclic route of ornithine biosynthesis. There are two variants of this pathway. In one, typified by the pathway in Escherichia coli, glutamate is acetylated by acetyl-CoA and acetylornithine is deacylated hydrolytically. In this pathway, feedback inhibition by arginine occurs at the initial acetylation of glutamate and not at the phosphorylation of NAG by NAGK. Homodimeric NAGK-NC are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239782 [Multi-domain]  Cd Length: 252  Bit Score: 43.94  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282   3 VLKIGGSVLTEKHTEEKkvrmeVLDRIASEIAPRADGLILVHGAGSF--------GHPEAIRHGVGRRFSTEGVLKTHQS 74
Cdd:cd04249    2 VIKLGGALLETEAALEQ-----LFSALSEYQQQHNRQLVIVHGGGCVvdellkklNFPSEKKNGLRVTPKEQIPYITGAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282  75 VCLLNRIVVSALVRGGVPAVpvsplGCAIADGGRLVSMEMTPILHMV---------------ERGLVPVLHGDVVMDRTL 139
Cdd:cd04249   77 AGTANKQLMAQAIKAGLKPV-----GLSLADGGMTAVTQLDPELGAVgkatandpsllndllKAGFLPIISSIGADDQGQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282 140 GAAVVSGDALVAhIAKGLGAHHVgMGTSAQGVLDAHGRTIPEVTEHNIEQVRQwvrpsgGGDATGGMVGKVEELWRLA-- 217
Cdd:cd04249  152 LMNVNADQAATA-IAQLLNADLV-LLSDVSGVLDADKQLISELNAKQAAELIE------QGVITDGMIVKVNAALDAAqs 223

                        250       260       270
                 ....*....|....*....|....*....|...
gi 757131282 218 -GEGIE--SWVFSAldegAVAAFLDGHPVGTRV 247
Cdd:cd04249  224 lRRGIDiaSWQYPE----QLTALLAGEPVGTKI 252
ArgB COG0548
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ...
 3-211 3.38e-05

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: 43.87  E-value: 3.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282   3 VLKIGGSVLTEKhteekkvrmEVLDRIASEIAP-RADG--LILVHGAGsfghPEaI-----RHGV------GRRFST--- 65
Cdd:COG0548   27 VIKYGGEAMEDE---------ELKAALAQDIALlKSLGirPVLVHGGG----PQ-InellkRLGIesefvnGLRVTDeet 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282  66 ----EGVLkthqsVCLLNRIVVSALVRGGVPAVPVS----------PLGcaIADG------GRLVSMEMTPILHMVERGL 125
Cdd:COG0548   93 levvEMVL-----AGKVNKEIVALLSQGGGNAVGLSgkdgnlitarPLG--VGDGvdlghvGEVRRVDPELIRALLDAGY 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282 126 VPVLhgdvvmdRTLGAAV------VSGDALVAHIAKGLGAHHVGMGTSAQGVLDAHGRTIPEVTehnIEQVRQWVRpsgG 199
Cdd:COG0548  166 IPVI-------SPIGYSPtgevynINADTVAGAIAAALKAEKLILLTDVPGVLDDPGSLISELT---AAEAEELIA---D 232

                        250
                 ....*....|..
gi 757131282 200 GDATGGMVGKVE 211
Cdd:COG0548  233 GVISGGMIPKLE 244
PRK14058 PRK14058
[LysW]-aminoadipate/[LysW]-glutamate kinase;
1-249 5.82e-05

[LysW]-aminoadipate/[LysW]-glutamate kinase;


Pssm-ID: 237599 [Multi-domain]  Cd Length: 268  Bit Score: 43.35  E-value: 5.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282   1 MKVLKIGGSVLTEKhteekkvrMEVLDRIASeIAPRADGLILVHGAGS--------FGH-PEAIRH--GVGRRFSTEGVL 69
Cdd:PRK14058   1 MIVVKIGGSVGIDP--------EDALIDVAS-LWADGERVVLVHGGSDevnellerLGIePRFVTSpsGVTSRYTDRETL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282  70 KTHQSV-CLLNRIVVSALVRGGVPAVPVSPLGCAIADG----------------------GRLVSMEMTPILHMVERGLV 126
Cdd:PRK14058  72 EVFIMAmALINKQLVERLQSLGVNAVGLSGLDGGLLEGkrkkavrvveegkkkiirgdytGKIEEVNTDLLKLLLKAGYL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282 127 PVLhgDVVMDRTLGAAV-VSGDALVAHIAKGLGAHHVGMGTSAQGVL---DAHGRTIPEVTEHNIEQVRQWVRpsgggda 202
Cdd:PRK14058 152 PVV--APPALSEEGEPLnVDGDRAAAAIAGALKAEALVLLSDVPGLLrdpPDEGSLIERITPEEAEELSKAAG------- 222

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 757131282 203 tGGMVGKVEelwrLAGEGIESWVF-----SALDEGAVAAFLDGHpvGTRVRN 249
Cdd:PRK14058 223 -GGMKKKVL----MAAEAVEGGVGrviiaDANVDDPISAALAGE--GTVIVN 267
AAK_G5K_ProB cd04242
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ...
 147-246 2.56e-04

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: 41.27  E-value: 2.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757131282 147 DALVAHIAKGLGAHHVGMGTSAQGVLDAHGRT------IPEVTEHnIEQVRQWVRPSGGGDATGGMVGKVEELWRLAGEG 220
Cdd:cd04242  145 DRLSALVAGLVNADLLILLSDVDGLYDKNPREnpdaklIPEVEEI-TDEIEAMAGGSGSSVGTGGMRTKLKAARIATEAG 223

                         90       100
                 ....*....|....*....|....*.
gi 757131282 221 IESWVFSALDEGAVAAFLDGHPVGTR 246
Cdd:cd04242  224 IPVVIANGRKPDVLLDILAGEAVGTL 249
 
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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