|
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
|
|
| |
