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Conserved domains on  [gi|295789370|pdb|3K4O|B]
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Chain B, isopentenyl phosphate kinase

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;
10-262 8.27e-115

isopentenyl phosphate kinase;


:

Pssm-ID: 468614 [Multi-domain]  Cd Length: 258  Bit Score: 329.95  E-value: 8.27e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B        10 ILKLGGSILSDKNVPYSIKWDNLERIAMEIKNALDYyknqnkeIKLILVHGGGAFGHPVAKKYLKIEDG-KKIFINMEKG 88
Cdd:NF040647   2 ILKLGGSVITDKDIYPKIDWDNLERIAKEISNALDE-------DKLIIVHGGGSFGHPKAKKYGIGEGInGEEFERKRKG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B        89 FWEIQRAMRRFNNIIIDTLQSYDIPAVSIQPSSFVVFGDK--LIFDTSAIKEMLKRNLVPVIHGDIVIDDKNGYRIISGD 166
Cdd:NF040647  75 FWETQNAMRRLNNLVCDALIEYGIPAVSIQPSSFIRTGNKriLHFDLDLIKKYLELGFVPVLYGDVVLDNNIKYGILSGD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       167 DIVPYLANELKADLILYATDVDGVLIDN----KPIKRIDKNNIYKILNYLSGSNSIDVTGGMKYKIEM---IRKNKCRGF 239
Cdd:NF040647 155 QIIPYLAKKLKPDRVILGSDVDGVYDKNpkkyPDAKLIDKVNSLDDLESLEGTNNVDVTGGMYGKVKEllkLAELGIESY 234

                        250       260
                 ....*....|....*....|....
3K4O_B       240 VFNGNKANNIYKALLGE-VEGTEI 262
Cdd:NF040647 235 IINGNKPENIYKALGGEkVIGTVI 258
 
Name Accession Description Interval E-value
IPPK_Arch NF040647
isopentenyl phosphate kinase;
10-262 8.27e-115

isopentenyl phosphate kinase;


Pssm-ID: 468614 [Multi-domain]  Cd Length: 258  Bit Score: 329.95  E-value: 8.27e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B        10 ILKLGGSILSDKNVPYSIKWDNLERIAMEIKNALDYyknqnkeIKLILVHGGGAFGHPVAKKYLKIEDG-KKIFINMEKG 88
Cdd:NF040647   2 ILKLGGSVITDKDIYPKIDWDNLERIAKEISNALDE-------DKLIIVHGGGSFGHPKAKKYGIGEGInGEEFERKRKG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B        89 FWEIQRAMRRFNNIIIDTLQSYDIPAVSIQPSSFVVFGDK--LIFDTSAIKEMLKRNLVPVIHGDIVIDDKNGYRIISGD 166
Cdd:NF040647  75 FWETQNAMRRLNNLVCDALIEYGIPAVSIQPSSFIRTGNKriLHFDLDLIKKYLELGFVPVLYGDVVLDNNIKYGILSGD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       167 DIVPYLANELKADLILYATDVDGVLIDN----KPIKRIDKNNIYKILNYLSGSNSIDVTGGMKYKIEM---IRKNKCRGF 239
Cdd:NF040647 155 QIIPYLAKKLKPDRVILGSDVDGVYDKNpkkyPDAKLIDKVNSLDDLESLEGTNNVDVTGGMYGKVKEllkLAELGIESY 234

                        250       260
                 ....*....|....*....|....
3K4O_B       240 VFNGNKANNIYKALLGE-VEGTEI 262
Cdd:NF040647 235 IINGNKPENIYKALGGEkVIGTVI 258
COG1608 COG1608
Isopentenyl phosphate kinase [Lipid transport and metabolism];
8-263 7.63e-109

Isopentenyl phosphate kinase [Lipid transport and metabolism];


Pssm-ID: 441216 [Multi-domain]  Cd Length: 254  Bit Score: 314.85  E-value: 7.63e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B        8 LTILKLGGSILSDKNVPYSIKWDNLERIAMEIKNALDyyknqnkeIKLILVHGGGAFGHPVAKKYlkiEDGKKIFINMEK 87
Cdd:COG1608   1 MIVLKLGGSVITDKDKPETVRRDALERIAREIAAALD--------LDLVIVHGGGSFGHPVAKKY---GLHGTLGTEDAE 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       88 GFWEIQRAMRRFNNIIIDTLQSYDIPAVSIQPSSFVVF--GDKLIFDTSAIKEMLKRNLVPVIHGDIVIDDKNGYRIISG 165
Cdd:COG1608  70 GVSETHRAMRELNRIVVDALLEAGVPAVSVPPSSFAVRdnGRILSFDTEPIKEMLEEGFVPVLHGDVVFDAERGFTILSG 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B      166 DDIVPYLANELKADLILYATDVDGVLIDN---KPIKRIDKNNIYKILNYLSGSNSIDVTGGMKYKIEMIRKNKCRG---F 239
Cdd:COG1608 150 DEIVVYLAKELKPERVGLATDVDGVYDDDpkgKLIPEITRSNFDEVLDALGGSAGTDVTGGMAGKVEELLELAKPGvevY 229

                       250       260
                ....*....|....*....|....*
3K4O_B      240 VFNGNKANNIYKALLGE-VEGTEID 263
Cdd:COG1608 230 IFNGNKPGNLSAALRGEeVRGTRIR 254
AAK_FomA-like cd04241
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ...
 8-262 3.06e-103

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: 300.33  E-value: 3.06e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B        8 LTILKLGGSILSDKNVPYSIKWDNLERIAMEIKNALDyyknqnkeIKLILVHGGGAFGHPVAKKYLKiedGKKIFINMEK 87
Cdd:cd04241   1 MIILKLGGSVITDKDRPETIREENLERIARELAEAID--------EKLVLVHGGGSFGHPKAKEYGL---PDGDGSFSAE 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       88 GFWEIQRAMRRFNNIIIDTLQSYDIPAVSIQPSSFVVF--GDKLIFDTSAIKEMLKRNLVPVIHGDIVIDDKNGYRIISG 165
Cdd:cd04241  70 GVAETHEAMLELNSIVVDALLEAGVPAVSVPPSSFFVTenGRIVSFDLEVIKELLDRGFVPVLHGDVVLDEGGGITILSG 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B      166 DDIVPYLANELKADLILYATDVDGVLIDN----KPIKRIDKNNIYKILNYLsGSNSIDVTGGMKYKIEMIRKNKCRG--- 238
Cdd:cd04241 150 DDIVVELAKALKPERVIFLTDVDGVYDKPppdaKLIPEIDVGSLEDILAAL-GSAGTDVTGGMAGKIEELLELARRGiev 228

                       250       260
                ....*....|....*....|....
3K4O_B      239 FVFNGNKANNIYKALLGEVEGTEI 262
Cdd:cd04241 229 YIFNGDKPENLYRALLGNFIGTRI 252
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 7-242 6.51e-44

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: 148.67  E-value: 6.51e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B          7 MLTILKLGGSILSDKnvpysikwDNLERIAMEIKNALdyyknqNKEIKLILVHGGGAFGHPVAKKYlKIEDGKKIFINME 86
Cdd:pfam00696   1 KRVVIKLGGSSLTDK--------ERLKRLADEIAALL------EEGRKLVVVHGGGAFADGLLALL-GLSPRFARLTDAE 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B         87 KGFWEIQRAMRRFNNIIIDTLQSYDIPAVSIQPSSFVVFGDKLI------FDTSAIKEMLKRNLVPVIHGDIVIDDKNGY 160
Cdd:pfam00696  66 TLEVATMDALGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIddvvtrIDTEALEELLEAGVVPVITGFIGIDPEGEL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B        161 RIISGDDIVPYLANELKADLILYATDVDGVLIDNKpiKRIDKNNIYKILNY---LSGSNSIDVTGGMKYKI----EMIRK 233
Cdd:pfam00696 146 GRGSSDTLAALLAEALGADKLIILTDVDGVYTADP--RKVPDAKLIPEISYdelLELLASGLATGGMKVKLpaalEAARR 223


                  ....*....
3K4O_B        234 NKCRGFVFN 242
Cdd:pfam00696 224 GGIPVVIVN 232
argB TIGR00761
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ...
 10-231 5.80e-10

acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many prokaryotes and the N-acetylglutamate kinase domains of multifunctional proteins from yeasts. This enzyme is the second step in the "acetylated" ornithine biosynthesis pathway. A related group of enzymes representing the first step of the pathway contain a homologous domain and are excluded from this model. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273256 [Multi-domain]  Cd Length: 231  Bit Score: 58.06  E-value: 5.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B         10 ILKLGGSILSDknvpysikwdNLERIAMEIKNaldYYKNQnkeIKLILVHGGG--------AFGHPVAKK-YLKIEDGKK 80
Cdd:TIGR00761   3 VIKIGGAAISD----------LLEAFASDIAF---LRAVG---IKPVIVHGGGpeinelleALGIPPEFKnGLRVTDKET 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B         81 IfinmekgfwEIQRA--MRRFNNIIIDTLQSYDIPAVSIQPSSFVVF-GDKLIFD------------TSAIKEMLKRNLV 145
Cdd:TIGR00761  67 L---------EVVEMvlIGQVNKELVALLNKHGINAIGLTGGDGQLFtARYLDKEdlgyvgeikkvnKALIEALLKAGYI 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B        146 PVIhGDIVIDDKNGYRIISGDDIVPYLANELKADLILYATDVDGVLiDNKPIKRIDKNNIYKILNYLSGSnsiDVTGGMK 225
Cdd:TIGR00761 138 PVI-SSLALTAEGQALNVNADTAAGALAAALGAEKLVLLTDVPGIL-NGDGQSLISEIPLDEIEQLIKQG---IIKGGMI 212


                  ....*.
3K4O_B        226 YKIEMI 231
Cdd:TIGR00761 213 PKVNAA 218
PRK14058 PRK14058
[LysW]-aminoadipate/[LysW]-glutamate kinase;
132-262 2.81e-06

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


Pssm-ID: 237599 [Multi-domain]  Cd Length: 268  Bit Score: 47.20  E-value: 2.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       132 DTSAIKEMLKRNLVPVIhGDIVIDDKNGYRIISGDDIVPYLANELKADLILYATDVDGVLID----NKPIKRIDKNNIYK 207
Cdd:PRK14058 138 NTDLLKLLLKAGYLPVV-APPALSEEGEPLNVDGDRAAAAIAGALKAEALVLLSDVPGLLRDppdeGSLIERITPEEAEE 216

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
3K4O_B       208 ILNYlsgsnsidVTGGMKYKIEMIRKNKCRG----FVFNGNKANNIYKALLGevEGTEI 262
Cdd:PRK14058 217 LSKA--------AGGGMKKKVLMAAEAVEGGvgrvIIADANVDDPISAALAG--EGTVI 265
 
Name Accession Description Interval E-value
IPPK_Arch NF040647
isopentenyl phosphate kinase;
10-262 8.27e-115

isopentenyl phosphate kinase;


Pssm-ID: 468614 [Multi-domain]  Cd Length: 258  Bit Score: 329.95  E-value: 8.27e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B        10 ILKLGGSILSDKNVPYSIKWDNLERIAMEIKNALDYyknqnkeIKLILVHGGGAFGHPVAKKYLKIEDG-KKIFINMEKG 88
Cdd:NF040647   2 ILKLGGSVITDKDIYPKIDWDNLERIAKEISNALDE-------DKLIIVHGGGSFGHPKAKKYGIGEGInGEEFERKRKG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B        89 FWEIQRAMRRFNNIIIDTLQSYDIPAVSIQPSSFVVFGDK--LIFDTSAIKEMLKRNLVPVIHGDIVIDDKNGYRIISGD 166
Cdd:NF040647  75 FWETQNAMRRLNNLVCDALIEYGIPAVSIQPSSFIRTGNKriLHFDLDLIKKYLELGFVPVLYGDVVLDNNIKYGILSGD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       167 DIVPYLANELKADLILYATDVDGVLIDN----KPIKRIDKNNIYKILNYLSGSNSIDVTGGMKYKIEM---IRKNKCRGF 239
Cdd:NF040647 155 QIIPYLAKKLKPDRVILGSDVDGVYDKNpkkyPDAKLIDKVNSLDDLESLEGTNNVDVTGGMYGKVKEllkLAELGIESY 234

                        250       260
                 ....*....|....*....|....
3K4O_B       240 VFNGNKANNIYKALLGE-VEGTEI 262
Cdd:NF040647 235 IINGNKPENIYKALGGEkVIGTVI 258
COG1608 COG1608
Isopentenyl phosphate kinase [Lipid transport and metabolism];
8-263 7.63e-109

Isopentenyl phosphate kinase [Lipid transport and metabolism];


Pssm-ID: 441216 [Multi-domain]  Cd Length: 254  Bit Score: 314.85  E-value: 7.63e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B        8 LTILKLGGSILSDKNVPYSIKWDNLERIAMEIKNALDyyknqnkeIKLILVHGGGAFGHPVAKKYlkiEDGKKIFINMEK 87
Cdd:COG1608   1 MIVLKLGGSVITDKDKPETVRRDALERIAREIAAALD--------LDLVIVHGGGSFGHPVAKKY---GLHGTLGTEDAE 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       88 GFWEIQRAMRRFNNIIIDTLQSYDIPAVSIQPSSFVVF--GDKLIFDTSAIKEMLKRNLVPVIHGDIVIDDKNGYRIISG 165
Cdd:COG1608  70 GVSETHRAMRELNRIVVDALLEAGVPAVSVPPSSFAVRdnGRILSFDTEPIKEMLEEGFVPVLHGDVVFDAERGFTILSG 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B      166 DDIVPYLANELKADLILYATDVDGVLIDN---KPIKRIDKNNIYKILNYLSGSNSIDVTGGMKYKIEMIRKNKCRG---F 239
Cdd:COG1608 150 DEIVVYLAKELKPERVGLATDVDGVYDDDpkgKLIPEITRSNFDEVLDALGGSAGTDVTGGMAGKVEELLELAKPGvevY 229

                       250       260
                ....*....|....*....|....*
3K4O_B      240 VFNGNKANNIYKALLGE-VEGTEID 263
Cdd:COG1608 230 IFNGNKPGNLSAALRGEeVRGTRIR 254
AAK_FomA-like cd04241
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ...
 8-262 3.06e-103

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: 300.33  E-value: 3.06e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B        8 LTILKLGGSILSDKNVPYSIKWDNLERIAMEIKNALDyyknqnkeIKLILVHGGGAFGHPVAKKYLKiedGKKIFINMEK 87
Cdd:cd04241   1 MIILKLGGSVITDKDRPETIREENLERIARELAEAID--------EKLVLVHGGGSFGHPKAKEYGL---PDGDGSFSAE 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       88 GFWEIQRAMRRFNNIIIDTLQSYDIPAVSIQPSSFVVF--GDKLIFDTSAIKEMLKRNLVPVIHGDIVIDDKNGYRIISG 165
Cdd:cd04241  70 GVAETHEAMLELNSIVVDALLEAGVPAVSVPPSSFFVTenGRIVSFDLEVIKELLDRGFVPVLHGDVVLDEGGGITILSG 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B      166 DDIVPYLANELKADLILYATDVDGVLIDN----KPIKRIDKNNIYKILNYLsGSNSIDVTGGMKYKIEMIRKNKCRG--- 238
Cdd:cd04241 150 DDIVVELAKALKPERVIFLTDVDGVYDKPppdaKLIPEIDVGSLEDILAAL-GSAGTDVTGGMAGKIEELLELARRGiev 228

                       250       260
                ....*....|....*....|....
3K4O_B      239 FVFNGNKANNIYKALLGEVEGTEI 262
Cdd:cd04241 229 YIFNGDKPENLYRALLGNFIGTRI 252
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 7-242 6.51e-44

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: 148.67  E-value: 6.51e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B          7 MLTILKLGGSILSDKnvpysikwDNLERIAMEIKNALdyyknqNKEIKLILVHGGGAFGHPVAKKYlKIEDGKKIFINME 86
Cdd:pfam00696   1 KRVVIKLGGSSLTDK--------ERLKRLADEIAALL------EEGRKLVVVHGGGAFADGLLALL-GLSPRFARLTDAE 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B         87 KGFWEIQRAMRRFNNIIIDTLQSYDIPAVSIQPSSFVVFGDKLI------FDTSAIKEMLKRNLVPVIHGDIVIDDKNGY 160
Cdd:pfam00696  66 TLEVATMDALGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIddvvtrIDTEALEELLEAGVVPVITGFIGIDPEGEL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B        161 RIISGDDIVPYLANELKADLILYATDVDGVLIDNKpiKRIDKNNIYKILNY---LSGSNSIDVTGGMKYKI----EMIRK 233
Cdd:pfam00696 146 GRGSSDTLAALLAEALGADKLIILTDVDGVYTADP--RKVPDAKLIPEISYdelLELLASGLATGGMKVKLpaalEAARR 223


                  ....*....
3K4O_B        234 NKCRGFVFN 242
Cdd:pfam00696 224 GGIPVVIVN 232
AAK_UMPK-like cd04239
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ...
 8-263 1.17e-19

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: 84.90  E-value: 1.17e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B        8 LTILKLGGSILSDKNVPYSIkwDNLERIAMEIKNALDyyknqnKEIKLILVHGGGAFGHPVAKKYLKIEDGKKIFINMEK 87
Cdd:cd04239   1 RIVLKLSGEALAGEGGGIDP--EVLKEIAREIKEVVD------LGVEVAIVVGGGNIARGYIAAARGMPRATADYIGMLA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       88 gfwEIQRAMrrfnnIIIDTLQSYDIPAVsiQPSSFVVFGDKLIFDTSAIKEMLKRNLVPVIHGDIVIddkngyriisgdd 167
Cdd:cd04239  73 ---TVMNAL-----ALQDALEKLGVKTR--VMSAIPMQGVAEPYIRRRAIRHLEKGRIVIFGGGTGN------------- 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B      168 ivPY---------LANELKADLILYATDVDGVLiDNKPikRIDKNNI-YKILNYL----SGSNSIDVTGgmkykIEMIRK 233
Cdd:cd04239 130 --PGfttdtaaalRAEEIGADVLLKATNVDGVY-DADP--KKNPDAKkYDRISYDellkKGLKVMDATA-----LTLCRR 199

                       250       260       270
                ....*....|....*....|....*....|
3K4O_B      234 NKCRGFVFNGNKANNIYKALLGEVEGTEID 263
Cdd:cd04239 200 NKIPIIVFNGLKPGNLLRALKGEHVGTLIE 229
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 10-262 3.41e-15

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: 72.86  E-value: 3.41e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       10 ILKLGGSILSDKnvpysikwDNLERIAMEIKnaldyyKNQNKEIKLILVHGGGAFGHPVakkYLKIEDGKKIFINMEKGF 89
Cdd:cd02115   1 VIKFGGSSVSSE--------ERLRNLARILV------KLASEGGRVVVVHGAGPQITDE---LLAHGELLGYARGLRITD 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       90 WE----IQRAMRRFNNIIIDTLQSYDIPAVSIQPSSFVVFGDKLIF-------DTSAIKEMLKRNLVPVIHGDIVIDDKN 158
Cdd:cd02115  64 REtdalAAMGEGMSNLLIAAALEQHGIKAVPLDLTQAGFASPNQGHvgkitkvSTDRLKSLLENGILPILSGFGGTDEKE 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B      159 GYRIISGD-DIVP-YLANELKADLILYATDVDGVLIDNKPI----KRIDKNNIYKILNYLSgsnsidvTGGMKYK---IE 229
Cdd:cd02115 144 TGTLGRGGsDSTAaLLAAALKADRLVILTDVDGVYTADPRKvpdaKLLSELTYEEAAELAY-------AGAMVLKpkaAD 216

                       250       260       270
                ....*....|....*....|....*....|...
3K4O_B      230 MIRKNKCRGFVFNGNKANNIyKALLGEVEGTEI 262
Cdd:cd02115 217 PAARAGIPVRIANTENPGAL-ALFTPDGGGTLI 248
AAK_UMPK-PyrH-Pf cd04253
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ...
 8-263 1.74e-10

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: 59.18  E-value: 1.74e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B        8 LTILKLGGSILSDKNvpysiKWDNLERIAMEIKNALDYYKnqnkeikLILVHGGGAfghpVAKKYlkIEDGKKIFINmEK 87
Cdd:cd04253   1 RIVISLGGSVLAPEK-----DADFIKEYANVLRKISDGHK-------VAVVVGGGR----LAREY--ISVARKLGAS-EA 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       88 GFWEIQRAMRRFNNIIIDTLQSYDIPAVsiqPSSFVVFgdklifdtsaiKEMLKRNLVPVIHGDividdKNGYriiSGDD 167
Cdd:cd04253  62 FLDEIGIMATRLNARLLIAALGDAYPPV---PTSYEEA-----------LEAMFTGKIVVMGGT-----EPGQ---STDA 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B      168 IVPYLANELKADLILYATDVDGVLID----NKPIKRIDKNNIYKILNYLS------GSNS-IDVTGgmkykIEMIRKNKC 236
Cdd:cd04253 120 VAALLAERLGADLLINATNVDGVYSKdprkDPDAKKFDRLSADELIDIVGksswkaGSNEpFDPLA-----AKIIERSGI 194

                       250       260
                ....*....|....*....|....*..
3K4O_B      237 RGFVFNGNKANNIYKALLGEVEGTEID 263
Cdd:cd04253 195 KTIVVDGRDPENLERALKGEFVGTIIE 221
argB TIGR00761
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ...
 10-231 5.80e-10

acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many prokaryotes and the N-acetylglutamate kinase domains of multifunctional proteins from yeasts. This enzyme is the second step in the "acetylated" ornithine biosynthesis pathway. A related group of enzymes representing the first step of the pathway contain a homologous domain and are excluded from this model. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273256 [Multi-domain]  Cd Length: 231  Bit Score: 58.06  E-value: 5.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B         10 ILKLGGSILSDknvpysikwdNLERIAMEIKNaldYYKNQnkeIKLILVHGGG--------AFGHPVAKK-YLKIEDGKK 80
Cdd:TIGR00761   3 VIKIGGAAISD----------LLEAFASDIAF---LRAVG---IKPVIVHGGGpeinelleALGIPPEFKnGLRVTDKET 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B         81 IfinmekgfwEIQRA--MRRFNNIIIDTLQSYDIPAVSIQPSSFVVF-GDKLIFD------------TSAIKEMLKRNLV 145
Cdd:TIGR00761  67 L---------EVVEMvlIGQVNKELVALLNKHGINAIGLTGGDGQLFtARYLDKEdlgyvgeikkvnKALIEALLKAGYI 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B        146 PVIhGDIVIDDKNGYRIISGDDIVPYLANELKADLILYATDVDGVLiDNKPIKRIDKNNIYKILNYLSGSnsiDVTGGMK 225
Cdd:TIGR00761 138 PVI-SSLALTAEGQALNVNADTAAGALAAALGAEKLVLLTDVPGIL-NGDGQSLISEIPLDEIEQLIKQG---IIKGGMI 212


                  ....*.
3K4O_B        226 YKIEMI 231
Cdd:TIGR00761 213 PKVNAA 218
AAK_NAGK-UC cd04251
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ...
 10-230 2.75e-08

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: 53.14  E-value: 2.75e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       10 ILKLGGSILSDknvpysikwdnLERIAMEIknaldyyknQNKEIKLILVHGGG--------AFGHPvaKKYLKIEDGK-- 79
Cdd:cd04251   2 VVKIGGSVVSD-----------LDKVIDDI---------ANFGERLIVVHGGGnyvneylkRLGVE--PKFVTSPSGIrs 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       80 --------KIFInMekgfweiqrAMRRFNNIIIDTLQSYDIPAVSI-------------QPSSFVVFGDKLIFD---TSA 135
Cdd:cd04251  60 rytdketlEVFV-M---------VMGLINKKIVARLHSLGVKAVGLtgldgrlleakrkEIVRVNERGRKMIIRggyTGK 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B      136 IKE--------MLKRNLVPVIhGDIVIDDKNGYRIISGDDIVPYLANELKADLILYATDVDGVLIDNKPIKRIDKNNIYK 207
Cdd:cd04251 130 VEKvnsdlieaLLDAGYLPVV-SPVAYSEEGEPLNVDGDRAAAAIAAALKAERLILLTDVEGLYLDGRVIERITVSDAES 208

                       250       260
                ....*....|....*....|...
3K4O_B      208 ILNYlsgsnsidVTGGMKYKIEM 230
Cdd:cd04251 209 LLEK--------AGGGMKRKLLA 223
AAK_NAGK-like cd04238
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ...
 10-262 8.20e-08

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: 51.74  E-value: 8.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       10 ILKLGGSILSDKNVpysikwdnLERIAMEIKNaldyYKNQNkeIKLILVHGGGafghPVAKKYLKIEDGKKIFIN----- 84
Cdd:cd04238   2 VIKYGGSAMKDEEL--------KEAFADDIVL----LKQVG--INPVIVHGGG----PEINELLKRLGIESEFVNglrvt 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       85 ----MEKgfweIQRAMR-RFNNIIIDTLQSYDIPAV--------SIQPSSFVVFGDKLIF-------DTSAIKEMLKRNL 144
Cdd:cd04238  64 dketMEI----VEMVLAgKVNKELVSLLNRAGGKAVglsgkdggLIKAEKKEEKDIDLGFvgevtevNPELLETLLEAGY 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B      145 VPVIhGDIVIDDKNGYRIISGDDIVPYLANELKADLILYATDVDGVLIDN-KPIKRIDKNNIykilNYLSGSNSIdvTGG 223
Cdd:cd04238 140 IPVI-APIAVDEDGETYNVNADTAAGAIAAALKAEKLILLTDVPGVLDDPgSLISELTPKEA----EELIEDGVI--SGG 212

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
3K4O_B      224 MKYKIEMIRK--NKCRGFVF--NGNKANNIYKALLGEVE-GTEI 262
Cdd:cd04238 213 MIPKVEAALEalEGGVRKVHiiDGRVPHSLLLELFTDEGiGTMI 256
AAK_G5K_ProB cd04242
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ...
 134-260 2.89e-07

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: 50.13  E-value: 2.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B      134 SAIKEMLKRNLVPVIH-------GDIVIDDkNgyriisgDDIVPYLANELKADLILYATDVDGVLIDN-------KPIKR 199
Cdd:cd04242 114 NTLETLLELGVIPIINendtvatEEIRFGD-N-------DRLSALVAGLVNADLLILLSDVDGLYDKNprenpdaKLIPE 185

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
3K4O_B      200 IDKNNIYkILNYLSGSNSIDVTGGMKYKIE---MIRKNKCRGFVFNGNKANNIYKALLGEVEGT 260
Cdd:cd04242 186 VEEITDE-IEAMAGGSGSSVGTGGMRTKLKaarIATEAGIPVVIANGRKPDVLLDILAGEAVGT 248
AAK_NAGK-NC cd04249
AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation ...
 10-262 4.89e-07

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: 49.72  E-value: 4.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       10 ILKLGGSILSDKNvpysikwdnleriAME-IKNALDYYKnQNKEIKLILVHGGGAF--------GHPVAKKY-LKIEDGK 79
Cdd:cd04249   2 VIKLGGALLETEA-------------ALEqLFSALSEYQ-QQHNRQLVIVHGGGCVvdellkklNFPSEKKNgLRVTPKE 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       80 KIFI-------NMEKGFweIQRAMRRFNNIIIDTLQSYDIPAVSIQPSSFVVFGDKLIFDTSAIKEMLKRNLVPVIhGDI 152
Cdd:cd04249  68 QIPYitgalagTANKQL--MAQAIKAGLKPVGLSLADGGMTAVTQLDPELGAVGKATANDPSLLNDLLKAGFLPII-SSI 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B      153 VIDDKNGYRIISGDDIVPYLANELKADLILYaTDVDGVLIDNK-PIKRIDKNNIYKILNylSGSnsidVTGGMKYKIEM- 230
Cdd:cd04249 145 GADDQGQLMNVNADQAATAIAQLLNADLVLL-SDVSGVLDADKqLISELNAKQAAELIE--QGV----ITDGMIVKVNAa 217

                       250       260       270
                ....*....|....*....|....*....|....*
3K4O_B      231 --IRKNKCRGF-VFNGNKANNIYKALLGEVEGTEI 262
Cdd:cd04249 218 ldAAQSLRRGIdIASWQYPEQLTALLAGEPVGTKI 252
AAK_UMPK-PyrH-Ec cd04254
UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) ...
 173-263 7.33e-07

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: 48.64  E-value: 7.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B      173 ANELKADLILYATDVDGVLiDNKPikRIDKNNI-YKILNYLS----GSNSIDVTGgmkykIEMIRKNKCRGFVFNGNKAN 247
Cdd:cd04254 144 AIEINADVILKATKVDGVY-DADP--KKNPNAKrYDHLTYDEvlskGLKVMDATA-----FTLCRDNNLPIVVFNINEPG 215

                        90
                ....*....|....*.
3K4O_B      248 NIYKALLGEVEGTEID 263
Cdd:cd04254 216 NLLKAVKGEGVGTLIS 231
AAK_UC cd04240
AAK_UC: Uncharacterized (UC) amino acid kinase-like proteins found mainly in archaea and a few ...
 10-262 1.01e-06

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: 48.13  E-value: 1.01e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       10 ILKLGGSILSdknvpysikwdnleriamEIKNALDYYKNQNKEiKLILVHGGGAFGHPVAKKYlkiedgKKIFINMEKGF 89
Cdd:cd04240   1 VVKIGGSLIR------------------EAVRLLRWLKTLSGG-GVVIVPGGGPFADVVRRYQ------ERKGLSDAAAH 55

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       90 WEIQRAMRRFNNIIIDTLQSydipavsiqpssfvvfgdKLIFDTSAIKEMLKRNLVPVI--HGDIVIDD--KNGYRIISg 165
Cdd:cd04240  56 WMAILAMEQYGYLLADLEPR------------------LVARTLAELTDVLERGKIAILlpYRLLLDTDplPHSWEVTS- 116

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B      166 DDIVPYLANELKADLILYATDVDGVLIDN-KPIKRIDKNNiykilnyLSGSNSIDvtggmKYKIEMIRKNKCRGFVFNGN 244
Cdd:cd04240 117 DSIAAWLAKKLGAKRLVIVTDVDGIYEKDgKLVNEIAAAE-------LLGETSVD-----PAFPRLLTKYGIRCYVVNGD 184

                       250
                ....*....|....*....
3K4O_B      245 KANNIYKALLG-EVEGTEI 262
Cdd:cd04240 185 DPERVLAALRGrEGVGTRI 203
PRK14058 PRK14058
[LysW]-aminoadipate/[LysW]-glutamate kinase;
132-262 2.81e-06

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


Pssm-ID: 237599 [Multi-domain]  Cd Length: 268  Bit Score: 47.20  E-value: 2.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       132 DTSAIKEMLKRNLVPVIhGDIVIDDKNGYRIISGDDIVPYLANELKADLILYATDVDGVLID----NKPIKRIDKNNIYK 207
Cdd:PRK14058 138 NTDLLKLLLKAGYLPVV-APPALSEEGEPLNVDGDRAAAAIAGALKAEALVLLSDVPGLLRDppdeGSLIERITPEEAEE 216

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
3K4O_B       208 ILNYlsgsnsidVTGGMKYKIEMIRKNKCRG----FVFNGNKANNIYKALLGevEGTEI 262
Cdd:PRK14058 217 LSKA--------AGGGMKKKVLMAAEAVEGGvgrvIIADANVDDPISAALAG--EGTVI 265
AAK_P5CS_ProBA cd04256
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ...
 133-260 7.83e-06

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: 46.27  E-value: 7.83e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B      133 TSAIKEMLKRNLVPVIH-GDIVIDDKNGYRIISG-------DDIVPYLANELKADLILYATDVDGVLidNKPIKRIDKNN 204
Cdd:cd04256 140 NGTLEELLRLNIIPIINtNDAVSPPPEPDEDLQGvisikdnDSLAARLAVELKADLLILLSDVDGLY--DGPPGSDDAKL 217

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
3K4O_B      205 IYkilNYLS--------GSNSIDVTGGMKYKIE---MIRKNKCRGFVFNGNKANNIYKALLGEVEGT 260
Cdd:cd04256 218 IH---TFYPgdqqsitfGTKSRVGTGGMEAKVKaalWALQGGTSVVITNGMAGDVITKILEGKKVGT 281
PRK00942 PRK00942
acetylglutamate kinase; Provisional
 132-229 1.58e-05

acetylglutamate kinase; Provisional


Pssm-ID: 234869 [Multi-domain]  Cd Length: 283  Bit Score: 45.10  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       132 DTSAIKEMLKRNLVPVIhGDIVIDDKNGYRIISGDDIVPYLANELKADLILYATDVDGVLIDN-KPIKRIDKNNIYKILN 210
Cdd:PRK00942 151 NPALLEALLEAGYIPVI-SPIGVGEDGETYNINADTAAGAIAAALGAEKLILLTDVPGVLDDKgQLISELTASEAEELIE 229

                         90
                 ....*....|....*....
3K4O_B       211 ylSGSnsidVTGGMKYKIE 229
Cdd:PRK00942 230 --DGV----ITGGMIPKVE 242
P5CS TIGR01092
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ...
 133-260 4.14e-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: 44.51  E-value: 4.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B        133 TSAIKEMLKRNLVPVIH-GDIVIDDKNGYRIISG-----DDIVPYLANELKADLILYATDVDGvLIDNKPIKRIDKnniy 206
Cdd:TIGR01092 131 NETVHELLRMNVVPVVNeNDAVSTRAAPYSDSQGifwdnDSLAALLALELKADLLILLSDVEG-LYDGPPSDDDSK---- 205

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
3K4O_B        207 KILNYLSGSNSIDVT---------GGMKYKIEMIRKNKCRG---FVFNGNKANNIYKALLGEVEGT 260
Cdd:TIGR01092 206 LIDTFYKEKHQGEITfgtksrlgrGGMTAKVKAAVWAAYGGtpvIIASGTAPKNITKVVEGKKVGT 271
PRK12354 PRK12354
carbamate kinase; Reviewed
 128-200 2.57e-04

carbamate kinase; Reviewed


Pssm-ID: 183466  Cd Length: 307  Bit Score: 41.74  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       128 KLIFDTSAIKEMLKRNLVpVI---HGDI-VIDDKNGYRI-----ISGDDIVPYLANELKADLILYATDVDGVLID----- 193
Cdd:PRK12354 160 KRIVEIRPIRWLLEKGHL-VIcagGGGIpVVYDADGKLHgveavIDKDLAAALLAEQLDADLLLILTDVDAVYLDwgkpt 238


                 ....*..
3K4O_B       194 NKPIKRI 200
Cdd:PRK12354 239 QRAIAQA 245
AAK_NAGK-C cd04250
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ...
 132-229 4.94e-04

AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in some bacteria and photosynthetic organisms using the non-acetylated, cyclic route of ornithine biosynthesis. In this pathway, glutamate is first N-acetylated and then phosphorylated by NAGK to give phosphoryl NAG, which is converted to NAG-ornithine. There are two variants of this pathway. In one, typified by the pathway in Thermotoga maritima and Pseudomonas aeruginosa, the acetyl group is recycled by reversible transacetylation from acetylornithine to glutamate. The phosphorylation of NAG by NAGK is feedback inhibited by arginine. In photosynthetic organisms, NAGK is the target of the nitrogen-signaling protein PII. Hexameric formation of NAGK domains appears to be essential to both arginine inhibition and NAGK-PII complex formation. NAGK-C are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239783 [Multi-domain]  Cd Length: 279  Bit Score: 40.57  E-value: 4.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B      132 DTSAIKEMLKRNLVPVIhGDIVIDDKNGYRIISGDDIVPYLANELKADLILYATDVDGVLID----NKPIKRIDKNNiyk 207
Cdd:cd04250 147 NPELLETLLEAGYIPVI-APVGVGEDGETYNINADTAAGAIAAALKAEKLILLTDVAGVLDDpndpGSLISEISLKE--- 222

                        90       100
                ....*....|....*....|..
3K4O_B      208 iLNYLSGSNSIdvTGGMKYKIE 229
Cdd:cd04250 223 -AEELIADGII--SGGMIPKVE 241
AAK_CK cd04235
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ...
 130-262 5.27e-04

AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and carbamoyl phosphate (CP) utilization with the production of ATP from ADP and CP. Both CK (this CD) and nonhomologous CP synthetase synthesize carbamoyl phosphate, an essential precursor of arginine and pyrimidine bases, in the presence of ATP, bicarbonate, and ammonia. CK is a homodimer of 33 kDa subunits and is a member of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239768  Cd Length: 308  Bit Score: 40.57  E-value: 5.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B      130 IFDTSAIKEMLKRNLVPVIH--GDI-VIDDKNGYR----IISGDDIVPYLANELKADLILYATDVDGVLID-NKPI-KRI 200
Cdd:cd04235 168 IVEIEAIKTLVDNGVIVIAAggGGIpVVREGGGLKgveaVIDKDLASALLAEEINADLLVILTDVDNVYINfGKPNqKAL 247

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3K4O_B      201 DKNNIYKILNYLS------GSnsidvtggMKYKIE-MIRknkcrgFVFNGNKA------NNIYKALLGEVeGTEI 262
Cdd:cd04235 248 EQVTVEELEKYIEegqfapGS--------MGPKVEaAIR------FVESGGKKaiitslENAEAALEGKA-GTVI 307
ArgB COG0548
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ...
 132-229 6.66e-04

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


Pssm-ID: 440314 [Multi-domain]  Cd Length: 283  Bit Score: 40.40  E-value: 6.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B      132 DTSAIKEMLKRNLVPVIhGDIVIDDK-NGYRIiSGDDIVPYLANELKADLILYATDVDGVL-IDNKPIKRIDKNNIYKIL 209
Cdd:COG0548 153 DPELIRALLDAGYIPVI-SPIGYSPTgEVYNI-NADTVAGAIAAALKAEKLILLTDVPGVLdDPGSLISELTAAEAEELI 230

                        90       100
                ....*....|....*....|
3K4O_B      210 nylsgsNSIDVTGGMKYKIE 229
Cdd:COG0548 231 ------ADGVISGGMIPKLE 244
PRK12353 PRK12353
putative amino acid kinase; Reviewed
 130-262 9.41e-04

putative amino acid kinase; Reviewed


Pssm-ID: 237071  Cd Length: 314  Bit Score: 39.75  E-value: 9.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       130 IFDTSAIKEMLKRNLVPVI--HGDI-VIDDKNGYR----IISGDDIVPYLANELKADLILYATDVDGVLID-NKP-IKRI 200
Cdd:PRK12353 172 IVEIEAIKTLVDAGQVVIAagGGGIpVIREGGGLKgveaVIDKDFASAKLAELVDADLLIILTAVDKVYINfGKPnQKKL 251

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3K4O_B       201 DKNNIYKILNYLS------GSnsidvtggMKYKIEmirknKCRGFVFN--GNKA-----NNIYKALLGEVeGTEI 262
Cdd:PRK12353 252 DEVTVSEAEKYIEegqfapGS--------MLPKVE-----AAISFVESrpGRKAiitslEKAKEALEGKA-GTVI 312
PLN02418 PLN02418
delta-1-pyrroline-5-carboxylate synthase
 135-260 1.28e-03

delta-1-pyrroline-5-carboxylate synthase


Pssm-ID: 215230  Cd Length: 718  Bit Score: 40.09  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       135 AIKEMLKRNLVPVIH-GDIVIDDKNGYRIISG-----DDIVPYLANELKADLILYATDVDGvLIDNKPIKRIDKnniyKI 208
Cdd:PLN02418 141 TVESLLDLRVIPIFNeNDAVSTRRAPYEDSSGifwdnDSLAALLALELKADLLILLSDVEG-LYTGPPSDPSSK----LI 215

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
3K4O_B       209 LNYLSGSNSIDVT---------GGMKYKIEMIRKNKCRG---FVFNGNKANNIYKALLGEVEGT 260
Cdd:PLN02418 216 HTYIKEKHQDEITfgeksrvgrGGMTAKVKAAVNAASAGipvVITSGYALDNIRKVLRGERVGT 279
PRK12454 PRK12454
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
 130-262 1.38e-03

carbamate kinase-like carbamoyl phosphate synthetase; Reviewed


Pssm-ID: 183535  Cd Length: 313  Bit Score: 39.60  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       130 IFDTSAIKEMLKRNLVPVIHGD---IVIDDKNGYR----IISGDDIVPYLANELKADLILYATDVDGVLI-----DNKPI 197
Cdd:PRK12454 172 IVEIEVIKALVENGFIVIASGGggiPVIEEDGELKgveaVIDKDLASELLAEELNADIFIILTDVEKVYLnygkpDQKPL 251

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3K4O_B       198 KRIDKNNIYKIlnYLSGSNSidvTGGMKYKIEM-IRknkcrgFVFNGNKA------NNIYKALLGEVeGTEI 262
Cdd:PRK12454 252 DKVTVEEAKKY--YEEGHFK---AGSMGPKILAaIR------FVENGGKRaiiaslEKAVEALEGKT-GTRI 311
ArcC COG0549
Carbamate kinase [Amino acid transport and metabolism];
130-196 3.02e-03

Carbamate kinase [Amino acid transport and metabolism];


Pssm-ID: 440315  Cd Length: 313  Bit Score: 38.52  E-value: 3.02e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
3K4O_B      130 IFDTSAIKEMLKRNLVpVI---HGDI-VIDDKNGyrIISGDDIVP-------YLANELKADLILYATDVDGVLID-NKP 196
Cdd:COG0549 171 IVEIDAIKALLEAGVI-VIaagGGGIpVVRDEDG--GLKGVEAVIdkdlasaLLAEELDADLLLILTDVDKVYINfGKP 246
PLN02512 PLN02512
acetylglutamate kinase
 132-229 3.70e-03

acetylglutamate kinase


Pssm-ID: 178128  Cd Length: 309  Bit Score: 38.13  E-value: 3.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       132 DTSAIKEMLKRNLVPVIHGdiVIDDKNG--YRIiSGDDIVPYLANELKADLILYATDVDGVLID-NKP---IKRIDKNNI 205
Cdd:PLN02512 175 DPTVLRPLVDDGHIPVIAT--VAADEDGqaYNI-NADTAAGEIAAALGAEKLILLTDVAGVLEDkDDPgslVKELDIKGV 251

                         90       100
                 ....*....|....*....|....*..
3K4O_B       206 YKIlnylsgsnsID---VTGGMKYKIE 229
Cdd:PLN02512 252 RKL---------IAdgkIAGGMIPKVE 269
ASKHA_NBD_PilM cd24049
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ...
 32-63 7.31e-03

nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.


Pssm-ID: 466899 [Multi-domain]  Cd Length: 339  Bit Score: 37.26  E-value: 7.31e-03
                        10        20        30
                ....*....|....*....|....*....|....
3K4O_B       32 LERIAMEIKNALDYYKNQNKE--IKLILVHGGGA 63
Cdd:cd24049 255 LERLVSEIRRSLDYYRSQNGGepIDKIYLTGGGS 288
PRK12314 PRK12314
gamma-glutamyl kinase; Provisional
 133-260 8.91e-03

gamma-glutamyl kinase; Provisional


Pssm-ID: 183430 [Multi-domain]  Cd Length: 266  Bit Score: 36.76  E-value: 8.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       133 TSAIKEMLKRNLVPVIH-GDIVIDDKNGYRIISGDDIVPYLANELKADLILYATDVDGVLIDN-------KPIKRIdkNN 204
Cdd:PRK12314 123 KNTFESLLELGILPIVNeNDAVATDEIDTKFGDNDRLSAIVAKLVKADLLIILSDIDGLYDKNprinpdaKLRSEV--TE 200

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B       205 IYK-ILNYLSGSNSIDVTGGMKYKI---EMIRKNKCRGFVFNGNKANNIYKALLGEVEGT 260
Cdd:PRK12314 201 ITEeILALAGGAGSKFGTGGMVTKLkaaKFLMEAGIKMVLANGFNPSDILDFLEGESIGT 260
MetL1 COG0527
Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the ...
 106-200 9.88e-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: 9.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K4O_B      106 TLQSYDIPAVSIQPSSFVVFGD--------KLIFDTSAIKEMLKRNLVPVIHGDIVIDDKNgyRII----SGDDI--VpY 171
Cdd:COG0527  84 ALQELGVPAVSLDGRQAGIITDdnhgkariDLIETPERIRELLEEGKVVVVAGFQGVTEDG--EITtlgrGGSDTtaV-A 160

                        90       100       110
                ....*....|....*....|....*....|....*..
3K4O_B      172 LANELKADLI-LYaTDVDGV------LIDN-KPIKRI 200
Cdd:COG0527 161 LAAALKADECeIW-TDVDGVytadprIVPDaRKLPEI 196
 
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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