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Conserved domains on  [gi|1525684052|ref|WP_124349491|]
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1-phosphofructokinase [Pseudomonas chlororaphis]

Protein Classification

1-phosphofructokinase family hexose kinase( domain architecture ID 10003020)

1-phosphofructokinase family hexose kinase such as 1-phosphofructokinase, which catalyzes the ATP-dependent conversion of D-fructose 1-phosphate to D-fructose 1,6-bisphosphate and is involved in the utilization of fructose as a sole carbon and energy source

CATH:  3.40.1190.20
EC:  2.7.1.-
Gene Ontology:  GO:0008443|GO:0016310|GO:0005524
PubMed:  8382990|12095261
SCOP:  3001268

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
4-306 4.63e-128

1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];


:

Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 367.15  E-value: 4.63e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052   4 ILTLTLNPALDLTVQLTRLEPGQVNRSEAMHTHAAGKGVNVAQVLADLGHQLTVSGFLGEDNPQAFEALFARRGFVDAFI 83
Cdd:COG1105     1 ILTVTLNPALDRTYEVDELEPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFTGEFIEELLDEEGIPTDFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  84 RVPGETRSNIKLAE-QDGRITDLNGPGPEVDAAAQQALLERLEQIAPGHDAVVVAGSLPRGVSPQWLHALLTRLKALGLK 162
Cdd:COG1105    81 PIEGETRINIKIVDpSDGTETEINEPGPEISEEELEALLERLEELLKEGDWVVLSGSLPPGVPPDFYAELIRLARARGAK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 163 VALDTSGEALRAGLAAGPWLVKPNTEELAEALGSPLLSLATQAAAARRLHAQGVEHVVISHGAEGVNWFSAAPALQALPP 242
Cdd:COG1105   161 VVLDTSGEALKAALEAGPDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVYRAKPP 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525684052 243 KVSVASTVGAGDSLLAGMLHGLLSAHAFEQTLRTATAIAAMAVTQIGFGITDAAQLAQLEQGVR 306
Cdd:COG1105   241 KVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTGLPDREDVEELLAQVE 304
 
Name Accession Description Interval E-value
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
4-306 4.63e-128

1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 367.15  E-value: 4.63e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052   4 ILTLTLNPALDLTVQLTRLEPGQVNRSEAMHTHAAGKGVNVAQVLADLGHQLTVSGFLGEDNPQAFEALFARRGFVDAFI 83
Cdd:COG1105     1 ILTVTLNPALDRTYEVDELEPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFTGEFIEELLDEEGIPTDFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  84 RVPGETRSNIKLAE-QDGRITDLNGPGPEVDAAAQQALLERLEQIAPGHDAVVVAGSLPRGVSPQWLHALLTRLKALGLK 162
Cdd:COG1105    81 PIEGETRINIKIVDpSDGTETEINEPGPEISEEELEALLERLEELLKEGDWVVLSGSLPPGVPPDFYAELIRLARARGAK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 163 VALDTSGEALRAGLAAGPWLVKPNTEELAEALGSPLLSLATQAAAARRLHAQGVEHVVISHGAEGVNWFSAAPALQALPP 242
Cdd:COG1105   161 VVLDTSGEALKAALEAGPDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVYRAKPP 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525684052 243 KVSVASTVGAGDSLLAGMLHGLLSAHAFEQTLRTATAIAAMAVTQIGFGITDAAQLAQLEQGVR 306
Cdd:COG1105   241 KVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTGLPDREDVEELLAQVE 304
pfkB TIGR03828
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ...
 4-307 5.78e-126

1-phosphofructokinase; This enzyme acts in concert with the fructose-specific phosphotransferase system (PTS) which imports fructose as fructose-1-phosphate. The action of 1-phosphofructokinase results in beta-D-fructose-1,6-bisphosphate and is an entry point into glycolysis (GenProp0688).


Pssm-ID: 274804 [Multi-domain]  Cd Length: 304  Bit Score: 361.91  E-value: 5.78e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052   4 ILTLTLNPALDLTVQLTRLEPGQVNRSEAMHTHAAGKGVNVAQVLADLGHQLTVSGFLGEDNPQAFEALFARRGFVDAFI 83
Cdd:TIGR03828   1 IYTVTLNPAIDLTIELDGLTLGEVNRVESTRIDAGGKGINVSRVLKNLGVDVVALGFLGGFTGDFIEALLREEGIKTDFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  84 RVPGETRSNIKLAEQDGRITDLNGPGPEVDAAAQQALLERLEQIAPGHDAVVVAGSLPRGVSPQWLHALLTRLKALGLKV 163
Cdd:TIGR03828  81 RVPGETRINVKIKEPSGTETKLNGPGPEISEEELEALLEKLRAQLAEGDWLVLSGSLPPGVPPDFYAELIALAREKGAKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 164 ALDTSGEALRAGLAAGPWLVKPNTEELAEALGSPLLSLATQAAAARRLHAQGVEHVVISHGAEGVNWFSAAPALQALPPK 243
Cdd:TIGR03828 161 ILDTSGEALRDGLKAKPFLIKPNDEELEELFGRELKTLEEIIEAARELLDLGAENVLISLGADGALLVTKEGALFAQPPK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525684052 244 VSVASTVGAGDSLLAGMLHGLLSAHAFEQTLRTATAIAAMAVTQIGFGITDAAQLAQLEQGVRV 307
Cdd:TIGR03828 241 GEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEGTGLPDPEDIEELLPQVTI 304
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 3-291 1.78e-122

1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.


Pssm-ID: 238570 [Multi-domain]  Cd Length: 289  Bit Score: 352.61  E-value: 1.78e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052   3 KILTLTLNPALDLTVQLTRLEPGQVNRSEAMHTHAAGKGVNVAQVLADLGHQLTVSGFLGEDNPQAFEALFARRGFVDAF 82
Cdd:cd01164     1 MIYTVTLNPAIDLTIELDQLQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFTGDFFEALLKEEGIPDDF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  83 IRVPGETRSNIKLAEQDGRITDLNGPGPEVDAAAQQALLERLEQIAPGHDAVVVAGSLPRGVSPQWLHALLTRLKALGLK 162
Cdd:cd01164    81 VEVAGETRINVKIKEEDGTETEINEPGPEISEEELEALLEKLKALLKKGDIVVLSGSLPPGVPADFYAELVRLAREKGAR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 163 VALDTSGEALRAGLAAGPWLVKPNTEELAEALGSPLLSLATQAAAARRLHAQGVEHVVISHGAEGVNWFSAAPALQALPP 242
Cdd:cd01164   161 VILDTSGEALLAALAAKPFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVYRASPP 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1525684052 243 KVSVASTVGAGDSLLAGMLHGLLSAHAFEQTLRTATAIAAMAVTQIGFG 291
Cdd:cd01164   241 KVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
fruK PRK09513
1-phosphofructokinase; Provisional
 1-310 6.19e-113

1-phosphofructokinase; Provisional


Pssm-ID: 181923 [Multi-domain]  Cd Length: 312  Bit Score: 329.35  E-value: 6.19e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052   1 MAKILTLTLNPALDLTVQLTRLEPGQVNRSEAMHTHAAGKGVNVAQVLADLGHQLTVSGFLGEDNPQAFEALFARRGFVD 80
Cdd:PRK09513    2 SRRVATITLNPAYDLVGFCPEIERGEVNLVKTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDNQDGFQQLFSELGIAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  81 AFIRVPGETRSNIKLAEQDGRITDLNGPGPEVDAAAQQALLERLEQIAPGHDAVVVAGSLPRGVSPQWLHALLTRLKALG 160
Cdd:PRK09513   82 RFQVVQGRTRINVKLTEKDGEVTDFNFSGFEVTPADWERFVTDSLSWLGQFDMVAVSGSLPRGVSPEAFTDWMTRLRSQC 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 161 LKVALDTSGEALRAGLAAGPWLVKPNTEELAEALGSPLLSLATQAAAARRLHAQGVEHVVISHGAEGVNWFSAAPALQAL 240
Cdd:PRK09513  162 PCIIFDSSREALVAGLKAAPWLVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVNASGEWIAK 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 241 PPKVSVASTVGAGDSLLAGMLHGLLSAHAFEQTLRTATAIAAMAVTQIGFGITDAAQLAQLEQGVRVHPL 310
Cdd:PRK09513  242 PPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSALAVSQSNVGITDRPQLAAMMARVDLTPF 311
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 24-289 1.57e-43

pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 150.96  E-value: 1.57e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  24 PGQVNRSEAMHTHAAGKGVNVAQVLADLGHQLTVSGFLGEDNP-QAFEALFARRGFVDAFIRVPGETRSNIKLAEQDGRI 102
Cdd:pfam00294  20 PGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFgEFLLQELKKEGVDTDYVVIDEDTRTGTALIEVDGDG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 103 -TDLNGPGPEVDAAAQQALLERLEQIAPGhDAVVVAGSLPRGVSPQWLHALLTRLKALGLKVA--LDTSGEALRAG--LA 177
Cdd:pfam00294 100 eRTIVFNRGAAADLTPEELEENEDLLENA-DLLYISGSLPLGLPEATLEELIEAAKNGGTFDPnlLDPLGAAREALleLL 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 178 AGPWLVKPNTEELAEALGSPLLSLATQAAAARRLHAQGVEHVVISHGAEGVNWFSAAPALQALP-PKVSVASTVGAGDSL 256
Cdd:pfam00294 179 PLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEVHVPAvPKVKVVDTTGAGDSF 258

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1525684052 257 LAGMLHGLLSAHAFEQTLRTATAIAAMAVTQIG 289
Cdd:pfam00294 259 VGGFLAGLLAGKSLEEALRFANAAAALVVQKSG 291
 
Name Accession Description Interval E-value
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
4-306 4.63e-128

1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 367.15  E-value: 4.63e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052   4 ILTLTLNPALDLTVQLTRLEPGQVNRSEAMHTHAAGKGVNVAQVLADLGHQLTVSGFLGEDNPQAFEALFARRGFVDAFI 83
Cdd:COG1105     1 ILTVTLNPALDRTYEVDELEPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFTGEFIEELLDEEGIPTDFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  84 RVPGETRSNIKLAE-QDGRITDLNGPGPEVDAAAQQALLERLEQIAPGHDAVVVAGSLPRGVSPQWLHALLTRLKALGLK 162
Cdd:COG1105    81 PIEGETRINIKIVDpSDGTETEINEPGPEISEEELEALLERLEELLKEGDWVVLSGSLPPGVPPDFYAELIRLARARGAK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 163 VALDTSGEALRAGLAAGPWLVKPNTEELAEALGSPLLSLATQAAAARRLHAQGVEHVVISHGAEGVNWFSAAPALQALPP 242
Cdd:COG1105   161 VVLDTSGEALKAALEAGPDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVYRAKPP 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525684052 243 KVSVASTVGAGDSLLAGMLHGLLSAHAFEQTLRTATAIAAMAVTQIGFGITDAAQLAQLEQGVR 306
Cdd:COG1105   241 KVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTGLPDREDVEELLAQVE 304
pfkB TIGR03828
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ...
 4-307 5.78e-126

1-phosphofructokinase; This enzyme acts in concert with the fructose-specific phosphotransferase system (PTS) which imports fructose as fructose-1-phosphate. The action of 1-phosphofructokinase results in beta-D-fructose-1,6-bisphosphate and is an entry point into glycolysis (GenProp0688).


Pssm-ID: 274804 [Multi-domain]  Cd Length: 304  Bit Score: 361.91  E-value: 5.78e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052   4 ILTLTLNPALDLTVQLTRLEPGQVNRSEAMHTHAAGKGVNVAQVLADLGHQLTVSGFLGEDNPQAFEALFARRGFVDAFI 83
Cdd:TIGR03828   1 IYTVTLNPAIDLTIELDGLTLGEVNRVESTRIDAGGKGINVSRVLKNLGVDVVALGFLGGFTGDFIEALLREEGIKTDFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  84 RVPGETRSNIKLAEQDGRITDLNGPGPEVDAAAQQALLERLEQIAPGHDAVVVAGSLPRGVSPQWLHALLTRLKALGLKV 163
Cdd:TIGR03828  81 RVPGETRINVKIKEPSGTETKLNGPGPEISEEELEALLEKLRAQLAEGDWLVLSGSLPPGVPPDFYAELIALAREKGAKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 164 ALDTSGEALRAGLAAGPWLVKPNTEELAEALGSPLLSLATQAAAARRLHAQGVEHVVISHGAEGVNWFSAAPALQALPPK 243
Cdd:TIGR03828 161 ILDTSGEALRDGLKAKPFLIKPNDEELEELFGRELKTLEEIIEAARELLDLGAENVLISLGADGALLVTKEGALFAQPPK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1525684052 244 VSVASTVGAGDSLLAGMLHGLLSAHAFEQTLRTATAIAAMAVTQIGFGITDAAQLAQLEQGVRV 307
Cdd:TIGR03828 241 GEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEGTGLPDPEDIEELLPQVTI 304
1-PFK TIGR03168
hexose kinase, 1-phosphofructokinase family; This family consists largely of ...
 4-306 1.80e-125

hexose kinase, 1-phosphofructokinase family; This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases.


Pssm-ID: 274464 [Multi-domain]  Cd Length: 303  Bit Score: 360.74  E-value: 1.80e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052   4 ILTLTLNPALDLTVQLTRLEPGQVNRSEAMHTHAAGKGVNVAQVLADLGHQLTVSGFLGEDNPQAFEALFARRGFVDAFI 83
Cdd:TIGR03168   1 IYTVTLNPAIDLTIEVDGLTPGEVNRVAAVRKDAGGKGINVARVLARLGAEVVATGFLGGFTGEFIEALLAEEGIKNDFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  84 RVPGETRSNIKLAEQDGRITDLNGPGPEVDAAAQQALLERLEQIAPGHDAVVVAGSLPRGVSPQWLHALLTRLKALGLKV 163
Cdd:TIGR03168  81 EVKGETRINVKIKESSGEETELNEPGPEISEEELEQLLEKLRELLASGDIVVISGSLPPGVPPDFYAQLIAIARKKGAKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 164 ALDTSGEALRAGLAAGPWLVKPNTEELAEALGSPLLSLATQAAAARRLHAQGVEHVVISHGAEGVNWFSAAPALQALPPK 243
Cdd:TIGR03168 161 ILDTSGEALREALAAKPFLIKPNHEELEELFGRELKTLEEIIEAARELLDRGAENVLVSLGADGALLVTKEGALKATPPK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1525684052 244 VSVASTVGAGDSLLAGMLHGLLSAHAFEQTLRTATAIAAMAVTQIGFGITDAAQLAQLEQGVR 306
Cdd:TIGR03168 241 VEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPGTGLPDPEDVEELLDQVT 303
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 3-291 1.78e-122

1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.


Pssm-ID: 238570 [Multi-domain]  Cd Length: 289  Bit Score: 352.61  E-value: 1.78e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052   3 KILTLTLNPALDLTVQLTRLEPGQVNRSEAMHTHAAGKGVNVAQVLADLGHQLTVSGFLGEDNPQAFEALFARRGFVDAF 82
Cdd:cd01164     1 MIYTVTLNPAIDLTIELDQLQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFTGDFFEALLKEEGIPDDF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  83 IRVPGETRSNIKLAEQDGRITDLNGPGPEVDAAAQQALLERLEQIAPGHDAVVVAGSLPRGVSPQWLHALLTRLKALGLK 162
Cdd:cd01164    81 VEVAGETRINVKIKEEDGTETEINEPGPEISEEELEALLEKLKALLKKGDIVVLSGSLPPGVPADFYAELVRLAREKGAR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 163 VALDTSGEALRAGLAAGPWLVKPNTEELAEALGSPLLSLATQAAAARRLHAQGVEHVVISHGAEGVNWFSAAPALQALPP 242
Cdd:cd01164   161 VILDTSGEALLAALAAKPFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVYRASPP 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1525684052 243 KVSVASTVGAGDSLLAGMLHGLLSAHAFEQTLRTATAIAAMAVTQIGFG 291
Cdd:cd01164   241 KVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
fruK PRK09513
1-phosphofructokinase; Provisional
 1-310 6.19e-113

1-phosphofructokinase; Provisional


Pssm-ID: 181923 [Multi-domain]  Cd Length: 312  Bit Score: 329.35  E-value: 6.19e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052   1 MAKILTLTLNPALDLTVQLTRLEPGQVNRSEAMHTHAAGKGVNVAQVLADLGHQLTVSGFLGEDNPQAFEALFARRGFVD 80
Cdd:PRK09513    2 SRRVATITLNPAYDLVGFCPEIERGEVNLVKTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDNQDGFQQLFSELGIAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  81 AFIRVPGETRSNIKLAEQDGRITDLNGPGPEVDAAAQQALLERLEQIAPGHDAVVVAGSLPRGVSPQWLHALLTRLKALG 160
Cdd:PRK09513   82 RFQVVQGRTRINVKLTEKDGEVTDFNFSGFEVTPADWERFVTDSLSWLGQFDMVAVSGSLPRGVSPEAFTDWMTRLRSQC 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 161 LKVALDTSGEALRAGLAAGPWLVKPNTEELAEALGSPLLSLATQAAAARRLHAQGVEHVVISHGAEGVNWFSAAPALQAL 240
Cdd:PRK09513  162 PCIIFDSSREALVAGLKAAPWLVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVNASGEWIAK 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 241 PPKVSVASTVGAGDSLLAGMLHGLLSAHAFEQTLRTATAIAAMAVTQIGFGITDAAQLAQLEQGVRVHPL 310
Cdd:PRK09513  242 PPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSALAVSQSNVGITDRPQLAAMMARVDLTPF 311
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 24-289 1.57e-43

pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 150.96  E-value: 1.57e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  24 PGQVNRSEAMHTHAAGKGVNVAQVLADLGHQLTVSGFLGEDNP-QAFEALFARRGFVDAFIRVPGETRSNIKLAEQDGRI 102
Cdd:pfam00294  20 PGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFgEFLLQELKKEGVDTDYVVIDEDTRTGTALIEVDGDG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 103 -TDLNGPGPEVDAAAQQALLERLEQIAPGhDAVVVAGSLPRGVSPQWLHALLTRLKALGLKVA--LDTSGEALRAG--LA 177
Cdd:pfam00294 100 eRTIVFNRGAAADLTPEELEENEDLLENA-DLLYISGSLPLGLPEATLEELIEAAKNGGTFDPnlLDPLGAAREALleLL 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 178 AGPWLVKPNTEELAEALGSPLLSLATQAAAARRLHAQGVEHVVISHGAEGVNWFSAAPALQALP-PKVSVASTVGAGDSL 256
Cdd:pfam00294 179 PLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEVHVPAvPKVKVVDTTGAGDSF 258

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1525684052 257 LAGMLHGLLSAHAFEQTLRTATAIAAMAVTQIG 289
Cdd:pfam00294 259 VGGFLAGLLAGKSLEEALRFANAAAALVVQKSG 291
PRK13508 PRK13508
tagatose-6-phosphate kinase; Provisional
 4-280 7.54e-40

tagatose-6-phosphate kinase; Provisional


Pssm-ID: 237405 [Multi-domain]  Cd Length: 309  Bit Score: 141.78  E-value: 7.54e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052   4 ILTLTLNPALDLTVQLTRLEPGQVNRSEAMHTHAAGKGVNVAQVLADLGHQLTVSGFLGEDNPQafealFARRGFVD--- 80
Cdd:PRK13508    2 ILTVTLNPSIDISYPLDELKLDTVNRVVDVSKTAGGKGLNVTRVLSEFGENVLATGLIGGELGQ-----FIAEHLDDqik 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  81 -AFIRVPGETRSNIKLAeQDGRITDLNGPGPEVDAAAQQALLERLEQIAPGHDAVVVAGSLPRGVSPQWLHALLTRLKAL 159
Cdd:PRK13508   77 hAFYKIKGETRNCIAIL-HEGQQTEILEKGPEISVQEADGFLHHFKQLLESVEVVAISGSLPAGLPVDYYAQLIELANQA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 160 GLKVALDTSGEALRAGLAAG--PWLVKPNTEELAEALGSPLL-SLATQAAAARRLHAQGVEHVVISHGAEGVNWFSAAPA 236
Cdd:PRK13508  156 GKPVVLDCSGAALQAVLESPykPTVIKPNIEELSQLLGKEVSeDLDELKEVLQQPLFEGIEWIIVSLGADGAFAKHNDTF 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1525684052 237 LQALPPKVSVASTVGAGDSLLAGMLHGLLSAHAFEQTLRTATAI 280
Cdd:PRK13508  236 YKVDIPKIEVVNPVGSGDSTVAGIASGLLHQEDDADLLKKANVL 279
PRK10294 PRK10294
6-phosphofructokinase 2; Provisional
 1-307 2.08e-31

6-phosphofructokinase 2; Provisional


Pssm-ID: 182361 [Multi-domain]  Cd Length: 309  Bit Score: 119.50  E-value: 2.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052   1 MAKILTLTLNPALDLTVQLTRLEPGQVNRSEAMHTHAAGKGVNVAQVLADLGHQLTVSGFLGEDNPQAFEALFARRGFVD 80
Cdd:PRK10294    1 MVRIYTLTLAPSLDSATITPQIYPEGKLRCSAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLADENVPV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  81 AFIRVPGETRSNIKL-AEQDGRITDLNGPGPEVDAAAQQALLERLEQIAPGhDAVVVAGSLPRGVSPQWLHALLTRLKAL 159
Cdd:PRK10294   81 ATVEAKDWTRQNLHVhVEASGEQYRFVMPGAALNEDEFRQLEEQVLEIESG-AILVISGSLPPGVKLEKLTQLISAAQKQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 160 GLKVALDTSGEALRAGLAAGPW-LVKPNTEELAEALGSPLLSLATQAAAARRLHAQGVEH-VVISHGAEGVNWFSAAPAL 237
Cdd:PRK10294  160 GIRCIIDSSGDALSAALAIGNIeLVKPNQKELSALVNRDLTQPDDVRKAAQELVNSGKAKrVVVSLGPQGALGVDSENCI 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525684052 238 QALPPKVSVASTVGAGDSLLAGMlhgllsahafeqTLRTA--TAIAAMAVtqigFGITdAAQLAQLEQGVRV 307
Cdd:PRK10294  240 QVVPPPVKSQSTVGAGDSMVGAM------------TLKLAenASLEEMVR----FGVA-AGSAATLNQGTRL 294
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 12-289 3.10e-31

Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 440290 [Multi-domain]  Cd Length: 301  Bit Score: 118.45  E-value: 3.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  12 ALDLTVQLTRL-EPGQVNRSEAMHTHAAGKGVNVAQVLADLGHQLTVSGFLGED-NPQAFEALFARRGF-VDAFIRVPGE 88
Cdd:COG0524     9 LVDLVARVDRLpKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDpFGDFLLAELRAEGVdTSGVRRDPGA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  89 --TRSNIKLAEQDGRITDLNgpgPEVDAAAQQALLErlEQIAPGHDAVVVAGSLPRG-VSPQWLHALLTRLKALGLKVAL 165
Cdd:COG0524    89 ptGLAFILVDPDGERTIVFY---RGANAELTPEDLD--EALLAGADILHLGGITLASePPREALLAALEAARAAGVPVSL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 166 DTS---------GEALRAGLAAGPWLvKPNTEELAEALGSPllslaTQAAAARRLHAQGVEHVVISHGAEGVNWFSAAPA 236
Cdd:COG0524   164 DPNyrpalwepaRELLRELLALVDIL-FPNEEEAELLTGET-----DPEEAAAALLARGVKLVVVTLGAEGALLYTGGEV 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1525684052 237 LQALPPKVSVASTVGAGDSLLAGMLHGLLSAHAFEQTLRTATAIAAMAVTQIG 289
Cdd:COG0524   238 VHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPG 290
RfaE COG2870
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ...
 43-300 2.49e-25

ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442117 [Multi-domain]  Cd Length: 321  Bit Score: 102.97  E-value: 2.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  43 NVAQVLADLGHQLTVSGFLGEDNP-QAFEALFARRGFVDAFIRVPGETRSNIKLaeqdgRITDLN--------GPGPEVD 113
Cdd:COG2870    60 NVAANLAALGAQVTLVGVVGDDEAgRELRRLLEEAGIDTDGLVVDPRRPTTTKT-----RVIAGGqqllrldfEDRFPLS 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 114 AAAQQALLERLEQIAPGHDAVVVA----GSLprgvSPQWLHALLTRLKALGLKVALDTSGeaLRAGLAAGPWLVKPNTEE 189
Cdd:COG2870   135 AELEARLLAALEAALPEVDAVILSdygkGVL----TPELIQALIALARAAGKPVLVDPKG--RDFSRYRGATLLTPNLKE 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 190 LAEALGSPLLSLATQAAAARRL-HAQGVEHVVISHGAEGVNWFSAAPALQALPPKVS-VASTVGAGDSLLAGMLHGLLSA 267
Cdd:COG2870   209 AEAAVGIPIADEEELVAAAAELlERLGLEALLVTRGEEGMTLFDADGPPHHLPAQAReVFDVTGAGDTVIATLALALAAG 288

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1525684052 268 HAFEQTLRTATAIAAMAVTQIGFGITDAAQLAQ 300
Cdd:COG2870   289 ASLEEAAELANLAAGIVVGKLGTATVSPEELLA 321
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 17-289 4.16e-22

2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.


Pssm-ID: 238571 [Multi-domain]  Cd Length: 294  Bit Score: 93.79  E-value: 4.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  17 VQLTRLEPGQVNRSEAMHTHAAGKGVNVAQVLADLGHQLTVSGFLGEDNP-QAFEALFARRGFVDAFIRVPGETRSNIKL 95
Cdd:cd01166    10 VDLSPPGGGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFgRFILAELRREGVDTSHVRVDPGRPTGLYF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  96 AEQDGritdlnGPGPEV-----DAAAQQALLERL-EQIAPGHDAVVVAGSLP--RGVSPQWLHALLTRLKALGLKVALDT 167
Cdd:cd01166    90 LEIGA------GGERRVlyyraGSAASRLTPEDLdEAALAGADHLHLSGITLalSESAREALLEALEAAKARGVTVSFDL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 168 -------SGEALRAGLAAGPWLVK---PNTEELAEALGSPllSLATQAAAARRLHAqGVEHVVISHGAEGVNWFSAAPAL 237
Cdd:cd01166   164 nyrpklwSAEEAREALEELLPYVDivlPSEEEAEALLGDE--DPTDAAERALALAL-GVKAVVVKLGAEGALVYTGGGRV 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1525684052 238 QALPPKVSVASTVGAGDSLLAGMLHGLLSAHAFEQTLRTATAIAAMAVTQIG 289
Cdd:cd01166   241 FVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPG 292
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
 35-289 6.38e-20

RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.


Pssm-ID: 238577 [Multi-domain]  Cd Length: 304  Bit Score: 88.00  E-value: 6.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  35 THAAGKGVNVAQVLADLGHQLTVSGFLGED-NPQAFEALFARRGFVDAFIRVPGE--TRSN--IKLAEQDGRITDLNGPg 109
Cdd:cd01172    36 EIRLGGAANVANNLASLGAKVTLLGVVGDDeAGDLLRKLLEKEGIDTDGIVDEGRptTTKTrvIARNQQLLRVDREDDS- 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 110 pEVDAAAQQALLERLEQIAPGHDAVVVAGSLPRGVSPQWLHALLTRLKALGLKVALDtSGEALRAgLAAGPWLVKPNTEE 189
Cdd:cd01172   115 -PLSAEEEQRLIERIAERLPEADVVILSDYGKGVLTPRVIEALIAAARELGIPVLVD-PKGRDYS-KYRGATLLTPNEKE 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 190 LAEALGSPLLSLATQAAAARRLHAQ-GVEHVVISHGAEGVNWFSAAPALQALPPKVS-VASTVGAGDSLLAGMLHGLLSA 267
Cdd:cd01172   192 AREALGDEINDDDELEAAGEKLLELlNLEALLVTLGEEGMTLFERDGEVQHIPALAKeVYDVTGAGDTVIATLALALAAG 271

                         250       260
                  ....*....|....*....|..
gi 1525684052 268 HAFEQTLRTATAIAAMAVTQIG 289
Cdd:cd01172   272 ADLEEAAFLANAAAGVVVGKVG 293
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 13-289 6.76e-20

Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.


Pssm-ID: 238579 [Multi-domain]  Cd Length: 292  Bit Score: 87.61  E-value: 6.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  13 LDLTVQLTRL-EPGQVNRSEAMHTHAAGKGVNVAQVLADLGHQLTVSGFLGED-NPQAFEALFARRGFVDAFIRVPGETR 90
Cdd:cd01174    10 VDLVTRVDRLpKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDaFGDELLENLREEGIDVSYVEVVVGAP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  91 S---NIKLAEqDGRITDLNGPGpeVDAAAQQALLERLEQIAPGHDAVVVAGSLPrgvsPQWLHALLTRLKALGLKVALDT 167
Cdd:cd01174    90 TgtaVITVDE-SGENRIVVVPG--ANGELTPADVDAALELIAAADVLLLQLEIP----LETVLAALRAARRAGVTVILNP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 168 SG-EALRAGLAAGPWLVKPNTEELAEALGSPLLSLATQAAAARRLHAQGVEHVVISHGAEGVnWFSAAPALQALPP-KVS 245
Cdd:cd01174   163 APaRPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGA-LLASGGEVEHVPAfKVK 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1525684052 246 VASTVGAGDSLLAGMLHGLLSAHAFEQTLRTATAIAAMAVTQIG 289
Cdd:cd01174   242 AVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPG 285
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
 24-289 5.76e-15

Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.


Pssm-ID: 238572 [Multi-domain]  Cd Length: 295  Bit Score: 73.82  E-value: 5.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  24 PGQVNRSEAMHTHAAGKGVNVAQVLADLGHQLTVSGFLGEDNP-QAFEALFARRGFVDAFIRVPGETRSNIKLAEqdgri 102
Cdd:cd01167    14 PEGSGAPETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFgDFLLETLKEAGVDTRGIQFDPAAPTTLAFVT----- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 103 tdLNGPGP-----EVDAAAQQALLERLEQIAPGHDAVVVAGSLP--RGVSPQWLHALLTRLKALGLKVALDTSgeaLRAG 175
Cdd:cd01167    89 --LDADGErsfefYRGPAADLLLDTELNPDLLSEADILHFGSIAlaSEPSRSALLELLEAAKKAGVLISFDPN---LRPP 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 176 LAAGPW--------------LVKPNTEELAealgsPLLSLATQAAAARRLHAQGVEHVVISHGAEGVNWFSAAPALQALP 241
Cdd:cd01167   164 LWRDEEeareriaelleladIVKLSDEELE-----LLFGEEDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGVGEVPG 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1525684052 242 PKVSVASTVGAGDSLLAGMLHGLLSA-------HAFEQTLRTATAIAAMAVTQIG 289
Cdd:cd01167   239 IPVEVVDTTGAGDAFVAGLLAQLLSRgllaldeDELAEALRFANAVGALTCTKAG 293
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 78-265 1.78e-14

ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).


Pssm-ID: 238177 [Multi-domain]  Cd Length: 196  Bit Score: 70.59  E-value: 1.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  78 FVDAFIRVPGETRSNIklaEQDGRITDLNGPGPEVDAAAQQALLErLEQIAPGHDAVVVAGSLPRGVSPQ-WLHALLTRl 156
Cdd:cd00287     9 LVDVILRVDALPLPGG---LVRPGDTEERAGGGAANVAVALARLG-VSVTLVGADAVVISGLSPAPEAVLdALEEARRR- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 157 kalGLKVALDTSGEALRAG------LAAGPWLVKPNTEELAEALGSPLLSLATQAAAARRLHAQGVEHVVISHGAEGVNW 230
Cdd:cd00287    84 ---GVPVVLDPGPRAVRLDgeelekLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIV 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1525684052 231 FSAAPALQALPP-KVSVASTVGAGDSLLAGMLHGLL 265
Cdd:cd00287   161 ATRGGTEVHVPAfPVKVVDTTGAGDAFLAALAAGLA 196
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 24-285 1.61e-11

YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238916 [Multi-domain]  Cd Length: 288  Bit Score: 63.87  E-value: 1.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  24 PGQVNRSeamhthAAGKGVNVAQVLADLGHQLTVSGFLGEDN-PQAFEALFARRGFVDAFIRVPGE-TRSNIKLAEQDGr 101
Cdd:cd01941    27 PGHVKQS------PGGVGRNIAENLARLGVSVALLSAVGDDSeGESILEESEKAGLNVRGIVFEGRsTASYTAILDKDG- 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 102 itDLNGPGpeVDAAAQQAL----LERLEQIAPGHDAVVVAGSLPRGVspqwLHALLTRLKALGLKVALD-TSGEALR--A 174
Cdd:cd01941   100 --DLVVAL--ADMDIYELLtpdfLRKIREALKEAKPIVVDANLPEEA----LEYLLALAAKHGVPVAFEpTSAPKLKklF 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 175 GLAAGPWLVKPNTEELAEALGSPLLSLATQAAAARRLHAQGVEHVVISHGAEGVNWFSAAPAL--QALPPKVS--VASTV 250
Cdd:cd01941   172 YLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGVetKLFPAPQPetVVNVT 251

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1525684052 251 GAGDSLLAGMLHGLLSAHAFEQTLRTATAIAAMAV 285
Cdd:cd01941   252 GAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTL 286
PRK11142 PRK11142
ribokinase; Provisional
 185-289 1.21e-09

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 58.34  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 185 PNTEElAEAL-GSPLLSLATQAAAARRLHAQGVEHVVISHGAEGVnWFSAAPALQALP-PKVSVASTVGAGDSLLAGMLH 262
Cdd:PRK11142  184 PNETE-AEKLtGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGV-WLSENGEGQRVPgFRVQAVDTIAAGDTFNGALVT 261

                          90       100
                  ....*....|....*....|....*..
gi 1525684052 263 GLLSAHAFEQTLRTATAIAAMAVTQIG 289
Cdd:PRK11142  262 ALLEGKPLPEAIRFAHAAAAIAVTRKG 288
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
 22-289 1.31e-09

Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238922 [Multi-domain]  Cd Length: 265  Bit Score: 57.81  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  22 LEPGQVNRSEAMHTHAAGKGVNVAQVLADLGHQLTVSGFLGEDN--PQAFEALFARRGFVDAFIRvPGETRSNIKLAEQD 99
Cdd:cd01947    20 PQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEigIQSLEELESGGDKHTVAWR-DKPTRKTLSFIDPN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 100 GRITDLNGPGPEVDAAAQQALLErleqiapgHDAVVVAGSLPrgVSPQWLHALLTRLKALGLkvaldtsgeALRAGLAAG 179
Cdd:cd01947    99 GERTITVPGERLEDDLKWPILDE--------GDGVFITAAAV--DKEAIRKCRETKLVILQV---------TPRVRVDEL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 180 PWLVKPNTEELAEALGSPLLSLATQAAAARRlhaqgvEHVVISHGAEGVNWFSAAPALQALPPKVSVASTVGAGDSLLAG 259
Cdd:cd01947   160 NQALIPLDILIGSRLDPGELVVAEKIAGPFP------RYLIVTEGELGAILYPGGRYNHVPAKKAKVPDSTGAGDSFAAG 233

                         250       260       270
                  ....*....|....*....|....*....|
gi 1525684052 260 MLHGLLSAHAFEQTLRTATAIAAMAVTQIG 289
Cdd:cd01947   234 FIYGLLKGWSIEEALELGAQCGAICVSHFG 263
PRK09954 PRK09954
sugar kinase;
24-284 1.80e-09

sugar kinase;


Pssm-ID: 182165 [Multi-domain]  Cd Length: 362  Bit Score: 58.02  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  24 PGQVNRSEAMHTHAAGKGVNVAQVLADLGHQLTVSGFLGEDnpqaF--EALF--ARRGFVD--AFIRVPGE-TRSNIKLA 96
Cdd:PRK09954   79 PQAASHPGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDD----FygETLLeeTRRAGVNvsGCIRLHGQsTSTYLAIA 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  97 EQDGRItdlngpgpeVDAAAQQALLERLE-QIAPG------HDAVVVAGSlprGVSPQWLHALLTrlKALGLKVALDTSG 169
Cdd:PRK09954  155 NRQDET---------VLAINDTHILQQLTpQLLNGsrdlirHAGVVLADC---NLTAEALEWVFT--LADEIPVFVDTVS 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 170 EaLRAGlAAGPWL-----VKPNTEELAEALGSPLLSLATQAAAARRLHAQGVEHVVISHGAEGVnWFSAAPALQAL--PP 242
Cdd:PRK09954  221 E-FKAG-KIKHWLahihtLKPTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDESV-FCSEKDGEQFLltAP 297

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1525684052 243 KVSVASTVGAGDSLLAGMLHGLLSAHAFEQTLRTATAIAAMA 284
Cdd:PRK09954  298 AHTTVDSFGADDGFMAGLVYSFLEGYSFRDSARFAMACAAIS 339
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
 12-289 8.50e-09

YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238919 [Multi-domain]  Cd Length: 289  Bit Score: 55.51  E-value: 8.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  12 ALDLTVQLTRLePGQVNRSEAMH-THAAGKGVNVAQVLADLGHQLTVSGFLGEDNpqafEALFARRGFVDAFIRVPGETR 90
Cdd:cd01944     9 VVDIVLDVDKL-PASGGDIEAKSkSYVIGGGFNVMVAASRLGIPTVNAGPLGNGN----WADQIRQAMRDEGIEILLPPR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  91 SN------IKLAEQDGRITDLNGPGPEVDAAAQqaLLERLeQIAPGhDAVVVAGS--LPRGVSPQWLHALLTRLKALGLK 162
Cdd:cd01944    84 GGddggclVALVEPDGERSFISISGAEQDWSTE--WFATL-TVAPY-DYVYLSGYtlASENASKVILLEWLEALPAGTTL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 163 V------ALDTSGEALRAGLAAGPWLvKPNTEELAEALGsPLLSLAtqAAAARRLHAQGVEHVVISHGAEGVNWFSAAPA 236
Cdd:cd01944   160 VfdpgprISDIPDTILQALMAKRPIW-SCNREEAAIFAE-RGDPAA--EASALRIYAKTAAPVVVRLGSNGAWIRLPDGN 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1525684052 237 LQALPP-KVSVASTVGAGDSLLAGMLHGLLSAHAFEQTLRTATAIAAMAVTQIG 289
Cdd:cd01944   236 THIIPGfKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
PLN02341 PLN02341
pfkB-type carbohydrate kinase family protein
 187-291 1.07e-07

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215195 [Multi-domain]  Cd Length: 470  Bit Score: 52.91  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 187 TEELAEALGSplLSLATQAAAARRLHAQGVEHVVISHGAEGVNWFSAAPALQALPPKVSVASTVGAGDSLLAGMLHGLLS 266
Cdd:PLN02341  292 TSEEAEALTG--IRNPILAGQELLRPGIRTKWVVVKMGSKGSILVTRSSVSCAPAFKVNVVDTVGCGDSFAAAIALGYIH 369

                          90       100
                  ....*....|....*....|....*
gi 1525684052 267 AHAFEQTLRTATAIAAMAVTQIGFG 291
Cdd:PLN02341  370 NLPLVNTLTLANAVGAATAMGCGAG 394
ribokinase_group_A cd01942
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ...
 12-289 1.42e-07

Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238917 [Multi-domain]  Cd Length: 279  Bit Score: 51.93  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  12 ALDLTVQLTRLePGQvNRSE---AMHTHAAGKGVNVAQVLADLGHQLTVSGFLGEDN-PQAFEALFARRGFVDAFIRV-- 85
Cdd:cd01942     9 NYDIILKVESF-PGP-FESVlvkDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFhGRLYLEELREEGVDTSHVRVvd 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  86 PGETRSNIKLAEQDGRITDLNGPGPevdaaaqqalLERLEQIAPGHDAVVVAGSLPRGVSPQWLHALltRLKALGLKVAL 165
Cdd:cd01942    87 EDSTGVAFILTDGDDNQIAYFYPGA----------MDELEPNDEADPDGLADIVHLSSGPGLIELAR--ELAAGGITVSF 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 166 DT-------SGEALRAGLAAGPWLVkPNTEELA---EALGSPLLSLATqaaaarrlhaqGVEHVVISHGAEGVNWFSAAP 235
Cdd:cd01942   155 DPgqelprlSGEELEEILERADILF-VNDYEAEllkERTGLSEAELAS-----------GVRVVVVTLGPKGAIVFEDGE 222

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1525684052 236 ALQALP-PKVSVASTVGAGDSLLAGMLHGLLSAHAFEQTLRTATAIAAMAVTQIG 289
Cdd:cd01942   223 EVEVPAvPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRG 277
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 144-289 1.47e-07

Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.


Pssm-ID: 238573 [Multi-domain]  Cd Length: 312  Bit Score: 51.85  E-value: 1.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 144 VSPQWLHALLTRLKALGLKVALDtsgealragLAAgPWLVKPNTEELAEALG---------SPLLSLATQA-----AAAR 209
Cdd:cd01168   158 VPPEAILLAAEHAKENGVKIALN---------LSA-PFIVQRFKEALLELLPyvdilfgneEEAEALAEAEttddlEAAL 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 210 RLHAQGVEHVVISHGAEGVNWFSAAPALQALPPKVSVA-STVGAGDSLLAGMLHGLLSAHAFEQTLRTATAIAAMAVTQI 288
Cdd:cd01168   228 KLLALRCRIVVITQGAKGAVVVEGGEVYPVPAIPVEKIvDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQL 307


                  .
gi 1525684052 289 G 289
Cdd:cd01168   308 G 308
ribokinase_group_B cd01945
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ...
 37-289 5.39e-07

Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time. .


Pssm-ID: 238920 [Multi-domain]  Cd Length: 284  Bit Score: 49.98  E-value: 5.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  37 AAGKGVNVAQVLADLGHQLTVSGFLGEDN-PQAFEALFARRGFVDAFIRVPGETRSNIKLAEQDGRITDLNGPGPEVDAA 115
Cdd:cd01945    35 GGGNAANAAVAVARLGGQARLIGVVGDDAiGRLILAELAAEGVDTSFIVVAPGARSPISSITDITGDRATISITAIDTQA 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 116 AQQALLErleQIAPGHDAVVVAGSLPRGVSPqwlhaLLTRLKALGLKVALDTSGEALRAglaagpwlvkpnTEELAEAL- 194
Cdd:cd01945   115 APDSLPD---AILGGADAVLVDGRQPEAALH-----LAQEARARGIPIPLDLDGGGLRV------------LEELLPLAd 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 195 -------GSPLLSLATQAAAARRLHAQGVEHVVISHGAEGVNWFSAAPALQALP-PKVSVASTVGAGDSLLAGMLHGLLS 266
Cdd:cd01945   175 haicsenFLRPNTGSADDEALELLASLGIPFVAVTLGEAGCLWLERDGELFHVPaFPVEVVDTTGAGDVFHGAFAHALAE 254

                         250       260
                  ....*....|....*....|...
gi 1525684052 267 AHAFEQTLRTATAIAAMAVTQIG 289
Cdd:cd01945   255 GMPLREALRFASAAAALKCRGLG 277
PTZ00292 PTZ00292
ribokinase; Provisional
 13-289 5.64e-07

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 50.12  E-value: 5.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  13 LDLTVQLTRL-EPGQVNRSEAMHTHAAGKGVNVAQVLADLGHQLTVSGFLGED-NPQAFEALFARRGFVDAFIRVpgetr 90
Cdd:PTZ00292   26 TDLIGYVDRMpQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDgFGSDTIKNFKRNGVNTSFVSR----- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  91 sniklaeqdgritdlngpgpEVDAAAQQALLerLEQIAPGHDAVVVAGSLPRGVSPQWLHALLTRLKALG------LKVA 164
Cdd:PTZ00292  101 --------------------TENSSTGLAMI--FVDTKTGNNEIVIIPGANNALTPQMVDAQTDNIQNICkylicqNEIP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 165 LDTSGEALRAGLAAG-------------------------PWLVKPNTEELAEALGSPLLSLATQAAAARRLHAQGVEHV 219
Cdd:PTZ00292  159 LETTLDALKEAKERGcytvfnpapapklaeveiikpflkyVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENV 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525684052 220 VISHGAEG-VNWFSAAPALQALPPKVSVASTVGAGDSLLAGMLHGLLSAHAFEQTLRTATAIAAMAVTQIG 289
Cdd:PTZ00292  239 IITLGANGcLIVEKENEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHG 309
PRK09850 PRK09850
pseudouridine kinase; Provisional
 39-286 1.24e-06

pseudouridine kinase; Provisional


Pssm-ID: 182111 [Multi-domain]  Cd Length: 313  Bit Score: 49.22  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  39 GKGVNVAQVLADLGHQLTVSGFLGED-NPQAFEALFARRG-FVDAFIRVPGE-TRSNIKLAEQDGR----ITDLNgpgpE 111
Cdd:PRK09850   41 GVGRNIAQNLALLGNKAWLLSAVGSDfYGQSLLTQTNQSGvYVDKCLIVPGEnTSSYLSLLDNTGEmlvaINDMN----I 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 112 VDAAAQQALLERLEQIAPGHdaVVVAGSlprGVSPQWLHALLTrlKALGLKVALDTSGE----ALRAGLAAGPWLvKPNT 187
Cdd:PRK09850  117 SNAITAEYLAQHREFIQRAK--VIVADC---NISEEALAWILD--NAANVPVFVDPVSAwkcvKVRDRLNQIHTL-KPNR 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 188 EElAEAL-GSPLLSLATQAAAARRLHAQGVEHVVISHGAEGVnWFS--AAPALQALPPKVSVASTVGAGDSLLAGMLHGL 264
Cdd:PRK09850  189 LE-AETLsGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGV-YYSdiSGESGWSAPIKTNVINVTGAGDAMMAGLASCW 266

                         250       260
                  ....*....|....*....|..
gi 1525684052 265 LSAHAFEQTLRTATAIAAMAVT 286
Cdd:PRK09850  267 VDGMPFAESVRFAQGCSSMALS 288
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 170-287 1.12e-05

Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.


Pssm-ID: 238578 [Multi-domain]  Cd Length: 254  Bit Score: 46.04  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 170 EALRAGLAAGPWLVKPNTEELAEALGSPLLSLATQAAAARRLHAQGVEHVVISHGAEGVN------WFSAAPALQALPPK 243
Cdd:cd01173   127 PVYRDLLVPLADIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTSVELADDdriemlGSTATEAWLVQRPK 206

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1525684052 244 VS-VASTVGAGDSLLAGMLHGLLSAHAFEQTLRTATAI--AAMAVTQ 287
Cdd:cd01173   207 IPfPAYFNGTGDLFAALLLARLLKGKSLAEALEKALNFvhEVLEATY 253
Fructoselysine_kinase_like cd01940
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ...
 39-282 1.22e-05

Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.


Pssm-ID: 238915 [Multi-domain]  Cd Length: 264  Bit Score: 45.81  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052  39 GKGVNVAQVLADLGHQltvSGFLG----EDNPQAFEALFARRGFVDAFIRV-PGETRSNIKLAEQDGRI---TDLNGPGP 110
Cdd:cd01940    23 GNALNVAVYAKRLGHE---SAYIGavgnDDAGAHVRSTLKRLGVDISHCRVkEGENAVADVELVDGDRIfglSNKGGVAR 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 111 EVDAAAQQALLErleqiapGHDaVVVAGSLPRGVSpqwLHALLTRLKALGLKVALDTSGEALRAGLA-AGPWL--VKPNT 187
Cdd:cd01940   100 EHPFEADLEYLS-------QFD-LVHTGIYSHEGH---LEKALQALVGAGALISFDFSDRWDDDYLQlVCPYVdfAFFSA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 188 EELAEALGSPLLslatqaaaaRRLHAQGVEHVVISHGAEGVNWFSAAPALQALPPKVSVASTVGAGDSLLAGMLHGLL-S 266
Cdd:cd01940   169 SDLSDEEVKAKL---------KEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLaG 239

                         250
                  ....*....|....*.
gi 1525684052 267 AHAFEQTLRTATAIAA 282
Cdd:cd01940   240 GTAIAEAMRQGAQFAA 255
PRK09434 PRK09434
aminoimidazole riboside kinase; Provisional
 183-289 2.67e-05

aminoimidazole riboside kinase; Provisional


Pssm-ID: 236514 [Multi-domain]  Cd Length: 304  Bit Score: 44.93  E-value: 2.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 183 VKPNTEELAEALGSPLLSLATQAAAARrlhaQGVEHVVISHGAEGVnWFSAAPALQALP-PKVSVASTVGAGDSLLAGML 261
Cdd:PRK09434  184 VKLSEEELCFLSGTSQLEDAIYALADR----YPIALLLVTLGAEGV-LVHTRGQVQHFPaPSVDPVDTTGAGDAFVAGLL 258

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1525684052 262 HGLLSAHAFEQTLRTATAIA------AMAVTQIG 289
Cdd:PRK09434  259 AGLSQAGLWTDEAELAEIIAqaqacgALATTAKG 292
PRK09813 PRK09813
fructoselysine 6-kinase; Provisional
 130-285 6.42e-05

fructoselysine 6-kinase; Provisional


Pssm-ID: 182090 [Multi-domain]  Cd Length: 260  Bit Score: 43.57  E-value: 6.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 130 GHDAVVVAgslprgvspQWLHA--LLTRLKALGLKVALDTSG-------EALRAGLAAGPWLVKPNTEELAEALgsplls 200
Cdd:PRK09813  113 QYDIVHAA---------IWGHAedAFPQLHAAGKLTAFDFSDkwdsplwQTLVPHLDYAFASAPQEDEFLRLKM------ 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 201 latqaaaaRRLHAQGVEHVVISHGAEGVNWFSAAPALQALPPKVSVASTVGAGDSLLAGMLHGLLSAHAFEQTLRTATAI 280
Cdd:PRK09813  178 --------KAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTAC 249


                  ....*
gi 1525684052 281 AAMAV 285
Cdd:PRK09813  250 AAKTI 254
PLN02630 PLN02630
pfkB-type carbohydrate kinase family protein
 219-310 1.88e-04

pfkB-type carbohydrate kinase family protein


Pssm-ID: 178237  Cd Length: 335  Bit Score: 42.49  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 219 VVISHGAEGVNWFSAAPALQALP-PKVSVASTvGAGDSLLAGMLHGLLSAHAFEQTLRTATAIAAMAVTQIGFGITDAAQ 297
Cdd:PLN02630  206 VIVTNGKKGCRIYWKDGEMRVPPfPAIQVDPT-GAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLAVEQVGIPKFDLRQ 284

                          90
                  ....*....|...
gi 1525684052 298 LAQLEQGVRVHPL 310
Cdd:PLN02630  285 LQRVKDEVQRRKM 297
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 170-288 2.04e-04

Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 441841 [Multi-domain]  Cd Length: 272  Bit Score: 42.06  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 170 EALRAGLAAGPWLVKPNTEELAEALGSPLLSLATQAAAARRLHAQGVEHVVISH----------------GAEGVnWFSA 233
Cdd:COG2240   129 EFIMRRLVPLADIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTSvplddtpadkignlavTADGA-WLVE 207

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1525684052 234 APALQALPPkvsvastvGAGD----SLLAGMLHGllsahafeQTLRTATAIAAMAVTQI 288
Cdd:COG2240   208 TPLLPFSPN--------GTGDlfaaLLLAHLLRG--------KSLEEALERAAAFVYEV 250
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 182-256 8.52e-04

Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.


Pssm-ID: 430062 [Multi-domain]  Cd Length: 246  Bit Score: 40.16  E-value: 8.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 182 LVKPNTEELAEALGSPLLSLATQAAAARRLHAQGVEHVVI------SHGAEGVNWFSAAPALQALP-PKVSVASTVGAGD 254
Cdd:pfam08543 122 LITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIkgghleGEEAVVTDVLYDGGGFYTLEaPRIPTKNTHGTGC 201


                  ..
gi 1525684052 255 SL 256
Cdd:pfam08543 202 TL 203
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 182-258 6.04e-03

bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 37.80  E-value: 6.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525684052 182 LVKPNTEELAEALGSPLLSLATQA-AAARRLHAQGVEHVVI-----SHGAEGVNWFSAAPALQALP-PKVSVASTVGAGD 254
Cdd:PRK06427  136 LITPNLPEAEALTGLPIADTEDEMkAAARALHALGCKAVLIkgghlLDGEESVDWLFDGEGEERFSaPRIPTKNTHGTGC 215


                  ....
gi 1525684052 255 SLLA 258
Cdd:PRK06427  216 TLSA 219
 
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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