|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
38-458 |
0e+00 |
|
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar. The family corresponds to hexokinase PI and PII, which are also known as hexokinase-1/hexokinase-A and hexokinase-2/hexokinase-B, respectively.
Pssm-ID: 466937 [Multi-domain] Cd Length: 428 Bit Score: 827.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 38 TETLQAVTKHFISELEKGLSKKGGNIPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKLGGDRTFDTTQSKYRLPDA 117
Cdd:cd24087 1 TERLRKITDHFISELEKGLSKKGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNGKFDITQSKYRLPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 118 MRTtQNPDELWEFIADSLKAFIDEQFPQGISEPIPLGFTFSFPASQNKINEGILQRWTKGFDIPNIENHDVVPMLQKQIT 197
Cdd:cd24087 81 LKT-GTGEELWDFIADCLKKFVEEHFPGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQKALK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 198 KRNIPIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQgklSDDIPPSAPMAINCEYGSFDNEH 277
Cdd:cd24087 160 KRNVPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLE---HDDIPPDSPMAINCEYGAFDNEH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 278 VVLPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGFIFKNQDLSKFDKPFVMDTSYPARIEEDPFEN 357
Cdd:cd24087 237 LVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDPFEN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 358 LEDTDDLFQNEFGINTTVQERKLIRRLSELIGARAARLSVCGIAAICQKRGYKTGHIAADGSVYNRYPGFKEKAANALKD 437
Cdd:cd24087 317 LEDTDDLFQHFFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKKRGYKTCHVAADGSVYNKYPGFKERAAQALKD 396
|
410 420
....*....|....*....|.
gi 6321184 438 IYGWTQtslDDYPIKIVPAED 458
Cdd:cd24087 397 IFGWDG---EDDPIKTVPAED 414
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
38-458 |
0e+00 |
|
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. It is a putative glucokinase that functions in phosphorylation of aldohexoses and glucose uptake. It is involved in sporulation and required for the full activation of the early meiotic inducer IME1. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar.
Pssm-ID: 466868 [Multi-domain] Cd Length: 431 Bit Score: 571.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 38 TETLQAVTKHFISELEKGLSKKGGNIPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKL-GGDRTFDTTQSKYRLPD 116
Cdd:cd24018 1 VSKLEEIVKHFLSEMEKGLEGDGGSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLdGNGGIFIIVQRKYKIPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 117 AMRTTQNpDELWEFIADSLKAFIDEQ-FPQGISEPIPLGFTFSFPASQNKINEGILQRWTKGFDIPNIENHDVVPMLQKQ 195
Cdd:cd24018 81 EAKTGTG-EELFDFIAECIAEFLEEHnLDLQSDKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQNA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 196 ITKRNIPIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQgKLSDDIPPSAPMAINCEYGSFDN 275
Cdd:cd24018 160 LDRRGVNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLT-SPSGSVTKSDEMIINTEWGAFDN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 276 EHVVLPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGFIFKNQDLSKFDKPFVMDTSYPARIEEDPF 355
Cdd:cd24018 239 EREVLPLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEADTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 356 ENLEDTDDLFQNEFGI-NTTVQERKLIRRLSELIGARAARLSVCGIAAICQKRG---YKTGHIAADGSVYNRYPGFKEKA 431
Cdd:cd24018 319 PDLDAVRDILKELLAIdNTTLEDRKLIKRICELVSTRAARLSAAAIAAILLKRGsllPEPVTVGIDGSVYEKYPGFKDRL 398
|
410 420
....*....|....*....|....*..
gi 6321184 432 ANALKDIYGWTQTSlddyPIKIVPAED 458
Cdd:cd24018 399 SEALRELFGPEVKA----NISLVLAKD 421
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
38-438 |
1.90e-142 |
|
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 (GLK-2) from fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (also known as glucokinase-1, EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. It is a putative glucokinase that functions in phosphorylation of aldohexoses and glucose uptake. It is involved in sporulation and required for the full activation of the early meiotic inducer IME1. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar. The family corresponds to glucokinase-1 and glucokinase-2.
Pssm-ID: 466938 [Multi-domain] Cd Length: 445 Bit Score: 416.03 E-value: 1.90e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 38 TETLQAVTKHFISELEKGLSKKGGNIPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKLGGDRTFDTTQSKYRLPDA 117
Cdd:cd24088 1 DEKLDKLTAEFQRQMEKGLAKHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHGDGTFSLRQEKSKIPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 118 MRTTQNPDELWEFIADSLKAFI----DEQFPQGIS-EPIPLGFTFSFPASQNKINEGILQRWTKGFDIPNIENHDVVPML 192
Cdd:cd24088 81 LKTGVTAKDLFDYLAKSVEAFLtkhhGDSFAAGKDdDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 193 QKQITKRNIPIEVVALINDTTGTLVASYYTDPE---TKMGVIFGTGVNGAYYDVCSDIEKLQGKLSDDIPPSApMAINCE 269
Cdd:cd24088 161 QDELDRQGIPVKVVALVNDTVGTLLARSYTSPEisgAVLGAIFGTGTNGAYLEDLEKIKKLDDSSRVGKGKTH-MVINTE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 270 YGSFDNEHVVLPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQG--FIFKNQDLS-KFDKPFVMDTSY 346
Cdd:cd24088 240 WGSFDNELKVLPTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGlfLIQYNDKSPsALNTPYGLDTAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 347 PARIEEDPFENLEDTDDLFQNEFGINT-TVQERKLIRRLSELIGARAARLSVCGIAAICQKRG-----YKTG-HIAADGS 419
Cdd:cd24088 320 LSAIEIDSEAELRATRKVLLDDLGLPApSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGalnksYDGEiNIGVDGS 399
|
410
....*....|....*....
gi 6321184 420 VYNRYPGFKEKAANALKDI 438
Cdd:cd24088 400 VIEFYPGFESMLREALRLL 418
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
39-458 |
3.38e-134 |
|
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition.
Pssm-ID: 466869 [Multi-domain] Cd Length: 427 Bit Score: 394.22 E-value: 3.38e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 39 ETLQAVTKHFISELEKGLSK---KGGNIPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKLGGDRTFDTTQSKYRLP 115
Cdd:cd24019 5 EQLEEIMDRLLKEMEKGLSKdthPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGGSQVKMESEIYAIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 116 -DAMRTTQnpDELWEFIADSLKAFIDEQfpqGIS-EPIPLGFTFSFPASQNKINEGILQRWTKGFDIPNIENHDVVPMLQ 193
Cdd:cd24019 85 eEIMTGTG--EQLFDYIAECLAEFLEKN---GLKdKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLLQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 194 KQITKRNIP-IEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQGKLSDdiPPSapMAINCEYGS 272
Cdd:cd24019 160 EAIKRRGDIkVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKWDGDEGD--PGQ--VIINTEWGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 273 FDNEHVV-LPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGFIFKNQDLSKFDKPFVMDTSYPARIE 351
Cdd:cd24019 236 FGDNGVLdFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 352 EDPFENLEDTDDLFQNEFGINTTVQERKLIRRLSELIGARAARLSVCGIAAICQKRGYKTGHIAADGSVYNRYPGFKEKA 431
Cdd:cd24019 316 SDNEGDFSNTREILKELGLEDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNRKEVTVGVDGSLYKYHPKFHKRM 395
|
410 420
....*....|....*....|....*..
gi 6321184 432 ANALKDIYGwtqtslDDYPIKIVPAED 458
Cdd:cd24019 396 HETLKELVP------PGCKFKLMLSED 416
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
38-458 |
1.32e-125 |
|
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466850 [Multi-domain] Cd Length: 357 Bit Score: 369.68 E-value: 1.32e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 38 TETLQAVTKHFISELEKGLSKKGGNIPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKLGGDRTFDTTQSKYRLPDA 117
Cdd:cd24000 1 DEDLKEITDAFLEELEKGLAGEPSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGKGIEVTISKKYEIPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 118 MRTtQNPDELWEFIADSLKAFIDEQfpqGISEPIPLGFTFSFPASQNKINEGILQRWTKGFDIPNIENHDVVPMLQKQIT 197
Cdd:cd24000 81 IKT-ASAEEFFDFIADCIAEFLKEN---GLKKPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDALK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 198 KRNIPIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEklqgklsddiPPSAPMAINCEYGSFDNEh 277
Cdd:cd24000 157 KRGLPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNIL----------LGDGGMIINTEWGNFGKN- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 278 vVLPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQgfifknqdlskfdkpfvmdtsyparieedpfen 357
Cdd:cd24000 226 -SLPRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE--------------------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 358 ledtddlfqnefginttvqerkLIRRLSELIGARAARLSVCGIAAICQKRGYKTG---HIAADGSVYNRYPGFKEKAANA 434
Cdd:cd24000 272 ----------------------ILRKICELVAERSARLAAAAIAALLRKTGDSPEkkiTIAVDGSLFEKYPGYRERLEEY 329
|
410 420
....*....|....*....|....
gi 6321184 435 LKDIYGwtqtslDDYPIKIVPAED 458
Cdd:cd24000 330 LKELLG------RGIRIELVLVED 347
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
37-440 |
2.18e-119 |
|
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases act as sugar sensors in higher plants. They may regulate sugar-dependent gene repression or activation. They mediate the effects of sugar on plant growth and development independently of its catalytic activity or the sugar metabolism. They may also regulate the execution of program cell death in plant cells, as well as promote roots and leaves growth.
Pssm-ID: 466870 [Multi-domain] Cd Length: 439 Bit Score: 356.97 E-value: 2.18e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 37 PTETLQAVTKHFISELEKGLSKKGGN-IPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKLGG--DRTFDTTQSKYR 113
Cdd:cd24020 2 PVSRLRQVADAMVVEMEAGLASEGGSkLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGkeGRVDKQEYEEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 114 LPDAMRTTQNpDELWEFIADSLKAFIDE----QFPQGisEPIPLGFTFSFPASQNKINEGILQRWTKGFDIPNIENHDVV 189
Cdd:cd24020 82 IPPELMVGTS-EELFDFIAGELAKFVATegegFHPEG--EKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 190 PMLQKQITKRNIPIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQGKLsddiPPSAPMAINCE 269
Cdd:cd24020 159 ELLEEALERQGLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGL----PRSGEMVINTE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 270 YGSFDNEHvvLPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGFIFKNQDLSKFDKPFVMDTSYPAR 349
Cdd:cd24020 235 WGNFRSSH--LPRTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 350 IEEDPFENLEDTDDLFQNEFGI-NTTVQERKLIRRLSELIGARAARLSVCGIAAICQKRGYKTGH--------IAADGSV 420
Cdd:cd24020 313 MHEDDSPDLETVARILKDALGIdDTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLGRDGGGsspaqrtvVAVDGGL 392
|
410 420
....*....|....*....|
gi 6321184 421 YNRYPGFKEKAANALKDIYG 440
Cdd:cd24020 393 YEHYPKFREYMQQALVELLG 412
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
227-458 |
7.67e-103 |
|
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by this family and pfam00349. Some members of the family have two copies of each of these domains.
Pssm-ID: 461028 Cd Length: 236 Bit Score: 307.11 E-value: 7.67e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 227 KMGVIFGTGVNGAYYDVCSDIEKLQGKLsddiPPSAPMAINCEYGSFDNEHV-VLPRTKYDITIDEESPRPGQQTFEKMS 305
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKL----PKSGEMIINTEWGAFGDNGLlPLPRTEYDKELDAESPNPGFQPFEKMI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 306 SGYYLGEILRLALMDMYKQGFIFKNQDlSKFDKPFVMDTSYPARIEEDPFENLEDTDDLFQNEFGINT-TVQERKLIRRL 384
Cdd:pfam03727 77 SGMYLGELVRLVLLDLAEEGLLFKGQS-EKLKTPYSLDTSFLSAIESDPSEDLETTREILEELLGIETvTEEDRKIVRRI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321184 385 SELIGARAARLSVCGIAAICQKRG-YKTGHIAADGSVYNRYPGFKEKAANALKDIYGwtqtslDDYPIKIVPAED 458
Cdd:pfam03727 156 CEAVSTRAARLVAAGIAAILKKIGrDKKVTVGVDGSVYEKYPGFRERLQEALRELLG------PGDKVVLVLAED 224
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
26-221 |
4.12e-101 |
|
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by this family and pfam03727. Some members of the family have two copies of each of these domains.
Pssm-ID: 459774 [Multi-domain] Cd Length: 197 Bit Score: 301.34 E-value: 4.12e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 26 QIENFEKIFTVPTETLQAVTKHFISELEKGLSKKG-GNIPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKLGGDRT 104
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGsSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGGDGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 105 FDTTQSKYRLPDAMRTTqNPDELWEFIADSLKAFIDEQFPQGISE-PIPLGFTFSFPASQNKINEGILQRWTKGFDIPNI 183
Cdd:pfam00349 81 FEITQEKYKIPEELMTG-TGEELFDFIADCIAEFLKEHGLEDFEEkELPLGFTFSFPVEQTSLDSGTLIRWTKGFDIPGV 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 6321184 184 ENHDVVPMLQKQITKRNIPIEVVALINDTTGTLVASYY 221
Cdd:pfam00349 160 VGKDVVQLLQEALERRGLPVKVVALVNDTVGTLMAGAY 197
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
20-458 |
5.59e-98 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 302.75 E-value: 5.59e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 20 PKELMQQIENFekiFTVPTETLQAVTKHFISELEKGL----SKKGGNIP------MIPGWVMDFPTGKESGDFLAIDLGG 89
Cdd:PTZ00107 7 QRVRLASLVNQ---FTMSKEKLKELVDYFLYELVEGLeahrRHRNLWIPnecsfkMLDSCVYNLPTGKEKGVYYAIDFGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 90 TNLRVVLVKLGGDRTFDTTQSKYRLPDA--------MRTTQNPDELWEFIADSLKAFIDE-QFPQGISEPIPLGFTFSFP 160
Cdd:PTZ00107 84 TNFRAVRVSLRGGGKMERTQSKFSLPKSallgekglLDKKATATDLFDHIAKSIKKMMEEnGDPEDLNKPVPVGFTFSFP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 161 ASQNKINEGILQRWTKGFDIP-----NIENHDVVPMLQKQITKRNIPIEVVALINDTTGTLVASYYTD----PETKMGVI 231
Cdd:PTZ00107 164 CTQLSVNNAILIDWTKGFETGratndPVEGKDVGELLNDAFKRNNVPANVVAVLNDTVGTLISCAYQKpkntPPCQVGVI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 232 FGTGVNGAYYDVCSDIEKLQGKLsddippsapmaINCEYGSFDNEhvvLPRTKYDITIDEESPRPGQQTFEKMSSGYYLG 311
Cdd:PTZ00107 244 IGTGSNACYFEPEVSAYGYAGTP-----------INMECGNFDSK---LPITPYDLEMDWYTPNRGRQQFEKMISGAYLG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 312 EILRLALMDmykqgfIFKNQDLSKFDKPFVMDTSYPARIEEDPFENLEDTDDLFQNEFGINTTVQERKLIRRLSELIGAR 391
Cdd:PTZ00107 310 EISRRLIVH------LLQLKAPPKMWQSGSFESEDASMILNDQSPDLQFSRQVIKEAWDVDLTDEDLYTIRKICELVRGR 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321184 392 AARLSVCGIAAICQKRGYKTGH--IAADGSVYNRYPGFKEKAANALKDIYGWTQTSlddypIKIVPAED 458
Cdd:PTZ00107 384 AAQLAAAFIAAPAKKTRTVQGKatVAIDGSVYVKNPWFRRLLQEYINSILGPDAGN-----VVFYLADD 447
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
24-458 |
3.83e-97 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 299.57 E-value: 3.83e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 24 MQQIENFEKI--FTVPTETLQAVTKHFISELEKGLSKKGGNIPMIPGWVmDFPTG-KESGDFLAIDLGGTNLRVVLVKLG 100
Cdd:COG5026 3 KLLVDAFLKRhgFDLSSIDLEEIAAKFQEEMEKGLEGKKSSLKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRFD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 101 GDRTFDTTQ-SKYRLPDAMRTTQNpDELWEFIADSLKAFIDEQFPqgisepipLGFTFSFPASQNKINEGILQRWTKGFD 179
Cdd:COG5026 82 GEGTFEIENfKSFPLPGTSSEITA-EEFFDFIADYIEPLLDESYK--------LGFCFSFPAEQLPDKDGRLIQWTKEIK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 180 IPNIENHDVVPMLQKQITKRN-IPIEVVALINDTTGTLVASYYTDPETK----MGVIFGTGVNGAYYDVCSDIEKLQGkl 254
Cdd:COG5026 153 TPGVEGKNIGELLEAALARKGlDNVKPVAILNDTVATLLAGAYADPDDGysgyIGSILGTGHNTCYLEPNAPIGKLPA-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 255 sddipPSAPMAINCEYGSFDnehvVLPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGfIFKNQDLS 334
Cdd:COG5026 231 -----YEGPMIINMESGNFN----KLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 335 KFDKPFVMDTSYPARIEEDPFENLEDTDDLFQnefgiNTTVQERKLIRRLSELIGARAARLSVCGIAAICQKRG-YKTGH 413
Cdd:COG5026 301 VFETPYSLTTVDMSRFLADPSDEKEILSQCLE-----AGSEEDREILREIADAIVERAARLVAATLAGILLHLGpGKTPL 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 6321184 414 ----IAADGSVYNRYPGFKEKAANALKDIYgwtqTSLDDYPIKIVPAED 458
Cdd:COG5026 376 kphcIAIDGSTYEKMPGLAEKIEYALQEYL----LGEKGRYVEFVLVEN 420
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
39-438 |
9.78e-91 |
|
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the second two domains of types I to III hexokinases. Type I enzyme may have a catabolic function, producing H6P for energy production in glycolysis; it is bound to the mitochondrial membrane, which enables the coordination of glycolysis with the TCA cycle. Types II and III enzyme may have anabolic functions, providing H6P for glycogen or lipid synthesis.
Pssm-ID: 466941 [Multi-domain] Cd Length: 433 Bit Score: 283.28 E-value: 9.78e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 39 ETLQAVTKHFISELEKGLSKKGGN---IPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKL--GGDRTFDTTQSKYR 113
Cdd:cd24091 5 DQLLEVKARMRAEMERGLRKETHAsapVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVrsGKWRGVEMHNKIYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 114 LP-DAMRTTQnpDELWEFIADSLKAFIDEQFPQGISepIPLGFTFSFPASQNKINEGILQRWTKGFDIPNIENHDVVPML 192
Cdd:cd24091 85 IPqEIMQGTG--EELFDHIVQCIADFLEYMGLKGVS--LPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 193 QKQITKRN-IPIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQGKlsddippSAPMAINCEYG 271
Cdd:cd24091 161 REAIKRREeFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGE-------EGRMCINMEWG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 272 SF-DNEHVVLPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGFIFKNQDLSKFDKPFVMDTSYPARI 350
Cdd:cd24091 234 AFgDNGCLDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 351 EEDPFENLEDTDDLFQneFGINTTVQERKLIRRLSELIGARAARLSVCGIAAICQKRGYKTG------HIAADGSVYNRY 424
Cdd:cd24091 314 ESDRLALLQVRAILQQ--LGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGldhlnvTVGVDGTLYKLH 391
|
410
....*....|....
gi 6321184 425 PGFKEKAANALKDI 438
Cdd:cd24091 392 PHFSRVMHETVKEL 405
|
|
| PLN02362 |
PLN02362 |
hexokinase |
21-440 |
5.64e-89 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 281.00 E-value: 5.64e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 21 KELMQQIENFEKIFTVPTETLQAVTKHFISELEKGLSKKGGN-IPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKL 99
Cdd:PLN02362 35 RRVVGVLKELEEACETPVGRLRQVVDAMAVEMHAGLASEGGSkLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 100 GGDRTFDTTQSKYRLP---DAMRTTQnpDELWEFIADSLKAFIDEQfpQGISEPIP-----LGFTFSFPASQNKINEGIL 171
Cdd:PLN02362 115 GGQRSSILSQDVERHPipqHLMNSTS--EVLFDFIASSLKQFVEKE--ENGSEFSQvrrreLGFTFSFPVKQTSISSGIL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 172 QRWTKGFDIPNIENHDVVPMLQKQITKRNIPIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQ 251
Cdd:PLN02362 191 IKWTKGFAISDMVGKDVAECLQGALNRRGLDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQ 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 252 GKLSDdippSAPMAINCEYGSFDNEHvvLPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGFIFKNQ 331
Cdd:PLN02362 271 GLLTT----SGSMVVNMEWGNFWSSH--LPRTSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIFGPV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 332 DlSKFDKPFVMDTSYPARIEEDPFENLEDTDDLFQNEFGI-NTTVQERKLIRRLSELIGARAARLSVCGIAAICQKRG-- 408
Cdd:PLN02362 345 S-SRLSTPFVLRTPSVAAMHEDDSPELQEVARILKETLGIsEVPLKVRKLVVKICDVVTRRAARLAAAGIVGILKKIGrd 423
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 6321184 409 ----------------YKTGHIAADGSVYNRYPGFKEKAANALKDIYG 440
Cdd:PLN02362 424 gsggitsgrsrsdiqiMRRTVVAVEGGLYTNYTMFREYLHEALNEILG 471
|
|
| PLN02914 |
PLN02914 |
hexokinase |
30-440 |
7.08e-85 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 269.83 E-value: 7.08e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 30 FEKIFTVPTETLQAVTKHFISELEKGLSKKGG-NIPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKLGG--DRTFD 106
Cdd:PLN02914 44 LQKDCATPLPVLRHVADAMAADMRAGLAVDGGgDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGkdERVIA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 107 TTQSKYRLPDAMRTTQNpDELWEFIADSLKAFIDEQ-----FPQGISEPIplGFTFSFPASQNKINEGILQRWTKGFDIP 181
Cdd:PLN02914 124 TEFEQVSIPQELMFGTS-EELFDFIASGLANFVAKEggkfhLPEGRKREI--GFTFSFPVKQTSIDSGILMKWTKGFAVS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 182 NIENHDVVPMLQKQITKRNIPIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQGKLSDdippS 261
Cdd:PLN02914 201 GTAGKDVVACLNEAMERQGLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKSS----S 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 262 APMAINCEYGSFDNehvVLPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGFIFKNQDLSKFDKPFV 341
Cdd:PLN02914 277 GRTIINTEWGAFSD---GLPLTEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 342 MDTSYPARIEEDPFENLEDTDDLFQNEFGINTTVQERKLIRRLSELIGARAARLSVCGIAAICQK-----RGYKTGH--- 413
Cdd:PLN02914 354 LRTPHLCAMQQDNSDDLQAVGSILYDVLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKmeedsKGMIFGKrtv 433
|
410 420
....*....|....*....|....*..
gi 6321184 414 IAADGSVYNRYPGFKEKAANALKDIYG 440
Cdd:PLN02914 434 VAMDGGLYEKYPQYRRYMQDAVTELLG 460
|
|
| PLN02405 |
PLN02405 |
hexokinase |
24-440 |
2.00e-82 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 263.62 E-value: 2.00e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 24 MQQIENFEKIFTVPTETLQAVTKHFISELEKGLSKKGGN-IPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKLGG- 101
Cdd:PLN02405 38 MEILKEFEEDCATPIGKLRQVADAMTVEMHAGLASEGGSkLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGk 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 102 -DRTFDTTQSKYRLPDAMrTTQNPDELWEFIADSLKAFIDEQFPQgiSEPIP-----LGFTFSFPASQNKINEGILQRWT 175
Cdd:PLN02405 118 dGRVVKQEFEEVSIPPHL-MTGSSDALFDFIAAALAKFVATEGED--FHLPPgrqreLGFTFSFPVKQTSISSGTLIKWT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 176 KGFDIPNIENHDVVPMLQKQITKRNIPIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQGKLs 255
Cdd:PLN02405 195 KGFSIDDAVGQDVVGELTKAMERVGLDMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGLL- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 256 ddiPPSAPMAINCEYGSFDNEHvvLPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGFIFKNQDLSK 335
Cdd:PLN02405 274 ---PKSGEMVINMEWGNFRSSH--LPLTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPK 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 336 FDKPFVMDTSYPARIEEDPFENLEDTDDLFQNEFGI-NTTVQERKLIRRLSELIGARAARLSVCGIAAICQKRGYKTGH- 413
Cdd:PLN02405 349 LKIPFILRTPDMSAMHHDTSPDLKVVGSKLKDILEIpNTSLKMRKVVVELCNIVATRGARLSAAGIYGILKKLGRDTVKd 428
|
410 420 430
....*....|....*....|....*....|....
gi 6321184 414 -------IAADGSVYNRYPGFKEKAANALKDIYG 440
Cdd:PLN02405 429 gekqksvIAMDGGLFEHYTEFSKCMESTLKELLG 462
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
39-436 |
3.63e-82 |
|
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of types I and II hexokinases.
Pssm-ID: 466939 [Multi-domain] Cd Length: 429 Bit Score: 260.86 E-value: 3.63e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 39 ETLQAVTKHFISELEKGLSK---KGGNIPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKLG--GDRTFDTTQSKYR 113
Cdd:cd24089 5 ETLLDISRRFRKEMEKGLGKdthPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNdeKNQKVEMESQVYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 114 LPDAMrTTQNPDELWEFIADSLKAFIDEQFPQGisEPIPLGFTFSFPASQNKINEGILQRWTKGFDIPNIENHDVVPMLQ 193
Cdd:cd24089 85 IPEEI-MHGSGTQLFDHVAECLADFMDKQKIKD--KKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 194 KQITKR-NIPIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQGklsDDippsAPMAINCEYGS 272
Cdd:cd24089 162 KAIRRRgDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEG---DE----GRMCINTEWGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 273 F-DNEHVVLPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGFIFKNQDLSKFDKPFVMDTSYPARIE 351
Cdd:cd24089 235 FgDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 352 EDPfENLEDTDDLFQnEFGINTTVQERKLIRRLSELIGARAARLSVCGIAAICQK-RGYKTGH-----IAADGSVYNRYP 425
Cdd:cd24089 315 KEK-EGLANAKEILT-RLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRlRENKGLErlrttVGVDGSVYKKHP 392
|
410
....*....|.
gi 6321184 426 GFKEKAANALK 436
Cdd:cd24089 393 QFSKRLHKAVR 403
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
39-438 |
1.66e-81 |
|
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the second two domains of type I hexokinase.
Pssm-ID: 466977 [Multi-domain] Cd Length: 434 Bit Score: 259.46 E-value: 1.66e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 39 ETLQAVTKHFISELEKGLSKKGGN---IPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKL--GGDRTFDTTQSKYR 113
Cdd:cd24127 5 DMLLEVKKRMRAEMELGLRKQTHNnavVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIrsGKKRTVEMHNKIYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 114 LP-DAMRTTQnpDELWEFIADSLKAFIDEQfpqGISEP-IPLGFTFSFPASQNKINEGILQRWTKGFDIPNIENHDVVPM 191
Cdd:cd24127 85 IPiEIMQGTG--EELFDHIVSCISDFLDYM---GIKGPrMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 192 LQKQITKRN-IPIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQGKlsddippSAPMAINCEY 270
Cdd:cd24127 160 LRDAIKRREeFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGD-------QGQMCINMEW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 271 GSF-DNEHVVLPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGFIFKNQDLSKFDKPFVMDTSYPAR 349
Cdd:cd24127 233 GAFgDNGCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 350 IEEDPFENLEDTDDLFQneFGINTTVQERKLIRRLSELIGARAARLSVCGIAAICQK----RGYKTGHI--AADGSVYNR 423
Cdd:cd24127 313 IESDRLALLQVRAILQQ--LGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKirenRGLDHLNVtvGVDGTLYKL 390
|
410
....*....|....*
gi 6321184 424 YPGFKEKAANALKDI 438
Cdd:cd24127 391 HPHFSRIMHQTVKEL 405
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
39-427 |
2.04e-81 |
|
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 (HKDC1) from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. HKDC1 is a putative novel fifth hexokinase found in vertebrates. It may be involved in whole-body glucose use. The model corresponds to the second two domains of HKDC1.
Pssm-ID: 466980 [Multi-domain] Cd Length: 433 Bit Score: 259.09 E-value: 2.04e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 39 ETLQAVTKHFISELEKGLSKKG---GNIPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKL-GGDRTFDTTQSKYRL 114
Cdd:cd24130 5 DQLQEVKQKMRTELEYGLKKEThptASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIrSGRRSVRMYNKIFAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 115 P-DAMRTTQnpDELWEFIADSLKAFIDEQFPQGISepIPLGFTFSFPASQNKINEGILQRWTKGFDIPNIENHDVVPMLQ 193
Cdd:cd24130 85 PlEIMQGTG--EELFDHIVQCIADFLDYMGLKGAR--LPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDMLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 194 KQITKRN-IPIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQGKlsddippSAPMAINCEYGS 272
Cdd:cd24130 161 EAIKRRNeFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGD-------EGRMCINTEWGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 273 F-DNEHVVLPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGFIFKNQDLSKFDKPFVMDTSYPARIE 351
Cdd:cd24130 234 FgDNGCIDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 352 EDPFENLEDTDDLFQneFGINTTVQERKLIRRLSELIGARAARLSVCGIAAICQKRGYKTG------HIAADGSVYNRYP 425
Cdd:cd24130 314 SDRLALLQVRRILQQ--LGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGldrldiTVGVDGTLYKLHP 391
|
..
gi 6321184 426 GF 427
Cdd:cd24130 392 HF 393
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
39-438 |
3.12e-80 |
|
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the second two domains of type II hexokinase.
Pssm-ID: 466978 [Multi-domain] Cd Length: 435 Bit Score: 255.98 E-value: 3.12e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 39 ETLQAVTKHFISELEKGLSKKGGN---IPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKL--GGDRTFDTTQSKYR 113
Cdd:cd24128 5 DQLLEVKRRMKVEMERGLSKETHAsapVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVrnGKWRGVEMHNKIYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 114 LP-DAMRTTQnpDELWEFIADSLKAFIDEQFPQGISepIPLGFTFSFPASQNKINEGILQRWTKGFDIPNIENHDVVPML 192
Cdd:cd24128 85 IPqEVMHGTG--EELFDHIVHCIADFLEYMGMKGVS--LPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 193 QKQITKR-NIPIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQGKlsddippSAPMAINCEYG 271
Cdd:cd24128 161 KEAIHRReEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGE-------EGRMCVNMEWG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 272 SF-DNEHVVLPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGFIFKNQDLSKFDKPFVMDTSYPARI 350
Cdd:cd24128 234 AFgDNGCLDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 351 EEDPFENLEDTDDLfqNEFGINTTVQERKLIRRLSELIGARAARLSVCGIAAICQK----RGYKTGHI--AADGSVYNRY 424
Cdd:cd24128 314 ESDRLALLQVRAIL--QHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKirenRGLDALKVtvGVDGTLYKLH 391
|
410
....*....|....
gi 6321184 425 PGFKEKAANALKDI 438
Cdd:cd24128 392 PHFAKVMHETVKDL 405
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
26-430 |
7.38e-77 |
|
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to type IV hexokinase. It is found in the liver and pancreatic beta-cells, where it is controlled by insulin (activation) and glucagon (inhibition). In pancreatic beta-cells, type IV enzyme acts as a glucose sensor to modify insulin secretion. Mutations in type IV hexokinase have been associated with diabetes mellitus.
Pssm-ID: 466942 [Multi-domain] Cd Length: 444 Bit Score: 247.49 E-value: 7.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 26 QIENFEKIFTVPTETLQAVTKHFISELEKGL---SKKGGNIPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKLG-- 100
Cdd:cd24092 1 LVEQILAEFQLQEEDLKKVMRRMQKEMDRGLrleTHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 101 --GDRTFDTTQSKYRLP-DAMrtTQNPDELWEFIADSLKAFIDEQfpQGISEPIPLGFTFSFPASQNKINEGILQRWTKG 177
Cdd:cd24092 81 eeGQWSVKTKHQMYSIPeDAM--TGTAEMLFDYISECISDFLDKH--QMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 178 FDIPNIENHDVVPMLQKQITKR-NIPIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQGKlsd 256
Cdd:cd24092 157 FKASGAEGNNVVGLLRDAIKRRgDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGD--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 257 dippSAPMAINCEYGSF-DNEHVVLPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGFIFKNQDLSK 335
Cdd:cd24092 234 ----EGRMCVNTEWGAFgDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 336 FDKPFVMDTSYPARIEedpfenlEDTDDLFQ-----NEFGINTTVQERKLIRRLSELIGARAARLSVCGIAAI----CQK 406
Cdd:cd24092 310 LRTRGAFETRFVSQVE-------SDTGDRKQiynilSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVinrmRES 382
|
410 420
....*....|....*....|....*.
gi 6321184 407 RGYKTGHIAA--DGSVYNRYPGFKEK 430
Cdd:cd24092 383 RSEDVMRITVgvDGSVYKLHPSFKER 408
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
39-430 |
1.72e-75 |
|
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 (HKDC1) from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. HKDC1 is a putative novel fifth hexokinase found in vertebrates. It may be involved in whole-body glucose use. The model corresponds to the first two domains of HKDC1.
Pssm-ID: 466976 [Multi-domain] Cd Length: 429 Bit Score: 243.60 E-value: 1.72e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 39 ETLQAVTKHFISELEKGLSKKG---GNIPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKLG--GDRTFDTTQSKYR 113
Cdd:cd24126 5 DTLLDIMTRFRAEMEKGLAKDTnptAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSedGKQKVQMESQFYP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 114 LPDAMrTTQNPDELWEFIADSLKAFIDEQfpqGIS-EPIPLGFTFSFPASQNKINEGILQRWTKGFDIPNIENHDVVPML 192
Cdd:cd24126 85 TPEEI-IHGTGTELFDYVAECLADFMKKK---GIKhKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 193 QKQITK-RNIPIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQGKlsddippSAPMAINCEYG 271
Cdd:cd24126 161 RKAIRKhKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGD-------EGRMCINTEWG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 272 SF-DNEHVVLPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGFIFKNQDLSKFDKPFVMDTSYPARI 350
Cdd:cd24126 234 AFgDDGSLEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 351 EEdPFENLEDTDDLFQnEFGINTTVQERKLIRRLSELIGARAARLSVCGIAAIC--------QKRGYKTghIAADGSVYN 422
Cdd:cd24126 314 EK-YKEGLYNTREILS-DLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILtrlrenkkLERLRTT--VGMDGTVYK 389
|
....*...
gi 6321184 423 RYPGFKEK 430
Cdd:cd24126 390 THPQYAKR 397
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
39-436 |
6.95e-75 |
|
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of type II hexokinase.
Pssm-ID: 466975 [Multi-domain] Cd Length: 429 Bit Score: 242.11 E-value: 6.95e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 39 ETLQAVTKHFISELEKGLSKKG---GNIPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKL--GGDRTFDTTQSKYR 113
Cdd:cd24125 5 ETLLEISKRFRKEMEKGLGATThptAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVsdNGLQKVEMENQIYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 114 LP-DAMRTTQNpdELWEFIADSLKAFIDEQfpqGISEP-IPLGFTFSFPASQNKINEGILQRWTKGFDIPNIENHDVVPM 191
Cdd:cd24125 85 IPeDIMRGSGT--QLFDHIAECLANFMDKL---QIKDKkLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 192 LQKQITKR-NIPIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQGKlsddippSAPMAINCEY 270
Cdd:cd24125 160 LRKAIQKRgDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGD-------EGRMCINMEW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 271 GSFDNEHVVLP-RTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGFIFKNQDLSKFDKPFVMDTSYPAR 349
Cdd:cd24125 233 GAFGDDGSLDDiRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 350 IEEDPfENLEDTDDLFQNeFGINTTVQERKLIRRLSELIGARAARLSVCGIAAICQKRGYKTG------HIAADGSVYNR 423
Cdd:cd24125 313 IEGEK-DGIRKAREVLMR-LGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGeerlrsTIGVDGSVYKK 390
|
410
....*....|...
gi 6321184 424 YPGFKEKAANALK 436
Cdd:cd24125 391 HPHFARRLHKTVR 403
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
41-438 |
4.29e-74 |
|
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the second two domains of type III hexokinase.
Pssm-ID: 466979 [Multi-domain] Cd Length: 430 Bit Score: 240.17 E-value: 4.29e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 41 LQAVTKHFISELEKGLSKK---GGNIPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKLGgDRTFDTTQSKYRLPDA 117
Cdd:cd24129 7 LAAVQAQMRKEMAKGLRGEthaAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVG-TAGVQITSEIYSIPET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 118 MrTTQNPDELWEFIADSLkafIDEQFPQGIS-EPIPLGFTFSFPASQNKINEGILQRWTKGFDIPNIENHDVVPMLQKQI 196
Cdd:cd24129 86 V-AQGTGQQLFDHIVDCI---VDFQQKQGLSgQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLLREAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 197 TKR-NIPIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQGKlsddippSAPMAINCEYGSF-D 274
Cdd:cd24129 162 TRKqAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGD-------SGRMCINMEWGAFgD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 275 NEHVVLPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGFIFKNQDLSKFDKPFVMDTSYPARIEEDP 354
Cdd:cd24129 235 NGCLAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 355 FeNLEDTDDLFQnEFGINTTVQERKLIRRLSELIGARAARLSVCGIAAICQKRGYKTG------HIAADGSVYNRYPGFK 428
Cdd:cd24129 315 L-ALRQVRAILE-DLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGldelavTVGVDGTLYKLHPRFS 392
|
410
....*....|
gi 6321184 429 EKAANALKDI 438
Cdd:cd24129 393 SLVQATVREL 402
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
24-430 |
2.56e-66 |
|
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of type I hexokinase.
Pssm-ID: 466974 [Multi-domain] Cd Length: 473 Bit Score: 221.03 E-value: 2.56e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 24 MQQIENFEKIFTVPTETLQAVTKHFISELEKGLSKK---GGNIPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKLG 100
Cdd:cd24124 18 VKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDfnpTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 101 GDR--TFDTTQSKYRLPDAMrTTQNPDELWEFIADSLKAFIDEQfpQGISEPIPLGFTFSFPASQNKINEGILQRWTKGF 178
Cdd:cd24124 98 HEKnqNVHMESEVYDTPENI-VHGSGSQLFDHVAECLGDFMEKR--KIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 179 DIPNIENHDVVPMLQKQITKR-NIPIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQGKlsdd 257
Cdd:cd24124 175 KASGVEGADVVKLLNKAIKKRgDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGD---- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 258 ippSAPMAINCEYGSFDNEHVVLP-RTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGFIFKNQDLSKF 336
Cdd:cd24124 251 ---EGRMCINTEWGAFGDDGSLEDiRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPEL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 337 DKPFVMDTSYPARIEEDPfENLEDTDDLFqNEFGINTTVQERKLIRRLSELIGARAARLSVCGIAAICQKRGYKTG---- 412
Cdd:cd24124 328 LTRGKFNTSDVSAIEKNK-EGLHNAKEIL-TRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGtprl 405
|
410 420
....*....|....*....|
gi 6321184 413 --HIAADGSVYNRYPGFKEK 430
Cdd:cd24124 406 rtTVGVDGSLYKTHPQYSRR 425
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
35-429 |
1.01e-60 |
|
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of type III hexokinase.
Pssm-ID: 466940 [Multi-domain] Cd Length: 431 Bit Score: 205.16 E-value: 1.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 35 TVPTETLQAVTKHFISELEKGLSKKGGNIP---MIPGWVMDFPTGKESGDFLAIDLG--GTNLRVVLVKLGGDRTF--DT 107
Cdd:cd24090 1 KVTRAQLQQIQASLLGSMEQALRGQASPAPavrMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHrvEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 108 TQSKYRLPDAMrtTQNP-DELWEFIADSLKAFIDEQ-FPQgisEPIPLGFTFSFPASQNKINEGILQRWTKGFDIPNIEN 185
Cdd:cd24090 81 RSQEFVIPQEV--MLGAgQQLFDFAAHCLSEFLDGQpVPK---QGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 186 HDVVPMLQKQITKRNI-PIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQgklsddiPPSAPM 264
Cdd:cd24090 156 QDVVQLLRDAIQRQGAyNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLD-------EDRGRV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 265 AINCEYGSFDNEHVVLP-RTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGFIFKNQDLSKFDKPFVMD 343
Cdd:cd24090 229 CVSVEWGSFSDDGALGPvLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSIL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 344 TSYPARIeEDPFENLEDTDDLFQnEFGINTTVQERKLIRRLSELIGARAARLSVCGIAAIC----QKRGYKTGHI--AAD 417
Cdd:cd24090 309 LEHVAEM-EDPSAGAARVRAILQ-DLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLshlqHSREQQTLQVavATG 386
|
410
....*....|..
gi 6321184 418 GSVYNRYPGFKE 429
Cdd:cd24090 387 GRVCERHPRFCS 398
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
37-428 |
5.83e-47 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 169.67 E-value: 5.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 37 PTETLQAVTKHFISELEKGLSKKG-GNIPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKLGG--DRTFDTTQSKYR 113
Cdd:PLN02596 52 PVSKLWEVADALVSDMTASLTAEEtTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGknEPISDLYREEIS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 114 LP-DAMRTTQNpdELWEFIADSLKAFIDEQFPQ---GISEPIPLGFTFSFPASQNKINEGILQRWtKGFDIPNIENHDVV 189
Cdd:PLN02596 132 IPsNVLNGTSQ--ELFDYIALELAKFVAEHPGDeadTPERVKKLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 190 PMLQKQITKRNIPIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQGKlsddIPPSAPMAINCE 269
Cdd:PLN02596 209 NDINRALEKHGLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSP----SPESQEIVISTE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 270 YGSFDNEHvvLPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGFIFKNQDLSKFDKPFVMDTSYPAR 349
Cdd:PLN02596 285 WGNFNSCH--LPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAA 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 350 IEEDPFENLEDTDDLFQNEFGI-NTTVQERKLIRRLSELIGARAARLSVCGIAAICQKRGY---KTGHIAADGSVYNRYP 425
Cdd:PLN02596 363 MHQDTSEDHEVVNEKLKEIFGItDSTPMAREVVAEVCDIVAERGARLAGAGIVGIIKKLGRienKKSVVTVEGGLYEHYR 442
|
...
gi 6321184 426 GFK 428
Cdd:PLN02596 443 VFR 445
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
82-239 |
1.09e-07 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 53.36 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 82 FLAIDLGGTNLRVVLVKLGGdrtfdTTQSKYRLPdaMRTTQNPDELWEFIADSLKAFIDEqfpQGISEPIPLGFTFSFPA 161
Cdd:COG1940 7 VIGIDIGGTKIKAALVDLDG-----EVLARERIP--TPAGAGPEAVLEAIAELIEELLAE---AGISRGRILGIGIGVPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 162 SQNKiNEGILQRWTKgfdIPNIENHDVVPMLQKQItkrNIPievVALINDTTGTLVASYY----TDPETKMGVIFGTGVN 237
Cdd:COG1940 77 PVDP-ETGVVLNAPN---LPGWRGVPLAELLEERL---GLP---VFVENDANAAALAEAWfgagRGADNVVYLTLGTGIG 146
|
..
gi 6321184 238 GA 239
Cdd:COG1940 147 GG 148
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
82-241 |
1.56e-05 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 46.90 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 82 FLAIDLGGTNLRVVLVklggDRTFDTTQSKYRlpdamRTT--QNPDELwefiaDSLKAFIDEQFPQGISEP--IPLGftf 157
Cdd:PRK09698 6 VLGIDMGGTHIRFCLV----DAEGEILHCEKK-----RTAevIAPDLV-----SGLGEMIDEYLRRFNARChgIVMG--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 158 sFPASQNKINEGILQrwtkgfdIPNI-----ENHDVVPMLQKQItkrNIPievVALINDTTGTL---VASYYTDPETKMG 229
Cdd:PRK09698 69 -FPALVSKDRRTVIS-------TPNLpltalDLYDLADKLENTL---NCP---VFFSRDVNLQLlwdVKENNLTQQLVLG 134
|
170
....*....|....*...
gi 6321184 230 VIFGTG------VNGAYY 241
Cdd:PRK09698 135 AYLGTGmgfavwMNGAPW 152
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
82-241 |
2.43e-05 |
|
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1.55), also called allokinase, catalyzes the phosphorylation of D-allose to D-allose 6-phosphate. It has also low level glucokinase activity in vitro. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466920 [Multi-domain] Cd Length: 293 Bit Score: 46.00 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 82 FLAIDLGGTNLRVVLVklggDRTFDTTQSKYRLPDAMRTTQNPDelwEFIADSLKAFIDEQF--PQGISepiplgftFSF 159
Cdd:cd24070 3 VLGIDIGGTNIRIGLV----DEDGKLLDFEKVPSKDLLRAGDPV---EVLADLIREYIEEAGlkPAAIV--------IGV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 160 PASQNKINEGILQrwtkgfdIPNI---ENHDVVPMLQKQItkrNIPievVALINDTT----GTLVASYYTDPETKMGVIF 232
Cdd:cd24070 68 PGTVDKDRRTVIS-------TPNIpglDGVNLADILENKL---GIP---VILERDVNllllYDMRAGNLDDEGVVLGFYI 134
|
....*....
gi 6321184 233 GTGVNGAYY 241
Cdd:cd24070 135 GTGIGNAIL 143
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
83-211 |
3.11e-04 |
|
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family corresponds to a group of proteins including sugar kinases, transcriptional repressors, and yet uncharacterized open reading frames. ROK family sugar kinases phosphorylate a range of structurally distinct hexoses including the key carbon source D-glucose, various glucose epimers, and several acetylated hexosamines. The sugar kinases include N-acetyl-D-glucosamine kinase (NAGK; EC 2.7.1.59), polyphosphate glucokinase (PPGK; EC 2.7.1.63/EC 2.7.1.2), glucokinase (GLK; EC 2.7.1.2), fructokinase (FRK; EC 2.7.1.4), hexokinase (HK; EC 2.7.1.1), D-allose kinase (AlsK; EC 2.7.1.55), bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE; EC 3.2.1.183/EC 2.7.1.60), N-acetylmannosamine kinase (NanK; EC 2.7.1.60), beta-glucoside kinase (BglK; EC 2.7.1.85), and N-acetylglucosamine kinase (EC 2.7.1.59). The family also contains the repressor proteins, such as N-acetylglucosamine repressor (NagC), xylose repressor (XylR), cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and protein Mlc. ROK kinases harbor a conserved N-terminal ATP binding motif of sequence DxGxT, while ROK repressors possess a N-terminal extension that contains a canonical helix-turn-helix DNA binding motif. The ROK family proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466849 [Multi-domain] Cd Length: 239 Bit Score: 42.45 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321184 83 LAIDLGGTNLRVVLVKLGGdrtfdTTQSKYRLPdaMRTTQNPDELWEFIADSLKAFIDEqfpQGISEPIpLGFTFSFPAS 162
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDG-----EILARERVP--TPAEEGPEAVLDRIAELIEELLAE---AGVRERI-LGIGIGVPGP 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 6321184 163 qnkIN--EGILQRWtkgfdiPNIENHDVVPmLQKQITKR-NIPievVALIND 211
Cdd:cd23763 70 ---VDpeTGIVLFA------PNLPWWKNVP-LRELLEERlGLP---VVVEND 108
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
82-141 |
2.45e-03 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 40.20 E-value: 2.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321184 82 FLAIDLGGTNLRVVLVKLGGdRTFDTTQSKYRL--PDAMRTTQNPDELWEFIADSLKAFIDE 141
Cdd:COG1070 3 VLGIDIGTTSVKAVLFDADG-EVVASASAEYPLssPHPGWAEQDPEDWWEAVVEAIRELLAK 63
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
82-141 |
2.71e-03 |
|
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466787 [Multi-domain] Cd Length: 392 Bit Score: 39.86 E-value: 2.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321184 82 FLAIDLGGTNLRVVLVKLGGdRTFDTTQSKYRL--PDAMRTTQNPDELWEFIADSLKAFIDE 141
Cdd:cd00366 2 LLGIDIGTTSVKAALFDEDG-NLVASASREYPLiyPQPGWAEQDPEDWWQAVVEAIREVLAK 62
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
82-137 |
4.38e-03 |
|
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466790 [Multi-domain] Cd Length: 478 Bit Score: 39.46 E-value: 4.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 6321184 82 FLAIDLGGTNLRVVLVKLGGdRTFDTTQSKYRL--PDAMRTTQNPDELWEFIADSLKA 137
Cdd:cd07770 2 ILGIDIGTTSTKAVLFDEDG-RVVASSSAEYPLirPEPGWAEQDPEEILEAVLEALKE 58
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
83-148 |
6.08e-03 |
|
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.
Pssm-ID: 395295 [Multi-domain] Cd Length: 245 Bit Score: 38.47 E-value: 6.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321184 83 LAIDLGGTNLRVVLVklggDRTFDTTQSKYR-----LPDAMRTTQNPDELWEFIADSL-----KAFIDEQFPQGIS 148
Cdd:pfam00370 3 LGIDCGTTSTKAILF----NEQGKIIAVAQLenpqiTPHPGWAEQDPDEIWQAVAQCIaktlsQLGISLKQIKGIG 74
|
|
| |
