|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02362 |
PLN02362 |
hexokinase |
1-498 |
0e+00 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 920.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 1 MGKVAVAFAAVAVVAACSVAAVMVGRRMKSRRKWRTVVEILKELEDDCDTPVGRLRQVVDAMAVEMHAGLASEGGSKLKM 80
Cdd:PLN02362 1 MGKVAVGLAAAAAVAACAVAAVMVGRRVKSRRKWRRVVGVLKELEEACETPVGRLRQVVDAMAVEMHAGLASEGGSKLKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 81 LLTFVDDLPTGREKGTYYALHLGGTYFRILRVLLGDQRSYLDVQDVERHPIPSHLMNSTSEVLFNFLAFSLERFIEKEEN 160
Cdd:PLN02362 81 LLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRSSILSQDVERHPIPQHLMNSTSEVLFDFIASSLKQFVEKEEN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 161 GSD-SQGVRRELAFTFSFPVKHTSISSGVLIKWTKGFEISEMVGQDIAECLQGALNRRGLDMHVAALVNDTVGALSLGYY 239
Cdd:PLN02362 161 GSEfSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRRGLDMRVAALVNDTVGTLALGHY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 240 HDPDTVVAVVFGTGSNACYLERTDAIIKCQGLLTTSGSMVVNMEWGNFWSSHLPRTSYDIDLDAESSNANDMGFEKMISG 319
Cdd:PLN02362 241 HDPDTVAAVIIGTGTNACYLERTDAIIKCQGLLTTSGSMVVNMEWGNFWSSHLPRTSYDIDLDAESPNPNDQGFEKMISG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 320 MYLGDIVRRVILRMSEDSDIFGPISPVLSEPYVLRTNSVSAIHEDDTPELQEVARILKD-IGVSDVPLKVRKLVVKICDV 398
Cdd:PLN02362 321 MYLGDIVRRVILRMSQESDIFGPVSSRLSTPFVLRTPSVAAMHEDDSPELQEVARILKEtLGISEVPLKVRKLVVKICDV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 399 VTRRAGRLAAAGIAGILKKIGRDGSGGITSGRSRSEIQMQKRTVVAVEGGLYMNYTMFREYMEEALVEILGEEVSQYVVV 478
Cdd:PLN02362 401 VTRRAARLAAAGIVGILKKIGRDGSGGITSGRSRSDIQIMRRTVVAVEGGLYTNYTMFREYLHEALNEILGEDVAQHVIL 480
|
490 500
....*....|....*....|
gi 1789594716 479 KAMEDGSSIGSALLVASLQS 498
Cdd:PLN02362 481 KATEDGSGIGSALLAASYSS 500
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
50-495 |
0e+00 |
|
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: 733.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 50 TPVGRLRQVVDAMAVEMHAGLASEGGSKLKMLLTFVDDLPTGREKGTYYALHLGGTYFRILRVLLGDQRSYLDVQDVERH 129
Cdd:cd24020 1 TPVSRLRQVADAMVVEMEAGLASEGGSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 130 PIPSHLMNSTSEVLFNFLAFSLERFIEKEENGSDSQGVRRELAFTFSFPVKHTSISSGVLIKWTKGFEISEMVGQDIAEC 209
Cdd:cd24020 81 PIPPELMVGTSEELFDFIAGELAKFVATEGEGFHPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 210 LQGALNRRGLDMHVAALVNDTVGALSLGYYHDPDTVVAVVFGTGSNACYLERTDAIIKCQGLLTTSGSMVVNMEWGNFWS 289
Cdd:cd24020 161 LEEALERQGLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGLPRSGEMVINTEWGNFRS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 290 SHLPRTSYDIDLDAESSNANDMGFEKMISGMYLGDIVRRVILRMSEDSDIFGPISPV-LSEPYVLRTNSVSAIHEDDTPE 368
Cdd:cd24020 241 SHLPRTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSkLEIPFILRTPDMSAMHEDDSPD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 369 LQEVARILKDI-GVSDVPLKVRKLVVKICDVVTRRAGRLAAAGIAGILKKIGRDGSGGitsgrsrseiQMQKRTVVAVEG 447
Cdd:cd24020 321 LETVARILKDAlGIDDTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLGRDGGGS----------SPAQRTVVAVDG 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1789594716 448 GLYMNYTMFREYMEEALVEILGEEVSQYVVVKAMEDGSSIGSALLVAS 495
Cdd:cd24020 391 GLYEHYPKFREYMQQALVELLGDEAADSVELELSNDGSGIGAALLAAA 438
|
|
| PLN02405 |
PLN02405 |
hexokinase |
26-495 |
0e+00 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 557.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 26 RRMKSRRKWRTVVEILKELEDDCDTPVGRLRQVVDAMAVEMHAGLASEGGSKLKMLLTFVDDLPTGREKGTYYALHLGGT 105
Cdd:PLN02405 26 RRMKSSGKWARAMEILKEFEEDCATPIGKLRQVADAMTVEMHAGLASEGGSKLKMLISYVDNLPSGDEKGLFYALDLGGT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 106 YFRILRVLLGDQRSYLDVQDVERHPIPSHLMNSTSEVLFNFLAFSLERFIEKE-ENGSDSQGVRRELAFTFSFPVKHTSI 184
Cdd:PLN02405 106 NFRVLRVLLGGKDGRVVKQEFEEVSIPPHLMTGSSDALFDFIAAALAKFVATEgEDFHLPPGRQRELGFTFSFPVKQTSI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 185 SSGVLIKWTKGFEISEMVGQDIAECLQGALNRRGLDMHVAALVNDTVGALSLGYYHDPDTVVAVVFGTGSNACYLERTDA 264
Cdd:PLN02405 186 SSGTLIKWTKGFSIDDAVGQDVVGELTKAMERVGLDMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 265 IIKCQGLLTTSGSMVVNMEWGNFWSSHLPRTSYDIDLDAESSNANDMGFEKMISGMYLGDIVRRVILRMSEDSDIFGPIS 344
Cdd:PLN02405 266 IPKWHGLLPKSGEMVINMEWGNFRSSHLPLTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 345 PV-LSEPYVLRTNSVSAIHEDDTPELQEVARILKDI-GVSDVPLKVRKLVVKICDVVTRRAGRLAAAGIAGILKKIGRDg 422
Cdd:PLN02405 346 PPkLKIPFILRTPDMSAMHHDTSPDLKVVGSKLKDIlEIPNTSLKMRKVVVELCNIVATRGARLSAAGIYGILKKLGRD- 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1789594716 423 sggitsgrSRSEIQMQKrTVVAVEGGLYMNYTMFREYMEEALVEILGEEVSQYVVVKAMEDGSSIGSALLVAS 495
Cdd:PLN02405 425 --------TVKDGEKQK-SVIAMDGGLFEHYTEFSKCMESTLKELLGEEVSESIEVEHSNDGSGIGAALLAAS 488
|
|
| PLN02914 |
PLN02914 |
hexokinase |
27-495 |
1.40e-172 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 495.17 E-value: 1.40e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 27 RMKSRRKWRTVVEILKELEDDCDTPVGRLRQVVDAMAVEMHAGLASEGGSKLKMLLTFVDDLPTGREKGTYYALHLGGTY 106
Cdd:PLN02914 27 RMAVRSNAVSVAPILTKLQKDCATPLPVLRHVADAMAADMRAGLAVDGGGDLKMILSYVDSLPSGNEKGLFYALDLGGTN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 107 FRILRVLLGDQRSYLDVQDVERHPIPSHLMNSTSEVLFNFLAFSLERFIEKEENGSD-SQGVRRELAFTFSFPVKHTSIS 185
Cdd:PLN02914 107 FRVLRVQLGGKDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFVAKEGGKFHlPEGRKREIGFTFSFPVKQTSID 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 186 SGVLIKWTKGFEISEMVGQDIAECLQGALNRRGLDMHVAALVNDTVGALSLGYYHDPDTVVAVVFGTGSNACYLERTDAI 265
Cdd:PLN02914 187 SGILMKWTKGFAVSGTAGKDVVACLNEAMERQGLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 266 IKCQGLLTTSGSMVVNMEWGNFwSSHLPRTSYDIDLDAESSNANDMGFEKMISGMYLGDIVRRVILRMSEDSDIFGPISP 345
Cdd:PLN02914 267 PKLQGQKSSSGRTIINTEWGAF-SDGLPLTEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVP 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 346 V-LSEPYVLRTNSVSAIHEDDTPELQEVARILKDIGVSDVPLKVRKLVVKICDVVTRRAGRLAAAGIAGILKKIGRDgSG 424
Cdd:PLN02914 346 EkLSTPFALRTPHLCAMQQDNSDDLQAVGSILYDVLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEED-SK 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1789594716 425 GITSGrsrseiqmqKRTVVAVEGGLYMNYTMFREYMEEALVEILGEEVSQYVVVKAMEDGSSIGSALLVAS 495
Cdd:PLN02914 425 GMIFG---------KRTVVAMDGGLYEKYPQYRRYMQDAVTELLGLELSKNIAIEHTKDGSGIGAALLAAT 486
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
54-492 |
5.89e-149 |
|
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: 432.44 E-value: 5.89e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 54 RLRQVVDAMAVEMHAGLASEGGSkLKMLLTFVDDLPTGREKGTYYALHLGGTYFRILRV-LLGDQRSYLDVQdvERHPIP 132
Cdd:cd24018 3 KLEEIVKHFLSEMEKGLEGDGGS-LPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVtLDGNGGIFIIVQ--RKYKIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 133 SHLMNSTSEVLFNFLAFSLERFIEkEENGSDSQGVRRELAFTFSFPVKHTSISSGVLIKWTKGFEISEMVGQDIAECLQG 212
Cdd:cd24018 80 DEAKTGTGEELFDFIAECIAEFLE-EHNLDLQSDKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 213 ALNRRGLDMHVAALVNDTVGALSLGYYHDPDTVVAVVFGTGSNACYLERTDAIIKCQ---GLLTTSGSMVVNMEWGNFWS 289
Cdd:cd24018 159 ALDRRGVNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTspsGSVTKSDEMIINTEWGAFDN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 290 SH--LPRTSYDIDLDAESSNANDMGFEKMISGMYLGDIVRRVILRMSEDSDIF-GPISPVLSEPYVLRTNSVSAIHEDDT 366
Cdd:cd24018 239 ERevLPLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFsGKSSELLNEPYSLDTAFLSRIEADTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 367 PELQEVARILKDIGVSDVP-LKVRKLVVKICDVVTRRAGRLAAAGIAGILKKIGRDgsggitsgrsrseiqMQKRTVVAV 445
Cdd:cd24018 319 PDLDAVRDILKELLAIDNTtLEDRKLIKRICELVSTRAARLSAAAIAAILLKRGSL---------------LPEPVTVGI 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1789594716 446 EGGLYMNYTMFREYMEEALVEILGEEVSQYVVVKAMEDGSSIGSALL 492
Cdd:cd24018 384 DGSVYEKYPGFKDRLSEALRELFGPEVKANISLVLAKDGSGLGAAII 430
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
55-494 |
2.11e-132 |
|
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: 390.36 E-value: 2.11e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 55 LRQVVDAMAVEMHAGLASEG--GSKLKMLLTFVDDLPTGREKGTYYALHLGGTYFRILRVLLGDQRSYldVQDVERHPIP 132
Cdd:cd24019 7 LEEIMDRLLKEMEKGLSKDThpTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGGSQV--KMESEIYAIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 133 SHLMNSTSEVLFNFLAFSLERFIEKeeNGSDSQGVrrELAFTFSFPVKHTSISSGVLIKWTKGFEISEMVGQDIAECLQG 212
Cdd:cd24019 85 EEIMTGTGEQLFDYIAECLAEFLEK--NGLKDKKL--PLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLLQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 213 ALNRRGL-DMHVAALVNDTVGALSLGYYHDPDTVVAVVFGTGSNACYLERTDAIIKCQGLLTTSGSMVVNMEWGNFWSSH 291
Cdd:cd24019 161 AIKRRGDiKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKWDGDEGDPGQVIINTEWGAFGDNG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 292 ---LPRTSYDIDLDAESSNANDMGFEKMISGMYLGDIVRRVILRMSEDSDIF-GPISPVLSEPYVLRTNSVSAIHEDDTP 367
Cdd:cd24019 241 vldFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFrGQLSEELLTRGSFETKYVSEIESDNEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 368 ELQEVARILKDIGVSDVPLKVRKLVVKICDVVTRRAGRLAAAGIAGILKKIGRdgsggitsgrsrseiqmqKRTVVAVEG 447
Cdd:cd24019 321 DFSNTREILKELGLEDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNR------------------KEVTVGVDG 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1789594716 448 GLYMNYTMFREYMEEALVEILGEEVSqyvvVKAM--EDGSSIGSALLVA 494
Cdd:cd24019 383 SLYKYHPKFHKRMHETLKELVPPGCK----FKLMlsEDGSGKGAALVAA 427
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
29-495 |
1.12e-126 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 378.06 E-value: 1.12e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 29 KSRRKWRTVVEILKELEDDCDTPVGRLRQVVDAMAVEMHAGLASEGGSKLKMLLTFVDDLPTGREKGTYYALHLGGTYFR 108
Cdd:PLN02596 30 RKERQWKHTQRILRKFARECATPVSKLWEVADALVSDMTASLTAEETTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 109 ILRVLLGDQRSylDVQDVERH--PIPSHLMNSTSEVLFNFLAFSLERFIeKEENGSDSQGVRRE--LAFTFSFPVKHTSI 184
Cdd:PLN02596 110 LLRARLGGKNE--PISDLYREeiSIPSNVLNGTSQELFDYIALELAKFV-AEHPGDEADTPERVkkLGFTVSYPVDQAAA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 185 SSGVLIKWtKGFEISEMVGQDIAECLQGALNRRGLDMHVAALVNDTVGALSLGYYHDPDTVVAVVFGTGSNACYLERTDA 264
Cdd:PLN02596 187 SSGSAIKW-KSFSADDTVGKALVNDINRALEKHGLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 265 IIKCQGLLTTSGSMVVNMEWGNFWSSHLPRTSYDIDLDAESSNANDMGFEKMISGMYLGDIVRRVILRMSEDSDIFGP-I 343
Cdd:PLN02596 266 IPKWQSPSPESQEIVISTEWGNFNSCHLPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDtL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 344 SPVLSEPYVLRTNSVSAIHEDDTPELQEVARILKDI-GVSDVPLKVRKLVVKICDVVTRRAGRLAAAGIAGILKKIGRDG 422
Cdd:PLN02596 346 PPKLTTPYLLRSPDMAAMHQDTSEDHEVVNEKLKEIfGITDSTPMAREVVAEVCDIVAERGARLAGAGIVGIIKKLGRIE 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1789594716 423 SggitsgrsrseiqmqKRTVVAVEGGLYMNYTMFREYMEEALVEILGEEVSQYVVVKAMEDGSSIGSALLVAS 495
Cdd:PLN02596 426 N---------------KKSVVTVEGGLYEHYRVFRNYLHSSVWEMLGSELSDNVVIEHSHGGSGAGALFLAAC 483
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
54-493 |
5.64e-115 |
|
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: 343.10 E-value: 5.64e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 54 RLRQVVDAMAVEMHAGLASEGGSkLKMLLTFVDDLPTGREKGTYYALHLGGTYFRILRVLLGDQRSYldVQDVERHPIPS 133
Cdd:cd24000 3 DLKEITDAFLEELEKGLAGEPSS-LKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGKGIE--VTISKKYEIPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 134 HLMNSTSEVLFNFLAFSLERFIEKEENGSDSQgvrreLAFTFSFPVKHTSISSGVLIKWTKGFEISEMVGQDIAECLQGA 213
Cdd:cd24000 80 EIKTASAEEFFDFIADCIAEFLKENGLKKPLP-----LGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 214 LNRRGLDMHVAALVNDTVGALSLGYYHDPDTVVAVVFGTGSNACYLERTDAIikcqglLTTSGSMVVNMEWGNFWSSHLP 293
Cdd:cd24000 155 LKKRGLPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNI------LLGDGGMIINTEWGNFGKNSLP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 294 RTSYDIDLDAESSNANDMGFEKMISGMYLGDIVRRVILRMsedsdifgpispvlsepyvlrtnsvsaiheddtpelqeva 373
Cdd:cd24000 229 RTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDL---------------------------------------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 374 rilkdigvsdvplkVRKLVVKICDVVTRRAGRLAAAGIAGILKKIGRDGSGGITsgrsrseiqmqkrtvVAVEGGLYMNY 453
Cdd:cd24000 269 --------------ADEILRKICELVAERSARLAAAAIAALLRKTGDSPEKKIT---------------IAVDGSLFEKY 319
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1789594716 454 TMFREYMEEALVEILGEEvsQYVVVKAMEDGSSIGSALLV 493
Cdd:cd24000 320 PGYRERLEEYLKELLGRG--IRIELVLVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
54-494 |
8.69e-114 |
|
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: 342.82 E-value: 8.69e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 54 RLRQVVDAMAVEMHAGLASEGGSkLKMLLTFVDDLPTGREKGTYYALHLGGTYFRILRVLLGDQRSYLDVQDVERhpIPS 133
Cdd:cd24087 3 RLRKITDHFISELEKGLSKKGGN-IPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNGKFDITQSKYR--LPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 134 HLMNSTSEVLFNFLAFSLERFIEKEENGSDSQGVrrELAFTFSFPVKHTSISSGVLIKWTKGFEISEMVGQDIAECLQGA 213
Cdd:cd24087 80 ELKTGTGEELWDFIADCLKKFVEEHFPGGKSEPL--PLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 214 LNRRGLDMHVAALVNDTVGALSLGYYHDPDTVVAVVFGTGSNACYLERTDAIIKCQGL-LTTSGSMVVNMEWGNFWSSH- 291
Cdd:cd24087 158 LKKRNVPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEHDdIPPDSPMAINCEYGAFDNEHl 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 292 -LPRTSYDIDLDAESSNANDMGFEKMISGMYLGDIVRRVILRMSEDSDIF-GPISPVLSEPYVLRTNSVSAIHEDDTPEL 369
Cdd:cd24087 238 vLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFkGQDTSKLEKPYVMDTSFLSRIEEDPFENL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 370 QEVARILKDIGVSDVPLKVRKLVVKICDVVTRRAGRLAAAGIAGILKKIGRDGSGgitsgrsrseiqmqkrtvVAVEGGL 449
Cdd:cd24087 318 EDTDDLFQHFFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKKRGYKTCH------------------VAADGSV 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1789594716 450 YMNYTMFREYMEEALVEILGEEVSQY-VVVKAMEDGSSIGSALLVA 494
Cdd:cd24087 380 YNKYPGFKERAAQALKDIFGWDGEDDpIKTVPAEDGSGVGAAIIAA 425
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
65-491 |
7.02e-113 |
|
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: 340.91 E-value: 7.02e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 65 EMHAGLASEGGSkLKMLLTFVDDLPTGREKGTYYALHLGGTYFRILRV-LLGDQRSYLDVqdvERHPIPSHLMNS-TSEV 142
Cdd:cd24088 14 QMEKGLAKHGKG-MAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVeLHGDGTFSLRQ---EKSKIPDELKTGvTAKD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 143 LFNFLAFSLERFIEK---EENGSDSQGVRRELAFTFSFPVKHTSISSGVLIKWTKGFEISEMVGQDIAECLQGALNRRGL 219
Cdd:cd24088 90 LFDYLAKSVEAFLTKhhgDSFAAGKDDDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVVKLLQDELDRQGI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 220 DMHVAALVNDTVGALSLGYYHDPD---TVVAVVFGTGSNACYLERTDAIIKcqgLLTTS------GSMVVNMEWGNFWS- 289
Cdd:cd24088 170 PVKVVALVNDTVGTLLARSYTSPEisgAVLGAIFGTGTNGAYLEDLEKIKK---LDDSSrvgkgkTHMVINTEWGSFDNe 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 290 -SHLPRTSYDIDLDAESSNANDMGFEKMISGMYLGDIVRRVILRMSEDSDIFGPISPVLSE----PYVLRTNSVSAIHED 364
Cdd:cd24088 247 lKVLPTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFLIQYNDKSPSalntPYGLDTAVLSAIEID 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 365 DTPELQEVARIL-KDIGVSDVPLKVRKLVVKICDVVTRRAGRLAAAGIAGILkkigrdgsggITSGRSRSEiqmQKRTV- 442
Cdd:cd24088 327 SEAELRATRKVLlDDLGLPAPSLEDAEAVRKISRAIGRRAARLSAVAIAAIL----------IKTGALNKS---YDGEIn 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1789594716 443 VAVEGGLYMNYTMFREYMEEALVEIL-GEEVSQYVVVKAMEDGSSIGSAL 491
Cdd:cd24088 394 IGVDGSVIEFYPGFESMLREALRLLLiGAEGEKRIKIGIAKDGSGVGAAL 443
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
55-494 |
1.26e-98 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 305.06 E-value: 1.26e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 55 LRQVVDAMAVEMHAGLASEGG---------SKLKMLLTFVDDLPTGREKGTYYALHLGGTYFRILRV-LLGDQRSYLDVQ 124
Cdd:PTZ00107 25 LKELVDYFLYELVEGLEAHRRhrnlwipneCSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFRAVRVsLRGGGKMERTQS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 125 DVE----RHPIPSHLMN--STSEVLFNFLAFSLERFIEkeENGSDSQ-GVRRELAFTFSFPVKHTSISSGVLIKWTKGFE 197
Cdd:PTZ00107 105 KFSlpksALLGEKGLLDkkATATDLFDHIAKSIKKMME--ENGDPEDlNKPVPVGFTFSFPCTQLSVNNAILIDWTKGFE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 198 ISEMV-----GQDIAECLQGALNRRGLDMHVAALVNDTVGALSLGYYHD----PDTVVAVVFGTGSNACYLERTDAIIKC 268
Cdd:PTZ00107 183 TGRATndpveGKDVGELLNDAFKRNNVPANVVAVLNDTVGTLISCAYQKpkntPPCQVGVIIGTGSNACYFEPEVSAYGY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 269 QGllttsgsMVVNMEWGNFwSSHLPRTSYDIDLDAESSNANDMGFEKMISGMYLGDIVRRVILRMSEDSdifgpISPVLS 348
Cdd:PTZ00107 263 AG-------TPINMECGNF-DSKLPITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLLQLK-----APPKMW 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 349 EPYVLRTNSVSAIHEDDTPELQEVARILKDIGVSDVPLKVRKLVVKICDVVTRRAGRLAAAGIAGILKKIGRdgsggits 428
Cdd:PTZ00107 330 QSGSFESEDASMILNDQSPDLQFSRQVIKEAWDVDLTDEDLYTIRKICELVRGRAAQLAAAFIAAPAKKTRT-------- 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1789594716 429 grsrseiqMQKRTVVAVEGGLYMNYTMFREYMEEALVEILGEEVSQYVVVKAmEDGSSIGSALLVA 494
Cdd:PTZ00107 402 --------VQGKATVAIDGSVYVKNPWFRRLLQEYINSILGPDAGNVVFYLA-DDGSGKGAAIIAA 458
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
55-491 |
6.70e-96 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 296.87 E-value: 6.70e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 55 LRQVVDAMAVEMHAGLASEGGSkLKMLLTFVDdLPTG-REKGTYYALHLGGTYFRILRVLLGDQRSYLdVQDVERHPIPS 133
Cdd:COG5026 22 LEEIAAKFQEEMEKGLEGKKSS-LKMLPSYLG-LPTGvKETGPVIALDAGGTNFRVALVRFDGEGTFE-IENFKSFPLPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 134 HLMNSTSEVLFNFLAFSLERFIEKeengsdsqgvRRELAFTFSFPVKHTSISSGVLIKWTKGFEISEMVGQDIAECLQGA 213
Cdd:COG5026 99 TSSEITAEEFFDFIADYIEPLLDE----------SYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNIGELLEAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 214 LNRRGLDmHV--AALVNDTVGALSLGYYHDPDTV----VAVVFGTGSNACYLERTDAIIKcqgLLTTSGSMVVNMEWGNF 287
Cdd:COG5026 169 LARKGLD-NVkpVAILNDTVATLLAGAYADPDDGysgyIGSILGTGHNTCYLEPNAPIGK---LPAYEGPMIINMESGNF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 288 wsSHLPRTSYDIDLDAESSNANDMGFEKMISGMYLGDIVRRVILRMSEDSDIFGPISPVLSEPYVLRTNSVSAIHEDDTP 367
Cdd:COG5026 245 --NKLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEGLFSPGFSEVFETPYSLTTVDMSRFLADPSD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 368 ELQEVARILKDIGVSDvplkvRKLVVKICDVVTRRAGRLAAAGIAGILKKIGRDGSggitsgrsrseiqMQKRTVVAVEG 447
Cdd:COG5026 323 EKEILSQCLEAGSEED-----REILREIADAIVERAARLVAATLAGILLHLGPGKT-------------PLKPHCIAIDG 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1789594716 448 GLYmnYTM--FREYMEEALVEILGEEVSQYVVVKAMEDGSSIGSAL 491
Cdd:COG5026 385 STY--EKMpgLAEKIEYALQEYLLGEKGRYVEFVLVENASLLGAAI 428
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
245-495 |
1.55e-95 |
|
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: 289.01 E-value: 1.55e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 245 VVAVVFGTGSNACYLERTDAIIKCQGLLTTSGSMVVNMEWGNFWSSH---LPRTSYDIDLDAESSNANDMGFEKMISGMY 321
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKLPKSGEMIINTEWGAFGDNGllpLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 322 LGDIVRRVILRMSEDSDIFGPISPVLSEPYVLRTNSVSAIHEDDTPELQEVARILKDI-GVSDVPLKVRKLVVKICDVVT 400
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKGQSEKLKTPYSLDTSFLSAIESDPSEDLETTREILEELlGIETVTEEDRKIVRRICEAVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 401 RRAGRLAAAGIAGILKKIGRDgsggitsgrsrseiqmqKRTVVAVEGGLYMNYTMFREYMEEALVEILGeeVSQYVVVKA 480
Cdd:pfam03727 161 TRAARLVAAGIAAILKKIGRD-----------------KKVTVGVDGSVYEKYPGFRERLQEALRELLG--PGDKVVLVL 221
|
250
....*....|....*
gi 1789594716 481 MEDGSSIGSALLVAS 495
Cdd:pfam03727 222 AEDGSGVGAALIAAV 236
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
40-239 |
6.45e-87 |
|
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: 265.14 E-value: 6.45e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 40 ILKELEDDCDTPVGRLRQVVDAMAVEMHAGLASEGGSKLKMLLTFVDDLPTGREKGTYYALHLGGTYFRILRVLLGDQRS 119
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGGDGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 120 YLDVQdvERHPIPSHLMNSTSEVLFNFLAFSLERFIeKEENGSDSQGVRRELAFTFSFPVKHTSISSGVLIKWTKGFEIS 199
Cdd:pfam00349 81 FEITQ--EKYKIPEELMTGTGEELFDFIADCIAEFL-KEHGLEDFEEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDIP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1789594716 200 EMVGQDIAECLQGALNRRGLDMHVAALVNDTVGALSLGYY 239
Cdd:pfam00349 158 GVVGKDVVQLLQEALERRGLPVKVVALVNDTVGTLMAGAY 197
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
54-494 |
9.85e-84 |
|
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: 265.56 E-value: 9.85e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 54 RLRQVVDAMAVEMHAGLASE--GGSKLKMLLTFVDDLPTGREKGTYYALHLGGTYFRIL--RVLLGDQRSyldvqdVERH 129
Cdd:cd24091 6 QLLEVKARMRAEMERGLRKEthASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLlvKVRSGKWRG------VEMH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 130 ----PIPSHLMNSTSEVLFNFLAFSLERFIEKEengsDSQGVRRELAFTFSFPVKHTSISSGVLIKWTKGFEISEMVGQD 205
Cdd:cd24091 80 nkiyAIPQEIMQGTGEELFDHIVQCIADFLEYM----GLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 206 IAECLQGALNRRG-LDMHVAALVNDTVGALSLGYYHDPDTVVAVVFGTGSNACYLERTDAIIKCQGlltTSGSMVVNMEW 284
Cdd:cd24091 156 VVTLLREAIKRREeFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEG---EEGRMCINMEW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 285 GNF---WSSHLPRTSYDIDLDAESSNANDMGFEKMISGMYLGDIVRRVILRMSEDSDIF-GPISPVLSEPYVLRTNSVSA 360
Cdd:cd24091 233 GAFgdnGCLDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFrGQISERLKTRGIFETKFLSQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 361 IhEDDTPELQEVARILKDIGV---SDVPLkvrkLVVKICDVVTRRAGRLAAAGIAGILKKIGRDgsggitsgRSRSEIqm 437
Cdd:cd24091 313 I-ESDRLALLQVRAILQQLGLdstCDDSI----IVKEVCGVVSRRAAQLCGAGMAAVVDKIREN--------RGLDHL-- 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1789594716 438 qkRTVVAVEGGLYMNYTMFREYMEEALveilgEEVSQYVVVKAM--EDGSSIGSALLVA 494
Cdd:cd24091 378 --NVTVGVDGTLYKLHPHFSRVMHETV-----KELAPKCDVTFLqsEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
54-494 |
3.23e-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: 261.25 E-value: 3.23e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 54 RLRQVVDAMAVEMHAGLASEGG--SKLKMLLTFVDDLPTGREKGTYYALHLGGTYFRILRVLLGDQRSYLDVQDVERHPI 131
Cdd:cd24089 6 TLLDISRRFRKEMEKGLGKDTHptATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMESQVYAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 132 PSHLMNSTSEVLFNFLAFSLERFIEKEengsDSQGVRRELAFTFSFPVKHTSISSGVLIKWTKGFEISEMVGQDIAECLQ 211
Cdd:cd24089 86 PEEIMHGSGTQLFDHVAECLADFMDKQ----KIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 212 GALNRRG-LDMHVAALVNDTVGALSLGYYHDPDTVVAVVFGTGSNACYLERTDAIIKCQGlltTSGSMVVNMEWGNF--- 287
Cdd:cd24089 162 KAIRRRGdYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEG---DEGRMCINTEWGAFgdd 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 288 WSSHLPRTSYDIDLDAESSNANDMGFEKMISGMYLGDIVRRVILRMSEDSDIF-GPISPVLSEPYVLRTNSVSAIHEDDT 366
Cdd:cd24089 239 GSLEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFgGKISPELLTRGKFETKDVSAIEKEKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 367 pELQEVARILKDIGVSdvPLKVRKLVVK-ICDVVTRRAGRLAAAGIAGILKKIGRDgsggitSGRSRSeiqmqkRTVVAV 445
Cdd:cd24089 319 -GLANAKEILTRLGLD--PSEDDCVNVQhVCTIVSFRSANLCAATLAAILTRLREN------KGLERL------RTTVGV 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1789594716 446 EGGLYMNYTMFREYMEEALVEILGEEVSQYVVvkaMEDGSSIGSALLVA 494
Cdd:cd24089 384 DGSVYKKHPQFSKRLHKAVRRLVPDCDVRFLL---SEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
54-494 |
1.96e-76 |
|
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: 246.33 E-value: 1.96e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 54 RLRQVVDAMAVEMHAGLASE--GGSKLKMLLTFVDDLPTGREKGTYYALHLGGTYFRILRVLLGDQrsylDVQDV-ERHP 130
Cdd:cd24129 6 QLAAVQAQMRKEMAKGLRGEthAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTA----GVQITsEIYS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 131 IPSHLMNSTSEVLFNFLAFSLERFIEKEengsDSQGVRRELAFTFSFPVKHTSISSGVLIKWTKGFEISEMVGQDIAECL 210
Cdd:cd24129 82 IPETVAQGTGQQLFDHIVDCIVDFQQKQ----GLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 211 QGALNRR-GLDMHVAALVNDTVGALSLGYYHDPDTVVAVVFGTGSNACYLERTDAIikcQGLLTTSGSMVVNMEWGNFWS 289
Cdd:cd24129 158 REAATRKqAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNV---AGVPGDSGRMCINMEWGAFGD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 290 SH---LPRTSYDIDLDAESSNANDMGFEKMISGMYLGDIVRRVILRMSEDSDIF-GPISPVLSEPYVLRTNSVSAIhEDD 365
Cdd:cd24129 235 NGclaMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFrGKQIQRLQTRDIFKTKFLSEI-ESD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 366 TPELQEVARILKDIGV---SDVPLkvrkLVVKICDVVTRRAGRLAAAGIAGILKKIgRDGSGgitsgrsrseiQMQKRTV 442
Cdd:cd24129 314 SLALRQVRAILEDLGLpltSDDAL----LVLEVCQTVSQRAAQLCAAGVAAVVEKM-RENRG-----------LDELAVT 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1789594716 443 VAVEGGLYMNYTMFREYMEEALVEILGEEVsqyVVVKAMEDGSSIGSALLVA 494
Cdd:cd24129 378 VGVDGTLYKLHPRFSSLVQATVRELAPRCV---VTFLQSEDGSGKGAALVTA 426
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
55-494 |
2.91e-75 |
|
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: 243.67 E-value: 2.91e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 55 LRQVVDAMAVEMHAGLASE--GGSKLKMLLTFVDDLPTGREKGTYYALHLGGTYFRILRVLL--GDQRSyldvqdVERH- 129
Cdd:cd24127 7 LLEVKKRMRAEMELGLRKQthNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIrsGKKRT------VEMHn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 130 ---PIPSHLMNSTSEVLFNFLAFSLERFIEKeengSDSQGVRRELAFTFSFPVKHTSISSGVLIKWTKGFEISEMVGQDI 206
Cdd:cd24127 81 kiyAIPIEIMQGTGEELFDHIVSCISDFLDY----MGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 207 AECLQGALNRRG-LDMHVAALVNDTVGALSLGYYHDPDTVVAVVFGTGSNACYLERTDAIIKCQGlltTSGSMVVNMEWG 285
Cdd:cd24127 157 VTLLRDAIKRREeFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEG---DQGQMCINMEWG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 286 NFWSSHL---PRTSYDIDLDAESSNANDMGFEKMISGMYLGDIVRRVILRMSEDSDIF-GPISPVLSEPYVLRTNSVSAI 361
Cdd:cd24127 234 AFGDNGClddIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFrGQISETLKTRGIFETKFLSQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 362 hEDDTPELQEVARILKDIGVsDVPLKVRKLVVKICDVVTRRAGRLAAAGIAGILKKIGRDgsggitSGRSRSEIqmqkrt 441
Cdd:cd24127 314 -ESDRLALLQVRAILQQLGL-NSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIREN------RGLDHLNV------ 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1789594716 442 VVAVEGGLYMNYTMFREYMEEALVEILGEEVSQYVVvkaMEDGSSIGSALLVA 494
Cdd:cd24127 380 TVGVDGTLYKLHPHFSRIMHQTVKELSPKCNVSFLL---SEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
54-494 |
7.84e-75 |
|
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: 242.53 E-value: 7.84e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 54 RLRQVVDAMAVEMHAGLASE--GGSKLKMLLTFVDDLPTGREKGTYYALHLGGTYFRILRVLLGDQRSYLDVQDvERHPI 131
Cdd:cd24130 6 QLQEVKQKMRTELEYGLKKEthPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGRRSVRMYN-KIFAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 132 PSHLMNSTSEVLFNFLAFSLERFIEKeengSDSQGVRRELAFTFSFPVKHTSISSGVLIKWTKGFEISEMVGQDIAECLQ 211
Cdd:cd24130 85 PLEIMQGTGEELFDHIVQCIADFLDY----MGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDMLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 212 GALNRRG-LDMHVAALVNDTVGALSLGYYHDPDTVVAVVFGTGSNACYLERTDAIIKCQGlltTSGSMVVNMEWGNFWSS 290
Cdd:cd24130 161 EAIKRRNeFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEG---DEGRMCINTEWGGFGDN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 291 HLP---RTSYDIDLDAESSNANDMGFEKMISGMYLGDIVRRVILRMSEDSDIF-GPISPVLSEPYVLRTNSVSAIhEDDT 366
Cdd:cd24130 238 GCIddiRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFrGQISERLRTRGIFETKFLSQI-ESDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 367 PELQEVARILKDIGVsDVPLKVRKLVVKICDVVTRRAGRLAAAGIAGILKKIGRDgsggitSGRSRSEIqmqkrtVVAVE 446
Cdd:cd24130 317 LALLQVRRILQQLGL-DSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIREN------QGLDRLDI------TVGVD 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1789594716 447 GGLYMNYTMFREYMEEALVEILGEEVSQYVVvkaMEDGSSIGSALLVA 494
Cdd:cd24130 384 GTLYKLHPHFSRILQETVKELAPQCDVTFML---SEDGSGKGAALITA 428
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
55-494 |
7.57e-74 |
|
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: 239.75 E-value: 7.57e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 55 LRQVVDAMAVEMHAGLASEGGSK--LKMLLTFVDDLPTGREKGTYYALHLGGTYFRILRVLLG-DQRSYLDVQDvERHPI 131
Cdd:cd24126 7 LLDIMTRFRAEMEKGLAKDTNPTaaVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSeDGKQKVQMES-QFYPT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 132 PSHLMNSTSEVLFNFLAFSLERFIEKEengsDSQGVRRELAFTFSFPVKHTSISSGVLIKWTKGFEISEMVGQDIAECLQ 211
Cdd:cd24126 86 PEEIIHGTGTELFDYVAECLADFMKKK----GIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 212 GALNRRG-LDMHVAALVNDTVGALSLGYYHDPDTVVAVVFGTGSNACYLERTDAIIKCQGlltTSGSMVVNMEWGNFWSS 290
Cdd:cd24126 162 KAIRKHKdVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEG---DEGRMCINTEWGAFGDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 291 HLP---RTSYDIDLDAESSNANDMGFEKMISGMYLGDIVRRVILRMSEDSDIF-GPISPVLSEPYVLRTNSVSAIhEDDT 366
Cdd:cd24126 239 GSLediRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFkGQISPALRTKGKIETKHVAAI-EKYK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 367 PELQEVARILKDIGVSdvPLKVRKLVVK-ICDVVTRRAGRLAAAGIAGILKKIgrdgsggitsgrSRSEIQMQKRTVVAV 445
Cdd:cd24126 318 EGLYNTREILSDLGLE--PSEEDCIAVQhVCTIVSFRSANLCAAALAAILTRL------------RENKKLERLRTTVGM 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1789594716 446 EGGLYMNYTMFREYMEEALVEILGEEVSQYVVvkaMEDGSSIGSALLVA 494
Cdd:cd24126 384 DGTVYKTHPQYAKRLHKVVRRLVPSCDVRFLL---SESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
54-494 |
7.11e-73 |
|
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: 237.49 E-value: 7.11e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 54 RLRQVVDAMAVEMHAGLASE--GGSKLKMLLTFVDDLPTGREKGTYYALHLGGTYFRIL--RVLLGDQRSyldvqdVERH 129
Cdd:cd24128 6 QLLEVKRRMKVEMERGLSKEthASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLlvRVRNGKWRG------VEMH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 130 ----PIPSHLMNSTSEVLFNFLAFSLERFIEKeengSDSQGVRRELAFTFSFPVKHTSISSGVLIKWTKGFEISEMVGQD 205
Cdd:cd24128 80 nkiyAIPQEVMHGTGEELFDHIVHCIADFLEY----MGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 206 IAECLQGALNRR-GLDMHVAALVNDTVGALSLGYYHDPDTVVAVVFGTGSNACYLERTDAIIKCQGlltTSGSMVVNMEW 284
Cdd:cd24128 156 VVTLLKEAIHRReEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEG---EEGRMCVNMEW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 285 GNFWSSHLP---RTSYDIDLDAESSNANDMGFEKMISGMYLGDIVRRVILRMSEDSDIF-GPISPVLSEPYVLRTNSVSA 360
Cdd:cd24128 233 GAFGDNGCLddfRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFrGRISERLKTRGIFETKFLSQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 361 IhEDDTPELQEVARILKDIGVSDVpLKVRKLVVKICDVVTRRAGRLAAAGIAGILKKIgrdgsggitsgRSRSEIQMQKR 440
Cdd:cd24128 313 I-ESDRLALLQVRAILQHLGLEST-CDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKI-----------RENRGLDALKV 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1789594716 441 TvVAVEGGLYMNYTMFREYMEEALVEILGE-EVSqyvVVKAmEDGSSIGSALLVA 494
Cdd:cd24128 380 T-VGVDGTLYKLHPHFAKVMHETVKDLAPKcDVS---FLQS-EDGSGKGAALITA 429
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
55-494 |
9.34e-70 |
|
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: 230.27 E-value: 9.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 55 LRQVVDAMAVEMHAGLASEGG--SKLKMLLTFVDDLPTGREKGTYYALHLGGTYFRILRVLLGDQRSYLDVQDVERHPIP 132
Cdd:cd24124 35 LIDIMTRFRKEMKNGLSRDFNptATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 133 SHLMNSTSEVLFNFLAFSLERFIEKEEngsdSQGVRRELAFTFSFPVKHTSISSGVLIKWTKGFEISEMVGQDIAECLQG 212
Cdd:cd24124 115 ENIVHGSGSQLFDHVAECLGDFMEKRK----IKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLNK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 213 ALNRRG-LDMHVAALVNDTVGALSLGYYHDPDTVVAVVFGTGSNACYLERTDAIIKCQGlltTSGSMVVNMEWGNF---W 288
Cdd:cd24124 191 AIKKRGdYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEG---DEGRMCINTEWGAFgddG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 289 SSHLPRTSYDIDLDAESSNANDMGFEKMISGMYLGDIVRRVILRMSEDSDIF-GPISPVLSEPYVLRTNSVSAIhEDDTP 367
Cdd:cd24124 268 SLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFeGRITPELLTRGKFNTSDVSAI-EKNKE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 368 ELQEVARILKDIGVSdvPLKVRKLVVK-ICDVVTRRAGRLAAAGIAGILKKIgRDGSGgitSGRsrseiqmqKRTVVAVE 446
Cdd:cd24124 347 GLHNAKEILTRLGVE--PSDDDCVSVQhVCTIVSFRSANLVAATLGAILNRL-RDNKG---TPR--------LRTTVGVD 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1789594716 447 GGLYMNYTMFREYMEEALVEILGEEVSQYVVvkaMEDGSSIGSALLVA 494
Cdd:cd24124 413 GSLYKTHPQYSRRFHKTLRRLVPDSDVRFLL---SESGSGKGAAMVTA 457
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
55-494 |
1.42e-69 |
|
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: 228.63 E-value: 1.42e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 55 LRQVVDAMAVEMHAGLASEGG--SKLKMLLTFVDDLPTGREKGTYYALHLGGTYFRILRVLLGDQRSYLDVQDVERHPIP 132
Cdd:cd24125 7 LLEISKRFRKEMEKGLGATTHptAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMENQIYAIP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 133 SHLMNSTSEVLFNFLAFSLERFIEKeengSDSQGVRRELAFTFSFPVKHTSISSGVLIKWTKGFEISEMVGQDIAECLQG 212
Cdd:cd24125 87 EDIMRGSGTQLFDHIAECLANFMDK----LQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALLRK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 213 ALNRRG-LDMHVAALVNDTVGALSLGYYHDPDTVVAVVFGTGSNACYLERTDAIIKCQGlltTSGSMVVNMEWGNFWSSH 291
Cdd:cd24125 163 AIQKRGdFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEG---DEGRMCINMEWGAFGDDG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 292 L---PRTSYDIDLDAESSNANDMGFEKMISGMYLGDIVRRVILRMSEDSDIF-GPISPVLSEPYVLRTNSVSAIhEDDTP 367
Cdd:cd24125 240 SlddIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFgGKLSPELLNTGHFETKDVSDI-EGEKD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 368 ELQEVARILKDIGVSDVPLKVRKlVVKICDVVTRRAGRLAAAGIAGILKKIgRDGSGgitsgrsrseiQMQKRTVVAVEG 447
Cdd:cd24125 319 GIRKAREVLMRLGLDPTQEDCVA-THRICQIVSTRSASLCAATLAAVLQRI-KENKG-----------EERLRSTIGVDG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1789594716 448 GLYMNYTMFREYMEEALVEILGEEVSQYVvvkAMEDGSSIGSALLVA 494
Cdd:cd24125 386 SVYKKHPHFARRLHKTVRRLVPGCDVRFL---RSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
55-494 |
9.63e-64 |
|
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: 213.59 E-value: 9.63e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 55 LRQVVDAMAVEMHAGLASEG--GSKLKMLLTFVDDLPTGREKGTYYALHLGGTYFRILRVLLG-DQRSYLDVQDVER-HP 130
Cdd:cd24092 16 LKKVMRRMQKEMDRGLRLETheEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGeGEEGQWSVKTKHQmYS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 131 IPSHLMNSTSEVLFNFLAFSLERFIEKEengsDSQGVRRELAFTFSFPVKHTSISSGVLIKWTKGFEISEMVGQDIAECL 210
Cdd:cd24092 96 IPEDAMTGTAEMLFDYISECISDFLDKH----QMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVGLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 211 QGALNRRG-LDMHVAALVNDTVGALSLGYYHDPDTVVAVVFGTGSNACYLERTDAIIKCQGlltTSGSMVVNMEWGNFW- 288
Cdd:cd24092 172 RDAIKRRGdFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEG---DEGRMCVNTEWGAFGd 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 289 SSHLP--RTSYDIDLDAESSNANDMGFEKMISGMYLGDIVRRVILRMSEDSDIF-GPISPVLSEPYVLRTNSVSAIhEDD 365
Cdd:cd24092 249 SGELDefLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFhGEASEQLRTRGAFETRFVSQV-ESD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 366 TPELQEVARILKDIGVSDVPLKVrKLVVKICDVVTRRAGRLAAAGIAGILKKIgRDgsggitsgrSRSEIQMqkRTVVAV 445
Cdd:cd24092 328 TGDRKQIYNILSTLGLRPSTTDC-DIVRRACESVSTRAAHMCSAGLAGVINRM-RE---------SRSEDVM--RITVGV 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1789594716 446 EGGLYMNYTMFREYMeEALVEILGEEVSqyVVVKAMEDGSSIGSALLVA 494
Cdd:cd24092 395 DGSVYKLHPSFKERF-HASVRRLTPSCE--ITFIESEEGSGRGAALVSA 440
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
51-494 |
1.58e-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: 204.77 E-value: 1.58e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 51 PVGRLRQVVDAMAVEMHAGLASEGG--SKLKMLLTFVDDLPTGREKGTYYALHLG--GTYFRILRV-LLGDQRSYLDVQD 125
Cdd:cd24090 3 TRAQLQQIQASLLGSMEQALRGQASpaPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVtLTGIEGHRVEPRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 126 VErHPIPSHLMNSTSEVLFNFLAFSLERFIEKEEngSDSQGVrrELAFTFSFPVKHTSISSGVLIKWTKGFEISEMVGQD 205
Cdd:cd24090 83 QE-FVIPQEVMLGAGQQLFDFAAHCLSEFLDGQP--VPKQGL--QLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 206 IAECLQGALNRRGL-DMHVAALVNDTVGALSLGYYHDPDTVVAVVFGTGSNACYLERTDAIikcQGLLTTSGSMVVNMEW 284
Cdd:cd24090 158 VVQLLRDAIQRQGAyNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHV---AVLDEDRGRVCVSVEW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 285 GNF---WSSHLPRTSYDIDLDAESSNANDMGFEKMISGMYLGDIVRRVILRMSEDSDIF-GPISPVLSEPYVLRTNSVSA 360
Cdd:cd24090 235 GSFsddGALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFgGSTSPALRSQGSILLEHVAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789594716 361 IhEDDTPELQEVARILKDIGVSDVPLKVrKLVVKICDVVTRRAGRLAAAGIAGILKKIgrdgsggitsGRSRSEIQMQkr 440
Cdd:cd24090 315 M-EDPSAGAARVRAILQDLGLSPSASDV-ELVQHVCRAVCTRAAQLCAAALAAVLSHL----------QHSREQQTLQ-- 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1789594716 441 TVVAVEGGLYMNYTMFREYMEEAlVEILGEEVSQYVVVKAmeDGSSIGSALLVA 494
Cdd:cd24090 381 VAVATGGRVCERHPRFCSILQGT-VMLLAPECDVSFIPSV--DGGGRGVAMVTA 431
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
207-271 |
3.82e-03 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 39.48 E-value: 3.82e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1789594716 207 AECLQGALNRRGLDMHVAaLVNDTVGALSLGYYHDPDTVVAVvfGTGSNACYLERTDAIIKCQGL 271
Cdd:COG2971 80 AEALEAALRELFPFARVV-VVNDALAALAGALGGEDGIVVIA--GTGSIAAGRDGDGRTARVGGW 141
|
|
| |
