|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02405 |
PLN02405 |
hexokinase |
26-494 |
0e+00 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 936.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 26 KRKMKRDRRWAKAMEIVKEMQEKCGTPIWKLKQVADAMVVEMHAGLASEGGSKLKMLISYVDNLPSGDEKGLFYALDLGG 105
Cdd:PLN02405 25 RRRMKSSGKWARAMEILKEFEEDCATPIGKLRQVADAMTVEMHAGLASEGGSKLKMLISYVDNLPSGDEKGLFYALDLGG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 106 TNFRVMRVQLGGKDGGLVNQEFTEVSIPPNLMIGTSDALFDYIAAELAKFIAQEGQEFDLPPGKQRELGFTFSFPVMQTS 185
Cdd:PLN02405 105 TNFRVLRVLLGGKDGRVVKQEFEEVSIPPHLMTGSSDALFDFIAAALAKFVATEGEDFHLPPGRQRELGFTFSFPVKQTS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 186 IASGTLVRWTKGFSIDDAVGQDVVAELTRAMKRQGLDMRVSALVNDTVGTLAGGKYSYKDVVAAVILGTGSNAAYVEHAQ 265
Cdd:PLN02405 185 ISSGTLIKWTKGFSIDDAVGQDVVGELTKAMERVGLDMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQ 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 266 AIPKWHGDLPKSGEMVINMEWGNFRSSHLPLTEYDHAMDNESLNPGEQIFEKLISGMYLGEIVRRVLLKMAEEAAFFGDI 345
Cdd:PLN02405 265 AIPKWHGLLPKSGEMVINMEWGNFRSSHLPLTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 346 VPPKLKIPFILRTPDLSAMHHDTSSDLILVEKKLKDILEISNASLQTRKVVVELCNIVATRGSRLAAAGILGILKKIGRD 425
Cdd:PLN02405 345 VPPKLKIPFILRTPDMSAMHHDTSPDLKVVGSKLKDILEIPNTSLKMRKVVVELCNIVATRGARLSAAGIYGILKKLGRD 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050369668 426 TVKDMDEQKTVIAMDGGLFEHYSEYSKCLENTLNELLGEEVSKTISIEHANDGSGIGAALLAASHSLYL 494
Cdd:PLN02405 425 TVKDGEKQKSVIAMDGGLFEHYTEFSKCMESTLKELLGEEVSESIEVEHSNDGSGIGAALLAASHSLYL 493
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
51-490 |
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: 793.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 51 TPIWKLKQVADAMVVEMHAGLASEGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVQLGGKDGGLVNQEFTEV 130
Cdd:cd24020 1 TPVSRLRQVADAMVVEMEAGLASEGGSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 131 SIPPNLMIGTSDALFDYIAAELAKFIAQEGQEFDlPPGKQRELGFTFSFPVMQTSIASGTLVRWTKGFSIDDAVGQDVVA 210
Cdd:cd24020 81 PIPPELMVGTSEELFDFIAGELAKFVATEGEGFH-PEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 211 ELTRAMKRQGLDMRVSALVNDTVGTLAGGKYSYKDVVAAVILGTGSNAAYVEHAQAIPKWHGDLPKSGEMVINMEWGNFR 290
Cdd:cd24020 160 LLEEALERQGLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGLPRSGEMVINTEWGNFR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 291 SSHLPLTEYDHAMDNESLNPGEQIFEKLISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPDLSAMHHDTSS 370
Cdd:cd24020 240 SSHLPRTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMHEDDSP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 371 DLILVEKKLKDILEISNASLQTRKVVVELCNIVATRGSRLAAAGILGILKKIGRDTVKDMDEQKTVIAMDGGLFEHYSEY 450
Cdd:cd24020 320 DLETVARILKDALGIDDTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLGRDGGGSSPAQRTVVAVDGGLYEHYPKF 399
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2050369668 451 SKCLENTLNELLGEEVSKTISIEHANDGSGIGAALLAASH 490
Cdd:cd24020 400 REYMQQALVELLGDEAADSVELELSNDGSGIGAALLAAAH 439
|
|
| PLN02914 |
PLN02914 |
hexokinase |
41-493 |
0e+00 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 607.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 41 IVKEMQEKCGTPIWKLKQVADAMVVEMHAGLASEGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVQLGGKDG 120
Cdd:PLN02914 40 ILTKLQKDCATPLPVLRHVADAMAADMRAGLAVDGGGDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKDE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 121 GLVNQEFTEVSIPPNLMIGTSDALFDYIAAELAKFIAQEGQEFDLPPGKQRELGFTFSFPVMQTSIASGTLVRWTKGFSI 200
Cdd:PLN02914 120 RVIATEFEQVSIPQELMFGTSEELFDFIASGLANFVAKEGGKFHLPEGRKREIGFTFSFPVKQTSIDSGILMKWTKGFAV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 201 DDAVGQDVVAELTRAMKRQGLDMRVSALVNDTVGTLAGGKYSYKDVVAAVILGTGSNAAYVEHAQAIPKWHGDLPKSGEM 280
Cdd:PLN02914 200 SGTAGKDVVACLNEAMERQGLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKSSSGRT 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 281 VINMEWGNFrSSHLPLTEYDHAMDNESLNPGEQIFEKLISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPD 360
Cdd:PLN02914 280 IINTEWGAF-SDGLPLTEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALRTPH 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 361 LSAMHHDTSSDLILVEKKLKDILEISnASLQTRKVVVELCNIVATRGSRLAAAGILGILKKIGRDTVKDMDEQKTVIAMD 440
Cdd:PLN02914 359 LCAMQQDNSDDLQAVGSILYDVLGVE-ASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDSKGMIFGKRTVVAMD 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2050369668 441 GGLFEHYSEYSKCLENTLNELLGEEVSKTISIEHANDGSGIGAALLAASHSLY 493
Cdd:PLN02914 438 GGLYEKYPQYRRYMQDAVTELLGLELSKNIAIEHTKDGSGIGAALLAATNSKY 490
|
|
| PLN02362 |
PLN02362 |
hexokinase |
27-493 |
0e+00 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 582.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 27 RKMKRDRRWAKAMEIVKEMQEKCGTPIWKLKQVADAMVVEMHAGLASEGGSKLKMLISYVDNLPSGDEKGLFYALDLGGT 106
Cdd:PLN02362 26 RRVKSRRKWRRVVGVLKELEEACETPVGRLRQVVDAMAVEMHAGLASEGGSKLKMLLTFVDDLPTGSEIGTYYALDLGGT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 107 NFRVMRVQLGGKDGGLVNQEFTEVSIPPNLMIGTSDALFDYIAAELAKFIAQEGQEFDLPPGKQRELGFTFSFPVMQTSI 186
Cdd:PLN02362 106 NFRVLRVQLGGQRSSILSQDVERHPIPQHLMNSTSEVLFDFIASSLKQFVEKEENGSEFSQVRRRELGFTFSFPVKQTSI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 187 ASGTLVRWTKGFSIDDAVGQDVVAELTRAMKRQGLDMRVSALVNDTVGTLAGGKYSYKDVVAAVILGTGSNAAYVEHAQA 266
Cdd:PLN02362 186 SSGILIKWTKGFAISDMVGKDVAECLQGALNRRGLDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 267 IPKWHGDLPKSGEMVINMEWGNFRSSHLPLTEYDHAMDNESLNPGEQIFEKLISGMYLGEIVRRVLLKMAEEAAFFGDiV 346
Cdd:PLN02362 266 IIKCQGLLTTSGSMVVNMEWGNFWSSHLPRTSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIFGP-V 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 347 PPKLKIPFILRTPDLSAMHHDTSSDLILVEKKLKDILEISNASLQTRKVVVELCNIVATRGSRLAAAGILGILKKIGRD- 425
Cdd:PLN02362 345 SSRLSTPFVLRTPSVAAMHEDDSPELQEVARILKETLGISEVPLKVRKLVVKICDVVTRRAARLAAAGIVGILKKIGRDg 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050369668 426 -----------TVKDMdeQKTVIAMDGGLFEHYSEYSKCLENTLNELLGEEVSKTISIEHANDGSGIGAALLAASHSLY 493
Cdd:PLN02362 425 sggitsgrsrsDIQIM--RRTVVAVEGGLYTNYTMFREYLHEALNEILGEDVAQHVILKATEDGSGIGSALLAASYSSY 501
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
28-489 |
0e+00 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 544.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 28 KMKRDRRWAKAMEIVKEMQEKCGTPIWKLKQVADAMVVEMHAGLASEGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTN 107
Cdd:PLN02596 28 KRRKERQWKHTQRILRKFARECATPVSKLWEVADALVSDMTASLTAEETTTLNMLVSYVASLPSGDEKGLYYGLNLRGSN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 108 FRVMRVQLGGKDGGLVNQEFTEVSIPPNLMIGTSDALFDYIAAELAKFIAQEGQEFDLPPGKQRELGFTFSFPVMQTSIA 187
Cdd:PLN02596 108 FLLLRARLGGKNEPISDLYREEISIPSNVLNGTSQELFDYIALELAKFVAEHPGDEADTPERVKKLGFTVSYPVDQAAAS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 188 SGTLVRWtKGFSIDDAVGQDVVAELTRAMKRQGLDMRVSALVNDTVGTLAGGKYSYKDVVAAVILGTGSNAAYVEHAQAI 267
Cdd:PLN02596 188 SGSAIKW-KSFSADDTVGKALVNDINRALEKHGLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 268 PKWHGDLPKSGEMVINMEWGNFRSSHLPLTEYDHAMDNESLNPGEQIFEKLISGMYLGEIVRRVLLKMAEEAAFFGDIVP 347
Cdd:PLN02596 267 PKWQSPSPESQEIVISTEWGNFNSCHLPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 348 PKLKIPFILRTPDLSAMHHDTSSDLILVEKKLKDILEISNASLQTRKVVVELCNIVATRGSRLAAAGILGILKKIGRdtv 427
Cdd:PLN02596 347 PKLTTPYLLRSPDMAAMHQDTSEDHEVVNEKLKEIFGITDSTPMAREVVAEVCDIVAERGARLAGAGIVGIIKKLGR--- 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050369668 428 kdMDEQKTVIAMDGGLFEHYSEYSKCLENTLNELLGEEVSKTISIEHANDGSGIGAALLAAS 489
Cdd:PLN02596 424 --IENKKSVVTVEGGLYEHYRVFRNYLHSSVWEMLGSELSDNVVIEHSHGGSGAGALFLAAC 483
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
55-487 |
1.98e-166 |
|
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: 476.74 E-value: 1.98e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 55 KLKQVADAMVVEMHAGLASEGGSkLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVQLGGKDGG--LVNQEFTevsI 132
Cdd:cd24018 3 KLEEIVKHFLSEMEKGLEGDGGS-LPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNGGIfiIVQRKYK---I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 133 PPNLMIGTSDALFDYIAAELAKFIAQEGQefDLPPGKQRELGFTFSFPVMQTSIASGTLVRWTKGFSIDDAVGQDVVAEL 212
Cdd:cd24018 79 PDEAKTGTGEELFDFIAECIAEFLEEHNL--DLQSDKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 213 TRAMKRQGLDMRVSALVNDTVGTLAGGKYSYKDVVAAVILGTGSNAAYVEHAQAIPKWH---GDLPKSGEMVINMEWGNF 289
Cdd:cd24018 157 QNALDRRGVNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTspsGSVTKSDEMIINTEWGAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 290 RSSH--LPLTEYDHAMDNESLNPGEQIFEKLISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPDLSAMHHD 367
Cdd:cd24018 237 DNERevLPLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEAD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 368 TSSDLILVEKKLKDILEISNASLQTRKVVVELCNIVATRGSRLAAAGILGILKKIGRDTVKdmdeqKTVIAMDGGLFEHY 447
Cdd:cd24018 317 TSPDLDAVRDILKELLAIDNTTLEDRKLIKRICELVSTRAARLSAAAIAAILLKRGSLLPE-----PVTVGIDGSVYEKY 391
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2050369668 448 SEYSKCLENTLNELLGEEVSKTISIEHANDGSGIGAALLA 487
Cdd:cd24018 392 PGFKDRLSEALRELFGPEVKANISLVLAKDGSGLGAAIIA 431
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
55-488 |
1.62e-155 |
|
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: 448.91 E-value: 1.62e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 55 KLKQVADAMVVEMHAGLASEG--GSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVQLggKDGGLVNQEFTEVSI 132
Cdd:cd24019 6 QLEEIMDRLLKEMEKGLSKDThpTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTL--NGGSQVKMESEIYAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 133 PPNLMIGTSDALFDYIAAELAKFIAQEG-QEFDLPpgkqreLGFTFSFPVMQTSIASGTLVRWTKGFSIDDAVGQDVVAE 211
Cdd:cd24019 84 PEEIMTGTGEQLFDYIAECLAEFLEKNGlKDKKLP------LGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 212 LTRAMKRQGL-DMRVSALVNDTVGTLAGGKYSYKDVVAAVILGTGSNAAYVEHAQAIPKWHGDLPKSGEMVINMEWGNFR 290
Cdd:cd24019 158 LQEAIKRRGDiKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKWDGDEGDPGQVIINTEWGAFG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 291 SSH---LPLTEYDHAMDNESLNPGEQIFEKLISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPDLSAMHHD 367
Cdd:cd24019 238 DNGvldFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 368 TSSDLILVEKKLKDiLEISNASLQTRKVVVELCNIVATRGSRLAAAGILGILKKIGRdtvkdmdeQKTVIAMDGGLFEHY 447
Cdd:cd24019 318 NEGDFSNTREILKE-LGLEDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNR--------KEVTVGVDGSLYKYH 388
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2050369668 448 SEYSKCLENTLNELLGEEvsKTISIEHANDGSGIGAALLAA 488
Cdd:cd24019 389 PKFHKRMHETLKELVPPG--CKFKLMLSEDGSGKGAALVAA 427
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
56-487 |
3.94e-131 |
|
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: 384.32 E-value: 3.94e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 56 LKQVADAMVVEMHAGLASEGGSkLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVQLGGKdgGLVNQEFTEVSIPPN 135
Cdd:cd24000 4 LKEITDAFLEELEKGLAGEPSS-LKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGK--GIEVTISKKYEIPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 136 LMIGTSDALFDYIAAELAKFIAQEGQEFDLPpgkqreLGFTFSFPVMQTSIASGTLVRWTKGFSIDDAVGQDVVAELTRA 215
Cdd:cd24000 81 IKTASAEEFFDFIADCIAEFLKENGLKKPLP------LGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 216 MKRQGLDMRVSALVNDTVGTLAGGKYSYKDVVAAVILGTGSNAAYVEHAQAIpkwhgdLPKSGEMVINMEWGNFRSSHLP 295
Cdd:cd24000 155 LKKRGLPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNI------LLGDGGMIINTEWGNFGKNSLP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 296 LTEYDHAMDNESLNPGEQIFEKLISGMYLGEIVRRVLLKMAEEaaffgdivppklkipfilrtpdlsamhhdtssdlilv 375
Cdd:cd24000 229 RTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 376 ekklkdileisnaslqtrkVVVELCNIVATRGSRLAAAGILGILKKIGrdtvkDMDEQKTVIAMDGGLFEHYSEYSKCLE 455
Cdd:cd24000 272 -------------------ILRKICELVAERSARLAAAAIAALLRKTG-----DSPEKKITIAVDGSLFEKYPGYRERLE 327
|
410 420 430
....*....|....*....|....*....|..
gi 2050369668 456 NTLNELLGEEvsKTISIEHANDGSGIGAALLA 487
Cdd:cd24000 328 EYLKELLGRG--IRIELVLVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
55-487 |
7.20e-124 |
|
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: 369.03 E-value: 7.20e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 55 KLKQVADAMVVEMHAGLASEGGSkLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVQLGGKDGGLVNQEftEVSIPP 134
Cdd:cd24088 3 KLDKLTAEFQRQMEKGLAKHGKG-MAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHGDGTFSLRQE--KSKIPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 135 NLMIG-TSDALFDYIAAELAKFIAQEGQEfDLPPGKQRE---LGFTFSFPVMQTSIASGTLVRWTKGFSIDDAVGQDVVA 210
Cdd:cd24088 80 ELKTGvTAKDLFDYLAKSVEAFLTKHHGD-SFAAGKDDDrlkLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 211 ELTRAMKRQGLDMRVSALVNDTVGTLAGGKYSYKDVVAAV---ILGTGSNAAYVEHAQAIPKWH---GDLPKSGEMVINM 284
Cdd:cd24088 159 LLQDELDRQGIPVKVVALVNDTVGTLLARSYTSPEISGAVlgaIFGTGTNGAYLEDLEKIKKLDdssRVGKGKTHMVINT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 285 EWGNFRS--SHLPLTEYDHAMDNESLNPGEQIFEKLISGMYLGEIVRRVLLKMAEEAAFFG---DIVPPKLKIPFILRTP 359
Cdd:cd24088 239 EWGSFDNelKVLPTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFLIqynDKSPSALNTPYGLDTA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 360 DLSAMHHDTSSDLILVEKKLKDILEISNASLQTRKVVVELCNIVATRGSRLAAAGILGILKKIGRdtVKDMDEQKTVIAM 439
Cdd:cd24088 319 VLSAIEIDSEAELRATRKVLLDDLGLPAPSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGA--LNKSYDGEINIGV 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2050369668 440 DGGLFEHYSEYSKCLENTLNELL-GEEVSKTISIEHANDGSGIGAALLA 487
Cdd:cd24088 397 DGSVIEFYPGFESMLREALRLLLiGAEGEKRIKIGIAKDGSGVGAALCA 445
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
55-488 |
1.41e-120 |
|
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: 359.77 E-value: 1.41e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 55 KLKQVADAMVVEMHAGLASEGGSkLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVQLGGkdgglvNQEF----TEV 130
Cdd:cd24087 3 RLRKITDHFISELEKGLSKKGGN-IPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGG------NGKFditqSKY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 131 SIPPNLMIGTSDALFDYIAAELAKFIAQEgqeFDLPPGKQRELGFTFSFPVMQTSIASGTLVRWTKGFSIDDAVGQDVVA 210
Cdd:cd24087 76 RLPEELKTGTGEELWDFIADCLKKFVEEH---FPGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 211 ELTRAMKRQGLDMRVSALVNDTVGTLAGGKYSYKDVVAAVILGTGSNAAYVEHAQAIPKW-HGDLPKSGEMVINMEWGNF 289
Cdd:cd24087 153 MLQKALKKRNVPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLeHDDIPPDSPMAINCEYGAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 290 RSSH--LPLTEYDHAMDNESLNPGEQIFEKLISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPDLSAMHHD 367
Cdd:cd24087 233 DNEHlvLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 368 TSSDLILVEKKLKDILEIsNASLQTRKVVVELCNIVATRGSRLAAAGILGILKKigrdtvkdMDEQKTVIAMDGGLFEHY 447
Cdd:cd24087 313 PFENLEDTDDLFQHFFGL-ETTVPERKFIRRLAELIGTRAARLSACGIAAICKK--------RGYKTCHVAADGSVYNKY 383
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2050369668 448 SEYSKCLENTLNELLGEEVSKT-ISIEHANDGSGIGAALLAA 488
Cdd:cd24087 384 PGFKERAAQALKDIFGWDGEDDpIKTVPAEDGSGVGAAIIAA 425
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
55-488 |
9.57e-110 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 333.57 E-value: 9.57e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 55 KLKQVADAMVVEMHAGLASEGG---------SKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVQLGGKDGGLVNQ 125
Cdd:PTZ00107 24 KLKELVDYFLYELVEGLEAHRRhrnlwipneCSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFRAVRVSLRGGGKMERTQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 126 E-----FTEVSIPPNLMIGTSDA--LFDYIAAELAKFIAQEGQefDLPPGKQRELGFTFSFPVMQTSIASGTLVRWTKGF 198
Cdd:PTZ00107 104 SkfslpKSALLGEKGLLDKKATAtdLFDHIAKSIKKMMEENGD--PEDLNKPVPVGFTFSFPCTQLSVNNAILIDWTKGF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 199 S----IDDAV-GQDVVAELTRAMKRQGLDMRVSALVNDTVGTLAGGKY----SYKDVVAAVILGTGSNAAYVEHAQAIPK 269
Cdd:PTZ00107 182 EtgraTNDPVeGKDVGELLNDAFKRNNVPANVVAVLNDTVGTLISCAYqkpkNTPPCQVGVIIGTGSNACYFEPEVSAYG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 270 WHGdlpksgeMVINMEWGNFrSSHLPLTEYDHAMDNESLNPGEQIFEKLISGMYLGEIVRRVLLKMAEEAAffgdivPPK 349
Cdd:PTZ00107 262 YAG-------TPINMECGNF-DSKLPITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLLQLKA------PPK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 350 LKIPFILRTPDLSAMHHDTSSDLILVEKKLKDI--LEISNASLqtrKVVVELCNIVATRGSRLAAAGILGILKKIGRDTv 427
Cdd:PTZ00107 328 MWQSGSFESEDASMILNDQSPDLQFSRQVIKEAwdVDLTDEDL---YTIRKICELVRGRAAQLAAAFIAAPAKKTRTVQ- 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050369668 428 kdmdeQKTVIAMDGGLFEHYSEYSKCLENTLNELLGEEVSKTISIEhANDGSGIGAALLAA 488
Cdd:PTZ00107 404 -----GKATVAIDGSVYVKNPWFRRLLQEYINSILGPDAGNVVFYL-ADDGSGKGAAIIAA 458
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
247-489 |
4.27e-108 |
|
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: 320.98 E-value: 4.27e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 247 VAAVILGTGSNAAYVEHAQAIPKWHGDLPKSGEMVINMEWGNFRSSH---LPLTEYDHAMDNESLNPGEQIFEKLISGMY 323
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKLPKSGEMIINTEWGAFGDNGllpLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 324 LGEIVRRVLLKMAEEAAFFGDIVpPKLKIPFILRTPDLSAMHHDTSSDLILVEKKLKDILEISNASLQTRKVVVELCNIV 403
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKGQS-EKLKTPYSLDTSFLSAIESDPSEDLETTREILEELLGIETVTEEDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 404 ATRGSRLAAAGILGILKKIGRDTvkdmdeqKTVIAMDGGLFEHYSEYSKCLENTLNELLGeeVSKTISIEHANDGSGIGA 483
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-------KVTVGVDGSVYEKYPGFRERLQEALRELLG--PGDKVVLVLAEDGSGVGA 230
|
....*.
gi 2050369668 484 ALLAAS 489
Cdd:pfam03727 231 ALIAAV 236
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
55-488 |
3.36e-98 |
|
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: 302.46 E-value: 3.36e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 55 KLKQVADAMVVEMHAGLASEGG--SKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVQLGGKDGGLVNQEFTEVSI 132
Cdd:cd24089 6 TLLDISRRFRKEMEKGLGKDTHptATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMESQVYAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 133 PPNLMIGTSDALFDYIAAELAKFIAQEGQEfdlppGKQRELGFTFSFPVMQTSIASGTLVRWTKGFSIDDAVGQDVVAEL 212
Cdd:cd24089 86 PEEIMHGSGTQLFDHVAECLADFMDKQKIK-----DKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 213 TRAMKRQG-LDMRVSALVNDTVGTLAGGKYSYKDVVAAVILGTGSNAAYVEHAQAIPKWHGDlpkSGEMVINMEWGNFR- 290
Cdd:cd24089 161 RKAIRRRGdYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGD---EGRMCINTEWGAFGd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 291 --SSHLPLTEYDHAMDNESLNPGEQIFEKLISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPDLSAMHHDT 368
Cdd:cd24089 238 dgSLEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 369 SSdLILVEKKLKDIleISNASLQTRKVVVELCNIVATRGSRLAAAGILGILKKIGRDtvKDMDEQKTVIAMDGGLFEHYS 448
Cdd:cd24089 318 EG-LANAKEILTRL--GLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLREN--KGLERLRTTVGVDGSVYKKHP 392
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2050369668 449 EYSKCLENTLNELLGE-EVSKTISiehaNDGSGIGAALLAA 488
Cdd:cd24089 393 QFSKRLHKAVRRLVPDcDVRFLLS----EDGSGKGAAMVTA 429
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
41-241 |
2.13e-97 |
|
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: 292.10 E-value: 2.13e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 41 IVKEMQEKCGTPIWKLKQVADAMVVEMHAGLASEGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVQLGGKDG 120
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGGDGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 121 GLVNQEftEVSIPPNLMIGTSDALFDYIAAELAKFIAQEGQEFDlpPGKQRELGFTFSFPVMQTSIASGTLVRWTKGFSI 200
Cdd:pfam00349 81 FEITQE--KYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDF--EEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2050369668 201 DDAVGQDVVAELTRAMKRQGLDMRVSALVNDTVGTLAGGKY 241
Cdd:pfam00349 157 PGVVGKDVVQLLQEALERRGLPVKVVALVNDTVGTLMAGAY 197
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
56-489 |
1.87e-94 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 293.02 E-value: 1.87e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 56 LKQVADAMVVEMHAGLASEGGSkLKMLISYVdNLPSG-DEKGLFYALDLGGTNFRVMRVQLGGkDGGLVNQEFteVSIPp 134
Cdd:COG5026 22 LEEIAAKFQEEMEKGLEGKKSS-LKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRFDG-EGTFEIENF--KSFP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 135 nlMIGTS-----DALFDYIAAELAKFIaqegqefdlppGKQRELGFTFSFPVMQTSIASGTLVRWTKGFSIDDAVGQDVV 209
Cdd:COG5026 96 --LPGTSseitaEEFFDFIADYIEPLL-----------DESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 210 AELTRAMKRQGLD-MRVSALVNDTVGTLAGGKYSYKDVV----AAVILGTGSNAAYVEHAQAIPKWhgdLPKSGEMVINM 284
Cdd:COG5026 163 ELLEAALARKGLDnVKPVAILNDTVATLLAGAYADPDDGysgyIGSILGTGHNTCYLEPNAPIGKL---PAYEGPMIINM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 285 EWGNFrsSHLPLTEYDHAMDNESLNPGEQIFEKLISGMYLGEIVRRVLLKMAEEAAFFGDIvPPKLKIPFILRTPDLSAM 364
Cdd:COG5026 240 ESGNF--NKLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEGLFSPGF-SEVFETPYSLTTVDMSRF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 365 HHDTSSDLILVEKKLKDILEisnaslQTRKVVVELCNIVATRGSRLAAAGILGILKKIGrdtvKDMD-EQKTVIAMDGGL 443
Cdd:COG5026 317 LADPSDEKEILSQCLEAGSE------EDREILREIADAIVERAARLVAATLAGILLHLG----PGKTpLKPHCIAIDGST 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2050369668 444 FEHYSEYSKCLENTLNELLGEEVSKTISIEHANDGSGIGAALLAAS 489
Cdd:COG5026 387 YEKMPGLAEKIEYALQEYLLGEKGRYVEFVLVENASLLGAAIAAAL 432
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
55-488 |
1.15e-93 |
|
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: 290.99 E-value: 1.15e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 55 KLKQVADAMVVEMHAGLASE--GGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVQL-GGKDGGLvnQEFTEV- 130
Cdd:cd24091 6 QLLEVKARMRAEMERGLRKEthASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVrSGKWRGV--EMHNKIy 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 131 SIPPNLMIGTSDALFDYIAAELAKFIAQEGQEfdlppGKQRELGFTFSFPVMQTSIASGTLVRWTKGFSIDDAVGQDVVA 210
Cdd:cd24091 84 AIPQEIMQGTGEELFDHIVQCIADFLEYMGLK-----GVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 211 ELTRAMKR-QGLDMRVSALVNDTVGTLAGGKYSYKDVVAAVILGTGSNAAYVEHAQAIPKWHGDlpkSGEMVINMEWGNF 289
Cdd:cd24091 159 LLREAIKRrEEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGE---EGRMCINMEWGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 290 RSS----HLpLTEYDHAMDNESLNPGEQIFEKLISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPDLSAMH 365
Cdd:cd24091 236 GDNgcldDI-RTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 366 HDTSSdLILVEKKLKDI-LE-ISNASLqtrkVVVELCNIVATRGSRLAAAGILGILKKIGRDtvKDMDEQKTVIAMDGGL 443
Cdd:cd24091 315 SDRLA-LLQVRAILQQLgLDsTCDDSI----IVKEVCGVVSRRAAQLCGAGMAAVVDKIREN--RGLDHLNVTVGVDGTL 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2050369668 444 FEHYSEYSKCLENTLNELLGEEVsktISIEHANDGSGIGAALLAA 488
Cdd:cd24091 388 YKLHPHFSRVMHETVKELAPKCD---VTFLQSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
55-488 |
2.93e-89 |
|
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: 279.46 E-value: 2.93e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 55 KLKQVADAMVVEMHAGLASE--GGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVQLGGKDGGLVNQEFTevsI 132
Cdd:cd24129 6 QLAAVQAQMRKEMAKGLRGEthAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTAGVQITSEIYS---I 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 133 PPNLMIGTSDALFDYIAAELAKFiaqeGQEFDLPpGKQRELGFTFSFPVMQTSIASGTLVRWTKGFSIDDAVGQDVVAEL 212
Cdd:cd24129 83 PETVAQGTGQQLFDHIVDCIVDF----QQKQGLS-GQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 213 TRA-MKRQGLDMRVSALVNDTVGTLAGGKYSYKDVVAAVILGTGSNAAYVEHAQAIPKWHGDlpkSGEMVINMEWGNF-- 289
Cdd:cd24129 158 REAaTRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGD---SGRMCINMEWGAFgd 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 290 -RSSHLPLTEYDHAMDNESLNPGEQIFEKLISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPDLSAMHHDT 368
Cdd:cd24129 235 nGCLAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 369 ssdliLVEKKLKDILEISN--ASLQTRKVVVELCNIVATRGSRLAAAGILGILKKIGRDtvKDMDEQKTVIAMDGGLFEH 446
Cdd:cd24129 315 -----LALRQVRAILEDLGlpLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMREN--RGLDELAVTVGVDGTLYKL 387
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2050369668 447 YSEYSKCLENTLNELLGEEVsktISIEHANDGSGIGAALLAA 488
Cdd:cd24129 388 HPRFSSLVQATVRELAPRCV---VTFLQSEDGSGKGAALVTA 426
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
55-488 |
7.14e-86 |
|
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: 271.00 E-value: 7.14e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 55 KLKQVADAMVVEMHAGLASE--GGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVQL-GGKDGGlVNQEFTEVS 131
Cdd:cd24128 6 QLLEVKRRMKVEMERGLSKEthASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVrNGKWRG-VEMHNKIYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 132 IPPNLMIGTSDALFDYIAAELAKFIAQEGQEfdlppGKQRELGFTFSFPVMQTSIASGTLVRWTKGFSIDDAVGQDVVAE 211
Cdd:cd24128 85 IPQEVMHGTGEELFDHIVHCIADFLEYMGMK-----GVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 212 LTRAMKR-QGLDMRVSALVNDTVGTLAGGKYSYKDVVAAVILGTGSNAAYVEHAQAIPKWHGDlpkSGEMVINMEWGNFR 290
Cdd:cd24128 160 LKEAIHRrEEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGE---EGRMCVNMEWGAFG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 291 SSHLP---LTEYDHAMDNESLNPGEQIFEKLISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPDLSAMHHD 367
Cdd:cd24128 237 DNGCLddfRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 368 TssdliLVEKKLKDILEI--SNASLQTRKVVVELCNIVATRGSRLAAAGILGILKKIGRDtvKDMDEQKTVIAMDGGLFE 445
Cdd:cd24128 317 R-----LALLQVRAILQHlgLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIREN--RGLDALKVTVGVDGTLYK 389
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2050369668 446 HYSEYSKCLENTLNELlgeEVSKTISIEHANDGSGIGAALLAA 488
Cdd:cd24128 390 LHPHFAKVMHETVKDL---APKCDVSFLQSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
56-488 |
3.88e-85 |
|
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: 269.03 E-value: 3.88e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 56 LKQVADAMVVEMHAGLASEGGSK--LKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVQLGGKDGGLVNQEFTEVSIP 133
Cdd:cd24126 7 LLDIMTRFRAEMEKGLAKDTNPTaaVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMESQFYPTP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 134 PNLMIGTSDALFDYIAAELAKFIAQEGQEfdlppGKQRELGFTFSFPVMQTSIASGTLVRWTKGFSIDDAVGQDVVAELT 213
Cdd:cd24126 87 EEIIHGTGTELFDYVAECLADFMKKKGIK-----HKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 214 RAMKRQG-LDMRVSALVNDTVGTLAGGKYSYKDVVAAVILGTGSNAAYVEHAQAIPKWHGDlpkSGEMVINMEWGNFRSS 292
Cdd:cd24126 162 KAIRKHKdVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGD---EGRMCINTEWGAFGDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 293 HLP---LTEYDHAMDNESLNPGEQIFEKLISGMYLGEIVRRVLLKMAEEAAFFGDivppklKIPFILRTPDLSAMHHdts 369
Cdd:cd24126 239 GSLediRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKG------QISPALRTKGKIETKH--- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 370 sdLILVEKK---LKDILEI-SNASLQTRK----VVVELCNIVATRGSRLAAAGILGILKKIGRDtvKDMDEQKTVIAMDG 441
Cdd:cd24126 310 --VAAIEKYkegLYNTREIlSDLGLEPSEedciAVQHVCTIVSFRSANLCAAALAAILTRLREN--KKLERLRTTVGMDG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2050369668 442 GLFEHYSEYSKCLENTLNELLGE-EVSKTISiehaNDGSGIGAALLAA 488
Cdd:cd24126 386 TVYKTHPQYAKRLHKVVRRLVPScDVRFLLS----ESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
55-488 |
5.09e-85 |
|
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: 268.72 E-value: 5.09e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 55 KLKQVADAMVVEMHAGLASE--GGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVQL--GGKDGGLVNQEFtev 130
Cdd:cd24130 6 QLQEVKQKMRTELEYGLKKEthPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIrsGRRSVRMYNKIF--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 131 SIPPNLMIGTSDALFDYIAAELAKFIAQEGQEfdlppGKQRELGFTFSFPVMQTSIASGTLVRWTKGFSIDDAVGQDVVA 210
Cdd:cd24130 83 AIPLEIMQGTGEELFDHIVQCIADFLDYMGLK-----GARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 211 ELTRAMKRQG-LDMRVSALVNDTVGTLAGGKYSYKDVVAAVILGTGSNAAYVEHAQAIPKWHGDlpkSGEMVINMEWGNF 289
Cdd:cd24130 158 MLREAIKRRNeFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGD---EGRMCINTEWGGF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 290 RSSHLP---LTEYDHAMDNESLNPGEQIFEKLISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPDLSAMHH 366
Cdd:cd24130 235 GDNGCIddiRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIES 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 367 DTSSdLILVEKKLKDILeiSNASLQTRKVVVELCNIVATRGSRLAAAGILGILKKIGRDtvKDMDEQKTVIAMDGGLFEH 446
Cdd:cd24130 315 DRLA-LLQVRRILQQLG--LDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIREN--QGLDRLDITVGVDGTLYKL 389
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2050369668 447 YSEYSKCLENTLNELLGE-EVSKTISiehaNDGSGIGAALLAA 488
Cdd:cd24130 390 HPHFSRILQETVKELAPQcDVTFMLS----EDGSGKGAALITA 428
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
56-488 |
7.88e-85 |
|
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: 267.92 E-value: 7.88e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 56 LKQVADAMVVEMHAGLASEGG--SKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVQLGGKDGGLVNQEFTEVSIP 133
Cdd:cd24125 7 LLEISKRFRKEMEKGLGATTHptAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMENQIYAIP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 134 PNLMIGTSDALFDYIAAELAKFIAQEG-QEFDLPpgkqreLGFTFSFPVMQTSIASGTLVRWTKGFSIDDAVGQDVVAEL 212
Cdd:cd24125 87 EDIMRGSGTQLFDHIAECLANFMDKLQiKDKKLP------LGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 213 TRAMKRQG-LDMRVSALVNDTVGTLAGGKYSYKDVVAAVILGTGSNAAYVEHAQAIPKWHGDlpkSGEMVINMEWGNFRS 291
Cdd:cd24125 161 RKAIQKRGdFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGD---EGRMCINMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 292 SHL---PLTEYDHAMDNESLNPGEQIFEKLISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPDLSAMHHD- 367
Cdd:cd24125 238 DGSlddIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEk 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 368 ---TSSDLILVEKKLKDILEISNASLQtrkvvveLCNIVATRGSRLAAAGILGILKKIGRDtvKDMDEQKTVIAMDGGLF 444
Cdd:cd24125 318 dgiRKAREVLMRLGLDPTQEDCVATHR-------ICQIVSTRSASLCAATLAAVLQRIKEN--KGEERLRSTIGVDGSVY 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2050369668 445 EHYSEYSKCLENTLNELLGEEVSKTISIEhanDGSGIGAALLAA 488
Cdd:cd24125 389 KKHPHFARRLHKTVRRLVPGCDVRFLRSE---DGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
55-488 |
1.48e-83 |
|
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: 264.85 E-value: 1.48e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 55 KLKQVADAMVVEMHAGLASE--GGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVQLGGKDGGLVNQEFTEVSI 132
Cdd:cd24127 6 MLLEVKKRMRAEMELGLRKQthNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 133 PPNLMIGTSDALFDYIAAELAKFIAQEGQEfdlppGKQRELGFTFSFPVMQTSIASGTLVRWTKGFSIDDAVGQDVVAEL 212
Cdd:cd24127 86 PIEIMQGTGEELFDHIVSCISDFLDYMGIK-----GPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 213 TRAMKR-QGLDMRVSALVNDTVGTLAGGKYSYKDVVAAVILGTGSNAAYVEHAQAIPKWHGDlpkSGEMVINMEWGNFRS 291
Cdd:cd24127 161 RDAIKRrEEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGD---QGQMCINMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 292 SHL---PLTEYDHAMDNESLNPGEQIFEKLISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPDLSAMHHDT 368
Cdd:cd24127 238 NGClddIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 369 SSDLilvekKLKDILEI--SNASLQTRKVVVELCNIVATRGSRLAAAGILGILKKIGRDtvKDMDEQKTVIAMDGGLFEH 446
Cdd:cd24127 318 LALL-----QVRAILQQlgLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIREN--RGLDHLNVTVGVDGTLYKL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2050369668 447 YSEYSKCLENTLNELlgeEVSKTISIEHANDGSGIGAALLAA 488
Cdd:cd24127 391 HPHFSRIMHQTVKEL---SPKCNVSFLLSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
66-488 |
1.93e-82 |
|
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: 263.40 E-value: 1.93e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 66 EMHAGLASEGG--SKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVQLGGKDGGLVNQEFTEVSIPPNLMIGTSDA 143
Cdd:cd24124 45 EMKNGLSRDFNptATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVHGSGSQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 144 LFDYIAAELAKFI-AQEGQEFDLPpgkqreLGFTFSFPVMQTSIASGTLVRWTKGFSIDDAVGQDVVAELTRAMKRQG-L 221
Cdd:cd24124 125 LFDHVAECLGDFMeKRKIKDKKLP------VGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLNKAIKKRGdY 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 222 DMRVSALVNDTVGTLAGGKYSYKDVVAAVILGTGSNAAYVEHAQAIPKWHGDlpkSGEMVINMEWGNFR---SSHLPLTE 298
Cdd:cd24124 199 DANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGD---EGRMCINTEWGAFGddgSLEDIRTE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 299 YDHAMDNESLNPGEQIFEKLISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPDLSAMHHDTSSdlilvEKK 378
Cdd:cd24124 276 FDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEG-----LHN 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 379 LKDILEI--SNASLQTRKVVVELCNIVATRGSRLAAAGILGILKKIgRDTvKDMDEQKTVIAMDGGLFEHYSEYSKCLEN 456
Cdd:cd24124 351 AKEILTRlgVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRL-RDN-KGTPRLRTTVGVDGSLYKTHPQYSRRFHK 428
|
410 420 430
....*....|....*....|....*....|..
gi 2050369668 457 TLNELLGEEVSKTISIEhanDGSGIGAALLAA 488
Cdd:cd24124 429 TLRRLVPDSDVRFLLSE---SGSGKGAAMVTA 457
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
56-488 |
8.28e-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: 247.87 E-value: 8.28e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 56 LKQVADAMVVEMHAGLASEG--GSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVQLG-GKDGGL-VNQEFTEVS 131
Cdd:cd24092 16 LKKVMRRMQKEMDRGLRLETheEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGeGEEGQWsVKTKHQMYS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 132 IPPNLMIGTSDALFDYIAAELAKFIAQEGQEFdlppgKQRELGFTFSFPVMQTSIASGTLVRWTKGFSIDDAVGQDVVAE 211
Cdd:cd24092 96 IPEDAMTGTAEMLFDYISECISDFLDKHQMKH-----KKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVGL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 212 LTRAMKRQG-LDMRVSALVNDTVGTLAGGKYSYKDVVAAVILGTGSNAAYVEHAQAIPKWHGDlpkSGEMVINMEWGNF- 289
Cdd:cd24092 171 LRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGD---EGRMCVNTEWGAFg 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 290 RSSHLP--LTEYDHAMDNESLNPGEQIFEKLISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPDLSAMHHD 367
Cdd:cd24092 248 DSGELDefLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 368 TSSdlilvEKKLKDILEISN--ASLQTRKVVVELCNIVATRGSRLAAAGILGILKKIgRDTvKDMDEQKTVIAMDGGLFE 445
Cdd:cd24092 328 TGD-----RKQIYNILSTLGlrPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRM-RES-RSEDVMRITVGVDGSVYK 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2050369668 446 HYSEYSKCLENTLNELLGeevSKTISIEHANDGSGIGAALLAA 488
Cdd:cd24092 401 LHPSFKERFHASVRRLTP---SCEITFIESEEGSGRGAALVSA 440
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
52-488 |
2.75e-75 |
|
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: 243.29 E-value: 2.75e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 52 PIWKLKQVADAMVVEMHAGLASEGG--SKLKMLISYVDNLPSGDEKGLFYALDLG--GTNFRVMRVQLGGKDGGLVNQEF 127
Cdd:cd24090 3 TRAQLQQIQASLLGSMEQALRGQASpaPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 128 TEVSIPPNLMIGTSDALFDYIAAELAKFIaqEGQEFDLPPgkqRELGFTFSFPVMQTSIASGTLVRWTKGFSIDDAVGQD 207
Cdd:cd24090 83 QEFVIPQEVMLGAGQQLFDFAAHCLSEFL--DGQPVPKQG---LQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 208 VVAELTRAMKRQGL-DMRVSALVNDTVGTLAGGKYSYKDVVAAVILGTGSNAAYVEHAQAIPKWHGDlpkSGEMVINMEW 286
Cdd:cd24090 158 VVQLLRDAIQRQGAyNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDED---RGRVCVSVEW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 287 GNFR---SSHLPLTEYDHAMDNESLNPGEQIFEKLISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPDLSA 363
Cdd:cd24090 235 GSFSddgALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050369668 364 MhHDTSSDLILVEKKLKDILEISNASLQTRkvVVELCNIVATRGSRLAAAGILGILKKIGRDtvKDMDEQKTVIAMDGGL 443
Cdd:cd24090 315 M-EDPSAGAARVRAILQDLGLSPSASDVEL--VQHVCRAVCTRAAQLCAAALAAVLSHLQHS--REQQTLQVAVATGGRV 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2050369668 444 FEHYSEYSKCLENTLNeLLGEEVskTISIEHANDGSGIGAALLAA 488
Cdd:cd24090 390 CERHPRFCSILQGTVM-LLAPEC--DVSFIPSVDGGGRGVAMVTA 431
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
209-264 |
3.13e-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: 3.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2050369668 209 VAELTRAMKRQGLDMRVsALVNDTVGTLAGGkySYKDVVAAVILGTGSNAAYVEHA 264
Cdd:COG2971 80 AEALEAALRELFPFARV-VVVNDALAALAGA--LGGEDGIVVIAGTGSIAAGRDGD 132
|
|
| |
