|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02405 |
PLN02405 |
hexokinase |
1-536 |
0e+00 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 975.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 1 MGKVAVGAAIVCGATVCAAAALIVRHRMRSSGRWARAMAILTELEEKCGTPIGKLKQVGDAMTVEMHAGLASEGGSKLKM 80
Cdd:PLN02405 1 MGKVAVGAAVVCAAAVCAAAALVVRRRMKSSGKWARAMEILKEFEEDCATPIGKLRQVADAMTVEMHAGLASEGGSKLKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 81 LISYVDNLPTGDEKGLFYALDLGGTNFRVLRVQLGGNDGRVVNQEFTEVSIPPHLMVGTSDALFDYIAAELAKFVATEGQ 160
Cdd:PLN02405 81 LISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVSIPPHLMTGSSDALFDFIAAALAKFVATEGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 161 GFHLSPGRQRELGFTFSFPVRQLTIASGTLIKWTKGFSIDDTVGQDVVAELTKAMERQGLDMRVAALVNDTIGTLAGGRY 240
Cdd:PLN02405 161 DFHLPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMERVGLDMRVSALVNDTIGTLAGGRY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 241 FNNDVIAAVILGTGTNAAYVERAHAIPKWHGLLPKSGEMVINMEWGNFRSSHLPVTEYDHALDVESLNPGEQIFEKIISG 320
Cdd:PLN02405 241 YNPDVVAAVILGTGTNAAYVERAQAIPKWHGLLPKSGEMVINMEWGNFRSSHLPLTEYDHALDVESLNPGEQIFEKIISG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 321 MYLGDIVRRVLCRMAEEAAFFGDTVPPKLRVPFILRsaldsllkgmeledlpicwvlfavsqliimgylgiasgmTPDMS 400
Cdd:PLN02405 321 MYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILR---------------------------------------TPDMS 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 401 AIHHDTTSDLRVVGNKLKDILGITNTSLKTRKVVVELCNIVATRGARLSAAGIFGILKKLGRDTVREGEKQRTVIAMDGG 480
Cdd:PLN02405 362 AMHHDTSPDLKVVGSKLKDILEIPNTSLKMRKVVVELCNIVATRGARLSAAGIYGILKKLGRDTVKDGEKQKSVIAMDGG 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1925297022 481 LFEHYTKFSECLESTLKELLGKEISESIVIEHSNDGSGIGAALLAASHSQYLDVES 536
Cdd:PLN02405 442 LFEHYTEFSKCMESTLKELLGEEVSESIEVEHSNDGSGIGAALLAASHSLYLEVEE 497
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
50-528 |
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: 798.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 50 TPIGKLKQVGDAMTVEMHAGLASEGGSKLKMLISYVDNLPTGDEKGLFYALDLGGTNFRVLRVQLGGNDGRVVNQEFTEV 129
Cdd:cd24020 1 TPVSRLRQVADAMVVEMEAGLASEGGSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 130 SIPPHLMVGTSDALFDYIAAELAKFVATEGQGFHlSPGRQRELGFTFSFPVRQLTIASGTLIKWTKGFSIDDTVGQDVVA 209
Cdd:cd24020 81 PIPPELMVGTSEELFDFIAGELAKFVATEGEGFH-PEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 210 ELTKAMERQGLDMRVAALVNDTIGTLAGGRYFNNDVIAAVILGTGTNAAYVERAHAIPKWHGLLPKSGEMVINMEWGNFR 289
Cdd:cd24020 160 LLEEALERQGLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGLPRSGEMVINTEWGNFR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 290 SSHLPVTEYDHALDVESLNPGEQIFEKIISGMYLGDIVRRVLCRMAEEAAFFGDTVPPKLRVPFILRsaldsllkgmele 369
Cdd:cd24020 240 SSHLPRTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILR------------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 370 dlpicwvlfavsqliimgylgiasgmTPDMSAIHHDTTSDLRVVGNKLKDILGITNTSLKTRKVVVELCNIVATRGARLS 449
Cdd:cd24020 307 --------------------------TPDMSAMHEDDSPDLETVARILKDALGIDDTSLEARKVVVEVCDLVAERGARLA 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1925297022 450 AAGIFGILKKLGRDTVREGEKQRTVIAMDGGLFEHYTKFSECLESTLKELLGKEISESIVIEHSNDGSGIGAALLAASH 528
Cdd:cd24020 361 AAGIVGILKKLGRDGGGSSPAQRTVVAVDGGLYEHYPKFREYMQQALVELLGDEAADSVELELSNDGSGIGAALLAAAH 439
|
|
| PLN02362 |
PLN02362 |
hexokinase |
1-531 |
0e+00 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 611.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 1 MGKVAVGAAIVCGATVCAAAALIVRHRMRSSGRWARAMAILTELEEKCGTPIGKLKQVGDAMTVEMHAGLASEGGSKLKM 80
Cdd:PLN02362 1 MGKVAVGLAAAAAVAACAVAAVMVGRRVKSRRKWRRVVGVLKELEEACETPVGRLRQVVDAMAVEMHAGLASEGGSKLKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 81 LISYVDNLPTGDEKGLFYALDLGGTNFRVLRVQLGGNDGRVVNQEFTEVSIPPHLMVGTSDALFDYIAAELAKFVATEGQ 160
Cdd:PLN02362 81 LLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRSSILSQDVERHPIPQHLMNSTSEVLFDFIASSLKQFVEKEEN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 161 GFHLSPGRQRELGFTFSFPVRQLTIASGTLIKWTKGFSIDDTVGQDVVAELTKAMERQGLDMRVAALVNDTIGTLAGGRY 240
Cdd:PLN02362 161 GSEFSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRRGLDMRVAALVNDTVGTLALGHY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 241 FNNDVIAAVILGTGTNAAYVERAHAIPKWHGLLPKSGEMVINMEWGNFRSSHLPVTEYDHALDVESLNPGEQIFEKIISG 320
Cdd:PLN02362 241 HDPDTVAAVIIGTGTNACYLERTDAIIKCQGLLTTSGSMVVNMEWGNFWSSHLPRTSYDIDLDAESPNPNDQGFEKMISG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 321 MYLGDIVRRVLCRMAEEAAFFGdTVPPKLRVPFILRsaldsllkgmeledlpicwvlfavsqliimgylgiasgmTPDMS 400
Cdd:PLN02362 321 MYLGDIVRRVILRMSQESDIFG-PVSSRLSTPFVLR---------------------------------------TPSVA 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 401 AIHHDTTSDLRVVGNKLKDILGITNTSLKTRKVVVELCNIVATRGARLSAAGIFGILKKLGRDTV-------REGEKQ-- 471
Cdd:PLN02362 361 AMHEDDSPELQEVARILKETLGISEVPLKVRKLVVKICDVVTRRAARLAAAGIVGILKKIGRDGSggitsgrSRSDIQim 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1925297022 472 -RTVIAMDGGLFEHYTKFSECLESTLKELLGKEISESIVIEHSNDGSGIGAALLAASHSQY 531
Cdd:PLN02362 441 rRTVVAVEGGLYTNYTMFREYLHEALNEILGEDVAQHVILKATEDGSGIGSALLAASYSSY 501
|
|
| PLN02914 |
PLN02914 |
hexokinase |
23-531 |
0e+00 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 599.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 23 IVRHRMRSSGrwARAMAILTELEEKCGTPIGKLKQVGDAMTVEMHAGLASEGGSKLKMLISYVDNLPTGDEKGLFYALDL 102
Cdd:PLN02914 25 RSRMAVRSNA--VSVAPILTKLQKDCATPLPVLRHVADAMAADMRAGLAVDGGGDLKMILSYVDSLPSGNEKGLFYALDL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 103 GGTNFRVLRVQLGGNDGRVVNQEFTEVSIPPHLMVGTSDALFDYIAAELAKFVATEGQGFHLSPGRQRELGFTFSFPVRQ 182
Cdd:PLN02914 103 GGTNFRVLRVQLGGKDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFVAKEGGKFHLPEGRKREIGFTFSFPVKQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 183 LTIASGTLIKWTKGFSIDDTVGQDVVAELTKAMERQGLDMRVAALVNDTIGTLAGGRYFNNDVIAAVILGTGTNAAYVER 262
Cdd:PLN02914 183 TSIDSGILMKWTKGFAVSGTAGKDVVACLNEAMERQGLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVER 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 263 AHAIPKWHGLLPKSGEMVINMEWGNFrSSHLPVTEYDHALDVESLNPGEQIFEKIISGMYLGDIVRRVLCRMAEEAAFFG 342
Cdd:PLN02914 263 TDAIPKLQGQKSSSGRTIINTEWGAF-SDGLPLTEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 343 DTVPPKLRVPFILRsaldsllkgmeledlpicwvlfavsqliimgylgiasgmTPDMSAIHHDTTSDLRVVGNKLKDILG 422
Cdd:PLN02914 342 HFVPEKLSTPFALR---------------------------------------TPHLCAMQQDNSDDLQAVGSILYDVLG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 423 ItNTSLKTRKVVVELCNIVATRGARLSAAGIFGILKKLGRDTVREGEKQRTVIAMDGGLFEHYTKFSECLESTLKELLGK 502
Cdd:PLN02914 383 V-EASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDSKGMIFGKRTVVAMDGGLYEKYPQYRRYMQDAVTELLGL 461
|
490 500
....*....|....*....|....*....
gi 1925297022 503 EISESIVIEHSNDGSGIGAALLAASHSQY 531
Cdd:PLN02914 462 ELSKNIAIEHTKDGSGIGAALLAATNSKY 490
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
1-530 |
0e+00 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 552.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 1 MGKVAVGAAIVCGATVCAAAALIVRHRMRSSGRWARAMAILTELEEKCGTPIGKLKQVGDAMTVEMHAGLASEGGSKLKM 80
Cdd:PLN02596 2 MRKEVVVAATVATVAAVAAAVLMGRWKRRKERQWKHTQRILRKFARECATPVSKLWEVADALVSDMTASLTAEETTTLNM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 81 LISYVDNLPTGDEKGLFYALDLGGTNFRVLRVQLGGNDGRVVNQEFTEVSIPPHLMVGTSDALFDYIAAELAKFVATEGQ 160
Cdd:PLN02596 82 LVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNEPISDLYREEISIPSNVLNGTSQELFDYIALELAKFVAEHPG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 161 GFHLSPGRQRELGFTFSFPVRQLTIASGTLIKWtKGFSIDDTVGQDVVAELTKAMERQGLDMRVAALVNDTIGTLAGGRY 240
Cdd:PLN02596 162 DEADTPERVKKLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDINRALEKHGLKIRVFALVDDTIGNLAGGRY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 241 FNNDVIAAVILGTGTNAAYVERAHAIPKWHGLLPKSGEMVINMEWGNFRSSHLPVTEYDHALDVESLNPGEQIFEKIISG 320
Cdd:PLN02596 241 YNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSPSPESQEIVISTEWGNFNSCHLPITEFDASLDAESSNPGSRIFEKLTSG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 321 MYLGDIVRRVLCRMAEEAAFFGDTVPPKLRVPFILRSaldsllkgmeledlpicwvlfavsqliimgylgiasgmtPDMS 400
Cdd:PLN02596 321 MYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRS---------------------------------------PDMA 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 401 AIHHDTTSDLRVVGNKLKDILGITNTSLKTRKVVVELCNIVATRGARLSAAGIFGILKKLGRDtvregEKQRTVIAMDGG 480
Cdd:PLN02596 362 AMHQDTSEDHEVVNEKLKEIFGITDSTPMAREVVAEVCDIVAERGARLAGAGIVGIIKKLGRI-----ENKKSVVTVEGG 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1925297022 481 LFEHYTKFSECLESTLKELLGKEISESIVIEHSNDGSGIGAALLAASHSQ 530
Cdd:PLN02596 437 LYEHYRVFRNYLHSSVWEMLGSELSDNVVIEHSHGGSGAGALFLAACQTG 486
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
54-525 |
1.99e-157 |
|
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: 455.94 E-value: 1.99e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 54 KLKQVGDAMTVEMHAGLASEGGSkLKMLISYVDNLPTGDEKGLFYALDLGGTNFRVLRVQLGGNDGR--VVNQEFTevsI 131
Cdd:cd24018 3 KLEEIVKHFLSEMEKGLEGDGGS-LPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNGGIfiIVQRKYK---I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 132 PPHLMVGTSDALFDYIAAELAKFVATEGQGFHLSPGRqrELGFTFSFPVRQLTIASGTLIKWTKGFSIDDTVGQDVVAEL 211
Cdd:cd24018 79 PDEAKTGTGEELFDFIAECIAEFLEEHNLDLQSDKTI--PLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 212 TKAMERQGLDMRVAALVNDTIGTLAGGRYFNNDVIAAVILGTGTNAAYVERAHAIPKWH---GLLPKSGEMVINMEWGNF 288
Cdd:cd24018 157 QNALDRRGVNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTspsGSVTKSDEMIINTEWGAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 289 RSSH--LPVTEYDHALDVESLNPGEQIFEKIISGMYLGDIVRRVLCRMAEEAAFFGDTVPPKLRVPFILRSALdsllkgm 366
Cdd:cd24018 237 DNERevLPLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAF------- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 367 eledlpicwvlfavsqliimgylgiasgmtpdMSAIHHDTTSDLRVVGNKLKDILGITNTSLKTRKVVVELCNIVATRGA 446
Cdd:cd24018 310 --------------------------------LSRIEADTSPDLDAVRDILKELLAIDNTTLEDRKLIKRICELVSTRAA 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1925297022 447 RLSAAGIFGILKKLGRDtvregEKQRTVIAMDGGLFEHYTKFSECLESTLKELLGKEISESIVIEHSNDGSGIGAALLA 525
Cdd:cd24018 358 RLSAAAIAAILLKRGSL-----LPEPVTVGIDGSVYEKYPGFKDRLSEALRELFGPEVKANISLVLAKDGSGLGAAIIA 431
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
54-526 |
6.36e-142 |
|
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: 416.17 E-value: 6.36e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 54 KLKQVGDAMTVEMHAGLASEG--GSKLKMLISYVDNLPTGDEKGLFYALDLGGTNFRVLRVQLggNDGRVVNQEFTEVSI 131
Cdd:cd24019 6 QLEEIMDRLLKEMEKGLSKDThpTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTL--NGGSQVKMESEIYAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 132 PPHLMVGTSDALFDYIAAELAKFVATEGqgfhLSpGRQRELGFTFSFPVRQLTIASGTLIKWTKGFSIDDTVGQDVVAEL 211
Cdd:cd24019 84 PEEIMTGTGEQLFDYIAECLAEFLEKNG----LK-DKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 212 TKAMERQGL-DMRVAALVNDTIGTLAGGRYFNNDVIAAVILGTGTNAAYVERAHAIPKWHGLLPKSGEMVINMEWGNFRS 290
Cdd:cd24019 159 QEAIKRRGDiKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKWDGDEGDPGQVIINTEWGAFGD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 291 SH---LPVTEYDHALDVESLNPGEQIFEKIISGMYLGDIVRRVLCRMAEEAAFFGDTVPPKLRVPFILRsaldsllkgme 367
Cdd:cd24019 239 NGvldFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFE----------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 368 ledlpicwvlfavsqliimgylgiasgmTPDMSAIHHDTTSDLRVVGNKLKDiLGITNTSLKTRKVVVELCNIVATRGAR 447
Cdd:cd24019 308 ----------------------------TKYVSEIESDNEGDFSNTREILKE-LGLEDASDEDCEIVRYVCEAVSTRAAQ 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1925297022 448 LSAAGIFGILKKLGRdtvregekQRTVIAMDGGLFEHYTKFSECLESTLKELLGKEISESIVieHSNDGSGIGAALLAA 526
Cdd:cd24019 359 LVAAGIAALLNRMNR--------KEVTVGVDGSLYKYHPKFHKRMHETLKELVPPGCKFKLM--LSEDGSGKGAALVAA 427
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
55-525 |
3.29e-119 |
|
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: 355.43 E-value: 3.29e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 55 LKQVGDAMTVEMHAGLASEGGSkLKMLISYVDNLPTGDEKGLFYALDLGGTNFRVLRVQLGGNDGRVVNQEftEVSIPPH 134
Cdd:cd24000 4 LKEITDAFLEELEKGLAGEPSS-LKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGKGIEVTISK--KYEIPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 135 LMVGTSDALFDYIAAELAKFVATEGQGFHLSpgrqreLGFTFSFPVRQLTIASGTLIKWTKGFSIDDTVGQDVVAELTKA 214
Cdd:cd24000 81 IKTASAEEFFDFIADCIAEFLKENGLKKPLP------LGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 215 MERQGLDMRVAALVNDTIGTLAGGRYFNNDVIAAVILGTGTNAAYVERAHAIpkwhglLPKSGEMVINMEWGNFRSSHLP 294
Cdd:cd24000 155 LKKRGLPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNI------LLGDGGMIINTEWGNFGKNSLP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 295 VTEYDHALDVESLNPGEQIFEKIISGMYLGDIVRRVLCRMAEEaaffgdtvppklrvpfilrsaldsllkgmeledlpic 374
Cdd:cd24000 229 RTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 375 wvlfavsqliimgylgiasgmtpdmsaihhdttsdlrvvgnklkdilgitntslktrkVVVELCNIVATRGARLSAAGIF 454
Cdd:cd24000 272 ----------------------------------------------------------ILRKICELVAERSARLAAAAIA 293
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1925297022 455 GILKKLGRDTvregeKQRTVIAMDGGLFEHYTKFSECLESTLKELLGKEIseSIVIEHSNDGSGIGAALLA 525
Cdd:cd24000 294 ALLRKTGDSP-----EKKITIAVDGSLFEKYPGYRERLEEYLKELLGRGI--RIELVLVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
54-525 |
4.91e-118 |
|
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: 355.94 E-value: 4.91e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 54 KLKQVGDAMTVEMHAGLASEGGSkLKMLISYVDNLPTGDEKGLFYALDLGGTNFRVLRVQLGGNDGRVVNQEftEVSIPP 133
Cdd:cd24088 3 KLDKLTAEFQRQMEKGLAKHGKG-MAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHGDGTFSLRQE--KSKIPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 134 HLMVG-TSDALFDYIAAELAKFVATEGqGFHLSPGRQRE---LGFTFSFPVRQLTIASGTLIKWTKGFSIDDTVGQDVVA 209
Cdd:cd24088 80 ELKTGvTAKDLFDYLAKSVEAFLTKHH-GDSFAAGKDDDrlkLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 210 ELTKAMERQGLDMRVAALVNDTIGTLAGGRYFNNDVIAAV---ILGTGTNAAYVERAHAIPKwhgLLPKS------GEMV 280
Cdd:cd24088 159 LLQDELDRQGIPVKVVALVNDTVGTLLARSYTSPEISGAVlgaIFGTGTNGAYLEDLEKIKK---LDDSSrvgkgkTHMV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 281 INMEWGNFRS--SHLPVTEYDHALDVESLNPGEQIFEKIISGMYLGDIVRRVLCRMAEEAAFFG---DTVPPKLRVPFIL 355
Cdd:cd24088 236 INTEWGSFDNelKVLPTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFLIqynDKSPSALNTPYGL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 356 RSALdsllkgmeledlpicwvlfavsqliimgylgiasgmtpdMSAIHHDTTSDLRVVGNKLKDILGITNTSLKTRKVVV 435
Cdd:cd24088 316 DTAV---------------------------------------LSAIEIDSEAELRATRKVLLDDLGLPAPSLEDAEAVR 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 436 ELCNIVATRGARLSAAGIFGILKKLGRdtVREGEKQRTVIAMDGGLFEHYTKFSECLESTLKELL-GKEISESIVIEHSN 514
Cdd:cd24088 357 KISRAIGRRAARLSAVAIAAILIKTGA--LNKSYDGEINIGVDGSVIEFYPGFESMLREALRLLLiGAEGEKRIKIGIAK 434
|
490
....*....|.
gi 1925297022 515 DGSGIGAALLA 525
Cdd:cd24088 435 DGSGVGAALCA 445
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
54-526 |
1.87e-115 |
|
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: 348.60 E-value: 1.87e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 54 KLKQVGDAMTVEMHAGLASEGGSkLKMLISYVDNLPTGDEKGLFYALDLGGTNFRVLRVQLGGNDGRVVNQefTEVSIPP 133
Cdd:cd24087 3 RLRKITDHFISELEKGLSKKGGN-IPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNGKFDITQ--SKYRLPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 134 HLMVGTSDALFDYIAAELAKFVATEgqgFHLSPGRQRELGFTFSFPVRQLTIASGTLIKWTKGFSIDDTVGQDVVAELTK 213
Cdd:cd24087 80 ELKTGTGEELWDFIADCLKKFVEEH---FPGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 214 AMERQGLDMRVAALVNDTIGTLAGGRYFNNDVIAAVILGTGTNAAYVERAHAIPKWHGL-LPKSGEMVINMEWGNFRSSH 292
Cdd:cd24087 157 ALKKRNVPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEHDdIPPDSPMAINCEYGAFDNEH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 293 --LPVTEYDHALDVESLNPGEQIFEKIISGMYLGDIVRRVLCRMAEEAAFFGDTVPPKLRVPFILRSALdsllkgmeled 370
Cdd:cd24087 237 lvLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSF----------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 371 lpicwvlfavsqliimgylgiasgmtpdMSAIHHDTTSDLRVVGNKLKDILGItNTSLKTRKVVVELCNIVATRGARLSA 450
Cdd:cd24087 306 ----------------------------LSRIEEDPFENLEDTDDLFQHFFGL-ETTVPERKFIRRLAELIGTRAARLSA 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1925297022 451 AGIFGILKKLGrdtvregeKQRTVIAMDGGLFEHYTKFSECLESTLKELLGKEISES-IVIEHSNDGSGIGAALLAA 526
Cdd:cd24087 357 CGIAAICKKRG--------YKTCHVAADGSVYNKYPGFKERAAQALKDIFGWDGEDDpIKTVPAEDGSGVGAAIIAA 425
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
246-527 |
2.98e-99 |
|
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: 299.79 E-value: 2.98e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 246 IAAVILGTGTNAAYVERAHAIPKWHGLLPKSGEMVINMEWGNFRSSH---LPVTEYDHALDVESLNPGEQIFEKIISGMY 322
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKLPKSGEMIINTEWGAFGDNGllpLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 323 LGDIVRRVLCRMAEEAAFFGDtVPPKLRVPFILRsaldsllkgmeledlpicwvlfavsqliimgylgiasgmTPDMSAI 402
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKG-QSEKLKTPYSLD---------------------------------------TSFLSAI 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 403 HHDTTSDLRVVGNKLKDILGITNTSLKTRKVVVELCNIVATRGARLSAAGIFGILKKLGRDTvregekqRTVIAMDGGLF 482
Cdd:pfam03727 121 ESDPSEDLETTREILEELLGIETVTEEDRKIVRRICEAVSTRAARLVAAGIAAILKKIGRDK-------KVTVGVDGSVY 193
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1925297022 483 EHYTKFSECLESTLKELLGKEIseSIVIEHSNDGSGIGAALLAAS 527
Cdd:pfam03727 194 EKYPGFRERLQEALRELLGPGD--KVVLVLAEDGSGVGAALIAAV 236
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
54-526 |
4.05e-98 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 305.06 E-value: 4.05e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 54 KLKQVGDAMTVEMHAGLASEGG---------SKLKMLISYVDNLPTGDEKGLFYALDLGGTNFRVLRVQLGGNDGRVVNQ 124
Cdd:PTZ00107 24 KLKELVDYFLYELVEGLEAHRRhrnlwipneCSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFRAVRVSLRGGGKMERTQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 125 E-----FTEVSIPPHLMVGTSDA--LFDYIAAELAKFVatEGQGFHLSPGRQRELGFTFSFPVRQLTIASGTLIKWTKGF 197
Cdd:PTZ00107 104 SkfslpKSALLGEKGLLDKKATAtdLFDHIAKSIKKMM--EENGDPEDLNKPVPVGFTFSFPCTQLSVNNAILIDWTKGF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 198 S----IDDTV-GQDVVAELTKAMERQGLDMRVAALVNDTIGTLAGGRYF----NNDVIAAVILGTGTNAAYVERAHAIPK 268
Cdd:PTZ00107 182 EtgraTNDPVeGKDVGELLNDAFKRNNVPANVVAVLNDTVGTLISCAYQkpknTPPCQVGVIIGTGSNACYFEPEVSAYG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 269 WHGllpksgeMVINMEWGNFrSSHLPVTEYDHALDVESLNPGEQIFEKIISGMYLGDIVRRVLCRMAEEAAffgdtvppk 348
Cdd:PTZ00107 262 YAG-------TPINMECGNF-DSKLPITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLLQLKA--------- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 349 lrvpfilrsaldsllkgmeledLPICWVlfavsqliimgylgIASGMTPDMSAIHHDTTSDLRVVGNKLKDILGI--TNT 426
Cdd:PTZ00107 325 ----------------------PPKMWQ--------------SGSFESEDASMILNDQSPDLQFSRQVIKEAWDVdlTDE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 427 SLKTRKvvvELCNIVATRGARLSAAGIFGILKKLGRDTvregekQRTVIAMDGGLFEHYTKFSECLESTLKELLGKEIsE 506
Cdd:PTZ00107 369 DLYTIR---KICELVRGRAAQLAAAFIAAPAKKTRTVQ------GKATVAIDGSVYVKNPWFRRLLQEYINSILGPDA-G 438
|
490 500
....*....|....*....|
gi 1925297022 507 SIVIEHSNDGSGIGAALLAA 526
Cdd:PTZ00107 439 NVVFYLADDGSGKGAAIIAA 458
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
40-240 |
8.31e-95 |
|
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: 287.09 E-value: 8.31e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 40 ILTELEEKCGTPIGKLKQVGDAMTVEMHAGLASEGGSKLKMLISYVDNLPTGDEKGLFYALDLGGTNFRVLRVQLGGNDG 119
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGGDGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 120 RVVNQEftEVSIPPHLMVGTSDALFDYIAAELAKFVATEGQGFHlsPGRQRELGFTFSFPVRQLTIASGTLIKWTKGFSI 199
Cdd:pfam00349 81 FEITQE--KYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDF--EEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1925297022 200 DDTVGQDVVAELTKAMERQGLDMRVAALVNDTIGTLAGGRY 240
Cdd:pfam00349 157 PGVVGKDVVQLLQEALERRGLPVKVVALVNDTVGTLMAGAY 197
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
54-526 |
1.76e-90 |
|
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: 284.36 E-value: 1.76e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 54 KLKQVGDAMTVEMHAGLASEGG--SKLKMLISYVDNLPTGDEKGLFYALDLGGTNFRVLRVQLGGNDGRVVNQEFTEVSI 131
Cdd:cd24089 6 TLLDISRRFRKEMEKGLGKDTHptATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMESQVYAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 132 PPHLMVGTSDALFDYIAAELAKFVatEGQGFHlspGRQRELGFTFSFPVRQLTIASGTLIKWTKGFSIDDTVGQDVVAEL 211
Cdd:cd24089 86 PEEIMHGSGTQLFDHVAECLADFM--DKQKIK---DKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 212 TKAMERQG-LDMRVAALVNDTIGTLAGGRYFNNDVIAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNF-- 288
Cdd:cd24089 161 RKAIRRRGdYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEG---DEGRMCINTEWGAFgd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 289 -RSSHLPVTEYDHALDVESLNPGEQIFEKIISGMYLGDIVRRVLCRMAEEAAFFGDTVPPKLrvpfilrsaldsLLKGmE 367
Cdd:cd24089 238 dGSLEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPEL------------LTRG-K 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 368 LEdlpicwvlfavsqliimgylgiasgmTPDMSAIHHDTTSdLRVVGNKLKDiLGItNTSLKTRKVVVELCNIVATRGAR 447
Cdd:cd24089 305 FE--------------------------TKDVSAIEKEKEG-LANAKEILTR-LGL-DPSEDDCVNVQHVCTIVSFRSAN 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1925297022 448 LSAAGIFGILKKLGRDtvREGEKQRTVIAMDGGLFEHYTKFSECLESTLKeLLGKEISESIVIehSNDGSGIGAALLAA 526
Cdd:cd24089 356 LCAATLAAILTRLREN--KGLERLRTTVGVDGSVYKKHPQFSKRLHKAVR-RLVPDCDVRFLL--SEDGSGKGAAMVTA 429
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
65-527 |
6.54e-90 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 283.00 E-value: 6.54e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 65 EMHAGLASEGGSkLKMLISYVdNLPTG-DEKGLFYALDLGGTNFRVLRVQLGGNDGRVVNQEFTevsippHLMVGTS--- 140
Cdd:COG5026 32 EMEKGLEGKKSS-LKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRFDGEGTFEIENFKS------FPLPGTSsei 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 141 --DALFDYIAAELAKFVategqgfhlspGRQRELGFTFSFPVRQLTIASGTLIKWTKGFSIDDTVGQDVVAELTKAMERQ 218
Cdd:COG5026 104 taEEFFDFIADYIEPLL-----------DESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNIGELLEAALARK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 219 GLD-MRVAALVNDTIGTLAGGRY----FNNDVIAAVILGTGTNAAYVERAHAIPKwhgLLPKSGEMVINMEWGNFrsSHL 293
Cdd:COG5026 173 GLDnVKPVAILNDTVATLLAGAYadpdDGYSGYIGSILGTGHNTCYLEPNAPIGK---LPAYEGPMIINMESGNF--NKL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 294 PVTEYDHALDVESLNPGEQIFEKIISGMYLGDIVRRVLCRMAEEAAFFGDtVPPKLRVPFILRSAldsllkgmeledlpi 373
Cdd:COG5026 248 PRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEGLFSPG-FSEVFETPYSLTTV--------------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 374 cwvlfavsqliimgylgiasgmtpDMSAIHHDTTSDLRVVGNKLKDilgitnTSLKTRKVVVELCNIVATRGARLSAAGI 453
Cdd:COG5026 312 ------------------------DMSRFLADPSDEKEILSQCLEA------GSEEDREILREIADAIVERAARLVAATL 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1925297022 454 FGILKKLGRDtvrEGEKQRTVIAMDGGLFEHYTKFSECLESTLKELLGKEISESIVIEHSNDGSGIGAALLAAS 527
Cdd:COG5026 362 AGILLHLGPG---KTPLKPHCIAIDGSTYEKMPGLAEKIEYALQEYLLGEKGRYVEFVLVENASLLGAAIAAAL 432
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
54-526 |
3.78e-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: 267.87 E-value: 3.78e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 54 KLKQVGDAMTVEMHAGLASE--GGSKLKMLISYVDNLPTGDEKGLFYALDLGGTNFRVLRVQLGGNDGRVVNQEFTEVSI 131
Cdd:cd24091 6 QLLEVKARMRAEMERGLRKEthASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHNKIYAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 132 PPHLMVGTSDALFDYIAAELAKFVATEGQgfhlsPGRQRELGFTFSFPVRQLTIASGTLIKWTKGFSIDDTVGQDVVAEL 211
Cdd:cd24091 86 PQEIMQGTGEELFDHIVQCIADFLEYMGL-----KGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 212 TKAME-RQGLDMRVAALVNDTIGTLAGGRYFNNDVIAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNFRS 290
Cdd:cd24091 161 REAIKrREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEG---EEGRMCINMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 291 S----HLpVTEYDHALDVESLNPGEQIFEKIISGMYLGDIVRRVLCRMAEEAAFFGDTVPPKLRVPFILRsaldsllkgm 366
Cdd:cd24091 238 NgcldDI-RTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFE---------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 367 eledlpicwvlfavsqliimgylgiasgmTPDMSAIHHDTTSdLRVVGNKLKDiLGITNTSlKTRKVVVELCNIVATRGA 446
Cdd:cd24091 307 -----------------------------TKFLSQIESDRLA-LLQVRAILQQ-LGLDSTC-DDSIIVKEVCGVVSRRAA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 447 RLSAAGIFGILKKLGRDtvREGEKQRTVIAMDGGLFEHYTKFSECLESTLKELLGKEIsesIVIEHSNDGSGIGAALLAA 526
Cdd:cd24091 355 QLCGAGMAAVVDKIREN--RGLDHLNVTVGVDGTLYKLHPHFSRVMHETVKELAPKCD---VTFLQSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
54-526 |
4.16e-83 |
|
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: 265.21 E-value: 4.16e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 54 KLKQVGDAMTVEMHAGLASE--GGSKLKMLISYVDNLPTGDEKGLFYALDLGGTNFRVLRVQLGGNDGRVVNQEFTevsI 131
Cdd:cd24129 6 QLAAVQAQMRKEMAKGLRGEthAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTAGVQITSEIYS---I 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 132 PPHLMVGTSDALFDYIAAELAKFVATEGqgfhLSpGRQRELGFTFSFPVRQLTIASGTLIKWTKGFSIDDTVGQDVVAEL 211
Cdd:cd24129 83 PETVAQGTGQQLFDHIVDCIVDFQQKQG----LS-GQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 212 TKAMER-QGLDMRVAALVNDTIGTLAGGRYFNNDVIAAVILGTGTNAAYVERAHAIpkwhGLLP-KSGEMVINMEWGNF- 288
Cdd:cd24129 158 REAATRkQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNV----AGVPgDSGRMCINMEWGAFg 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 289 --RSSHLPVTEYDHALDVESLNPGEQIFEKIISGMYLGDIVRRVLCRMAEEAAFFGDTVPPKLRVPFILRSALdsllkgm 366
Cdd:cd24129 234 dnGCLAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKF------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 367 eledlpicwvlfavsqliimgylgiasgmtpdMSAIHHDTTSdLRVVGNKLKDiLGITNTSLKTRkVVVELCNIVATRGA 446
Cdd:cd24129 307 --------------------------------LSEIESDSLA-LRQVRAILED-LGLPLTSDDAL-LVLEVCQTVSQRAA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 447 RLSAAGIFGILKKLGRDtvREGEKQRTVIAMDGGLFEHYTKFSECLESTLKELLGKEIsesIVIEHSNDGSGIGAALLAA 526
Cdd:cd24129 352 QLCAAGVAAVVEKMREN--RGLDELAVTVGVDGTLYKLHPRFSSLVQATVRELAPRCV---VTFLQSEDGSGKGAALVTA 426
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
55-526 |
3.06e-80 |
|
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: 257.86 E-value: 3.06e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 55 LKQVGDAMTVEMHAGLASEGGSK--LKMLISYVDNLPTGDEKGLFYALDLGGTNFRVLRVQLGGNDGRVVNQEFTEVSIP 132
Cdd:cd24126 7 LLDIMTRFRAEMEKGLAKDTNPTaaVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMESQFYPTP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 133 PHLMVGTSDALFDYIAAELAKFVATEGQGFHLSPgrqreLGFTFSFPVRQLTIASGTLIKWTKGFSIDDTVGQDVVAELT 212
Cdd:cd24126 87 EEIIHGTGTELFDYVAECLADFMKKKGIKHKKLP-----LGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 213 KAMERQG-LDMRVAALVNDTIGTLAGGRYFNNDVIAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNFRSS 291
Cdd:cd24126 162 KAIRKHKdVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEG---DEGRMCINTEWGAFGDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 292 HLP---VTEYDHALDVESLNPGEQIFEKIISGMYLGDIVRRVLCRMAEEAAFFGDTVPPKLRVPFILRS----ALDSLLK 364
Cdd:cd24126 239 GSLediRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETkhvaAIEKYKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 365 GME-----LEDLpicwvlfavsqliimgylgiasGMTP---DMSAIHHdttsdlrvvgnklkdilgitntslktrkvvve 436
Cdd:cd24126 319 GLYntreiLSDL----------------------GLEPseeDCIAVQH-------------------------------- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 437 LCNIVATRGARLSAAGIFGILKKLgrdtvREGEKQ---RTVIAMDGGLFEHYTKFSECLESTLKELLGkeiSESIVIEHS 513
Cdd:cd24126 345 VCTIVSFRSANLCAAALAAILTRL-----RENKKLerlRTTVGMDGTVYKTHPQYAKRLHKVVRRLVP---SCDVRFLLS 416
|
490
....*....|...
gi 1925297022 514 NDGSGIGAALLAA 526
Cdd:cd24126 417 ESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
54-526 |
7.39e-77 |
|
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: 249.08 E-value: 7.39e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 54 KLKQVGDAMTVEMHAGLASE--GGSKLKMLISYVDNLPTGDEKGLFYALDLGGTNFRVLRVQL--GGNDGRVVNQEFtev 129
Cdd:cd24130 6 QLQEVKQKMRTELEYGLKKEthPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIrsGRRSVRMYNKIF--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 130 SIPPHLMVGTSDALFDYIAAELAKFVATEGQgfhlsPGRQRELGFTFSFPVRQLTIASGTLIKWTKGFSIDDTVGQDVVA 209
Cdd:cd24130 83 AIPLEIMQGTGEELFDHIVQCIADFLDYMGL-----KGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 210 ELTKAMERQG-LDMRVAALVNDTIGTLAGGRYFNNDVIAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNF 288
Cdd:cd24130 158 MLREAIKRRNeFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEG---DEGRMCINTEWGGF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 289 RSSHL---PVTEYDHALDVESLNPGEQIFEKIISGMYLGDIVRRVLCRMAEEAAFFGDTVPPKLRVPFILRSaldSLLKG 365
Cdd:cd24130 235 GDNGCiddIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFET---KFLSQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 366 MELEDLPICWVLFAVSQLiimgylgiasGMtpdmsaihhDTTSDLRVvgnklkdilgitntslktrkVVVELCNIVATRG 445
Cdd:cd24130 312 IESDRLALLQVRRILQQL----------GL---------DSTCEDSI--------------------IVKEVCGAVSRRA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 446 ARLSAAGIFGILKKLGRDtvREGEKQRTVIAMDGGLFEHYTKFSECLESTLKELLGKeisESIVIEHSNDGSGIGAALLA 525
Cdd:cd24130 353 AQLCGAGLAAIVEKIREN--QGLDRLDITVGVDGTLYKLHPHFSRILQETVKELAPQ---CDVTFMLSEDGSGKGAALIT 427
|
.
gi 1925297022 526 A 526
Cdd:cd24130 428 A 428
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
54-526 |
1.95e-76 |
|
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: 247.89 E-value: 1.95e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 54 KLKQVGDAMTVEMHAGLASE--GGSKLKMLISYVDNLPTGDEKGLFYALDLGGTNFRVLRVQLGGNDGRVVNQEFTEVSI 131
Cdd:cd24128 6 QLLEVKRRMKVEMERGLSKEthASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHNKIYAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 132 PPHLMVGTSDALFDYIAAELAKFVATEGQgfhlsPGRQRELGFTFSFPVRQLTIASGTLIKWTKGFSIDDTVGQDVVAEL 211
Cdd:cd24128 86 PQEVMHGTGEELFDHIVHCIADFLEYMGM-----KGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 212 TKAMER-QGLDMRVAALVNDTIGTLAGGRYFNNDVIAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNFRS 290
Cdd:cd24128 161 KEAIHRrEEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEG---EEGRMCVNMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 291 SHLP---VTEYDHALDVESLNPGEQIFEKIISGMYLGDIVRRVLCRMAEEAAFFGDTVPPKLRVPFILRSaldSLLKGME 367
Cdd:cd24128 238 NGCLddfRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFET---KFLSQIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 368 LEDLPICWVlfavsqLIIMGYLGIASgmTPDMSAIhhdttsdlrvvgnklkdilgitntslktrkvVVELCNIVATRGAR 447
Cdd:cd24128 315 SDRLALLQV------RAILQHLGLES--TCDDSII-------------------------------VKEVCTVVARRAAQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 448 LSAAGIFGILKKLGRDtvREGEKQRTVIAMDGGLFEHYTKFSECLESTLKELLGK-EISesivIEHSNDGSGIGAALLAA 526
Cdd:cd24128 356 LCGAGMAAVVDKIREN--RGLDALKVTVGVDGTLYKLHPHFAKVMHETVKDLAPKcDVS----FLQSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
55-526 |
2.28e-75 |
|
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of type II hexokinase.
Pssm-ID: 466975 [Multi-domain] Cd Length: 429 Bit Score: 245.19 E-value: 2.28e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 55 LKQVGDAMTVEMHAGLASEGG--SKLKMLISYVDNLPTGDEKGLFYALDLGGTNFRVLRVQLGGNDGRVVNQEFTEVSIP 132
Cdd:cd24125 7 LLEISKRFRKEMEKGLGATTHptAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMENQIYAIP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 133 PHLMVGTSDALFDYIAAELAKFVATEGqgfhlSPGRQRELGFTFSFPVRQLTIASGTLIKWTKGFSIDDTVGQDVVAELT 212
Cdd:cd24125 87 EDIMRGSGTQLFDHIAECLANFMDKLQ-----IKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 213 KAMERQG-LDMRVAALVNDTIGTLAGGRYFNNDVIAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNFRSS 291
Cdd:cd24125 162 KAIQKRGdFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEG---DEGRMCINMEWGAFGDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 292 HL---PVTEYDHALDVESLNPGEQIFEKIISGMYLGDIVRRVLCRMAEEAAFFGDTVPPklrvpfilrsaldsllkgmel 368
Cdd:cd24125 239 GSlddIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSP--------------------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 369 edlpicwvlfavsQLIIMGYLgiasgMTPDMSAIHHDttSDLRVVGNKLKDILGITNT---SLKTRKVvvelCNIVATRG 445
Cdd:cd24125 298 -------------ELLNTGHF-----ETKDVSDIEGE--KDGIRKAREVLMRLGLDPTqedCVATHRI----CQIVSTRS 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 446 ARLSAAGIFGILKKLGRDtvREGEKQRTVIAMDGGLFEHYTKFSECLESTLKELLGkeiSESIVIEHSNDGSGIGAALLA 525
Cdd:cd24125 354 ASLCAATLAAVLQRIKEN--KGEERLRSTIGVDGSVYKKHPHFARRLHKTVRRLVP---GCDVRFLRSEDGSGKGAAMVT 428
|
.
gi 1925297022 526 A 526
Cdd:cd24125 429 A 429
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
54-526 |
4.14e-74 |
|
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: 241.74 E-value: 4.14e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 54 KLKQVGDAMTVEMHAGLASE--GGSKLKMLISYVDNLPTGDEKGLFYALDLGGTNFRVLRVQLGGNDGRVVNQEFTEVSI 131
Cdd:cd24127 6 MLLEVKKRMRAEMELGLRKQthNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 132 PPHLMVGTSDALFDYIAAELAKFVATEGQgfhlsPGRQRELGFTFSFPVRQLTIASGTLIKWTKGFSIDDTVGQDVVAEL 211
Cdd:cd24127 86 PIEIMQGTGEELFDHIVSCISDFLDYMGI-----KGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 212 TKAME-RQGLDMRVAALVNDTIGTLAGGRYFNNDVIAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNFRS 290
Cdd:cd24127 161 RDAIKrREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEG---DQGQMCINMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 291 SHL---PVTEYDHALDVESLNPGEQIFEKIISGMYLGDIVRRVLCRMAEEAAFFGDTVPPKLRVPFILRSaldSLLKGME 367
Cdd:cd24127 238 NGClddIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFET---KFLSQIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 368 LEDLPICWVLFAVSQLIImgylgiasgmtpdmsaihhDTTSDLRVvgnklkdilgitntslktrkVVVELCNIVATRGAR 447
Cdd:cd24127 315 SDRLALLQVRAILQQLGL-------------------NSTCDDSI--------------------LVKTVCGVVSRRAAQ 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1925297022 448 LSAAGIFGILKKLGRDtvREGEKQRTVIAMDGGLFEHYTKFSECLESTLKELLGKeisESIVIEHSNDGSGIGAALLAA 526
Cdd:cd24127 356 LCGAGMAAVVDKIREN--RGLDHLNVTVGVDGTLYKLHPHFSRIMHQTVKELSPK---CNVSFLLSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
65-526 |
2.79e-72 |
|
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: 238.36 E-value: 2.79e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 65 EMHAGLASEGG--SKLKMLISYVDNLPTGDEKGLFYALDLGGTNFRVLRVQLGGNDGRVVNQEFTEVSIPPHLMVGTSDA 142
Cdd:cd24124 45 EMKNGLSRDFNptATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVHGSGSQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 143 LFDYIAAELAKFVatEGQGFHlspGRQRELGFTFSFPVRQLTIASGTLIKWTKGFSIDDTVGQDVVAELTKAMERQG-LD 221
Cdd:cd24124 125 LFDHVAECLGDFM--EKRKIK---DKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLNKAIKKRGdYD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 222 MRVAALVNDTIGTLAGGRYFNNDVIAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNFR---SSHLPVTEY 298
Cdd:cd24124 200 ANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEG---DEGRMCINTEWGAFGddgSLEDIRTEF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 299 DHALDVESLNPGEQIFEKIISGMYLGDIVRRVLCRMAEEAAFFGDTVPPKLrvpfilrsaldsLLKGmELEdlpicwvlf 378
Cdd:cd24124 277 DREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPEL------------LTRG-KFN--------- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 379 avsqliimgylgiasgmTPDMSAIHHDTTSDlrvvgNKLKDI---LGItNTSLKTRKVVVELCNIVATRGARLSAAGIFG 455
Cdd:cd24124 335 -----------------TSDVSAIEKNKEGL-----HNAKEIltrLGV-EPSDDDCVSVQHVCTIVSFRSANLVAATLGA 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1925297022 456 ILKKLgRDTvREGEKQRTVIAMDGGLFEHYTKFSECLESTLKELLGKEISESIViehSNDGSGIGAALLAA 526
Cdd:cd24124 392 ILNRL-RDN-KGTPRLRTTVGVDGSLYKTHPQYSRRFHKTLRRLVPDSDVRFLL---SESGSGKGAAMVTA 457
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
55-526 |
9.63e-71 |
|
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: 233.23 E-value: 9.63e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 55 LKQVGDAMTVEMHAGLASEG--GSKLKMLISYVDNLPTGDEKGLFYALDLGGTNFRVLRVQLGGNDGR--VVNQEFTEVS 130
Cdd:cd24092 16 LKKVMRRMQKEMDRGLRLETheEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGqwSVKTKHQMYS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 131 IPPHLMVGTSDALFDYIAAELAKFVATegqgfHLSPGRQRELGFTFSFPVRQLTIASGTLIKWTKGFSIDDTVGQDVVAE 210
Cdd:cd24092 96 IPEDAMTGTAEMLFDYISECISDFLDK-----HQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVGL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 211 LTKAMERQG-LDMRVAALVNDTIGTLAGGRYFNNDVIAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNF- 288
Cdd:cd24092 171 LRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEG---DEGRMCVNTEWGAFg 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 289 RSSHLP--VTEYDHALDVESLNPGEQIFEKIISGMYLGDIVRRVLCRMAEEAAFFGDTVPPKLRVpfilRSALDsllkgm 366
Cdd:cd24092 248 DSGELDefLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRT----RGAFE------ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 367 eledlpicwvlfavsqliimgylgiasgmTPDMSAIHHDtTSDLRVVGNKLKdILGITNTSLKTrKVVVELCNIVATRGA 446
Cdd:cd24092 318 -----------------------------TRFVSQVESD-TGDRKQIYNILS-TLGLRPSTTDC-DIVRRACESVSTRAA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 447 RLSAAGIFGILKKLgRDTVREgEKQRTVIAMDGGLFEHYTKFSECLESTLKELLGkeiSESIVIEHSNDGSGIGAALLAA 526
Cdd:cd24092 366 HMCSAGLAGVINRM-RESRSE-DVMRITVGVDGSVYKLHPSFKERFHASVRRLTP---SCEITFIESEEGSGRGAALVSA 440
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
51-526 |
1.24e-68 |
|
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: 227.50 E-value: 1.24e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 51 PIGKLKQVGDAMTVEMHAGLASEGG--SKLKMLISYVDNLPTGDEKGLFYALDLG--GTNFRVLRVQLGGNDGRVVNQEF 126
Cdd:cd24090 3 TRAQLQQIQASLLGSMEQALRGQASpaPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 127 TEVSIPPHLMVGTSDALFDYIAAELAKFVATEGqgfhlSPGRQRELGFTFSFPVRQLTIASGTLIKWTKGFSIDDTVGQD 206
Cdd:cd24090 83 QEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQP-----VPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 207 VVAELTKAMERQGL-DMRVAALVNDTIGTLAGGRYFNNDVIAAVILGTGTNAAYVERAHAIPKwhgLLPKSGEMVINMEW 285
Cdd:cd24090 158 VVQLLRDAIQRQGAyNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAV---LDEDRGRVCVSVEW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 286 GNF--RSSHLPV-TEYDHALDVESLNPGEQIFEKIISGMYLGDIVRRVLCRMAEEAAFFGDTVPPKLRVPFILRsaldsL 362
Cdd:cd24090 235 GSFsdDGALGPVlTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSIL-----L 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 363 LKGMELEDlpicwvlfavsqliimgylgIASGMtpdmsAIHHDTTSDLRVvgnklkdilgitNTSLKTRKVVVELCNIVA 442
Cdd:cd24090 310 EHVAEMED--------------------PSAGA-----ARVRAILQDLGL------------SPSASDVELVQHVCRAVC 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1925297022 443 TRGARLSAAGIFGILKKLGRDtvREGEKQRTVIAMDGGLFEHYTKFSECLESTLKeLLGKEISESIVieHSNDGSGIGAA 522
Cdd:cd24090 353 TRAAQLCAAALAAVLSHLQHS--REQQTLQVAVATGGRVCERHPRFCSILQGTVM-LLAPECDVSFI--PSVDGGGRGVA 427
|
....
gi 1925297022 523 LLAA 526
Cdd:cd24090 428 MVTA 431
|
|
| |
