|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02405 |
PLN02405 |
hexokinase |
1-497 |
0e+00 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 935.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 1 MGKVAVGATVVCAAAVCAAAVFIVRRRMQSSGKWARVIEILRVLEEDCATPIAKLKQVADAMTVEMHAGLASEGGSKLKM 80
Cdd:PLN02405 1 MGKVAVGAAVVCAAAVCAAAALVVRRRMKSSGKWARAMEILKEFEEDCATPIGKLRQVADAMTVEMHAGLASEGGSKLKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 81 LISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEFEEVSIPPHLMTGGSDELFNFIAEALAKFVATEGE 160
Cdd:PLN02405 81 LISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVSIPPHLMTGSSDALFDFIAAALAKFVATEGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 161 DFHLPAGRQRELGFTFSFPVRQTSLSSGTLIKWTKGFSIEDTVGADVVGELVKAMERVGLDMNVTALVNDTVGTLAGGRY 240
Cdd:PLN02405 161 DFHLPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMERVGLDMRVSALVNDTIGTLAGGRY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 241 YNSDVVAAVILGTGTNAAYVERAHAIPKWHGLLPKSGEMVINMEWGNFRSSHLPLTEYDHSLDFESLNPGEQILEKIISG 320
Cdd:PLN02405 241 YNPDVVAAVILGTGTNAAYVERAQAIPKWHGLLPKSGEMVINMEWGNFRSSHLPLTEYDHALDVESLNPGEQIFEKIISG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 321 MYLGEILRRVLLKMAEEAAFFGDTIPQKLRIPFIIRTPHMSAMHSDTSPDLKVVGSKLKDILEVSTTSLKMRKVVISICN 400
Cdd:PLN02405 321 MYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHDTSPDLKVVGSKLKDILEIPNTSLKMRKVVVELCN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 401 IIATRGARLSAAGIYGILKKIGKDVPKEGETQKSVIAMDGGLFEHYTQFSECMEISLKELLGDEASESVEVIHSNDGSGV 480
Cdd:PLN02405 401 IVATRGARLSAAGIYGILKKLGRDTVKDGEKQKSVIAMDGGLFEHYTEFSKCMESTLKELLGEEVSESIEVEHSNDGSGI 480
|
490
....*....|....*..
gi 1808789535 481 GAALLAASHSQYLEDSE 497
Cdd:PLN02405 481 GAALLAASHSLYLEVEE 497
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
50-489 |
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: 809.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 50 TPIAKLKQVADAMTVEMHAGLASEGGSKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEFEEV 129
Cdd:cd24020 1 TPVSRLRQVADAMVVEMEAGLASEGGSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 130 SIPPHLMTGGSDELFNFIAEALAKFVATEGEDFHlPAGRQRELGFTFSFPVRQTSLSSGTLIKWTKGFSIEDTVGADVVG 209
Cdd:cd24020 81 PIPPELMVGTSEELFDFIAGELAKFVATEGEGFH-PEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 210 ELVKAMERVGLDMNVTALVNDTVGTLAGGRYYNSDVVAAVILGTGTNAAYVERAHAIPKWHGLLPKSGEMVINMEWGNFR 289
Cdd:cd24020 160 LLEEALERQGLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGLPRSGEMVINTEWGNFR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 290 SSHLPLTEYDHSLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTIPQKLRIPFIIRTPHMSAMHSDTSP 369
Cdd:cd24020 240 SSHLPRTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMHEDDSP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 370 DLKVVGSKLKDILEVSTTSLKMRKVVISICNIIATRGARLSAAGIYGILKKIGKDVPKEGETQKSVIAMDGGLFEHYTQF 449
Cdd:cd24020 320 DLETVARILKDALGIDDTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLGRDGGGSSPAQRTVVAVDGGLYEHYPKF 399
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1808789535 450 SECMEISLKELLGDEASESVEVIHSNDGSGVGAALLAASH 489
Cdd:cd24020 400 REYMQQALVELLGDEAADSVELELSNDGSGIGAALLAAAH 439
|
|
| PLN02914 |
PLN02914 |
hexokinase |
23-492 |
0e+00 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 604.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 23 IVRRRMQSSGKWARVIEILRVLEEDCATPIAKLKQVADAMTVEMHAGLASEGGSKLKMLISYVDNLPSGEEHGFFYALDL 102
Cdd:PLN02914 23 RPRSRMAVRSNAVSVAPILTKLQKDCATPLPVLRHVADAMAADMRAGLAVDGGGDLKMILSYVDSLPSGNEKGLFYALDL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 103 GGTNFRVMRVLLGGKQGRVVKQEFEEVSIPPHLMTGGSDELFNFIAEALAKFVATEGEDFHLPAGRQRELGFTFSFPVRQ 182
Cdd:PLN02914 103 GGTNFRVLRVQLGGKDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFVAKEGGKFHLPEGRKREIGFTFSFPVKQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 183 TSLSSGTLIKWTKGFSIEDTVGADVVGELVKAMERVGLDMNVTALVNDTVGTLAGGRYYNSDVVAAVILGTGTNAAYVER 262
Cdd:PLN02914 183 TSIDSGILMKWTKGFAVSGTAGKDVVACLNEAMERQGLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVER 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 263 AHAIPKWHGLLPKSGEMVINMEWGNFrSSHLPLTEYDHSLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFG 342
Cdd:PLN02914 263 TDAIPKLQGQKSSSGRTIINTEWGAF-SDGLPLTEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 343 DTIPQKLRIPFIIRTPHMSAMHSDTSPDLKVVGSKLKDILEVStTSLKMRKVVISICNIIATRGARLSAAGIYGILKKIG 422
Cdd:PLN02914 342 HFVPEKLSTPFALRTPHLCAMQQDNSDDLQAVGSILYDVLGVE-ASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKME 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 423 KDVPKEGETQKSVIAMDGGLFEHYTQFSECMEISLKELLGDEASESVEVIHSNDGSGVGAALLAASHSQY 492
Cdd:PLN02914 421 EDSKGMIFGKRTVVAMDGGLYEKYPQYRRYMQDAVTELLGLELSKNIAIEHTKDGSGIGAALLAATNSKY 490
|
|
| PLN02362 |
PLN02362 |
hexokinase |
1-496 |
0e+00 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 594.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 1 MGKVAVGATVVCAAAVCAAAVFIVRRRMQSSGKWARVIEILRVLEEDCATPIAKLKQVADAMTVEMHAGLASEGGSKLKM 80
Cdd:PLN02362 1 MGKVAVGLAAAAAVAACAVAAVMVGRRVKSRRKWRRVVGVLKELEEACETPVGRLRQVVDAMAVEMHAGLASEGGSKLKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 81 LISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEFEEVSIPPHLMTGGSDELFNFIAEALAKFVATEGE 160
Cdd:PLN02362 81 LLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRSSILSQDVERHPIPQHLMNSTSEVLFDFIASSLKQFVEKEEN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 161 DFHLPAGRQRELGFTFSFPVRQTSLSSGTLIKWTKGFSIEDTVGADVVGELVKAMERVGLDMNVTALVNDTVGTLAGGRY 240
Cdd:PLN02362 161 GSEFSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRRGLDMRVAALVNDTVGTLALGHY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 241 YNSDVVAAVILGTGTNAAYVERAHAIPKWHGLLPKSGEMVINMEWGNFRSSHLPLTEYDHSLDFESLNPGEQILEKIISG 320
Cdd:PLN02362 241 HDPDTVAAVIIGTGTNACYLERTDAIIKCQGLLTTSGSMVVNMEWGNFWSSHLPRTSYDIDLDAESPNPNDQGFEKMISG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 321 MYLGEILRRVLLKMAEEAAFFGdTIPQKLRIPFIIRTPHMSAMHSDTSPDLKVVGSKLKDILEVSTTSLKMRKVVISICN 400
Cdd:PLN02362 321 MYLGDIVRRVILRMSQESDIFG-PVSSRLSTPFVLRTPSVAAMHEDDSPELQEVARILKETLGISEVPLKVRKLVVKICD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 401 IIATRGARLSAAGIYGILKKIGKD----------VPKEGETQKSVIAMDGGLFEHYTQFSECMEISLKELLGDEASESVE 470
Cdd:PLN02362 400 VVTRRAARLAAAGIVGILKKIGRDgsggitsgrsRSDIQIMRRTVVAVEGGLYTNYTMFREYLHEALNEILGEDVAQHVI 479
|
490 500
....*....|....*....|....*.
gi 1808789535 471 VIHSNDGSGVGAALLAASHSQYLEDS 496
Cdd:PLN02362 480 LKATEDGSGIGSALLAASYSSYSVDT 505
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
25-491 |
0e+00 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 517.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 25 RRRMQSSGKWARVIEILRVLEEDCATPIAKLKQVADAMTVEMHAGLASEGGSKLKMLISYVDNLPSGEEHGFFYALDLGG 104
Cdd:PLN02596 26 RWKRRKERQWKHTQRILRKFARECATPVSKLWEVADALVSDMTASLTAEETTTLNMLVSYVASLPSGDEKGLYYGLNLRG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 105 TNFRVMRVLLGGKQGRVVKQEFEEVSIPPHLMTGGSDELFNFIAEALAKFVATEGEDFHLPAGRQRELGFTFSFPVRQTS 184
Cdd:PLN02596 106 SNFLLLRARLGGKNEPISDLYREEISIPSNVLNGTSQELFDYIALELAKFVAEHPGDEADTPERVKKLGFTVSYPVDQAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 185 LSSGTLIKWtKGFSIEDTVGADVVGELVKAMERVGLDMNVTALVNDTVGTLAGGRYYNSDVVAAVILGTGTNAAYVERAH 264
Cdd:PLN02596 186 ASSGSAIKW-KSFSADDTVGKALVNDINRALEKHGLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQ 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 265 AIPKWHGLLPKSGEMVINMEWGNFRSSHLPLTEYDHSLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDT 344
Cdd:PLN02596 265 AIPKWQSPSPESQEIVISTEWGNFNSCHLPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 345 IPQKLRIPFIIRTPHMSAMHSDTSPDLKVVGSKLKDILEVSTTSLKMRKVVISICNIIATRGARLSAAGIYGILKKIGKD 424
Cdd:PLN02596 345 LPPKLTTPYLLRSPDMAAMHQDTSEDHEVVNEKLKEIFGITDSTPMAREVVAEVCDIVAERGARLAGAGIVGIIKKLGRI 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1808789535 425 vpkegETQKSVIAMDGGLFEHYTQFSECMEISLKELLGDEASESVEVIHSNDGSGVGAALLAASHSQ 491
Cdd:PLN02596 425 -----ENKKSVVTVEGGLYEHYRVFRNYLHSSVWEMLGSELSDNVVIEHSHGGSGAGALFLAACQTG 486
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
53-486 |
1.88e-165 |
|
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: 474.82 E-value: 1.88e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 53 AKLKQVADAMTVEMHAGLASEGGSkLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRV-LLGGKQGRVVKQEfeEVSI 131
Cdd:cd24018 2 SKLEEIVKHFLSEMEKGLEGDGGS-LPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVtLDGNGGIFIIVQR--KYKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 132 PPHLMTGGSDELFNFIAEALAKFVATEGEDFHLPAGRqrELGFTFSFPVRQTSLSSGTLIKWTKGFSIEDTVGADVVGEL 211
Cdd:cd24018 79 PDEAKTGTGEELFDFIAECIAEFLEEHNLDLQSDKTI--PLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 212 VKAMERVGLDMNVTALVNDTVGTLAGGRYYNSDVVAAVILGTGTNAAYVERAHAIPKWH---GLLPKSGEMVINMEWGNF 288
Cdd:cd24018 157 QNALDRRGVNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTspsGSVTKSDEMIINTEWGAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 289 RSSH--LPLTEYDHSLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTIPQKLRIPFIIRTPHMSAMHSD 366
Cdd:cd24018 237 DNERevLPLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEAD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 367 TSPDLKVVGSKLKDILEVSTTSLKMRKVVISICNIIATRGARLSAAGIYGILKKIGKDVPKegetqKSVIAMDGGLFEHY 446
Cdd:cd24018 317 TSPDLDAVRDILKELLAIDNTTLEDRKLIKRICELVSTRAARLSAAAIAAILLKRGSLLPE-----PVTVGIDGSVYEKY 391
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1808789535 447 TQFSECMEISLKELLGDEASESVEVIHSNDGSGVGAALLA 486
Cdd:cd24018 392 PGFKDRLSEALRELFGPEVKANISLVLAKDGSGLGAAIIA 431
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
54-487 |
7.72e-151 |
|
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: 437.36 E-value: 7.72e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 54 KLKQVADAMTVEMHAGLASEG--GSKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGkqGRVVKQEFEEVSI 131
Cdd:cd24019 6 QLEEIMDRLLKEMEKGLSKDThpTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNG--GSQVKMESEIYAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 132 PPHLMTGGSDELFNFIAEALAKFVATEG-EDFHLPagrqreLGFTFSFPVRQTSLSSGTLIKWTKGFSIEDTVGADVVGE 210
Cdd:cd24019 84 PEEIMTGTGEQLFDYIAECLAEFLEKNGlKDKKLP------LGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 211 LVKAMERVGL-DMNVTALVNDTVGTLAGGRYYNSDVVAAVILGTGTNAAYVERAHAIPKWHGLLPKSGEMVINMEWGNFR 289
Cdd:cd24019 158 LQEAIKRRGDiKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKWDGDEGDPGQVIINTEWGAFG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 290 SSH---LPLTEYDHSLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTIPQKLRIPFIIRTPHMSAMHSD 366
Cdd:cd24019 238 DNGvldFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 367 TSPDLKVVGSKLKDiLEVSTTSLKMRKVVISICNIIATRGARLSAAGIYGILKKIGKdvpkegetQKSVIAMDGGLFEHY 446
Cdd:cd24019 318 NEGDFSNTREILKE-LGLEDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNR--------KEVTVGVDGSLYKYH 388
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1808789535 447 TQFSECMEISLKELLGDEAseSVEVIHSNDGSGVGAALLAA 487
Cdd:cd24019 389 PKFHKRMHETLKELVPPGC--KFKLMLSEDGSGKGAALVAA 427
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
55-486 |
1.45e-124 |
|
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: 367.76 E-value: 1.45e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 55 LKQVADAMTVEMHAGLASEGGSkLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEfeEVSIPPH 134
Cdd:cd24000 4 LKEITDAFLEELEKGLAGEPSS-LKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGKGIEVTISK--KYEIPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 135 LMTGGSDELFNFIAEALAKFVATEGEDFHLPagrqreLGFTFSFPVRQTSLSSGTLIKWTKGFSIEDTVGADVVGELVKA 214
Cdd:cd24000 81 IKTASAEEFFDFIADCIAEFLKENGLKKPLP------LGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 215 MERVGLDMNVTALVNDTVGTLAGGRYYNSDVVAAVILGTGTNAAYVERAHAIpkwhglLPKSGEMVINMEWGNFRSSHLP 294
Cdd:cd24000 155 LKKRGLPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNI------LLGDGGMIINTEWGNFGKNSLP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 295 LTEYDHSLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEaaffgdtipqklripfiirtphmsamhsdtspdlkvv 374
Cdd:cd24000 229 RTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 375 gsklkdilevsttslkmrkVVISICNIIATRGARLSAAGIYGILKKIGKDvpkegETQKSVIAMDGGLFEHYTQFSECME 454
Cdd:cd24000 272 -------------------ILRKICELVAERSARLAAAAIAALLRKTGDS-----PEKKITIAVDGSLFEKYPGYRERLE 327
|
410 420 430
....*....|....*....|....*....|..
gi 1808789535 455 ISLKELLGDEasESVEVIHSNDGSGVGAALLA 486
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 ... |
53-486 |
3.27e-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: 370.19 E-value: 3.27e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 53 AKLKQVADAMTVEMHAGLASEGGSkLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEfeEVSIP 132
Cdd:cd24088 2 EKLDKLTAEFQRQMEKGLAKHGKG-MAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHGDGTFSLRQE--KSKIP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 133 PHLMTGG-SDELFNFIAEALAKFVATEGEDfHLPAGRQRE---LGFTFSFPVRQTSLSSGTLIKWTKGFSIEDTVGADVV 208
Cdd:cd24088 79 DELKTGVtAKDLFDYLAKSVEAFLTKHHGD-SFAAGKDDDrlkLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 209 GELVKAMERVGLDMNVTALVNDTVGTLAGGRYYNSDVVAAV---ILGTGTNAAYVERAHAIPKwhgLLPKS------GEM 279
Cdd:cd24088 158 KLLQDELDRQGIPVKVVALVNDTVGTLLARSYTSPEISGAVlgaIFGTGTNGAYLEDLEKIKK---LDDSSrvgkgkTHM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 280 VINMEWGNFRS--SHLPLTEYDHSLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFG---DTIPQKLRIPFI 354
Cdd:cd24088 235 VINTEWGSFDNelKVLPTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFLIqynDKSPSALNTPYG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 355 IRTPHMSAMHSDTSPDLKVVGSKLKDILEVSTTSLKMRKVVISICNIIATRGARLSAAGIYGILKKIGKDVPKEGETQKs 434
Cdd:cd24088 315 LDTAVLSAIEIDSEAELRATRKVLLDDLGLPAPSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSYDGEIN- 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1808789535 435 vIAMDGGLFEHYTQFSECMEISLKELL-GDEASESVEVIHSNDGSGVGAALLA 486
Cdd:cd24088 394 -IGVDGSVIEFYPGFESMLREALRLLLiGAEGEKRIKIGIAKDGSGVGAALCA 445
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
53-487 |
1.56e-122 |
|
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: 365.16 E-value: 1.56e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 53 AKLKQVADAMTVEMHAGLASEGGSkLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQgrvvkqEFE----E 128
Cdd:cd24087 2 ERLRKITDHFISELEKGLSKKGGN-IPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNG------KFDitqsK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 129 VSIPPHLMTGGSDELFNFIAEALAKFVategeDFHLPAGR--QRELGFTFSFPVRQTSLSSGTLIKWTKGFSIEDTVGAD 206
Cdd:cd24087 75 YRLPEELKTGTGEELWDFIADCLKKFV-----EEHFPGGKsePLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 207 VVGELVKAMERVGLDMNVTALVNDTVGTLAGGRYYNSDVVAAVILGTGTNAAYVERAHAIPKWHGL-LPKSGEMVINMEW 285
Cdd:cd24087 150 VVPMLQKALKKRNVPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEHDdIPPDSPMAINCEY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 286 GNFRSSH--LPLTEYDHSLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTIPQKLRIPFIIRTPHMSAM 363
Cdd:cd24087 230 GAFDNEHlvLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 364 HSDTSPDLKVVGSKLKDILEVSTTsLKMRKVVISICNIIATRGARLSAAGIYGILKKIGKdvpkegetQKSVIAMDGGLF 443
Cdd:cd24087 310 EEDPFENLEDTDDLFQHFFGLETT-VPERKFIRRLAELIGTRAARLSACGIAAICKKRGY--------KTCHVAADGSVY 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1808789535 444 EHYTQFSECMEISLKELLGDEASES-VEVIHSNDGSGVGAALLAA 487
Cdd:cd24087 381 NKYPGFKERAAQALKDIFGWDGEDDpIKTVPAEDGSGVGAAIIAA 425
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
246-488 |
2.15e-105 |
|
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: 314.04 E-value: 2.15e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 246 VAAVILGTGTNAAYVERAHAIPKWHGLLPKSGEMVINMEWGNFRSSH---LPLTEYDHSLDFESLNPGEQILEKIISGMY 322
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKLPKSGEMIINTEWGAFGDNGllpLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 323 LGEILRRVLLKMAEEAAFFGDTIPqKLRIPFIIRTPHMSAMHSDTSPDLKVVGSKLKDILEVSTTSLKMRKVVISICNII 402
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKGQSE-KLKTPYSLDTSFLSAIESDPSEDLETTREILEELLGIETVTEEDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 403 ATRGARLSAAGIYGILKKIGKDvpkegetQKSVIAMDGGLFEHYTQFSECMEISLKELLGdeASESVEVIHSNDGSGVGA 482
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRD-------KKVTVGVDGSVYEKYPGFRERLQEALRELLG--PGDKVVLVLAEDGSGVGA 230
|
....*.
gi 1808789535 483 ALLAAS 488
Cdd:pfam03727 231 ALIAAV 236
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
51-487 |
7.24e-105 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 321.24 E-value: 7.24e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 51 PIAKLKQVADAMTVEMHAGLASEGG---------SKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGkqGRV 121
Cdd:PTZ00107 21 SKEKLKELVDYFLYELVEGLEAHRRhrnlwipneCSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFRAVRVSLRG--GGK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 122 VKQEFEEVSIPPHLMTG---------GSDELFNFIAEALAKFVATEGEDFHLPagRQRELGFTFSFPVRQTSLSSGTLIK 192
Cdd:PTZ00107 99 MERTQSKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDPEDLN--KPVPVGFTFSFPCTQLSVNNAILID 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 193 WTKGFS----IEDTV-GADVVGELVKAMERVGLDMNVTALVNDTVGTLAGgRYY-----NSDVVAAVILGTGTNAAYVER 262
Cdd:PTZ00107 177 WTKGFEtgraTNDPVeGKDVGELLNDAFKRNNVPANVVAVLNDTVGTLIS-CAYqkpknTPPCQVGVIIGTGSNACYFEP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 263 AHAIPKWHGllpksgeMVINMEWGNFrSSHLPLTEYDHSLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAffg 342
Cdd:PTZ00107 256 EVSAYGYAG-------TPINMECGNF-DSKLPITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLLQLKA--- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 343 dtiPQKLRIPFIIRTPHMSAMHSDTSPDLKVVGSKLKDI--LEVSTTSLK-MRKvvisICNIIATRGARLSAAGIYGILK 419
Cdd:PTZ00107 325 ---PPKMWQSGSFESEDASMILNDQSPDLQFSRQVIKEAwdVDLTDEDLYtIRK----ICELVRGRAAQLAAAFIAAPAK 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1808789535 420 KIGKdvpkegETQKSVIAMDGGLFEHYTQFSECMEISLKELLGDEAsESVEVIHSNDGSGVGAALLAA 487
Cdd:PTZ00107 398 KTRT------VQGKATVAIDGSVYVKNPWFRRLLQEYINSILGPDA-GNVVFYLADDGSGKGAAIIAA 458
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
55-488 |
1.67e-97 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 301.11 E-value: 1.67e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 55 LKQVADAMTVEMHAGLASEGGSkLKMLISYVdNLPSG-EEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEFEevsipp 133
Cdd:COG5026 22 LEEIAAKFQEEMEKGLEGKKSS-LKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRFDGEGTFEIENFKS------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 134 HLMTGGS-----DELFNFIAEALAKFVategedfhlpaGRQRELGFTFSFPVRQTSLSSGTLIKWTKGFSIEDTVGADVV 208
Cdd:COG5026 94 FPLPGTSseitaEEFFDFIADYIEPLL-----------DESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 209 GELVKAMERVGLDmNV--TALVNDTVGTLAGGRY------YNSDVvaAVILGTGTNAAYVERAHAIPKwhgLLPKSGEMV 280
Cdd:COG5026 163 ELLEAALARKGLD-NVkpVAILNDTVATLLAGAYadpddgYSGYI--GSILGTGHNTCYLEPNAPIGK---LPAYEGPMI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 281 INMEWGNFrsSHLPLTEYDHSLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDtIPQKLRIPFIIRTPHM 360
Cdd:COG5026 237 INMESGNF--NKLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEGLFSPG-FSEVFETPYSLTTVDM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 361 SAMHSDTSPDLKVVGSKLKDILEVSttslkmRKVVISICNIIATRGARLSAAGIYGILKKIGKDVPKEGETqksVIAMDG 440
Cdd:COG5026 314 SRFLADPSDEKEILSQCLEAGSEED------REILREIADAIVERAARLVAATLAGILLHLGPGKTPLKPH---CIAIDG 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1808789535 441 GLFEHYTQFSECMEISLKELLGDEASESVEVIHSNDGSGVGAALLAAS 488
Cdd:COG5026 385 STYEKMPGLAEKIEYALQEYLLGEKGRYVEFVLVENASLLGAAIAAAL 432
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
53-487 |
1.35e-96 |
|
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: 298.61 E-value: 1.35e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 53 AKLKQVADAMTVEMHAGLASEGG--SKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEFEEVS 130
Cdd:cd24089 5 ETLLDISRRFRKEMEKGLGKDTHptATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMESQVYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 131 IPPHLMTGGSDELFNFIAEALAKFVATEG-EDFHLPagrqreLGFTFSFPVRQTSLSSGTLIKWTKGFSIEDTVGADVVG 209
Cdd:cd24089 85 IPEEIMHGSGTQLFDHVAECLADFMDKQKiKDKKLP------LGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 210 ELVKAMERVG-LDMNVTALVNDTVGTLAGGRYYNSDVVAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNF 288
Cdd:cd24089 159 LLRKAIRRRGdYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEG---DEGRMCINTEWGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 289 R---SSHLPLTEYDHSLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTIPQKLRIPFIIRTPHMSAMHS 365
Cdd:cd24089 236 GddgSLEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 366 DTSpDLKVVGSKLKDiLEVSTTSLKMRkVVISICNIIATRGARLSAAGIYGILKKIGKDvpKEGETQKSVIAMDGGLFEH 445
Cdd:cd24089 316 EKE-GLANAKEILTR-LGLDPSEDDCV-NVQHVCTIVSFRSANLCAATLAAILTRLREN--KGLERLRTTVGVDGSVYKK 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1808789535 446 YTQFSECMEISLKELLGDeasESVEVIHSNDGSGVGAALLAA 487
Cdd:cd24089 391 HPQFSKRLHKAVRRLVPD---CDVRFLLSEDGSGKGAAMVTA 429
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
40-240 |
2.19e-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: 2.19e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 40 ILRVLEEDCATPIAKLKQVADAMTVEMHAGLASEGGSKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKqg 119
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGGD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 120 RVVKQEFEEVSIPPHLMTGGSDELFNFIAEALAKFVATEGEDFHlpAGRQRELGFTFSFPVRQTSLSSGTLIKWTKGFSI 199
Cdd:pfam00349 79 GKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDF--EEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1808789535 200 EDTVGADVVGELVKAMERVGLDMNVTALVNDTVGTLAGGRY 240
Cdd:pfam00349 157 PGVVGKDVVQLLQEALERRGLPVKVVALVNDTVGTLMAGAY 197
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
54-487 |
8.42e-91 |
|
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the second two domains of types I to III hexokinases. Type I enzyme may have a catabolic function, producing H6P for energy production in glycolysis; it is bound to the mitochondrial membrane, which enables the coordination of glycolysis with the TCA cycle. Types II and III enzyme may have anabolic functions, providing H6P for glycogen or lipid synthesis.
Pssm-ID: 466941 [Multi-domain] Cd Length: 433 Bit Score: 283.67 E-value: 8.42e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 54 KLKQVADAMTVEMHAGLASE--GGSKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEFEEVSI 131
Cdd:cd24091 6 QLLEVKARMRAEMERGLRKEthASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHNKIYAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 132 PPHLMTGGSDELFNFIAEALAKFVATEGedfhlPAGRQRELGFTFSFPVRQTSLSSGTLIKWTKGFSIEDTVGADVVGEL 211
Cdd:cd24091 86 PQEIMQGTGEELFDHIVQCIADFLEYMG-----LKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 212 VKAMERVG-LDMNVTALVNDTVGTLAGGRYYNSDVVAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNFRS 290
Cdd:cd24091 161 REAIKRREeFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEG---EEGRMCINMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 291 S----HLpLTEYDHSLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTIPQKLRIPFIIRTPHMSAMHSD 366
Cdd:cd24091 238 NgcldDI-RTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 367 tSPDLKVVGSKLKDILEVSTTSLKMrkVVISICNIIATRGARLSAAGIYGILKKIGKDvpKEGETQKSVIAMDGGLFEHY 446
Cdd:cd24091 317 -RLALLQVRAILQQLGLDSTCDDSI--IVKEVCGVVSRRAAQLCGAGMAAVVDKIREN--RGLDHLNVTVGVDGTLYKLH 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1808789535 447 TQFSECMEISLKELlgdEASESVEVIHSNDGSGVGAALLAA 487
Cdd:cd24091 392 PHFSRVMHETVKEL---APKCDVTFLQSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
55-487 |
2.75e-90 |
|
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: 282.51 E-value: 2.75e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 55 LKQVADAMTVEMHAGLASEGGSK--LKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEFEEVSIP 132
Cdd:cd24126 7 LLDIMTRFRAEMEKGLAKDTNPTaaVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMESQFYPTP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 133 PHLMTGGSDELFNFIAEALAKFVATEG-EDFHLPagrqreLGFTFSFPVRQTSLSSGTLIKWTKGFSIEDTVGADVVGEL 211
Cdd:cd24126 87 EEIIHGTGTELFDYVAECLADFMKKKGiKHKKLP------LGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 212 VKAMERVG-LDMNVTALVNDTVGTLAGGRYYNSDVVAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNFRS 290
Cdd:cd24126 161 RKAIRKHKdVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEG---DEGRMCINTEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 291 SHLP---LTEYDHSLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTIPQKLRIPFIIRTPHMSAMHSdt 367
Cdd:cd24126 238 DGSLediRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEK-- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 368 spdLKVVGSKLKDILevstTSLKMRK------VVISICNIIATRGARLSAAGIYGILKKIGKDvpKEGETQKSVIAMDGG 441
Cdd:cd24126 316 ---YKEGLYNTREIL----SDLGLEPseedciAVQHVCTIVSFRSANLCAAALAAILTRLREN--KKLERLRTTVGMDGT 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1808789535 442 LFEHYTQFSECMEISLKELLgdeASESVEVIHSNDGSGVGAALLAA 487
Cdd:cd24126 387 VYKTHPQYAKRLHKVVRRLV---PSCDVRFLLSESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
53-487 |
8.36e-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: 278.69 E-value: 8.36e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 53 AKLKQVADAMTVEMHAGLASE--GGSKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEFeevS 130
Cdd:cd24129 5 DQLAAVQAQMRKEMAKGLRGEthAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTAGVQITSEIY---S 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 131 IPPHLMTGGSDELFNFIAEALAKFVATEGEdfhlpAGRQRELGFTFSFPVRQTSLSSGTLIKWTKGFSIEDTVGADVVGE 210
Cdd:cd24129 82 IPETVAQGTGQQLFDHIVDCIVDFQQKQGL-----SGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 211 LVKAMER-VGLDMNVTALVNDTVGTLAGGRYYNSDVVAAVILGTGTNAAYVERAHAIpkwhGLLP-KSGEMVINMEWGNF 288
Cdd:cd24129 157 LREAATRkQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNV----AGVPgDSGRMCINMEWGAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 289 ---RSSHLPLTEYDHSLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTIPQKLRIPFIIRTPHMSAMHS 365
Cdd:cd24129 233 gdnGCLAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIES 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 366 DTSPdLKVVGSKLKDILEVSTTSLKMrkVVISICNIIATRGARLSAAGIYGILKKIGKDvpKEGETQKSVIAMDGGLFEH 445
Cdd:cd24129 313 DSLA-LRQVRAILEDLGLPLTSDDAL--LVLEVCQTVSQRAAQLCAAGVAAVVEKMREN--RGLDELAVTVGVDGTLYKL 387
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1808789535 446 YTQFSECMEISLKELlgdEASESVEVIHSNDGSGVGAALLAA 487
Cdd:cd24129 388 HPRFSSLVQATVREL---APRCVVTFLQSEDGSGKGAALVTA 426
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
55-487 |
1.69e-84 |
|
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: 267.53 E-value: 1.69e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 55 LKQVADAMTVEMHAGLASEGG--SKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEFEEVSIP 132
Cdd:cd24125 7 LLEISKRFRKEMEKGLGATTHptAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMENQIYAIP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 133 PHLMTGGSDELFNFIAEALAKFVATEG-EDFHLPagrqreLGFTFSFPVRQTSLSSGTLIKWTKGFSIEDTVGADVVGEL 211
Cdd:cd24125 87 EDIMRGSGTQLFDHIAECLANFMDKLQiKDKKLP------LGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 212 VKAMERVG-LDMNVTALVNDTVGTLAGGRYYNSDVVAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNFRS 290
Cdd:cd24125 161 RKAIQKRGdFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEG---DEGRMCINMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 291 SHL---PLTEYDHSLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTIPQKLRIPFIIRTPHMSAMHSDT 367
Cdd:cd24125 238 DGSlddIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 368 SPDLKVVGSKLKDILEVSTTSLKMRKvviSICNIIATRGARLSAAGIYGILKKIGKDvpKEGETQKSVIAMDGGLFEHYT 447
Cdd:cd24125 318 DGIRKAREVLMRLGLDPTQEDCVATH---RICQIVSTRSASLCAATLAAVLQRIKEN--KGEERLRSTIGVDGSVYKKHP 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1808789535 448 QFSECMEISLKELLGDeasESVEVIHSNDGSGVGAALLAA 487
Cdd:cd24125 393 HFARRLHKTVRRLVPG---CDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
53-487 |
2.15e-83 |
|
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: 264.84 E-value: 2.15e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 53 AKLKQVADAMTVEMHAGLASE--GGSKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEFEEVS 130
Cdd:cd24128 5 DQLLEVKRRMKVEMERGLSKEthASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHNKIYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 131 IPPHLMTGGSDELFNFIAEALAKFVATEG-EDFHLPagrqreLGFTFSFPVRQTSLSSGTLIKWTKGFSIEDTVGADVVG 209
Cdd:cd24128 85 IPQEVMHGTGEELFDHIVHCIADFLEYMGmKGVSLP------LGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 210 ELVKAMERV-GLDMNVTALVNDTVGTLAGGRYYNSDVVAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNF 288
Cdd:cd24128 159 LLKEAIHRReEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEG---EEGRMCVNMEWGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 289 RSSHLP---LTEYDHSLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTIPQKLRIPFIIRTPHMSAMHS 365
Cdd:cd24128 236 GDNGCLddfRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIES 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 366 DTSPdLKVVGSKLKDILEVSTTSLKMrkVVISICNIIATRGARLSAAGIYGILKKIGKDvpKEGETQKSVIAMDGGLFEH 445
Cdd:cd24128 316 DRLA-LLQVRAILQHLGLESTCDDSI--IVKEVCTVVARRAAQLCGAGMAAVVDKIREN--RGLDALKVTVGVDGTLYKL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1808789535 446 YTQFSECMEISLKELlgdEASESVEVIHSNDGSGVGAALLAA 487
Cdd:cd24128 391 HPHFAKVMHETVKDL---APKCDVSFLQSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
54-487 |
2.16e-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: 2.16e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 54 KLKQVADAMTVEMHAGLASE--GGSKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEFEEVSI 131
Cdd:cd24127 6 MLLEVKKRMRAEMELGLRKQthNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 132 PPHLMTGGSDELFNFIAEALAKFVategeDFHLPAGRQRELGFTFSFPVRQTSLSSGTLIKWTKGFSIEDTVGADVVGEL 211
Cdd:cd24127 86 PIEIMQGTGEELFDHIVSCISDFL-----DYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 212 VKAMERVG-LDMNVTALVNDTVGTLAGGRYYNSDVVAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNFRS 290
Cdd:cd24127 161 RDAIKRREeFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEG---DQGQMCINMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 291 SHL---PLTEYDHSLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTIPQKLRIPFIIRTPHMSAMHSDT 367
Cdd:cd24127 238 NGClddIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 368 SPDLKvVGSKLKDILEVSTTSLKMrkVVISICNIIATRGARLSAAGIYGILKKIGKDvpKEGETQKSVIAMDGGLFEHYT 447
Cdd:cd24127 318 LALLQ-VRAILQQLGLNSTCDDSI--LVKTVCGVVSRRAAQLCGAGMAAVVDKIREN--RGLDHLNVTVGVDGTLYKLHP 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1808789535 448 QFSECMEISLKELlgdEASESVEVIHSNDGSGVGAALLAA 487
Cdd:cd24127 393 HFSRIMHQTVKEL---SPKCNVSFLLSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
54-487 |
9.00e-82 |
|
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: 260.64 E-value: 9.00e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 54 KLKQVADAMTVEMHAGLASE--GGSKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQgRVVKQEFEEVSI 131
Cdd:cd24130 6 QLQEVKQKMRTELEYGLKKEthPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGR-RSVRMYNKIFAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 132 PPHLMTGGSDELFNFIAEALAKFVategeDFHLPAGRQRELGFTFSFPVRQTSLSSGTLIKWTKGFSIEDTVGADVVGEL 211
Cdd:cd24130 85 PLEIMQGTGEELFDHIVQCIADFL-----DYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 212 VKAMERVG-LDMNVTALVNDTVGTLAGGRYYNSDVVAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNFRS 290
Cdd:cd24130 160 REAIKRRNeFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEG---DEGRMCINTEWGGFGD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 291 SHLP---LTEYDHSLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTIPQKLRIPFIIRTPHMSAMHSDT 367
Cdd:cd24130 237 NGCIddiRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 368 SPDLKVVGSkLKDILEVSTTSLKMrkVVISICNIIATRGARLSAAGIYGILKKIGKDvpKEGETQKSVIAMDGGLFEHYT 447
Cdd:cd24130 317 LALLQVRRI-LQQLGLDSTCEDSI--IVKEVCGAVSRRAAQLCGAGLAAIVEKIREN--QGLDRLDITVGVDGTLYKLHP 391
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1808789535 448 QFSECMEISLKELlgdEASESVEVIHSNDGSGVGAALLAA 487
Cdd:cd24130 392 HFSRILQETVKEL---APQCDVTFMLSEDGSGKGAALITA 428
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
65-487 |
8.71e-81 |
|
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: 259.16 E-value: 8.71e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 65 EMHAGLASEGG--SKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEFEEVSIPPHLMTGGSDE 142
Cdd:cd24124 45 EMKNGLSRDFNptATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVHGSGSQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 143 LFNFIAEALAKFVATEG-EDFHLPagrqreLGFTFSFPVRQTSLSSGTLIKWTKGFSIEDTVGADVVGELVKAMERVG-L 220
Cdd:cd24124 125 LFDHVAECLGDFMEKRKiKDKKLP------VGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLNKAIKKRGdY 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 221 DMNVTALVNDTVGTLAGGRYYNSDVVAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNFR---SSHLPLTE 297
Cdd:cd24124 199 DANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEG---DEGRMCINTEWGAFGddgSLEDIRTE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 298 YDHSLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTIPQKLRIPFIIRTPHMSAMHSDtspdlKVVGSK 377
Cdd:cd24124 276 FDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKN-----KEGLHN 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 378 LKDILevstTSLKMRK------VVISICNIIATRGARLSAAGIYGILKKI--GKDVPKegetQKSVIAMDGGLFEHYTQF 449
Cdd:cd24124 351 AKEIL----TRLGVEPsdddcvSVQHVCTIVSFRSANLVAATLGAILNRLrdNKGTPR----LRTTVGVDGSLYKTHPQY 422
|
410 420 430
....*....|....*....|....*....|....*...
gi 1808789535 450 SECMEISLKELLGDeasESVEVIHSNDGSGVGAALLAA 487
Cdd:cd24124 423 SRRFHKTLRRLVPD---SDVRFLLSESGSGKGAAMVTA 457
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
55-487 |
1.75e-78 |
|
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: 252.11 E-value: 1.75e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 55 LKQVADAMTVEMHAGLASEG--GSKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLG-GKQGR-VVKQEFEEVS 130
Cdd:cd24092 16 LKKVMRRMQKEMDRGLRLETheEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGeGEEGQwSVKTKHQMYS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 131 IPPHLMTGGSDELFNFIAEALAKFVategeDFHLPAGRQRELGFTFSFPVRQTSLSSGTLIKWTKGFSIEDTVGADVVGE 210
Cdd:cd24092 96 IPEDAMTGTAEMLFDYISECISDFL-----DKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVGL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 211 LVKAMERVG-LDMNVTALVNDTVGTLAGGRYYNSDVVAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNF- 288
Cdd:cd24092 171 LRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEG---DEGRMCVNTEWGAFg 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 289 RSSHLP--LTEYDHSLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTIPQKLRIPFIIRTPHMSAMHSD 366
Cdd:cd24092 248 DSGELDefLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 367 TSpDLKVVGSKLKDI-LEVSTTSLKMRKVVisiCNIIATRGARLSAAGIYGILKKIGKDvpKEGETQKSVIAMDGGLFEH 445
Cdd:cd24092 328 TG-DRKQIYNILSTLgLRPSTTDCDIVRRA---CESVSTRAAHMCSAGLAGVINRMRES--RSEDVMRITVGVDGSVYKL 401
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1808789535 446 YTQFSECMEISLKELlgdEASESVEVIHSNDGSGVGAALLAA 487
Cdd:cd24092 402 HPSFKERFHASVRRL---TPSCEITFIESEEGSGRGAALVSA 440
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
51-487 |
5.77e-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: 242.52 E-value: 5.77e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 51 PIAKLKQVADAMTVEMHAGLASEGG--SKLKMLISYVDNLPSGEEHGFFYALDLG--GTNFRVMRVLLGGKQGRVVKQEF 126
Cdd:cd24090 3 TRAQLQQIQASLLGSMEQALRGQASpaPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 127 EEVSIPPHLMTGGSDELFNFIAEALAKFVATegedfhLPAGRQR-ELGFTFSFPVRQTSLSSGTLIKWTKGFSIEDTVGA 205
Cdd:cd24090 83 QEFVIPQEVMLGAGQQLFDFAAHCLSEFLDG------QPVPKQGlQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 206 DVVGELVKAMERVGL-DMNVTALVNDTVGTLAGGRYYNSDVVAAVILGTGTNAAYVERAHAIPKwhgLLPKSGEMVINME 284
Cdd:cd24090 157 DVVQLLRDAIQRQGAyNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAV---LDEDRGRVCVSVE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 285 WGNFR---SSHLPLTEYDHSLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTIPQKLRIPFIIRTPHMS 361
Cdd:cd24090 234 WGSFSddgALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 362 AMHsdtspDLKVVGSKLKDILEVSTTSLKMRKV--VISICNIIATRGARLSAAGIYGILKKIGKDvpKEGETQKSVIAMD 439
Cdd:cd24090 314 EME-----DPSAGAARVRAILQDLGLSPSASDVelVQHVCRAVCTRAAQLCAAALAAVLSHLQHS--REQQTLQVAVATG 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1808789535 440 GGLFEHYTQFSECMEiSLKELLGDEAseSVEVIHSNDGSGVGAALLAA 487
Cdd:cd24090 387 GRVCERHPRFCSILQ-GTVMLLAPEC--DVSFIPSVDGGGRGVAMVTA 431
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
93-260 |
1.90e-04 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 43.35 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 93 EHGFFYALDLGGTNfrvMRVLLGGKQGRVVKQefEEVSIPPHlmtGGSDELFNFIAEALAKFVATEGEDFHLPAGrqreL 172
Cdd:COG1940 3 DAGYVIGIDIGGTK---IKAALVDLDGEVLAR--ERIPTPAG---AGPEAVLEAIAELIEELLAEAGISRGRILG----I 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808789535 173 GFTFSFPV---RQTSLSSGTLIKWTkgfsiedtvGADVVGELvkaMERVGLDmnvTALVND-TVGTLA-----GGRyyNS 243
Cdd:COG1940 71 GIGVPGPVdpeTGVVLNAPNLPGWR---------GVPLAELL---EERLGLP---VFVENDaNAAALAeawfgAGR--GA 133
|
170
....*....|....*..
gi 1808789535 244 DVVAAVILGTGTNAAYV 260
Cdd:COG1940 134 DNVVYLTLGTGIGGGIV 150
|
|
| |
