|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02405 |
PLN02405 |
hexokinase |
1-497 |
0e+00 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 936.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 1 MGKVAVGATVVCAAAVCAASVYIVRRRMQSSGKWARVIEILRVLEEDCATPIGKLRQVADAMTVEMHAGLASEGGSKLKM 80
Cdd:PLN02405 1 MGKVAVGAAVVCAAAVCAAAALVVRRRMKSSGKWARAMEILKEFEEDCATPIGKLRQVADAMTVEMHAGLASEGGSKLKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 81 LISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEAKEVSIPPHLMTSGSDELFNFIAEALANFVATEGE 160
Cdd:PLN02405 81 LISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVSIPPHLMTGSSDALFDFIAAALAKFVATEGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 161 DFHLPEGRQRELGFTFSFPVKQTSLSSGTLIKWTKGFSIEDTVGQDVVGALVKAMERVGLDMNVTALVNDTVGTLAGGRY 240
Cdd:PLN02405 161 DFHLPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMERVGLDMRVSALVNDTIGTLAGGRY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 241 YNPDVVAAVILGTGTNAAYVERAHAIPKWHGLLPKSGEMVINMEWGNFRSSHLPLTEYDHLLDFDSLNPGEQILEKIISG 320
Cdd:PLN02405 241 YNPDVVAAVILGTGTNAAYVERAQAIPKWHGLLPKSGEMVINMEWGNFRSSHLPLTEYDHALDVESLNPGEQIFEKIISG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 321 MYLGEILRRVLLKMADEAAFFGDSVPPKLRIPFIIRTPNMSAMHSDTSPDLKVVGSKLKDILEVPTTSLKMRKVVVSLCD 400
Cdd:PLN02405 321 MYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHDTSPDLKVVGSKLKDILEIPNTSLKMRKVVVELCN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 401 IIASRGARLSAAGIYGILKKLGRDAPKDGETQKSVIAMDGGLFEHYTQFSECMESSLKELLGDEASDSVEVIHSNDGSGV 480
Cdd:PLN02405 401 IVATRGARLSAAGIYGILKKLGRDTVKDGEKQKSVIAMDGGLFEHYTEFSKCMESTLKELLGEEVSESIEVEHSNDGSGI 480
|
490
....*....|....*..
gi 1516576638 481 GAALLAASHSQYLDDSE 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: 815.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 50 TPIGKLRQVADAMTVEMHAGLASEGGSKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEAKEV 129
Cdd:cd24020 1 TPVSRLRQVADAMVVEMEAGLASEGGSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 130 SIPPHLMTSGSDELFNFIAEALANFVATEGEDFHlPEGRQRELGFTFSFPVKQTSLSSGTLIKWTKGFSIEDTVGQDVVG 209
Cdd:cd24020 81 PIPPELMVGTSEELFDFIAGELAKFVATEGEGFH-PEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 210 ALVKAMERVGLDMNVTALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERAHAIPKWHGLLPKSGEMVINMEWGNFR 289
Cdd:cd24020 160 LLEEALERQGLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGLPRSGEMVINTEWGNFR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 290 SSHLPLTEYDHLLDFDSLNPGEQILEKIISGMYLGEILRRVLLKMADEAAFFGDSVPPKLRIPFIIRTPNMSAMHSDTSP 369
Cdd:cd24020 240 SSHLPRTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMHEDDSP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 370 DLKVVGSKLKDILEVPTTSLKMRKVVVSLCDIIASRGARLSAAGIYGILKKLGRDAPKDGETQKSVIAMDGGLFEHYTQF 449
Cdd:cd24020 320 DLETVARILKDALGIDDTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLGRDGGGSSPAQRTVVAVDGGLYEHYPKF 399
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1516576638 450 SECMESSLKELLGDEASDSVEVIHSNDGSGVGAALLAASH 489
Cdd:cd24020 400 REYMQQALVELLGDEAADSVELELSNDGSGIGAALLAAAH 439
|
|
| PLN02362 |
PLN02362 |
hexokinase |
1-496 |
0e+00 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 608.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 1 MGKVAVGATVVCAAAVCAASVYIVRRRMQSSGKWARVIEILRVLEEDCATPIGKLRQVADAMTVEMHAGLASEGGSKLKM 80
Cdd:PLN02362 1 MGKVAVGLAAAAAVAACAVAAVMVGRRVKSRRKWRRVVGVLKELEEACETPVGRLRQVVDAMAVEMHAGLASEGGSKLKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 81 LISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEAKEVSIPPHLMTSGSDELFNFIAEALANFVATEGE 160
Cdd:PLN02362 81 LLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRSSILSQDVERHPIPQHLMNSTSEVLFDFIASSLKQFVEKEEN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 161 DFHLPEGRQRELGFTFSFPVKQTSLSSGTLIKWTKGFSIEDTVGQDVVGALVKAMERVGLDMNVTALVNDTVGTLAGGRY 240
Cdd:PLN02362 161 GSEFSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRRGLDMRVAALVNDTVGTLALGHY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 241 YNPDVVAAVILGTGTNAAYVERAHAIPKWHGLLPKSGEMVINMEWGNFRSSHLPLTEYDHLLDFDSLNPGEQILEKIISG 320
Cdd:PLN02362 241 HDPDTVAAVIIGTGTNACYLERTDAIIKCQGLLTTSGSMVVNMEWGNFWSSHLPRTSYDIDLDAESPNPNDQGFEKMISG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 321 MYLGEILRRVLLKMADEAAFFGdSVPPKLRIPFIIRTPNMSAMHSDTSPDLKVVGSKLKDILEVPTTSLKMRKVVVSLCD 400
Cdd:PLN02362 321 MYLGDIVRRVILRMSQESDIFG-PVSSRLSTPFVLRTPSVAAMHEDDSPELQEVARILKETLGISEVPLKVRKLVVKICD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 401 IIASRGARLSAAGIYGILKKLGRDAP----------KDGETQKSVIAMDGGLFEHYTQFSECMESSLKELLGDEASDSVE 470
Cdd:PLN02362 400 VVTRRAARLAAAGIVGILKKIGRDGSggitsgrsrsDIQIMRRTVVAVEGGLYTNYTMFREYLHEALNEILGEDVAQHVI 479
|
490 500
....*....|....*....|....*.
gi 1516576638 471 VIHSNDGSGVGAALLAASHSQYLDDS 496
Cdd:PLN02362 480 LKATEDGSGIGSALLAASYSSYSVDT 505
|
|
| PLN02914 |
PLN02914 |
hexokinase |
22-492 |
0e+00 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 602.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 22 YIVRRRMQSSGkwARVIEILRVLEEDCATPIGKLRQVADAMTVEMHAGLASEGGSKLKMLISYVDNLPSGEEHGFFYALD 101
Cdd:PLN02914 24 PRSRMAVRSNA--VSVAPILTKLQKDCATPLPVLRHVADAMAADMRAGLAVDGGGDLKMILSYVDSLPSGNEKGLFYALD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 102 LGGTNFRVMRVLLGGKQGRVVKQEAKEVSIPPHLMTSGSDELFNFIAEALANFVATEGEDFHLPEGRQRELGFTFSFPVK 181
Cdd:PLN02914 102 LGGTNFRVLRVQLGGKDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFVAKEGGKFHLPEGRKREIGFTFSFPVK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 182 QTSLSSGTLIKWTKGFSIEDTVGQDVVGALVKAMERVGLDMNVTALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVE 261
Cdd:PLN02914 182 QTSIDSGILMKWTKGFAVSGTAGKDVVACLNEAMERQGLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 262 RAHAIPKWHGLLPKSGEMVINMEWGNFrSSHLPLTEYDHLLDFDSLNPGEQILEKIISGMYLGEILRRVLLKMADEAAFF 341
Cdd:PLN02914 262 RTDAIPKLQGQKSSSGRTIINTEWGAF-SDGLPLTEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLF 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 342 GDSVPPKLRIPFIIRTPNMSAMHSDTSPDLKVVGSKLKDILEVpTTSLKMRKVVVSLCDIIASRGARLSAAGIYGILKKL 421
Cdd:PLN02914 341 GHFVPEKLSTPFALRTPHLCAMQQDNSDDLQAVGSILYDVLGV-EASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKM 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1516576638 422 GRDAPKDGETQKSVIAMDGGLFEHYTQFSECMESSLKELLGDEASDSVEVIHSNDGSGVGAALLAASHSQY 492
Cdd:PLN02914 420 EEDSKGMIFGKRTVVAMDGGLYEKYPQYRRYMQDAVTELLGLELSKNIAIEHTKDGSGIGAALLAATNSKY 490
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
25-491 |
0e+00 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 521.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 25 RRRMQSSGKWARVIEILRVLEEDCATPIGKLRQVADAMTVEMHAGLASEGGSKLKMLISYVDNLPSGEEHGFFYALDLGG 104
Cdd:PLN02596 26 RWKRRKERQWKHTQRILRKFARECATPVSKLWEVADALVSDMTASLTAEETTTLNMLVSYVASLPSGDEKGLYYGLNLRG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 105 TNFRVMRVLLGGKQGRVVKQEAKEVSIPPHLMTSGSDELFNFIAEALANFVAT-EGEDFHLPEgRQRELGFTFSFPVKQT 183
Cdd:PLN02596 106 SNFLLLRARLGGKNEPISDLYREEISIPSNVLNGTSQELFDYIALELAKFVAEhPGDEADTPE-RVKKLGFTVSYPVDQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 184 SLSSGTLIKWtKGFSIEDTVGQDVVGALVKAMERVGLDMNVTALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERA 263
Cdd:PLN02596 185 AASSGSAIKW-KSFSADDTVGKALVNDINRALEKHGLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 264 HAIPKWHGLLPKSGEMVINMEWGNFRSSHLPLTEYDHLLDFDSLNPGEQILEKIISGMYLGEILRRVLLKMADEAAFFGD 343
Cdd:PLN02596 264 QAIPKWQSPSPESQEIVISTEWGNFNSCHLPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGD 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 344 SVPPKLRIPFIIRTPNMSAMHSDTSPDLKVVGSKLKDILEVPTTSLKMRKVVVSLCDIIASRGARLSAAGIYGILKKLGR 423
Cdd:PLN02596 344 TLPPKLTTPYLLRSPDMAAMHQDTSEDHEVVNEKLKEIFGITDSTPMAREVVAEVCDIVAERGARLAGAGIVGIIKKLGR 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1516576638 424 DapkdgETQKSVIAMDGGLFEHYTQFSECMESSLKELLGDEASDSVEVIHSNDGSGVGAALLAASHSQ 491
Cdd:PLN02596 424 I-----ENKKSVVTVEGGLYEHYRVFRNYLHSSVWEMLGSELSDNVVIEHSHGGSGAGALFLAACQTG 486
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
54-486 |
5.21e-168 |
|
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: 480.98 E-value: 5.21e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 54 KLRQVADAMTVEMHAGLASEGGSkLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRV-LLGGKQGRVVKQEakEVSIP 132
Cdd:cd24018 3 KLEEIVKHFLSEMEKGLEGDGGS-LPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVtLDGNGGIFIIVQR--KYKIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 133 PHLMTSGSDELFNFIAEALANFVATEGEDFHLPEGRqrELGFTFSFPVKQTSLSSGTLIKWTKGFSIEDTVGQDVVGALV 212
Cdd:cd24018 80 DEAKTGTGEELFDFIAECIAEFLEEHNLDLQSDKTI--PLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 213 KAMERVGLDMNVTALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERAHAIPKWH---GLLPKSGEMVINMEWGNFR 289
Cdd:cd24018 158 NALDRRGVNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTspsGSVTKSDEMIINTEWGAFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 290 SSH--LPLTEYDHLLDFDSLNPGEQILEKIISGMYLGEILRRVLLKMADEAAFFGDSVPPKLRIPFIIRTPNMSAMHSDT 367
Cdd:cd24018 238 NERevLPLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEADT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 368 SPDLKVVGSKLKDILEVPTTSLKMRKVVVSLCDIIASRGARLSAAGIYGILKKLGRDAPKdgetqKSVIAMDGGLFEHYT 447
Cdd:cd24018 318 SPDLDAVRDILKELLAIDNTTLEDRKLIKRICELVSTRAARLSAAAIAAILLKRGSLLPE-----PVTVGIDGSVYEKYP 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 1516576638 448 QFSECMESSLKELLGDEASDSVEVIHSNDGSGVGAALLA 486
Cdd:cd24018 393 GFKDRLSEALRELFGPEVKANISLVLAKDGSGLGAAIIA 431
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
54-487 |
1.08e-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: 439.28 E-value: 1.08e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 54 KLRQVADAMTVEMHAGLASEG--GSKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGkqGRVVKQEAKEVSI 131
Cdd:cd24019 6 QLEEIMDRLLKEMEKGLSKDThpTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNG--GSQVKMESEIYAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 132 PPHLMTSGSDELFNFIAEALANFVATEG-EDFHLPegrqreLGFTFSFPVKQTSLSSGTLIKWTKGFSIEDTVGQDVVGA 210
Cdd:cd24019 84 PEEIMTGTGEQLFDYIAECLAEFLEKNGlKDKKLP------LGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 211 LVKAMERVGL-DMNVTALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERAHAIPKWHGLLPKSGEMVINMEWGNFR 289
Cdd:cd24019 158 LQEAIKRRGDiKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKWDGDEGDPGQVIINTEWGAFG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 290 SSH---LPLTEYDHLLDFDSLNPGEQILEKIISGMYLGEILRRVLLKMADEAAFFGDSVPPKLRIPFIIRTPNMSAMHSD 366
Cdd:cd24019 238 DNGvldFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 367 TSPDLKVVGSKLKDiLEVPTTSLKMRKVVVSLCDIIASRGARLSAAGIYGILKKLGRdapkdgetQKSVIAMDGGLFEHY 446
Cdd:cd24019 318 NEGDFSNTREILKE-LGLEDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNR--------KEVTVGVDGSLYKYH 388
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1516576638 447 TQFSECMESSLKELLGDEAsdSVEVIHSNDGSGVGAALLAA 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 |
4.79e-128 |
|
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: 376.62 E-value: 4.79e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 55 LRQVADAMTVEMHAGLASEGGSkLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQeaKEVSIPPH 134
Cdd:cd24000 4 LKEITDAFLEELEKGLAGEPSS-LKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGKGIEVTIS--KKYEIPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 135 LMTSGSDELFNFIAEALANFVATEGEDFHLPegrqreLGFTFSFPVKQTSLSSGTLIKWTKGFSIEDTVGQDVVGALVKA 214
Cdd:cd24000 81 IKTASAEEFFDFIADCIAEFLKENGLKKPLP------LGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 215 MERVGLDMNVTALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERAHAIpkwhglLPKSGEMVINMEWGNFRSSHLP 294
Cdd:cd24000 155 LKKRGLPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNI------LLGDGGMIINTEWGNFGKNSLP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 295 LTEYDHLLDFDSLNPGEQILEKIISGMYLGEILRRVLLKMADEaaffgdsvppklripfiirtpnmsamhsdtspdlkvv 374
Cdd:cd24000 229 RTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 375 gsklkdilevpttslkmrkVVVSLCDIIASRGARLSAAGIYGILKKLGRDAPKdgetqKSVIAMDGGLFEHYTQFSECME 454
Cdd:cd24000 272 -------------------ILRKICELVAERSARLAAAAIAALLRKTGDSPEK-----KITIAVDGSLFEKYPGYRERLE 327
|
410 420 430
....*....|....*....|....*....|..
gi 1516576638 455 SSLKELLGDEasDSVEVIHSNDGSGVGAALLA 486
Cdd:cd24000 328 EYLKELLGRG--IRIELVLVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
54-487 |
1.98e-124 |
|
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: 370.17 E-value: 1.98e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 54 KLRQVADAMTVEMHAGLASEGGSkLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGkQGRVVKQEAKeVSIPP 133
Cdd:cd24087 3 RLRKITDHFISELEKGLSKKGGN-IPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGG-NGKFDITQSK-YRLPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 134 HLMTSGSDELFNFIAEALANFVategeDFHLPEGR--QRELGFTFSFPVKQTSLSSGTLIKWTKGFSIEDTVGQDVVGAL 211
Cdd:cd24087 80 ELKTGTGEELWDFIADCLKKFV-----EEHFPGGKsePLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 212 VKAMERVGLDMNVTALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERAHAIPKWHGL-LPKSGEMVINMEWGNFRS 290
Cdd:cd24087 155 QKALKKRNVPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEHDdIPPDSPMAINCEYGAFDN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 291 SH--LPLTEYDHLLDFDSLNPGEQILEKIISGMYLGEILRRVLLKMADEAAFFGDSVPPKLRIPFIIRTPNMSAMHSDTS 368
Cdd:cd24087 235 EHlvLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDPF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 369 PDLKVVGSKLKDILEVPTTsLKMRKVVVSLCDIIASRGARLSAAGIYGILKKLGRdapkdgetQKSVIAMDGGLFEHYTQ 448
Cdd:cd24087 315 ENLEDTDDLFQHFFGLETT-VPERKFIRRLAELIGTRAARLSACGIAAICKKRGY--------KTCHVAADGSVYNKYPG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1516576638 449 FSECMESSLKELLGDEASDS-VEVIHSNDGSGVGAALLAA 487
Cdd:cd24087 386 FKERAAQALKDIFGWDGEDDpIKTVPAEDGSGVGAAIIAA 425
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
54-486 |
1.70e-123 |
|
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: 368.26 E-value: 1.70e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 54 KLRQVADAMTVEMHAGLASEGGSkLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEakEVSIPP 133
Cdd:cd24088 3 KLDKLTAEFQRQMEKGLAKHGKG-MAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHGDGTFSLRQE--KSKIPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 134 HLMTSG-SDELFNFIAEALANFVATEGEDfHLPEGRQRE---LGFTFSFPVKQTSLSSGTLIKWTKGFSIEDTVGQDVVG 209
Cdd:cd24088 80 ELKTGVtAKDLFDYLAKSVEAFLTKHHGD-SFAAGKDDDrlkLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 210 ALVKAMERVGLDMNVTALVNDTVGTLAGGRYYNPDVVAAV---ILGTGTNAAYVERAHAIPKwhgLLPKS------GEMV 280
Cdd:cd24088 159 LLQDELDRQGIPVKVVALVNDTVGTLLARSYTSPEISGAVlgaIFGTGTNGAYLEDLEKIKK---LDDSSrvgkgkTHMV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 281 INMEWGNFRS--SHLPLTEYDHLLDFDSLNPGEQILEKIISGMYLGEILRRVLLKMADEAAFFG---DSVPPKLRIPFII 355
Cdd:cd24088 236 INTEWGSFDNelKVLPTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFLIqynDKSPSALNTPYGL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 356 RTPNMSAMHSDTSPDLKVVGSKLKDILEVPTTSLKMRKVVVSLCDIIASRGARLSAAGIYGILKKLGRDAPKDGETQKsv 435
Cdd:cd24088 316 DTAVLSAIEIDSEAELRATRKVLLDDLGLPAPSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSYDGEIN-- 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1516576638 436 IAMDGGLFEHYTQFSECMESSLKELL-GDEASDSVEVIHSNDGSGVGAALLA 486
Cdd:cd24088 394 IGVDGSVIEFYPGFESMLREALRLLLiGAEGEKRIKIGIAKDGSGVGAALCA 445
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
246-488 |
3.84e-106 |
|
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: 315.97 E-value: 3.84e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 246 VAAVILGTGTNAAYVERAHAIPKWHGLLPKSGEMVINMEWGNFRSSH---LPLTEYDHLLDFDSLNPGEQILEKIISGMY 322
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKLPKSGEMIINTEWGAFGDNGllpLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 323 LGEILRRVLLKMADEAAFFGDsVPPKLRIPFIIRTPNMSAMHSDTSPDLKVVGSKLKDILEVPTTSLKMRKVVVSLCDII 402
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKG-QSEKLKTPYSLDTSFLSAIESDPSEDLETTREILEELLGIETVTEEDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 403 ASRGARLSAAGIYGILKKLGRDapkdgetQKSVIAMDGGLFEHYTQFSECMESSLKELLGdeASDSVEVIHSNDGSGVGA 482
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRD-------KKVTVGVDGSVYEKYPGFRERLQEALRELLG--PGDKVVLVLAEDGSGVGA 230
|
....*.
gi 1516576638 483 ALLAAS 488
Cdd:pfam03727 231 ALIAAV 236
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
54-487 |
1.07e-103 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 318.16 E-value: 1.07e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 54 KLRQVADAMTVEMHAGLASEGG---------SKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGkqGRVVKQ 124
Cdd:PTZ00107 24 KLKELVDYFLYELVEGLEAHRRhrnlwipneCSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFRAVRVSLRG--GGKMER 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 125 EAKEVSIP-------PHLM--TSGSDELFNFIAEALANFVATEGEDFHLPEGrqRELGFTFSFPVKQTSLSSGTLIKWTK 195
Cdd:PTZ00107 102 TQSKFSLPksallgeKGLLdkKATATDLFDHIAKSIKKMMEENGDPEDLNKP--VPVGFTFSFPCTQLSVNNAILIDWTK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 196 GFS----IEDTV-GQDVVGALVKAMERVGLDMNVTALVNDTVGTLAgGRYY-----NPDVVAAVILGTGTNAAYVERAHA 265
Cdd:PTZ00107 180 GFEtgraTNDPVeGKDVGELLNDAFKRNNVPANVVAVLNDTVGTLI-SCAYqkpknTPPCQVGVIIGTGSNACYFEPEVS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 266 IPKWHGllpksgeMVINMEWGNFrSSHLPLTEYDHLLDFDSLNPGEQILEKIISGMYLGEILRRVLLKMADEAAffgdsv 345
Cdd:PTZ00107 259 AYGYAG-------TPINMECGNF-DSKLPITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLLQLKA------ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 346 PPKLRIPFIIRTPNMSAMHSDTSPDLKVVGSKLKDI--LEVPTTSLK-MRKVvvslCDIIASRGARLSAAGIYGILKKLG 422
Cdd:PTZ00107 325 PPKMWQSGSFESEDASMILNDQSPDLQFSRQVIKEAwdVDLTDEDLYtIRKI----CELVRGRAAQLAAAFIAAPAKKTR 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1516576638 423 RdapkdgETQKSVIAMDGGLFEHYTQFSECMESSLKELLGDEASDsVEVIHSNDGSGVGAALLAA 487
Cdd:PTZ00107 401 T------VQGKATVAIDGSVYVKNPWFRRLLQEYINSILGPDAGN-VVFYLADDGSGKGAAIIAA 458
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
55-488 |
8.45e-101 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 309.58 E-value: 8.45e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 55 LRQVADAMTVEMHAGLASEGGSkLKMLISYVdNLPSG-EEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEAKevsipp 133
Cdd:COG5026 22 LEEIAAKFQEEMEKGLEGKKSS-LKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRFDGEGTFEIENFKS------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 134 HLM--TSGS---DELFNFIAEALANFVategedfhlpeGRQRELGFTFSFPVKQTSLSSGTLIKWTKGFSIEDTVGQDVV 208
Cdd:COG5026 94 FPLpgTSSEitaEEFFDFIADYIEPLL-----------DESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 209 GALVKAMERVGLDmNV--TALVNDTVGTLAGGRYYNPDVV----AAVILGTGTNAAYVERAHAIPKwhgLLPKSGEMVIN 282
Cdd:COG5026 163 ELLEAALARKGLD-NVkpVAILNDTVATLLAGAYADPDDGysgyIGSILGTGHNTCYLEPNAPIGK---LPAYEGPMIIN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 283 MEWGNFrsSHLPLTEYDHLLDFDSLNPGEQILEKIISGMYLGEILRRVLLKMADEAAFFGDsVPPKLRIPFIIRTPNMSA 362
Cdd:COG5026 239 MESGNF--NKLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEGLFSPG-FSEVFETPYSLTTVDMSR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 363 MHSDTSPDLKVVGSKLKDILEvpttslKMRKVVVSLCDIIASRGARLSAAGIYGILKKLGrdaPKDGETQKSVIAMDGGL 442
Cdd:COG5026 316 FLADPSDEKEILSQCLEAGSE------EDREILREIADAIVERAARLVAATLAGILLHLG---PGKTPLKPHCIAIDGST 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1516576638 443 FEHYTQFSECMESSLKELLGDEASDSVEVIHSNDGSGVGAALLAAS 488
Cdd:COG5026 387 YEKMPGLAEKIEYALQEYLLGEKGRYVEFVLVENASLLGAAIAAAL 432
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
54-487 |
1.69e-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: 298.23 E-value: 1.69e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 54 KLRQVADAMTVEMHAGLASEGG--SKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEAKEVSI 131
Cdd:cd24089 6 TLLDISRRFRKEMEKGLGKDTHptATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMESQVYAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 132 PPHLMTSGSDELFNFIAEALANFVATEG-EDFHLPegrqreLGFTFSFPVKQTSLSSGTLIKWTKGFSIEDTVGQDVVGA 210
Cdd:cd24089 86 PEEIMHGSGTQLFDHVAECLADFMDKQKiKDKKLP------LGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 211 LVKAMERVG-LDMNVTALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNFR 289
Cdd:cd24089 160 LRKAIRRRGdYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEG---DEGRMCINTEWGAFG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 290 ---SSHLPLTEYDHLLDFDSLNPGEQILEKIISGMYLGEILRRVLLKMADEAAFFGDSVPPKLRIPFIIRTPNMSAMHSD 366
Cdd:cd24089 237 ddgSLEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 367 TSpDLKVVGSKLKDILEVPttSLKMRKVVVSLCDIIASRGARLSAAGIYGILKKLGRDapKDGETQKSVIAMDGGLFEHY 446
Cdd:cd24089 317 KE-GLANAKEILTRLGLDP--SEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLREN--KGLERLRTTVGVDGSVYKKH 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1516576638 447 TQFSECMESSLKELLGDeaSDsVEVIHSNDGSGVGAALLAA 487
Cdd:cd24089 392 PQFSKRLHKAVRRLVPD--CD-VRFLLSEDGSGKGAAMVTA 429
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
40-240 |
2.72e-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: 286.71 E-value: 2.72e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 40 ILRVLEEDCATPIGKLRQVADAMTVEMHAGLASEGGSKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQG 119
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGGDGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 120 RVVKQEakEVSIPPHLMTSGSDELFNFIAEALANFVATEGEDFHlpEGRQRELGFTFSFPVKQTSLSSGTLIKWTKGFSI 199
Cdd:pfam00349 81 FEITQE--KYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDF--EEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1516576638 200 EDTVGQDVVGALVKAMERVGLDMNVTALVNDTVGTLAGGRY 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 |
1.45e-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: 285.98 E-value: 1.45e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 54 KLRQVADAMTVEMHAGLASE--GGSKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEAKEVSI 131
Cdd:cd24091 6 QLLEVKARMRAEMERGLRKEthASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHNKIYAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 132 PPHLMTSGSDELFNFIAEALANFVATEGedfhlPEGRQRELGFTFSFPVKQTSLSSGTLIKWTKGFSIEDTVGQDVVGAL 211
Cdd:cd24091 86 PQEIMQGTGEELFDHIVQCIADFLEYMG-----LKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 212 VKAMERVG-LDMNVTALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNFRS 290
Cdd:cd24091 161 REAIKRREeFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEG---EEGRMCINMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 291 S----HLpLTEYDHLLDFDSLNPGEQILEKIISGMYLGEILRRVLLKMADEAAFFGDSVPPKLRIPFIIRTPNMSAMHSD 366
Cdd:cd24091 238 NgcldDI-RTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 367 tSPDLKVVGSKLKDiLEVPTTSlKMRKVVVSLCDIIASRGARLSAAGIYGILKKLGRDapKDGETQKSVIAMDGGLFEHY 446
Cdd:cd24091 317 -RLALLQVRAILQQ-LGLDSTC-DDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIREN--RGLDHLNVTVGVDGTLYKLH 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1516576638 447 TQFSECMESSLKELlgdEASDSVEVIHSNDGSGVGAALLAA 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 |
3.81e-88 |
|
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: 276.73 E-value: 3.81e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 55 LRQVADAMTVEMHAGLASEGGSK--LKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEAKEVSIP 132
Cdd:cd24126 7 LLDIMTRFRAEMEKGLAKDTNPTaaVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMESQFYPTP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 133 PHLMTSGSDELFNFIAEALANFVATEG-EDFHLPegrqreLGFTFSFPVKQTSLSSGTLIKWTKGFSIEDTVGQDVVGAL 211
Cdd:cd24126 87 EEIIHGTGTELFDYVAECLADFMKKKGiKHKKLP------LGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 212 VKAMERVG-LDMNVTALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNFRS 290
Cdd:cd24126 161 RKAIRKHKdVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEG---DEGRMCINTEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 291 SHLP---LTEYDHLLDFDSLNPGEQILEKIISGMYLGEILRRVLLKMADEAAFFGDSVPPKLRIPFIIRTPNMSAMHSdt 367
Cdd:cd24126 238 DGSLediRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEK-- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 368 spdLKVVGSKLKDILevptTSLKMRK------VVVSLCDIIASRGARLSAAGIYGILKKLGRDapKDGETQKSVIAMDGG 441
Cdd:cd24126 316 ---YKEGLYNTREIL----SDLGLEPseedciAVQHVCTIVSFRSANLCAAALAAILTRLREN--KKLERLRTTVGMDGT 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1516576638 442 LFEHYTQFSECMESSLKELLgdeASDSVEVIHSNDGSGVGAALLAA 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 ... |
54-487 |
1.27e-86 |
|
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: 272.91 E-value: 1.27e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 54 KLRQVADAMTVEMHAGLASE--GGSKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGgKQGrvVKQEAKEVSI 131
Cdd:cd24129 6 QLAAVQAQMRKEMAKGLRGEthAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVG-TAG--VQITSEIYSI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 132 PPHLMTSGSDELFNFIAEALANFVATEGEdfhlpEGRQRELGFTFSFPVKQTSLSSGTLIKWTKGFSIEDTVGQDVVGAL 211
Cdd:cd24129 83 PETVAQGTGQQLFDHIVDCIVDFQQKQGL-----SGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 212 VKAMER-VGLDMNVTALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERAHAIpkwhGLLP-KSGEMVINMEWGNF- 288
Cdd:cd24129 158 REAATRkQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNV----AGVPgDSGRMCINMEWGAFg 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 289 --RSSHLPLTEYDHLLDFDSLNPGEQILEKIISGMYLGEILRRVLLKMADEAAFFGDSVPPKLRIPFIIRTPNMSAMHSD 366
Cdd:cd24129 234 dnGCLAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 367 TSPdLKVVGSKLKDiLEVPTT---SLKMRKVvvslCDIIASRGARLSAAGIYGILKKLgrDAPKDGETQKSVIAMDGGLF 443
Cdd:cd24129 314 SLA-LRQVRAILED-LGLPLTsddALLVLEV----CQTVSQRAAQLCAAGVAAVVEKM--RENRGLDELAVTVGVDGTLY 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1516576638 444 EHYTQFSECMESSLKELlgdEASDSVEVIHSNDGSGVGAALLAA 487
Cdd:cd24129 386 KLHPRFSSLVQATVREL---APRCVVTFLQSEDGSGKGAALVTA 426
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
55-487 |
5.85e-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: 265.99 E-value: 5.85e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 55 LRQVADAMTVEMHAGLASEGG--SKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEAKEVSIP 132
Cdd:cd24125 7 LLEISKRFRKEMEKGLGATTHptAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMENQIYAIP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 133 PHLMTSGSDELFNFIAEALANFVATEG-EDFHLPegrqreLGFTFSFPVKQTSLSSGTLIKWTKGFSIEDTVGQDVVGAL 211
Cdd:cd24125 87 EDIMRGSGTQLFDHIAECLANFMDKLQiKDKKLP------LGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 212 VKAMERVG-LDMNVTALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNFRS 290
Cdd:cd24125 161 RKAIQKRGdFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEG---DEGRMCINMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 291 SHL---PLTEYDHLLDFDSLNPGEQILEKIISGMYLGEILRRVLLKMADEAAFFGDSVPPKLRIPFIIRTPNMSAMHSDT 367
Cdd:cd24125 238 DGSlddIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 368 SPDLKVVGSKLKDILE-VPTTSLKMRKVvvslCDIIASRGARLSAAGIYGILKKLGRDapKDGETQKSVIAMDGGLFEHY 446
Cdd:cd24125 318 DGIRKAREVLMRLGLDpTQEDCVATHRI----CQIVSTRSASLCAATLAAVLQRIKEN--KGEERLRSTIGVDGSVYKKH 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1516576638 447 TQFSECMESSLKELLGDeasDSVEVIHSNDGSGVGAALLAA 487
Cdd:cd24125 392 PHFARRLHKTVRRLVPG---CDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
54-487 |
9.48e-84 |
|
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: 265.62 E-value: 9.48e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 54 KLRQVADAMTVEMHAGLASE--GGSKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEAKEVSI 131
Cdd:cd24127 6 MLLEVKKRMRAEMELGLRKQthNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 132 PPHLMTSGSDELFNFIAEALANFVategeDFHLPEGRQRELGFTFSFPVKQTSLSSGTLIKWTKGFSIEDTVGQDVVGAL 211
Cdd:cd24127 86 PIEIMQGTGEELFDHIVSCISDFL-----DYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 212 VKAMERVG-LDMNVTALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNFRS 290
Cdd:cd24127 161 RDAIKRREeFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEG---DQGQMCINMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 291 SHL---PLTEYDHLLDFDSLNPGEQILEKIISGMYLGEILRRVLLKMADEAAFFGDSVPPKLRIPFIIRTPNMSAMHSDT 367
Cdd:cd24127 238 NGClddIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 368 SPDLKVvgsklKDILEV--PTTSLKMRKVVVSLCDIIASRGARLSAAGIYGILKKLGRDAPKDgeTQKSVIAMDGGLFEH 445
Cdd:cd24127 318 LALLQV-----RAILQQlgLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLD--HLNVTVGVDGTLYKL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1516576638 446 YTQFSECMESSLKELlgdEASDSVEVIHSNDGSGVGAALLAA 487
Cdd:cd24127 391 HPHFSRIMHQTVKEL---SPKCNVSFLLSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
54-487 |
2.13e-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: 2.13e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 54 KLRQVADAMTVEMHAGLASE--GGSKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEAKEVSI 131
Cdd:cd24128 6 QLLEVKRRMKVEMERGLSKEthASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHNKIYAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 132 PPHLMTSGSDELFNFIAEALANFVATEGEdfhlpEGRQRELGFTFSFPVKQTSLSSGTLIKWTKGFSIEDTVGQDVVGAL 211
Cdd:cd24128 86 PQEVMHGTGEELFDHIVHCIADFLEYMGM-----KGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 212 VKAMERV-GLDMNVTALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNFRS 290
Cdd:cd24128 161 KEAIHRReEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEG---EEGRMCVNMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 291 SHLP---LTEYDHLLDFDSLNPGEQILEKIISGMYLGEILRRVLLKMADEAAFFGDSVPPKLRIPFIIRTPNMSAMHSDT 367
Cdd:cd24128 238 NGCLddfRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 368 SPDLKVvgsklKDILEV--PTTSLKMRKVVVSLCDIIASRGARLSAAGIYGILKKLGRDapKDGETQKSVIAMDGGLFEH 445
Cdd:cd24128 318 LALLQV-----RAILQHlgLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIREN--RGLDALKVTVGVDGTLYKL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1516576638 446 YTQFSECMESSLKELlgdEASDSVEVIHSNDGSGVGAALLAA 487
Cdd:cd24128 391 HPHFAKVMHETVKDL---APKCDVSFLQSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
54-487 |
4.26e-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: 261.41 E-value: 4.26e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 54 KLRQVADAMTVEMHAGLASE--GGSKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQgRVVKQEAKEVSI 131
Cdd:cd24130 6 QLQEVKQKMRTELEYGLKKEthPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGR-RSVRMYNKIFAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 132 PPHLMTSGSDELFNFIAEALANFVategeDFHLPEGRQRELGFTFSFPVKQTSLSSGTLIKWTKGFSIEDTVGQDVVGAL 211
Cdd:cd24130 85 PLEIMQGTGEELFDHIVQCIADFL-----DYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 212 VKAMERVG-LDMNVTALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNFRS 290
Cdd:cd24130 160 REAIKRRNeFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEG---DEGRMCINTEWGGFGD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 291 SHLP---LTEYDHLLDFDSLNPGEQILEKIISGMYLGEILRRVLLKMADEAAFFGDSVPPKLRIPFIIRTPNMSAMHSDT 367
Cdd:cd24130 237 NGCIddiRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 368 SPDLKVVGSKLKDILEvptTSLKMRKVVVSLCDIIASRGARLSAAGIYGILKKLGRDapKDGETQKSVIAMDGGLFEHYT 447
Cdd:cd24130 317 LALLQVRRILQQLGLD---STCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIREN--QGLDRLDITVGVDGTLYKLHP 391
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1516576638 448 QFSECMESSLKELlgdEASDSVEVIHSNDGSGVGAALLAA 487
Cdd:cd24130 392 HFSRILQETVKEL---APQCDVTFMLSEDGSGKGAALITA 428
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
55-487 |
1.48e-80 |
|
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: 257.50 E-value: 1.48e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 55 LRQVADAMTVEMHAGLASEG--GSKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLG-GKQGR-VVKQEAKEVS 130
Cdd:cd24092 16 LKKVMRRMQKEMDRGLRLETheEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGeGEEGQwSVKTKHQMYS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 131 IPPHLMTSGSDELFNFIAEALANFVategeDFHLPEGRQRELGFTFSFPVKQTSLSSGTLIKWTKGFSIEDTVGQDVVGA 210
Cdd:cd24092 96 IPEDAMTGTAEMLFDYISECISDFL-----DKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVGL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 211 LVKAMERVG-LDMNVTALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNF- 288
Cdd:cd24092 171 LRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEG---DEGRMCVNTEWGAFg 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 289 RSSHLP--LTEYDHLLDFDSLNPGEQILEKIISGMYLGEILRRVLLKMADEAAFFGDSVPPKLRIPFIIRTPNMSAMHSD 366
Cdd:cd24092 248 DSGELDefLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 367 TSpDLKVVGSKLKDILEVPTTSlkMRKVVVSLCDIIASRGARLSAAGIYGILKKLgRDApKDGETQKSVIAMDGGLFEHY 446
Cdd:cd24092 328 TG-DRKQIYNILSTLGLRPSTT--DCDIVRRACESVSTRAAHMCSAGLAGVINRM-RES-RSEDVMRITVGVDGSVYKLH 402
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1516576638 447 TQFSECMESSLKELlgdEASDSVEVIHSNDGSGVGAALLAA 487
Cdd:cd24092 403 PSFKERFHASVRRL---TPSCEITFIESEEGSGRGAALVSA 440
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
55-487 |
4.62e-79 |
|
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: 254.54 E-value: 4.62e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 55 LRQVADAMTVEMHAGLASEGG--SKLKMLISYVDNLPSGEEHGFFYALDLGGTNFRVMRVLLGGKQGRVVKQEAKEVSIP 132
Cdd:cd24124 35 LIDIMTRFRKEMKNGLSRDFNptATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 133 PHLMTSGSDELFNFIAEALANFVATEG-EDFHLPegrqreLGFTFSFPVKQTSLSSGTLIKWTKGFSIEDTVGQDVVGAL 211
Cdd:cd24124 115 ENIVHGSGSQLFDHVAECLGDFMEKRKiKDKKLP------VGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 212 VKAMERVG-LDMNVTALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERAHAIPKWHGllpKSGEMVINMEWGNFR- 289
Cdd:cd24124 189 NKAIKKRGdYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEG---DEGRMCINTEWGAFGd 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 290 --SSHLPLTEYDHLLDFDSLNPGEQILEKIISGMYLGEILRRVLLKMADEAAFFGDSVPPKLRIPFIIRTPNMSAMHSDt 367
Cdd:cd24124 266 dgSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKN- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 368 spdlKVVGSKLKDILevptTSLKMRK------VVVSLCDIIASRGARLSAAGIYGILKKLgRDApKDGETQKSVIAMDGG 441
Cdd:cd24124 345 ----KEGLHNAKEIL----TRLGVEPsdddcvSVQHVCTIVSFRSANLVAATLGAILNRL-RDN-KGTPRLRTTVGVDGS 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1516576638 442 LFEHYTQFSECMESSLKELLGDeaSDsVEVIHSNDGSGVGAALLAA 487
Cdd:cd24124 415 LYKTHPQYSRRFHKTLRRLVPD--SD-VRFLLSESGSGKGAAMVTA 457
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
51-487 |
6.91e-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: 6.91e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 51 PIGKLRQVADAMTVEMHAGLASEGG--SKLKMLISYVDNLPSGEEHGFFYALDLG--GTNFRVMRVLLGGKQGRVVKQEA 126
Cdd:cd24090 3 TRAQLQQIQASLLGSMEQALRGQASpaPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 127 KEVSIPPHLMTSGSDELFNFIAEALANFVATegedfhLPEGRQR-ELGFTFSFPVKQTSLSSGTLIKWTKGFSIEDTVGQ 205
Cdd:cd24090 83 QEFVIPQEVMLGAGQQLFDFAAHCLSEFLDG------QPVPKQGlQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 206 DVVGALVKAMERVGL-DMNVTALVNDTVGTLAGGRYYNPDVVAAVILGTGTNAAYVERAHAIPKwhgLLPKSGEMVINME 284
Cdd:cd24090 157 DVVQLLRDAIQRQGAyNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAV---LDEDRGRVCVSVE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 285 WGNFR---SSHLPLTEYDHLLDFDSLNPGEQILEKIISGMYLGEILRRVLLKMADEAAFFGDSVPPKLRIPFIIRTPNMS 361
Cdd:cd24090 234 WGSFSddgALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 362 AMhSDTSPDLKVVGSKLKDILEVPTTSLKMRkvVVSLCDIIASRGARLSAAGIYGILKKLgRDApKDGETQKSVIAMDGG 441
Cdd:cd24090 314 EM-EDPSAGAARVRAILQDLGLSPSASDVEL--VQHVCRAVCTRAAQLCAAALAAVLSHL-QHS-REQQTLQVAVATGGR 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1516576638 442 LFEHYTQFSECMESSLKeLLGDEAsdSVEVIHSNDGSGVGAALLAA 487
Cdd:cd24090 389 VCERHPRFCSILQGTVM-LLAPEC--DVSFIPSVDGGGRGVAMVTA 431
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
93-260 |
5.05e-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: 42.19 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 93 EHGFFYALDLGGTNfrvMRVLLGGKQGRVVKQEakEVSIPPHlmtSGSDELFNFIAEALANFVATEGEDFHLPEGrqreL 172
Cdd:COG1940 3 DAGYVIGIDIGGTK---IKAALVDLDGEVLARE--RIPTPAG---AGPEAVLEAIAELIEELLAEAGISRGRILG----I 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516576638 173 GFTFSFPV---KQTSLSSGTLIKWTkgfsiedtvGQDVVGALvkaMERVGLDmnvTALVND-TVGTLA-----GGRYYnp 243
Cdd:COG1940 71 GIGVPGPVdpeTGVVLNAPNLPGWR---------GVPLAELL---EERLGLP---VFVENDaNAAALAeawfgAGRGA-- 133
|
170
....*....|....*..
gi 1516576638 244 DVVAAVILGTGTNAAYV 260
Cdd:COG1940 134 DNVVYLTLGTGIGGGIV 150
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
210-263 |
9.95e-03 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 37.94 E-value: 9.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1516576638 210 ALVKAMERVGLDMNVTaLVNDTVGTLAGGryYNPDVVAAVILGTGTNAAYVERA 263
Cdd:COG2971 82 ALEAALRELFPFARVV-VVNDALAALAGA--LGGEDGIVVIAGTGSIAAGRDGD 132
|
|
| |
