|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02405 |
PLN02405 |
hexokinase |
25-497 |
0e+00 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 966.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 25 RHRMRCSGRWARAMAILREFEENCGTPIGKLRQVADAMAVEMHAGLASEGGSKLKMLISYVDNLPSGEENGLFYALDLGG 104
Cdd:PLN02405 25 RRRMKSSGKWARAMEILKEFEEDCATPIGKLRQVADAMTVEMHAGLASEGGSKLKMLISYVDNLPSGDEKGLFYALDLGG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 105 TNFRVIRVLLGGKDGGVVKQEFEEVSIPPHLMTGSSDALFGFIATALANFVATESEGLHPSPGRQRELGFTFSFPVRQTS 184
Cdd:PLN02405 105 TNFRVLRVLLGGKDGRVVKQEFEEVSIPPHLMTGSSDALFDFIAAALAKFVATEGEDFHLPPGRQRELGFTFSFPVKQTS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 185 IASGNLIKWTKGFLIDDVVGQDVVGELTKAMERIGLDMRVSALVNDTIGTLAGGRYHNPDVIAAVILGTGTNAAYVERAQ 264
Cdd:PLN02405 185 ISSGTLIKWTKGFSIDDAVGQDVVGELTKAMERVGLDMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQ 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 265 AIPKWHGLLPKSGEMVINMEWGNFRSSHLPLTEYDQDLDVESLNPGEQIFEKIISGMYLGEIVRRVLLKMAEEAAFFGDI 344
Cdd:PLN02405 265 AIPKWHGLLPKSGEMVINMEWGNFRSSHLPLTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 345 VPPKLKIPFILRTPHMSAMHHDESSDLRVVGSKLKDILEIPHTSLKMRKAIVELCDIVATRGARLSAAGIVGIIKKLGRD 424
Cdd:PLN02405 345 VPPKLKIPFILRTPDMSAMHHDTSPDLKVVGSKLKDILEIPNTSLKMRKVVVELCNIVATRGARLSAAGIYGILKKLGRD 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050315041 425 TVKDGEKQKSVIAMDGGLYEHYSKFSTCMESTLKELLGEEVSDNIAVEQSNDGSGIGAALLAASHSQYLEVEE 497
Cdd:PLN02405 425 TVKDGEKQKSVIAMDGGLFEHYTEFSKCMESTLKELLGEEVSESIEVEHSNDGSGIGAALLAASHSLYLEVEE 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: 804.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 50 TPIGKLRQVADAMAVEMHAGLASEGGSKLKMLISYVDNLPSGEENGLFYALDLGGTNFRVIRVLLGGKDGGVVKQEFEEV 129
Cdd:cd24020 1 TPVSRLRQVADAMVVEMEAGLASEGGSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 130 SIPPHLMTGSSDALFGFIATALANFVATESEGLHPsPGRQRELGFTFSFPVRQTSIASGNLIKWTKGFLIDDVVGQDVVG 209
Cdd:cd24020 81 PIPPELMVGTSEELFDFIAGELAKFVATEGEGFHP-EGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 210 ELTKAMERIGLDMRVSALVNDTIGTLAGGRYHNPDVIAAVILGTGTNAAYVERAQAIPKWHGLLPKSGEMVINMEWGNFR 289
Cdd:cd24020 160 LLEEALERQGLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGLPRSGEMVINTEWGNFR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 290 SSHLPLTEYDQDLDVESLNPGEQIFEKIISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPHMSAMHHDESS 369
Cdd:cd24020 240 SSHLPRTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMHEDDSP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 370 DLRVVGSKLKDILEIPHTSLKMRKAIVELCDIVATRGARLSAAGIVGIIKKLGRDTVKDGEKQKSVIAMDGGLYEHYSKF 449
Cdd:cd24020 320 DLETVARILKDALGIDDTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLGRDGGGSSPAQRTVVAVDGGLYEHYPKF 399
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2050315041 450 STCMESTLKELLGEEVSDNIAVEQSNDGSGIGAALLAASH 489
Cdd:cd24020 400 REYMQQALVELLGDEAADSVELELSNDGSGIGAALLAAAH 439
|
|
| PLN02362 |
PLN02362 |
hexokinase |
1-492 |
0e+00 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 612.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 1 MGKVAVGAAVVCAATVCAAAALVVRHRMRCSGRWARAMAILREFEENCGTPIGKLRQVADAMAVEMHAGLASEGGSKLKM 80
Cdd:PLN02362 1 MGKVAVGLAAAAAVAACAVAAVMVGRRVKSRRKWRRVVGVLKELEEACETPVGRLRQVVDAMAVEMHAGLASEGGSKLKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 81 LISYVDNLPSGEENGLFYALDLGGTNFRVIRVLLGGKDGGVVKQEFEEVSIPPHLMTGSSDALFGFIATALANFVATESE 160
Cdd:PLN02362 81 LLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRSSILSQDVERHPIPQHLMNSTSEVLFDFIASSLKQFVEKEEN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 161 GLHPSPGRQRELGFTFSFPVRQTSIASGNLIKWTKGFLIDDVVGQDVVGELTKAMERIGLDMRVSALVNDTIGTLAGGRY 240
Cdd:PLN02362 161 GSEFSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRRGLDMRVAALVNDTVGTLALGHY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 241 HNPDVIAAVILGTGTNAAYVERAQAIPKWHGLLPKSGEMVINMEWGNFRSSHLPLTEYDQDLDVESLNPGEQIFEKIISG 320
Cdd:PLN02362 241 HDPDTVAAVIIGTGTNACYLERTDAIIKCQGLLTTSGSMVVNMEWGNFWSSHLPRTSYDIDLDAESPNPNDQGFEKMISG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 321 MYLGEIVRRVLLKMAEEAAFFGDiVPPKLKIPFILRTPHMSAMHHDESSDLRVVGSKLKDILEIPHTSLKMRKAIVELCD 400
Cdd:PLN02362 321 MYLGDIVRRVILRMSQESDIFGP-VSSRLSTPFVLRTPSVAAMHEDDSPELQEVARILKETLGISEVPLKVRKLVVKICD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 401 IVATRGARLSAAGIVGIIKKLGRDTV----------KDGEKQKSVIAMDGGLYEHYSKFSTCMESTLKELLGEEVSDNIA 470
Cdd:PLN02362 400 VVTRRAARLAAAGIVGILKKIGRDGSggitsgrsrsDIQIMRRTVVAVEGGLYTNYTMFREYLHEALNEILGEDVAQHVI 479
|
490 500
....*....|....*....|..
gi 2050315041 471 VEQSNDGSGIGAALLAASHSQY 492
Cdd:PLN02362 480 LKATEDGSGIGSALLAASYSSY 501
|
|
| PLN02914 |
PLN02914 |
hexokinase |
40-492 |
0e+00 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 606.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 40 ILREFEENCGTPIGKLRQVADAMAVEMHAGLASEGGSKLKMLISYVDNLPSGEENGLFYALDLGGTNFRVIRVLLGGKDG 119
Cdd:PLN02914 40 ILTKLQKDCATPLPVLRHVADAMAADMRAGLAVDGGGDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKDE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 120 GVVKQEFEEVSIPPHLMTGSSDALFGFIATALANFVATESEGLHPSPGRQRELGFTFSFPVRQTSIASGNLIKWTKGFLI 199
Cdd:PLN02914 120 RVIATEFEQVSIPQELMFGTSEELFDFIASGLANFVAKEGGKFHLPEGRKREIGFTFSFPVKQTSIDSGILMKWTKGFAV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 200 DDVVGQDVVGELTKAMERIGLDMRVSALVNDTIGTLAGGRYHNPDVIAAVILGTGTNAAYVERAQAIPKWHGLLPKSGEM 279
Cdd:PLN02914 200 SGTAGKDVVACLNEAMERQGLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKSSSGRT 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 280 VINMEWGNFrSSHLPLTEYDQDLDVESLNPGEQIFEKIISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPH 359
Cdd:PLN02914 280 IINTEWGAF-SDGLPLTEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALRTPH 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 360 MSAMHHDESSDLRVVGSKLKDILEIpHTSLKMRKAIVELCDIVATRGARLSAAGIVGIIKKLGRDTVKDGEKQKSVIAMD 439
Cdd:PLN02914 359 LCAMQQDNSDDLQAVGSILYDVLGV-EASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDSKGMIFGKRTVVAMD 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2050315041 440 GGLYEHYSKFSTCMESTLKELLGEEVSDNIAVEQSNDGSGIGAALLAASHSQY 492
Cdd:PLN02914 438 GGLYEKYPQYRRYMQDAVTELLGLELSKNIAIEHTKDGSGIGAALLAATNSKY 490
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
25-491 |
0e+00 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 536.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 25 RHRMRCSGRWARAMAILREFEENCGTPIGKLRQVADAMAVEMHAGLASEGGSKLKMLISYVDNLPSGEENGLFYALDLGG 104
Cdd:PLN02596 26 RWKRRKERQWKHTQRILRKFARECATPVSKLWEVADALVSDMTASLTAEETTTLNMLVSYVASLPSGDEKGLYYGLNLRG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 105 TNFRVIRVLLGGKDGGVVKQEFEEVSIPPHLMTGSSDALFGFIATALANFVATESEGLHPSPGRQRELGFTFSFPVRQTS 184
Cdd:PLN02596 106 SNFLLLRARLGGKNEPISDLYREEISIPSNVLNGTSQELFDYIALELAKFVAEHPGDEADTPERVKKLGFTVSYPVDQAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 185 IASGNLIKWtKGFLIDDVVGQDVVGELTKAMERIGLDMRVSALVNDTIGTLAGGRYHNPDVIAAVILGTGTNAAYVERAQ 264
Cdd:PLN02596 186 ASSGSAIKW-KSFSADDTVGKALVNDINRALEKHGLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQ 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 265 AIPKWHGLLPKSGEMVINMEWGNFRSSHLPLTEYDQDLDVESLNPGEQIFEKIISGMYLGEIVRRVLLKMAEEAAFFGDI 344
Cdd:PLN02596 265 AIPKWQSPSPESQEIVISTEWGNFNSCHLPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 345 VPPKLKIPFILRTPHMSAMHHDESSDLRVVGSKLKDILEIPHTSLKMRKAIVELCDIVATRGARLSAAGIVGIIKKLGRD 424
Cdd:PLN02596 345 LPPKLTTPYLLRSPDMAAMHQDTSEDHEVVNEKLKEIFGITDSTPMAREVVAEVCDIVAERGARLAGAGIVGIIKKLGRI 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050315041 425 tvkdgEKQKSVIAMDGGLYEHYSKFSTCMESTLKELLGEEVSDNIAVEQSNDGSGIGAALLAASHSQ 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. ... |
54-486 |
3.84e-169 |
|
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: 484.06 E-value: 3.84e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 54 KLRQVADAMAVEMHAGLASEGGSkLKMLISYVDNLPSGEENGLFYALDLGGTNFRVIRV-LLGGKDGGVVKQEfeEVSIP 132
Cdd:cd24018 3 KLEEIVKHFLSEMEKGLEGDGGS-LPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVtLDGNGGIFIIVQR--KYKIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 133 PHLMTGSSDALFGFIATALANFVATESEGLHPSPGRqrELGFTFSFPVRQTSIASGNLIKWTKGFLIDDVVGQDVVGELT 212
Cdd:cd24018 80 DEAKTGTGEELFDFIAECIAEFLEEHNLDLQSDKTI--PLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 213 KAMERIGLDMRVSALVNDTIGTLAGGRYHNPDVIAAVILGTGTNAAYVERAQAIPKWH---GLLPKSGEMVINMEWGNFR 289
Cdd:cd24018 158 NALDRRGVNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTspsGSVTKSDEMIINTEWGAFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 290 SSH--LPLTEYDQDLDVESLNPGEQIFEKIISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPHMSAMHHDE 367
Cdd:cd24018 238 NERevLPLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEADT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 368 SSDLRVVGSKLKDILEIPHTSLKMRKAIVELCDIVATRGARLSAAGIVGIIKKLGRDtvkdgEKQKSVIAMDGGLYEHYS 447
Cdd:cd24018 318 SPDLDAVRDILKELLAIDNTTLEDRKLIKRICELVSTRAARLSAAAIAAILLKRGSL-----LPEPVTVGIDGSVYEKYP 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 2050315041 448 KFSTCMESTLKELLGEEVSDNIAVEQSNDGSGIGAALLA 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 |
3.69e-152 |
|
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: 440.44 E-value: 3.69e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 54 KLRQVADAMAVEMHAGLASEG--GSKLKMLISYVDNLPSGEENGLFYALDLGGTNFRVIRVLLggKDGGVVKQEFEEVSI 131
Cdd:cd24019 6 QLEEIMDRLLKEMEKGLSKDThpTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTL--NGGSQVKMESEIYAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 132 PPHLMTGSSDALFGFIATALANFVatESEGLHpspGRQRELGFTFSFPVRQTSIASGNLIKWTKGFLIDDVVGQDVVGEL 211
Cdd:cd24019 84 PEEIMTGTGEQLFDYIAECLAEFL--EKNGLK---DKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 212 TKAMERIGL-DMRVSALVNDTIGTLAGGRYHNPDVIAAVILGTGTNAAYVERAQAIPKWHGLLPKSGEMVINMEWGNFRS 290
Cdd:cd24019 159 QEAIKRRGDiKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKWDGDEGDPGQVIINTEWGAFGD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 291 SH---LPLTEYDQDLDVESLNPGEQIFEKIISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPHMSAMHHDE 367
Cdd:cd24019 239 NGvldFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 368 SSDLRVVGSKLKDILEIPHTSLKMRkAIVELCDIVATRGARLSAAGIVGIIKKLGRDTVkdgekqksVIAMDGGLYEHYS 447
Cdd:cd24019 319 EGDFSNTREILKELGLEDASDEDCE-IVRYVCEAVSTRAAQLVAAGIAALLNRMNRKEV--------TVGVDGSLYKYHP 389
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2050315041 448 KFSTCMESTLKELLGEEVsdNIAVEQSNDGSGIGAALLAA 487
Cdd:cd24019 390 KFHKRMHETLKELVPPGC--KFKLMLSEDGSGKGAALVAA 427
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
55-486 |
8.89e-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: 365.83 E-value: 8.89e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 55 LRQVADAMAVEMHAGLASEGGSkLKMLISYVDNLPSGEENGLFYALDLGGTNFRVIRVLLGGKdgGVVKQEFEEVSIPPH 134
Cdd:cd24000 4 LKEITDAFLEELEKGLAGEPSS-LKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGK--GIEVTISKKYEIPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 135 LMTGSSDALFGFIATALANFVaTESEGLHPSPgrqreLGFTFSFPVRQTSIASGNLIKWTKGFLIDDVVGQDVVGELTKA 214
Cdd:cd24000 81 IKTASAEEFFDFIADCIAEFL-KENGLKKPLP-----LGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 215 MERIGLDMRVSALVNDTIGTLAGGRYHNPDVIAAVILGTGTNAAYVERAQAIpkwhglLPKSGEMVINMEWGNFRSSHLP 294
Cdd:cd24000 155 LKKRGLPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNI------LLGDGGMIINTEWGNFGKNSLP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 295 LTEYDQDLDVESLNPGEQIFEKIISGMYLGEIVRRVLLKMAEEaaffgdivppklkipfilrtphmsamhhdessdlrvv 374
Cdd:cd24000 229 RTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 375 gsklkdileiphtslkmrkAIVELCDIVATRGARLSAAGIVGIIKKLGRDTvkdgeKQKSVIAMDGGLYEHYSKFSTCME 454
Cdd:cd24000 272 -------------------ILRKICELVAERSARLAAAAIAALLRKTGDSP-----EKKITIAVDGSLFEKYPGYRERLE 327
|
410 420 430
....*....|....*....|....*....|..
gi 2050315041 455 STLKELLGEEvsDNIAVEQSNDGSGIGAALLA 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 ... |
65-486 |
3.84e-122 |
|
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: 364.79 E-value: 3.84e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 65 EMHAGLASEGGSkLKMLISYVDNLPSGEENGLFYALDLGGTNFRVIRVLLGGKDGGVVKQEfeEVSIPPHLMTG-SSDAL 143
Cdd:cd24088 14 QMEKGLAKHGKG-MAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHGDGTFSLRQE--KSKIPDELKTGvTAKDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 144 FGFIATALANFVATESEGLHPSPGRQRE--LGFTFSFPVRQTSIASGNLIKWTKGFLIDDVVGQDVVGELTKAMERIGLD 221
Cdd:cd24088 91 FDYLAKSVEAFLTKHHGDSFAAGKDDDRlkLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVVKLLQDELDRQGIP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 222 MRVSALVNDTIGTLAGGRYHNPDVIAAV---ILGTGTNAAYVERAQAIPKwhgLLPKS------GEMVINMEWGNFRS-- 290
Cdd:cd24088 171 VKVVALVNDTVGTLLARSYTSPEISGAVlgaIFGTGTNGAYLEDLEKIKK---LDDSSrvgkgkTHMVINTEWGSFDNel 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 291 SHLPLTEYDQDLDVESLNPGEQIFEKIISGMYLGEIVRRVLLKMAEEAAFFG---DIVPPKLKIPFILRTPHMSAMHHDE 367
Cdd:cd24088 248 KVLPTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFLIqynDKSPSALNTPYGLDTAVLSAIEIDS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 368 SSDLRVVGSKLKDILEIPHTSLKMRKAIVELCDIVATRGARLSAAGIVGIIKKLGRdtVKDGEKQKSVIAMDGGLYEHYS 447
Cdd:cd24088 328 EAELRATRKVLLDDLGLPAPSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGA--LNKSYDGEINIGVDGSVIEFYP 405
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2050315041 448 KFSTCMESTLKELL-GEEVSDNIAVEQSNDGSGIGAALLA 486
Cdd:cd24088 406 GFESMLREALRLLLiGAEGEKRIKIGIAKDGSGVGAALCA 445
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
54-487 |
1.34e-120 |
|
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar. The family corresponds to hexokinase PI and PII, which are also known as hexokinase-1/hexokinase-A and hexokinase-2/hexokinase-B, respectively.
Pssm-ID: 466937 [Multi-domain] Cd Length: 428 Bit Score: 360.15 E-value: 1.34e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 54 KLRQVADAMAVEMHAGLASEGGSkLKMLISYVDNLPSGEENGLFYALDLGGTNFRVIRVLLGGKdggvvkQEFE----EV 129
Cdd:cd24087 3 RLRKITDHFISELEKGLSKKGGN-IPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGN------GKFDitqsKY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 130 SIPPHLMTGSSDALFGFIATALANFVATESEGLHPSPgrqRELGFTFSFPVRQTSIASGNLIKWTKGFLIDDVVGQDVVG 209
Cdd:cd24087 76 RLPEELKTGTGEELWDFIADCLKKFVEEHFPGGKSEP---LPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 210 ELTKAMERIGLDMRVSALVNDTIGTLAGGRYHNPDVIAAVILGTGTNAAYVERAQAIPKWHGL-LPKSGEMVINMEWGNF 288
Cdd:cd24087 153 MLQKALKKRNVPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEHDdIPPDSPMAINCEYGAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 289 RSSH--LPLTEYDQDLDVESLNPGEQIFEKIISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPHMSAMHHD 366
Cdd:cd24087 233 DNEHlvLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 367 ESSDLRVVGSKLKDILEIpHTSLKMRKAIVELCDIVATRGARLSAAGIVGIIKKLGrdtvkdgeKQKSVIAMDGGLYEHY 446
Cdd:cd24087 313 PFENLEDTDDLFQHFFGL-ETTVPERKFIRRLAELIGTRAARLSACGIAAICKKRG--------YKTCHVAADGSVYNKY 383
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2050315041 447 SKFSTCMESTLKELLGEEVS-DNIAVEQSNDGSGIGAALLAA 487
Cdd:cd24087 384 PGFKERAAQALKDIFGWDGEdDPIKTVPAEDGSGVGAAIIAA 425
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
246-488 |
3.47e-109 |
|
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: 323.67 E-value: 3.47e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 246 IAAVILGTGTNAAYVERAQAIPKWHGLLPKSGEMVINMEWGNFRSSH---LPLTEYDQDLDVESLNPGEQIFEKIISGMY 322
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKLPKSGEMIINTEWGAFGDNGllpLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 323 LGEIVRRVLLKMAEEAAFFGDIVPpKLKIPFILRTPHMSAMHHDESSDLRVVGSKLKDILEIPHTSLKMRKAIVELCDIV 402
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKGQSE-KLKTPYSLDTSFLSAIESDPSEDLETTREILEELLGIETVTEEDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 403 ATRGARLSAAGIVGIIKKLGRDTvkdgekqKSVIAMDGGLYEHYSKFSTCMESTLKELLGeeVSDNIAVEQSNDGSGIGA 482
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-------KVTVGVDGSVYEKYPGFRERLQEALRELLG--PGDKVVLVLAEDGSGVGA 230
|
....*.
gi 2050315041 483 ALLAAS 488
Cdd:pfam03727 231 ALIAAV 236
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
54-487 |
4.44e-106 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 324.32 E-value: 4.44e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 54 KLRQVADAMAVEMHAGLASEGG---------SKLKMLISYVDNLPSGEENGLFYALDLGGTNFRVIRVLLGGkdGGVVKQ 124
Cdd:PTZ00107 24 KLKELVDYFLYELVEGLEAHRRhrnlwipneCSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFRAVRVSLRG--GGKMER 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 125 EFEEVSIPPHLMTG---------SSDALFGFIATALANFVatESEGLHPSPGRQRELGFTFSFPVRQTSIASGNLIKWTK 195
Cdd:PTZ00107 102 TQSKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMM--EENGDPEDLNKPVPVGFTFSFPCTQLSVNNAILIDWTK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 196 GF-----LIDDVVGQDVVGELTKAMERIGLDMRVSALVNDTIGTLAGGRY----HNPDVIAAVILGTGTNAAYVERAQAI 266
Cdd:PTZ00107 180 GFetgraTNDPVEGKDVGELLNDAFKRNNVPANVVAVLNDTVGTLISCAYqkpkNTPPCQVGVIIGTGSNACYFEPEVSA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 267 PKWHGllpksgeMVINMEWGNFrSSHLPLTEYDQDLDVESLNPGEQIFEKIISGMYLGEIVRRVLLKMAEEAAffgdivP 346
Cdd:PTZ00107 260 YGYAG-------TPINMECGNF-DSKLPITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLLQLKA------P 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 347 PKLKIPFILRTPHMSAMHHDESSDLRVVGSKLKDI--LEIPHTSLkmrKAIVELCDIVATRGARLSAAGIVGIIKKLGRD 424
Cdd:PTZ00107 326 PKMWQSGSFESEDASMILNDQSPDLQFSRQVIKEAwdVDLTDEDL---YTIRKICELVRGRAAQLAAAFIAAPAKKTRTV 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050315041 425 TvkdgekQKSVIAMDGGLYEHYSKFSTCMESTLKELLGEEVSDNIAVEqSNDGSGIGAALLAA 487
Cdd:PTZ00107 403 Q------GKATVAIDGSVYVKNPWFRRLLQEYINSILGPDAGNVVFYL-ADDGSGKGAAIIAA 458
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
55-488 |
8.57e-100 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 306.88 E-value: 8.57e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 55 LRQVADAMAVEMHAGLASEGGSkLKMLISYVdNLPSG-EENGLFYALDLGGTNFRVIRVLLGGKdggvvkQEFEEVSIPP 133
Cdd:COG5026 22 LEEIAAKFQEEMEKGLEGKKSS-LKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRFDGE------GTFEIENFKS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 134 HLMTGSS-----DALFGFIATALANFVateseglhpspGRQRELGFTFSFPVRQTSIASGNLIKWTKGFLIDDVVGQDVV 208
Cdd:COG5026 94 FPLPGTSseitaEEFFDFIADYIEPLL-----------DESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 209 GELTKAMERIGLD-MRVSALVNDTIGTLAGGRYHNPDVI----AAVILGTGTNAAYVERAQAIPKwhgLLPKSGEMVINM 283
Cdd:COG5026 163 ELLEAALARKGLDnVKPVAILNDTVATLLAGAYADPDDGysgyIGSILGTGHNTCYLEPNAPIGK---LPAYEGPMIINM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 284 EWGNFrsSHLPLTEYDQDLDVESLNPGEQIFEKIISGMYLGEIVRRVLLKMAEEAAFFGDIvPPKLKIPFILRTPHMSAM 363
Cdd:COG5026 240 ESGNF--NKLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEGLFSPGF-SEVFETPYSLTTVDMSRF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 364 HHDESSDLRVVGSKLKDILEiphtslKMRKAIVELCDIVATRGARLSAAGIVGIIKKLGrdtvKDGEKQKSV-IAMDGGL 442
Cdd:COG5026 317 LADPSDEKEILSQCLEAGSE------EDREILREIADAIVERAARLVAATLAGILLHLG----PGKTPLKPHcIAIDGST 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2050315041 443 YEHYSKFSTCMESTLKELLGEEVSDNIAVEQSNDGSGIGAALLAAS 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 |
9.46e-99 |
|
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: 304.00 E-value: 9.46e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 54 KLRQVADAMAVEMHAGLASEGG--SKLKMLISYVDNLPSGEENGLFYALDLGGTNFRVIRVLLGGKDGGVVKQEFEEVSI 131
Cdd:cd24089 6 TLLDISRRFRKEMEKGLGKDTHptATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMESQVYAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 132 PPHLMTGSSDALFGFIATALANFVatESEGLHpspGRQRELGFTFSFPVRQTSIASGNLIKWTKGFLIDDVVGQDVVGEL 211
Cdd:cd24089 86 PEEIMHGSGTQLFDHVAECLADFM--DKQKIK---DKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 212 TKAMERIG-LDMRVSALVNDTIGTLAGGRYHNPDVIAAVILGTGTNAAYVERAQAIPKWHGllpKSGEMVINMEWGNFR- 289
Cdd:cd24089 161 RKAIRRRGdYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEG---DEGRMCINTEWGAFGd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 290 --SSHLPLTEYDQDLDVESLNPGEQIFEKIISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPHMSAMhHDE 367
Cdd:cd24089 238 dgSLEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAI-EKE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 368 SSDLRVVGSKLKDILEIPhtSLKMRKAIVELCDIVATRGARLSAAGIVGIIKKLGRDtvKDGEKQKSVIAMDGGLYEHYS 447
Cdd:cd24089 317 KEGLANAKEILTRLGLDP--SEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLREN--KGLERLRTTVGVDGSVYKKHP 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2050315041 448 KFSTCMESTLKELLGEEvsdNIAVEQSNDGSGIGAALLAA 487
Cdd:cd24089 393 QFSKRLHKAVRRLVPDC---DVRFLLSEDGSGKGAAMVTA 429
|
|
| 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 |
3.46e-93 |
|
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the second two domains of types I to III hexokinases. Type I enzyme may have a catabolic function, producing H6P for energy production in glycolysis; it is bound to the mitochondrial membrane, which enables the coordination of glycolysis with the TCA cycle. Types II and III enzyme may have anabolic functions, providing H6P for glycogen or lipid synthesis.
Pssm-ID: 466941 [Multi-domain] Cd Length: 433 Bit Score: 289.83 E-value: 3.46e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 54 KLRQVADAMAVEMHAGLASE--GGSKLKMLISYVDNLPSGEENGLFYALDLGGTNFRVIRVLLGGKDGGVVKQEFEEVSI 131
Cdd:cd24091 6 QLLEVKARMRAEMERGLRKEthASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHNKIYAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 132 PPHLMTGSSDALFGFIATALANFVatESEGLHpspGRQRELGFTFSFPVRQTSIASGNLIKWTKGFLIDDVVGQDVVGEL 211
Cdd:cd24091 86 PQEIMQGTGEELFDHIVQCIADFL--EYMGLK---GVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 212 TKAMERIG-LDMRVSALVNDTIGTLAGGRYHNPDVIAAVILGTGTNAAYVERAQAIPKWHGllpKSGEMVINMEWGNFRS 290
Cdd:cd24091 161 REAIKRREeFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEG---EEGRMCINMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 291 S----HLpLTEYDQDLDVESLNPGEQIFEKIISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPHMSAMHHD 366
Cdd:cd24091 238 NgcldDI-RTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 367 ESSdLRVVGSKLKDiLEIPHTSlkmRKAIV--ELCDIVATRGARLSAAGIVGIIKKLGRDtvKDGEKQKSVIAMDGGLYE 444
Cdd:cd24091 317 RLA-LLQVRAILQQ-LGLDSTC---DDSIIvkEVCGVVSRRAAQLCGAGMAAVVDKIREN--RGLDHLNVTVGVDGTLYK 389
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2050315041 445 HYSKFSTCMESTLKELLGEEVsdnIAVEQSNDGSGIGAALLAA 487
Cdd:cd24091 390 LHPHFSRVMHETVKELAPKCD---VTFLQSEDGSGKGAALITA 429
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
40-240 |
3.88e-93 |
|
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: 281.31 E-value: 3.88e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 40 ILREFEENCGTPIGKLRQVADAMAVEMHAGLASEGGSKLKMLISYVDNLPSGEENGLFYALDLGGTNFRVIRVLLGGKdg 119
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGGD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 120 GVVKQEFEEVSIPPHLMTGSSDALFGFIATALANFVatESEGLHPSPGRQRELGFTFSFPVRQTSIASGNLIKWTKGFLI 199
Cdd:pfam00349 79 GKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFL--KEHGLEDFEEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2050315041 200 DDVVGQDVVGELTKAMERIGLDMRVSALVNDTIGTLAGGRY 240
Cdd:pfam00349 157 PGVVGKDVVQLLQEALERRGLPVKVVALVNDTVGTLMAGAY 197
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
54-487 |
1.87e-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: 280.23 E-value: 1.87e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 54 KLRQVADAMAVEMHAGLASE--GGSKLKMLISYVDNLPSGEENGLFYALDLGGTNFRVIRVLLGgKDGgvVKQEFEEVSI 131
Cdd:cd24129 6 QLAAVQAQMRKEMAKGLRGEthAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVG-TAG--VQITSEIYSI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 132 PPHLMTGSSDALFGFIATALANFvaTESEGLHpspGRQRELGFTFSFPVRQTSIASGNLIKWTKGFLIDDVVGQDVVGEL 211
Cdd:cd24129 83 PETVAQGTGQQLFDHIVDCIVDF--QQKQGLS---GQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 212 TKAMERI-GLDMRVSALVNDTIGTLAGGRYHNPDVIAAVILGTGTNAAYVERAQAIpkwhGLLP-KSGEMVINMEWGNF- 288
Cdd:cd24129 158 REAATRKqAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNV----AGVPgDSGRMCINMEWGAFg 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 289 --RSSHLPLTEYDQDLDVESLNPGEQIFEKIISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPHMSAMHHD 366
Cdd:cd24129 234 dnGCLAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 367 eSSDLRVVGSKLKDiLEIPHTSlKMRKAIVELCDIVATRGARLSAAGIVGIIKKLGRDtvKDGEKQKSVIAMDGGLYEHY 446
Cdd:cd24129 314 -SLALRQVRAILED-LGLPLTS-DDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMREN--RGLDELAVTVGVDGTLYKLH 388
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2050315041 447 SKFSTCMESTLKELlgeEVSDNIAVEQSNDGSGIGAALLAA 487
Cdd:cd24129 389 PRFSSLVQATVREL---APRCVVTFLQSEDGSGKGAALVTA 426
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
55-487 |
5.70e-86 |
|
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: 271.34 E-value: 5.70e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 55 LRQVADAMAVEMHAGLASEGGSK--LKMLISYVDNLPSGEENGLFYALDLGGTNFRVIRVLLGGKDGGVVKQEFEEVSIP 132
Cdd:cd24126 7 LLDIMTRFRAEMEKGLAKDTNPTaaVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMESQFYPTP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 133 PHLMTGSSDALFGFIATALANFVATeseglHPSPGRQRELGFTFSFPVRQTSIASGNLIKWTKGFLIDDVVGQDVVGELT 212
Cdd:cd24126 87 EEIIHGTGTELFDYVAECLADFMKK-----KGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 213 KAMERIG-LDMRVSALVNDTIGTLAGGRYHNPDVIAAVILGTGTNAAYVERAQAIPKWHGllpKSGEMVINMEWGNFRSS 291
Cdd:cd24126 162 KAIRKHKdVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEG---DEGRMCINTEWGAFGDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 292 HLP---LTEYDQDLDVESLNPGEQIFEKIISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPHMSAMHHDES 368
Cdd:cd24126 239 GSLediRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 369 ---------SDLRVVGSKlKDILEIPHtslkmrkaiveLCDIVATRGARLSAAGIVGIIKKLGRDtvKDGEKQKSVIAMD 439
Cdd:cd24126 319 glyntreilSDLGLEPSE-EDCIAVQH-----------VCTIVSFRSANLCAAALAAILTRLREN--KKLERLRTTVGMD 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2050315041 440 GGLYEHYSKFSTCMESTLKELLGeevSDNIAVEQSNDGSGIGAALLAA 487
Cdd:cd24126 385 GTVYKTHPQYAKRLHKVVRRLVP---SCDVRFLLSESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
54-487 |
3.58e-84 |
|
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: 266.77 E-value: 3.58e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 54 KLRQVADAMAVEMHAGLASE--GGSKLKMLISYVDNLPSGEENGLFYALDLGGTNFRVIRV-LLGGKDGGVVKQEfEEVS 130
Cdd:cd24128 6 QLLEVKRRMKVEMERGLSKEthASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVrVRNGKWRGVEMHN-KIYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 131 IPPHLMTGSSDALFGFIATALANFVatESEGLHpspGRQRELGFTFSFPVRQTSIASGNLIKWTKGFLIDDVVGQDVVGE 210
Cdd:cd24128 85 IPQEVMHGTGEELFDHIVHCIADFL--EYMGMK---GVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 211 LTKAMERI-GLDMRVSALVNDTIGTLAGGRYHNPDVIAAVILGTGTNAAYVERAQAIPKWHGllpKSGEMVINMEWGNFR 289
Cdd:cd24128 160 LKEAIHRReEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEG---EEGRMCVNMEWGAFG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 290 SSHLP---LTEYDQDLDVESLNPGEQIFEKIISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPHMSAMHHD 366
Cdd:cd24128 237 DNGCLddfRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 367 ESSDLRVvgsklKDILEipHTSLKMR---KAIV-ELCDIVATRGARLSAAGIVGIIKKLGRDtvKDGEKQKSVIAMDGGL 442
Cdd:cd24128 317 RLALLQV-----RAILQ--HLGLESTcddSIIVkEVCTVVARRAAQLCGAGMAAVVDKIREN--RGLDALKVTVGVDGTL 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2050315041 443 YEHYSKFSTCMESTLKELLGE-EVSdniaVEQSNDGSGIGAALLAA 487
Cdd:cd24128 388 YKLHPHFAKVMHETVKDLAPKcDVS----FLQSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
55-487 |
7.67e-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: 265.60 E-value: 7.67e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 55 LRQVADAMAVEMHAGLASEGG--SKLKMLISYVDNLPSGEENGLFYALDLGGTNFRVIRVLLggKDGGVVKQEFEE--VS 130
Cdd:cd24125 7 LLEISKRFRKEMEKGLGATTHptAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKV--SDNGLQKVEMENqiYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 131 IPPHLMTGSSDALFGFIATALANFVatESEGLHPspgRQRELGFTFSFPVRQTSIASGNLIKWTKGFLIDDVVGQDVVGE 210
Cdd:cd24125 85 IPEDIMRGSGTQLFDHIAECLANFM--DKLQIKD---KKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 211 LTKAMERIG-LDMRVSALVNDTIGTLAGGRYHNPDVIAAVILGTGTNAAYVERAQAIPKWHGllpKSGEMVINMEWGNFR 289
Cdd:cd24125 160 LRKAIQKRGdFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEG---DEGRMCINMEWGAFG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 290 SSHL---PLTEYDQDLDVESLNPGEQIFEKIISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPHMSAMHHD 366
Cdd:cd24125 237 DDGSlddIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 367 ESSDLRVVGSKLKDILEIPHTSLkmrKAIVELCDIVATRGARLSAAGIVGIIKKLGRDtvKDGEKQKSVIAMDGGLYEHY 446
Cdd:cd24125 317 KDGIRKAREVLMRLGLDPTQEDC---VATHRICQIVSTRSASLCAATLAAVLQRIKEN--KGEERLRSTIGVDGSVYKKH 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2050315041 447 SKFSTCMESTLKELLGEevsDNIAVEQSNDGSGIGAALLAA 487
Cdd:cd24125 392 PHFARRLHKTVRRLVPG---CDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
54-487 |
1.26e-81 |
|
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: 260.25 E-value: 1.26e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 54 KLRQVADAMAVEMHAGLASE--GGSKLKMLISYVDNLPSGEENGLFYALDLGGTNFRVIRV-LLGGKDGgvVKQEFEEVS 130
Cdd:cd24130 6 QLQEVKQKMRTELEYGLKKEthPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVkIRSGRRS--VRMYNKIFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 131 IPPHLMTGSSDALFGFIATALANFVatESEGLHpspGRQRELGFTFSFPVRQTSIASGNLIKWTKGFLIDDVVGQDVVGE 210
Cdd:cd24130 84 IPLEIMQGTGEELFDHIVQCIADFL--DYMGLK---GARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 211 LTKAMERIG-LDMRVSALVNDTIGTLAGGRYHNPDVIAAVILGTGTNAAYVERAQAIPKWHGllpKSGEMVINMEWGNFR 289
Cdd:cd24130 159 LREAIKRRNeFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEG---DEGRMCINTEWGGFG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 290 SSHLP---LTEYDQDLDVESLNPGEQIFEKIISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPHMSAMHHD 366
Cdd:cd24130 236 DNGCIddiRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 367 ESSDLRVvgsklKDILEIPHTSLKMRKAIV--ELCDIVATRGARLSAAGIVGIIKKLGRDtvKDGEKQKSVIAMDGGLYE 444
Cdd:cd24130 316 RLALLQV-----RRILQQLGLDSTCEDSIIvkEVCGAVSRRAAQLCGAGLAAIVEKIREN--QGLDRLDITVGVDGTLYK 388
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2050315041 445 HYSKFSTCMESTLKELLGEevsDNIAVEQSNDGSGIGAALLAA 487
Cdd:cd24130 389 LHPHFSRILQETVKELAPQ---CDVTFMLSEDGSGKGAALITA 428
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
54-487 |
1.97e-81 |
|
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: 259.46 E-value: 1.97e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 54 KLRQVADAMAVEMHAGLASE--GGSKLKMLISYVDNLPSGEENGLFYALDLGGTNFRVIRVLLGGKDGGVVKQEFEEVSI 131
Cdd:cd24127 6 MLLEVKKRMRAEMELGLRKQthNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 132 PPHLMTGSSDALFGFIATALANFVatESEGLHpspGRQRELGFTFSFPVRQTSIASGNLIKWTKGFLIDDVVGQDVVGEL 211
Cdd:cd24127 86 PIEIMQGTGEELFDHIVSCISDFL--DYMGIK---GPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 212 TKAMERIG-LDMRVSALVNDTIGTLAGGRYHNPDVIAAVILGTGTNAAYVERAQAIPKWHGllpKSGEMVINMEWGNFRS 290
Cdd:cd24127 161 RDAIKRREeFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEG---DQGQMCINMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 291 SHL---PLTEYDQDLDVESLNPGEQIFEKIISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPHMSAMHHDE 367
Cdd:cd24127 238 NGClddIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 368 SSDLRVvgsklKDILEIPHTSLKMRKAIV--ELCDIVATRGARLSAAGIVGIIKKLGRDtvKDGEKQKSVIAMDGGLYEH 445
Cdd:cd24127 318 LALLQV-----RAILQQLGLNSTCDDSILvkTVCGVVSRRAAQLCGAGMAAVVDKIREN--RGLDHLNVTVGVDGTLYKL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2050315041 446 YSKFSTCMESTLKELlgeEVSDNIAVEQSNDGSGIGAALLAA 487
Cdd:cd24127 391 HPHFSRIMHQTVKEL---SPKCNVSFLLSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
55-487 |
1.24e-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: 256.08 E-value: 1.24e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 55 LRQVADAMAVEMHAGLASEGG--SKLKMLISYVDNLPSGEENGLFYALDLGGTNFRVIRVLLGGKDGGVVKQEFEEVSIP 132
Cdd:cd24124 35 LIDIMTRFRKEMKNGLSRDFNptATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 133 PHLMTGSSDALFGFIATALANFVATESeglhpSPGRQRELGFTFSFPVRQTSIASGNLIKWTKGFLIDDVVGQDVVGELT 212
Cdd:cd24124 115 ENIVHGSGSQLFDHVAECLGDFMEKRK-----IKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 213 KAMERIG-LDMRVSALVNDTIGTLAGGRYHNPDVIAAVILGTGTNAAYVERAQAIPKWHGllpKSGEMVINMEWGNFR-- 289
Cdd:cd24124 190 KAIKKRGdYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEG---DEGRMCINTEWGAFGdd 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 290 -SSHLPLTEYDQDLDVESLNPGEQIFEKIISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPHMSAMHHDES 368
Cdd:cd24124 267 gSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 369 SDlrvvgSKLKDILeiphTSLKMRK------AIVELCDIVATRGARLSAAGIVGIIKKLgRDTvKDGEKQKSVIAMDGGL 442
Cdd:cd24124 347 GL-----HNAKEIL----TRLGVEPsdddcvSVQHVCTIVSFRSANLVAATLGAILNRL-RDN-KGTPRLRTTVGVDGSL 415
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2050315041 443 YEHYSKFSTCMESTLKELLGEEvsdNIAVEQSNDGSGIGAALLAA 487
Cdd:cd24124 416 YKTHPQYSRRFHKTLRRLVPDS---DVRFLLSESGSGKGAAMVTA 457
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
55-487 |
1.81e-77 |
|
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to type IV hexokinase. It is found in the liver and pancreatic beta-cells, where it is controlled by insulin (activation) and glucagon (inhibition). In pancreatic beta-cells, type IV enzyme acts as a glucose sensor to modify insulin secretion. Mutations in type IV hexokinase have been associated with diabetes mellitus.
Pssm-ID: 466942 [Multi-domain] Cd Length: 444 Bit Score: 249.41 E-value: 1.81e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 55 LRQVADAMAVEMHAGLASEG--GSKLKMLISYVDNLPSGEENGLFYALDLGGTNFRVIRVLLG-GKDGG-VVKQEFEEVS 130
Cdd:cd24092 16 LKKVMRRMQKEMDRGLRLETheEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGeGEEGQwSVKTKHQMYS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 131 IPPHLMTGSSDALFGFIATALANFVATeseglHPSPGRQRELGFTFSFPVRQTSIASGNLIKWTKGFLIDDVVGQDVVGE 210
Cdd:cd24092 96 IPEDAMTGTAEMLFDYISECISDFLDK-----HQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVGL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 211 LTKAMERIG-LDMRVSALVNDTIGTLAGGRYHNPDVIAAVILGTGTNAAYVERAQAIPKWHGllpKSGEMVINMEWGNF- 288
Cdd:cd24092 171 LRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEG---DEGRMCVNTEWGAFg 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 289 RSSHLP--LTEYDQDLDVESLNPGEQIFEKIISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPHMSAMHHD 366
Cdd:cd24092 248 DSGELDefLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 367 eSSDLRVVGSKLKDILEIPHTSlkmRKAIVEL-CDIVATRGARLSAAGIVGIIKKLgRDTvKDGEKQKSVIAMDGGLYEH 445
Cdd:cd24092 328 -TGDRKQIYNILSTLGLRPSTT---DCDIVRRaCESVSTRAAHMCSAGLAGVINRM-RES-RSEDVMRITVGVDGSVYKL 401
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2050315041 446 YSKFSTCMESTLKELLGeevSDNIAVEQSNDGSGIGAALLAA 487
Cdd:cd24092 402 HPSFKERFHASVRRLTP---SCEITFIESEEGSGRGAALVSA 440
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
51-487 |
1.35e-73 |
|
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: 239.05 E-value: 1.35e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 51 PIGKLRQVADAMAVEMHAGLASEGG--SKLKMLISYVDNLPSGEENGLFYALDLG--GTNFRVIRVLLGGKDGGVVKQEF 126
Cdd:cd24090 3 TRAQLQQIQASLLGSMEQALRGQASpaPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 127 EEVSIPPHLMTGSSDALFGFIATALANFVATEseglhPSPGRQRELGFTFSFPVRQTSIASGNLIKWTKGFLIDDVVGQD 206
Cdd:cd24090 83 QEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQ-----PVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 207 VVGELTKAMERIGL-DMRVSALVNDTIGTLAGGRYHNPDVIAAVILGTGTNAAYVERAQAIPKwhgLLPKSGEMVINMEW 285
Cdd:cd24090 158 VVQLLRDAIQRQGAyNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAV---LDEDRGRVCVSVEW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 286 GNFR---SSHLPLTEYDQDLDVESLNPGEQIFEKIISGMYLGEIVRRVLLKMAEEAAFFGDIVPPKLKIPFILRTPHMSA 362
Cdd:cd24090 235 GSFSddgALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050315041 363 MhHDESSDLRVVGSKLKDILEIPHTSLKMRkaIVELCDIVATRGARLSAAGIVGIIKKLGRDTvkdGEKQKSV-IAMDGG 441
Cdd:cd24090 315 M-EDPSAGAARVRAILQDLGLSPSASDVEL--VQHVCRAVCTRAAQLCAAALAAVLSHLQHSR---EQQTLQVaVATGGR 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2050315041 442 LYEHYSKFSTCMESTLKeLLGEEVsdNIAVEQSNDGSGIGAALLAA 487
Cdd:cd24090 389 VCERHPRFCSILQGTVM-LLAPEC--DVSFIPSVDGGGRGVAMVTA 431
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
210-263 |
6.84e-03 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 38.71 E-value: 6.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2050315041 210 ELTKAMERIGLDMRVsALVNDTIGTLAGGryHNPDVIAAVILGTGTNAAYVERA 263
Cdd:COG2971 82 ALEAALRELFPFARV-VVVNDALAALAGA--LGGEDGIVVIAGTGSIAAGRDGD 132
|
|
| |
