|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02405 |
PLN02405 |
hexokinase |
1-496 |
0e+00 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 936.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 1 MGKVAVGTTVVCTAAVCAVAVLVVRRRMQSSGKWGRVSAILKAFEEDCATPISKLRQVADAMAVEMHAGLASDGGSKLKM 80
Cdd:PLN02405 1 MGKVAVGAAVVCAAAVCAAAALVVRRRMKSSGKWARAMEILKEFEEDCATPIGKLRQVADAMTVEMHAGLASEGGSKLKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 81 LISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQDRVAKQEFEEVSIPPHLMTGGSDELFNFIAEALAKFVATEGE 160
Cdd:PLN02405 81 LISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVSIPPHLMTGSSDALFDFIAAALAKFVATEGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 161 DFHLPEGRQRELGFTFSFPVRQTSLSSGSLIKWTKGFSIDEAVGEDVVGALKKAMERVGLDMRVAALVNDTVGTLAGGRY 240
Cdd:PLN02405 161 DFHLPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMERVGLDMRVSALVNDTIGTLAGGRY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 241 YNPDVAAAVILGTGTNAAYVERATAIPKWHGPLPKSGEMVINMEWGNFRSSHLPLTEFDHTLDFESLNPGEQILEKIISG 320
Cdd:PLN02405 241 YNPDVVAAVILGTGTNAAYVERAQAIPKWHGLLPKSGEMVINMEWGNFRSSHLPLTEYDHALDVESLNPGEQIFEKIISG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 321 MYLGEILRRVLLKMAEEAAFFGDTVPSKLRIPFIIRTPHMSAMHNDTSPDLKIVGSKIKDILEVPTTSLKMRKVVISLCD 400
Cdd:PLN02405 321 MYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHDTSPDLKVVGSKLKDILEIPNTSLKMRKVVVELCN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 401 IIATRGARLSAAGIYGILKKLGRDTTSKEEVQKSVIAMDGGLFEHYKQFSECMESSLKELLGDEASGTIEVIHSNDGSGI 480
Cdd:PLN02405 401 IVATRGARLSAAGIYGILKKLGRDTVKDGEKQKSVIAMDGGLFEHYTEFSKCMESTLKELLGEEVSESIEVEHSNDGSGI 480
|
490
....*....|....*.
gi 727550411 481 GAALLAASHSLYLEES 496
Cdd:PLN02405 481 GAALLAASHSLYLEVE 496
|
|
| 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: 814.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 50 TPISKLRQVADAMAVEMHAGLASDGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQDRVAKQEFEEV 129
Cdd:cd24020 1 TPVSRLRQVADAMVVEMEAGLASEGGSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 130 SIPPHLMTGGSDELFNFIAEALAKFVATEGEDFHlPEGRQRELGFTFSFPVRQTSLSSGSLIKWTKGFSIDEAVGEDVVG 209
Cdd:cd24020 81 PIPPELMVGTSEELFDFIAGELAKFVATEGEGFH-PEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 210 ALKKAMERVGLDMRVAALVNDTVGTLAGGRYYNPDVAAAVILGTGTNAAYVERATAIPKWHGPLPKSGEMVINMEWGNFR 289
Cdd:cd24020 160 LLEEALERQGLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGLPRSGEMVINTEWGNFR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 290 SSHLPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPSKLRIPFIIRTPHMSAMHNDTSP 369
Cdd:cd24020 240 SSHLPRTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMHEDDSP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 370 DLKIVGSKIKDILEVPTTSLKMRKVVISLCDIIATRGARLSAAGIYGILKKLGRDTTSKEEVQKSVIAMDGGLFEHYKQF 449
Cdd:cd24020 320 DLETVARILKDALGIDDTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLGRDGGGSSPAQRTVVAVDGGLYEHYPKF 399
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 727550411 450 SECMESSLKELLGDEASGTIEVIHSNDGSGIGAALLAASH 489
Cdd:cd24020 400 REYMQQALVELLGDEAADSVELELSNDGSGIGAALLAAAH 439
|
|
| PLN02914 |
PLN02914 |
hexokinase |
37-492 |
0e+00 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 610.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 37 VSAILKAFEEDCATPISKLRQVADAMAVEMHAGLASDGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGG 116
Cdd:PLN02914 37 VAPILTKLQKDCATPLPVLRHVADAMAADMRAGLAVDGGGDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 117 KQDRVAKQEFEEVSIPPHLMTGGSDELFNFIAEALAKFVATEGEDFHLPEGRQRELGFTFSFPVRQTSLSSGSLIKWTKG 196
Cdd:PLN02914 117 KDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFVAKEGGKFHLPEGRKREIGFTFSFPVKQTSIDSGILMKWTKG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 197 FSIDEAVGEDVVGALKKAMERVGLDMRVAALVNDTVGTLAGGRYYNPDVAAAVILGTGTNAAYVERATAIPKWHGPLPKS 276
Cdd:PLN02914 197 FAVSGTAGKDVVACLNEAMERQGLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKSSS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 277 GEMVINMEWGNFrSSHLPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPSKLRIPFIIR 356
Cdd:PLN02914 277 GRTIINTEWGAF-SDGLPLTEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALR 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 357 TPHMSAMHNDTSPDLKIVGSKIKDILEVpTTSLKMRKVVISLCDIIATRGARLSAAGIYGILKKLGRDTTSKEEVQKSVI 436
Cdd:PLN02914 356 TPHLCAMQQDNSDDLQAVGSILYDVLGV-EASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDSKGMIFGKRTVV 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 727550411 437 AMDGGLFEHYKQFSECMESSLKELLGDEASGTIEVIHSNDGSGIGAALLAASHSLY 492
Cdd:PLN02914 435 AMDGGLYEKYPQYRRYMQDAVTELLGLELSKNIAIEHTKDGSGIGAALLAATNSKY 490
|
|
| PLN02362 |
PLN02362 |
hexokinase |
1-492 |
0e+00 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 601.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 1 MGKVAVGTTVVCTAAVCAVAVLVVRRRMQSSGKWGRVSAILKAFEEDCATPISKLRQVADAMAVEMHAGLASDGGSKLKM 80
Cdd:PLN02362 1 MGKVAVGLAAAAAVAACAVAAVMVGRRVKSRRKWRRVVGVLKELEEACETPVGRLRQVVDAMAVEMHAGLASEGGSKLKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 81 LISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQDRVAKQEFEEVSIPPHLMTGGSDELFNFIAEALAKFVATEGE 160
Cdd:PLN02362 81 LLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRSSILSQDVERHPIPQHLMNSTSEVLFDFIASSLKQFVEKEEN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 161 DFHLPEGRQRELGFTFSFPVRQTSLSSGSLIKWTKGFSIDEAVGEDVVGALKKAMERVGLDMRVAALVNDTVGTLAGGRY 240
Cdd:PLN02362 161 GSEFSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRRGLDMRVAALVNDTVGTLALGHY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 241 YNPDVAAAVILGTGTNAAYVERATAIPKWHGPLPKSGEMVINMEWGNFRSSHLPLTEFDHTLDFESLNPGEQILEKIISG 320
Cdd:PLN02362 241 HDPDTVAAVIIGTGTNACYLERTDAIIKCQGLLTTSGSMVVNMEWGNFWSSHLPRTSYDIDLDAESPNPNDQGFEKMISG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 321 MYLGEILRRVLLKMAEEAAFFGdTVPSKLRIPFIIRTPHMSAMHNDTSPDLKIVGSKIKDILEVPTTSLKMRKVVISLCD 400
Cdd:PLN02362 321 MYLGDIVRRVILRMSQESDIFG-PVSSRLSTPFVLRTPSVAAMHEDDSPELQEVARILKETLGISEVPLKVRKLVVKICD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 401 IIATRGARLSAAGIYGILKKLGRDTT----------SKEEVQKSVIAMDGGLFEHYKQFSECMESSLKELLGDEASGTIE 470
Cdd:PLN02362 400 VVTRRAARLAAAGIVGILKKIGRDGSggitsgrsrsDIQIMRRTVVAVEGGLYTNYTMFREYLHEALNEILGEDVAQHVI 479
|
490 500
....*....|....*....|..
gi 727550411 471 VIHSNDGSGIGAALLAASHSLY 492
Cdd:PLN02362 480 LKATEDGSGIGSALLAASYSSY 501
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
25-488 |
0e+00 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 531.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 25 RRRMQSSGKWGRVSAILKAFEEDCATPISKLRQVADAMAVEMHAGLASDGGSKLKMLISYVDNLPSGDEKGLFYALDLGG 104
Cdd:PLN02596 26 RWKRRKERQWKHTQRILRKFARECATPVSKLWEVADALVSDMTASLTAEETTTLNMLVSYVASLPSGDEKGLYYGLNLRG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 105 TNFRVMRVLLGGKQDRVAKQEFEEVSIPPHLMTGGSDELFNFIAEALAKFVAT-EGEDFHLPEgRQRELGFTFSFPVRQT 183
Cdd:PLN02596 106 SNFLLLRARLGGKNEPISDLYREEISIPSNVLNGTSQELFDYIALELAKFVAEhPGDEADTPE-RVKKLGFTVSYPVDQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 184 SLSSGSLIKWtKGFSIDEAVGEDVVGALKKAMERVGLDMRVAALVNDTVGTLAGGRYYNPDVAAAVILGTGTNAAYVERA 263
Cdd:PLN02596 185 AASSGSAIKW-KSFSADDTVGKALVNDINRALEKHGLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 264 TAIPKWHGPLPKSGEMVINMEWGNFRSSHLPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGD 343
Cdd:PLN02596 264 QAIPKWQSPSPESQEIVISTEWGNFNSCHLPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGD 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 344 TVPSKLRIPFIIRTPHMSAMHNDTSPDLKIVGSKIKDILEVPTTSLKMRKVVISLCDIIATRGARLSAAGIYGILKKLGR 423
Cdd:PLN02596 344 TLPPKLTTPYLLRSPDMAAMHQDTSEDHEVVNEKLKEIFGITDSTPMAREVVAEVCDIVAERGARLAGAGIVGIIKKLGR 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727550411 424 dttskEEVQKSVIAMDGGLFEHYKQFSECMESSLKELLGDEASGTIEVIHSNDGSGIGAALLAAS 488
Cdd:PLN02596 424 -----IENKKSVVTVEGGLYEHYRVFRNYLHSSVWEMLGSELSDNVVIEHSHGGSGAGALFLAAC 483
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
53-486 |
4.56e-166 |
|
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. It is a putative glucokinase that functions in phosphorylation of aldohexoses and glucose uptake. It is involved in sporulation and required for the full activation of the early meiotic inducer IME1. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar.
Pssm-ID: 466868 [Multi-domain] Cd Length: 431 Bit Score: 475.97 E-value: 4.56e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 53 SKLRQVADAMAVEMHAGLASDGGSkLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRV-LLGGKQDRVAKQEfeEVSI 131
Cdd:cd24018 2 SKLEEIVKHFLSEMEKGLEGDGGS-LPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVtLDGNGGIFIIVQR--KYKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 132 PPHLMTGGSDELFNFIAEALAKFVATEGEDFHLPEGRqrELGFTFSFPVRQTSLSSGSLIKWTKGFSIDEAVGEDVVGAL 211
Cdd:cd24018 79 PDEAKTGTGEELFDFIAECIAEFLEEHNLDLQSDKTI--PLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 212 KKAMERVGLDMRVAALVNDTVGTLAGGRYYNPDVAAAVILGTGTNAAYVERATAIPKWHGPL---PKSGEMVINMEWGNF 288
Cdd:cd24018 157 QNALDRRGVNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTSPSgsvTKSDEMIINTEWGAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 289 RSSH--LPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPSKLRIPFIIRTPHMSAMHND 366
Cdd:cd24018 237 DNERevLPLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEAD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 367 TSPDLKIVGSKIKDILEVPTTSLKMRKVVISLCDIIATRGARLSAAGIYGILKKlgRDTTSKEEVqksVIAMDGGLFEHY 446
Cdd:cd24018 317 TSPDLDAVRDILKELLAIDNTTLEDRKLIKRICELVSTRAARLSAAAIAAILLK--RGSLLPEPV---TVGIDGSVYEKY 391
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 727550411 447 KQFSECMESSLKELLGDEASGTIEVIHSNDGSGIGAALLA 486
Cdd:cd24018 392 PGFKDRLSEALRELFGPEVKANISLVLAKDGSGLGAAIIA 431
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
54-487 |
2.88e-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: 438.13 E-value: 2.88e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 54 KLRQVADAMAVEMHAGLASDG--GSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQDrvAKQEFEEVSI 131
Cdd:cd24019 6 QLEEIMDRLLKEMEKGLSKDThpTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGGSQ--VKMESEIYAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 132 PPHLMTGGSDELFNFIAEALAKFVATEG-EDFHLPegrqreLGFTFSFPVRQTSLSSGSLIKWTKGFSIDEAVGEDVVGA 210
Cdd:cd24019 84 PEEIMTGTGEQLFDYIAECLAEFLEKNGlKDKKLP------LGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 211 LKKAMERVGL-DMRVAALVNDTVGTLAGGRYYNPDVAAAVILGTGTNAAYVERATAIPKWHGPLPKSGEMVINMEWGNFR 289
Cdd:cd24019 158 LQEAIKRRGDiKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKWDGDEGDPGQVIINTEWGAFG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 290 SSH---LPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPSKLRIPFIIRTPHMSAMHND 366
Cdd:cd24019 238 DNGvldFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 367 TSPDLkivgSKIKDILE---VPTTSLKMRKVVISLCDIIATRGARLSAAGIYGILKKLGRdttskeevQKSVIAMDGGLF 443
Cdd:cd24019 318 NEGDF----SNTREILKelgLEDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNR--------KEVTVGVDGSLY 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 727550411 444 EHYKQFSECMESSLKELLGDEAsgTIEVIHSNDGSGIGAALLAA 487
Cdd:cd24019 386 KYHPKFHKRMHETLKELVPPGC--KFKLMLSEDGSGKGAALVAA 427
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
55-486 |
3.61e-126 |
|
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: 371.61 E-value: 3.61e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 55 LRQVADAMAVEMHAGLASDGGSkLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQDRVakQEFEEVSIPPH 134
Cdd:cd24000 4 LKEITDAFLEELEKGLAGEPSS-LKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGKGIEV--TISKKYEIPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 135 LMTGGSDELFNFIAEALAKFVATEGEDFHLPegrqreLGFTFSFPVRQTSLSSGSLIKWTKGFSIDEAVGEDVVGALKKA 214
Cdd:cd24000 81 IKTASAEEFFDFIADCIAEFLKENGLKKPLP------LGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 215 MERVGLDMRVAALVNDTVGTLAGGRYYNPDVAAAVILGTGTNAAYVERATAIpkwhgpLPKSGEMVINMEWGNFRSSHLP 294
Cdd:cd24000 155 LKKRGLPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNI------LLGDGGMIINTEWGNFGKNSLP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 295 LTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEaaffgdtvpsklripfiirtphmsamhndtspdlkiv 374
Cdd:cd24000 229 RTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 375 gskikdilevpttslkmrkVVISLCDIIATRGARLSAAGIYGILKKLGRDTTskeevQKSVIAMDGGLFEHYKQFSECME 454
Cdd:cd24000 272 -------------------ILRKICELVAERSARLAAAAIAALLRKTGDSPE-----KKITIAVDGSLFEKYPGYRERLE 327
|
410 420 430
....*....|....*....|....*....|..
gi 727550411 455 SSLKELLGDEASgtIEVIHSNDGSGIGAALLA 486
Cdd:cd24000 328 EYLKELLGRGIR--IELVLVEDGSLIGAALAA 357
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
53-487 |
8.30e-125 |
|
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: 370.94 E-value: 8.30e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 53 SKLRQVADAMAVEMHAGLASDGGSkLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQDRVAKQEfeEVSIP 132
Cdd:cd24087 2 ERLRKITDHFISELEKGLSKKGGN-IPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNGKFDITQS--KYRLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 133 PHLMTGGSDELFNFIAEALAKFVategeDFHLPEGR--QRELGFTFSFPVRQTSLSSGSLIKWTKGFSIDEAVGEDVVGA 210
Cdd:cd24087 79 EELKTGTGEELWDFIADCLKKFV-----EEHFPGGKsePLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 211 LKKAMERVGLDMRVAALVNDTVGTLAGGRYYNPDVAAAVILGTGTNAAYVERATAIPKW-HGPLPKSGEMVINMEWGNFR 289
Cdd:cd24087 154 LQKALKKRNVPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLeHDDIPPDSPMAINCEYGAFD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 290 SSH--LPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPSKLRIPFIIRTPHMSAMHNDT 367
Cdd:cd24087 234 NEHlvLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 368 SPDLKIVGSKIKDILEVPTTsLKMRKVVISLCDIIATRGARLSAAGIYGILKKLGrdttskeeVQKSVIAMDGGLFEHYK 447
Cdd:cd24087 314 FENLEDTDDLFQHFFGLETT-VPERKFIRRLAELIGTRAARLSACGIAAICKKRG--------YKTCHVAADGSVYNKYP 384
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 727550411 448 QFSECMESSLKELLGDEASGT-IEVIHSNDGSGIGAALLAA 487
Cdd:cd24087 385 GFKERAAQALKDIFGWDGEDDpIKTVPAEDGSGVGAAIIAA 425
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
53-486 |
3.89e-124 |
|
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 (GLK-2) from fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (also known as glucokinase-1, EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. It is a putative glucokinase that functions in phosphorylation of aldohexoses and glucose uptake. It is involved in sporulation and required for the full activation of the early meiotic inducer IME1. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar. The family corresponds to glucokinase-1 and glucokinase-2.
Pssm-ID: 466938 [Multi-domain] Cd Length: 445 Bit Score: 369.80 E-value: 3.89e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 53 SKLRQVADAMAVEMHAGLASDGGSkLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGkqDRVAKQEFEEVSIP 132
Cdd:cd24088 2 EKLDKLTAEFQRQMEKGLAKHGKG-MAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHG--DGTFSLRQEKSKIP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 133 PHLMTGG-SDELFNFIAEALAKFVATEGEDfHLPEGRQRE---LGFTFSFPVRQTSLSSGSLIKWTKGFSIDEAVGEDVV 208
Cdd:cd24088 79 DELKTGVtAKDLFDYLAKSVEAFLTKHHGD-SFAAGKDDDrlkLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 209 GALKKAMERVGLDMRVAALVNDTVGTLAGGRYYNPDVAAAV---ILGTGTNAAYVERATAIPKWHGPL---PKSGEMVIN 282
Cdd:cd24088 158 KLLQDELDRQGIPVKVVALVNDTVGTLLARSYTSPEISGAVlgaIFGTGTNGAYLEDLEKIKKLDDSSrvgKGKTHMVIN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 283 MEWGNFRS--SHLPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFG---DTVPSKLRIPFIIRT 357
Cdd:cd24088 238 TEWGSFDNelKVLPTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFLIqynDKSPSALNTPYGLDT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 358 PHMSAMHNDTSPDLKIVGSKIKDILEVPTTSLKMRKVVISLCDIIATRGARLSAAGIYGILKKLGRdtTSKEEVQKSVIA 437
Cdd:cd24088 318 AVLSAIEIDSEAELRATRKVLLDDLGLPAPSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGA--LNKSYDGEINIG 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 727550411 438 MDGGLFEHYKQFSECMESSLKELL-GDEASGTIEVIHSNDGSGIGAALLA 486
Cdd:cd24088 396 VDGSVIEFYPGFESMLREALRLLLiGAEGEKRIKIGIAKDGSGVGAALCA 445
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
51-487 |
1.09e-107 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 328.17 E-value: 1.09e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 51 PISKLRQVADAMAVEMHAGLASDGG---------SKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLL--GGKQD 119
Cdd:PTZ00107 21 SKEKLKELVDYFLYELVEGLEAHRRhrnlwipneCSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFRAVRVSLrgGGKME 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 120 RVAKQ---EFEEVSIPPHLM--TGGSDELFNFIAEALAKFVATEGEDFHLPEGrqRELGFTFSFPVRQTSLSSGSLIKWT 194
Cdd:PTZ00107 101 RTQSKfslPKSALLGEKGLLdkKATATDLFDHIAKSIKKMMEENGDPEDLNKP--VPVGFTFSFPCTQLSVNNAILIDWT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 195 KGFSIDEAV-----GEDVVGALKKAMERVGLDMRVAALVNDTVGTLAgGRYY-----NPDVAAAVILGTGTNAAYVERAT 264
Cdd:PTZ00107 179 KGFETGRATndpveGKDVGELLNDAFKRNNVPANVVAVLNDTVGTLI-SCAYqkpknTPPCQVGVIIGTGSNACYFEPEV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 265 AIPKWHGplpksgeMVINMEWGNFrSSHLPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAffgdt 344
Cdd:PTZ00107 258 SAYGYAG-------TPINMECGNF-DSKLPITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLLQLKA----- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 345 vPSKLRIPFIIRTPHMSAMHNDTSPDLKIVGSKIKDI--LEVPTTSLK-MRKVvislCDIIATRGARLSAAGIYGILKKL 421
Cdd:PTZ00107 325 -PPKMWQSGSFESEDASMILNDQSPDLQFSRQVIKEAwdVDLTDEDLYtIRKI----CELVRGRAAQLAAAFIAAPAKKT 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727550411 422 GRDTTskeevqKSVIAMDGGLFEHYKQFSECMESSLKELLGDEAsGTIEVIHSNDGSGIGAALLAA 487
Cdd:PTZ00107 400 RTVQG------KATVAIDGSVYVKNPWFRRLLQEYINSILGPDA-GNVVFYLADDGSGKGAAIIAA 458
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
246-488 |
1.52e-104 |
|
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: 311.73 E-value: 1.52e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 246 AAAVILGTGTNAAYVERATAIPKWHGPLPKSGEMVINMEWGNFRSSH---LPLTEFDHTLDFESLNPGEQILEKIISGMY 322
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKLPKSGEMIINTEWGAFGDNGllpLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 323 LGEILRRVLLKMAEEAAFFGDtVPSKLRIPFIIRTPHMSAMHNDTSPDLKIVGSKIKDILEVPTTSLKMRKVVISLCDII 402
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKG-QSEKLKTPYSLDTSFLSAIESDPSEDLETTREILEELLGIETVTEEDRKIVRRICEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 403 ATRGARLSAAGIYGILKKLGRDTtskeevqKSVIAMDGGLFEHYKQFSECMESSLKELLGdeASGTIEVIHSNDGSGIGA 482
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-------KVTVGVDGSVYEKYPGFRERLQEALRELLG--PGDKVVLVLAEDGSGVGA 230
|
....*.
gi 727550411 483 ALLAAS 488
Cdd:pfam03727 231 ALIAAV 236
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
54-487 |
8.53e-98 |
|
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of types I and II hexokinases.
Pssm-ID: 466939 [Multi-domain] Cd Length: 429 Bit Score: 301.69 E-value: 8.53e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 54 KLRQVADAMAVEMHAGLASDGG--SKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQDRVAKQEFEEVSI 131
Cdd:cd24089 6 TLLDISRRFRKEMEKGLGKDTHptATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMESQVYAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 132 PPHLMTGGSDELFNFIAEALAKFVATEG-EDFHLPegrqreLGFTFSFPVRQTSLSSGSLIKWTKGFSIDEAVGEDVVGA 210
Cdd:cd24089 86 PEEIMHGSGTQLFDHVAECLADFMDKQKiKDKKLP------LGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 211 LKKAMERVG-LDMRVAALVNDTVGTLAGGRYYNPDVAAAVILGTGTNAAYVERATAIPKWHGplpKSGEMVINMEWGNFR 289
Cdd:cd24089 160 LRKAIRRRGdYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEG---DEGRMCINTEWGAFG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 290 ---SSHLPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPSKLRIPFIIRTPHMSAMHND 366
Cdd:cd24089 237 ddgSLEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 367 TSpDLKIVGSKIKDILEVPttSLKMRKVVISLCDIIATRGARLSAAGIYGILKKLgrDTTSKEEVQKSVIAMDGGLFEHY 446
Cdd:cd24089 317 KE-GLANAKEILTRLGLDP--SEDDCVNVQHVCTIVSFRSANLCAATLAAILTRL--RENKGLERLRTTVGVDGSVYKKH 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 727550411 447 KQFSECMESSLKELLGDeasGTIEVIHSNDGSGIGAALLAA 487
Cdd:cd24089 392 PQFSKRLHKAVRRLVPD---CDVRFLLSEDGSGKGAAMVTA 429
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
40-240 |
1.56e-97 |
|
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by this family and pfam03727. Some members of the family have two copies of each of these domains.
Pssm-ID: 459774 [Multi-domain] Cd Length: 197 Bit Score: 292.49 E-value: 1.56e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 40 ILKAFEEDCATPISKLRQVADAMAVEMHAGLASDGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGkqD 119
Cdd:pfam00349 1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGG--D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 120 RVAKQEFEEVSIPPHLMTGGSDELFNFIAEALAKFVATEGEDFHlpEGRQRELGFTFSFPVRQTSLSSGSLIKWTKGFSI 199
Cdd:pfam00349 79 GKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDF--EEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 727550411 200 DEAVGEDVVGALKKAMERVGLDMRVAALVNDTVGTLAGGRY 240
Cdd:pfam00349 157 PGVVGKDVVQLLQEALERRGLPVKVVALVNDTVGTLMAGAY 197
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
55-488 |
8.62e-97 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 299.18 E-value: 8.62e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 55 LRQVADAMAVEMHAGLAsDGGSKLKMLISYVdNLPSG-DEKGLFYALDLGGTNFRVMRVLLGGKQdrvakqEFEEVSIPP 133
Cdd:COG5026 22 LEEIAAKFQEEMEKGLE-GKKSSLKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRFDGEG------TFEIENFKS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 134 HLMTGGS-----DELFNFIAEALAKFVategedfhlpeGRQRELGFTFSFPVRQTSLSSGSLIKWTKGFSIDEAVGEDVV 208
Cdd:COG5026 94 FPLPGTSseitaEEFFDFIADYIEPLL-----------DESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 209 GALKKAMERVGLD-MRVAALVNDTVGTLAGGRYYNPDVA----AAVILGTGTNAAYVERATAIPKWHGPlpkSGEMVINM 283
Cdd:COG5026 163 ELLEAALARKGLDnVKPVAILNDTVATLLAGAYADPDDGysgyIGSILGTGHNTCYLEPNAPIGKLPAY---EGPMIINM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 284 EWGNFrsSHLPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDtVPSKLRIPFIIRTPHMSAM 363
Cdd:COG5026 240 ESGNF--NKLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEGLFSPG-FSEVFETPYSLTTVDMSRF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 364 HNDTSPDLKIVGSKIKDILEvpttslKMRKVVISLCDIIATRGARLSAAGIYGILKKLGRDttsKEEVQKSVIAMDGGLF 443
Cdd:COG5026 317 LADPSDEKEILSQCLEAGSE------EDREILREIADAIVERAARLVAATLAGILLHLGPG---KTPLKPHCIAIDGSTY 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 727550411 444 EHYKQFSECMESSLKELLGDEASGTIEVIHSNDGSGIGAALLAAS 488
Cdd:COG5026 388 EKMPGLAEKIEYALQEYLLGEKGRYVEFVLVENASLLGAAIAAAL 432
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
52-487 |
6.92e-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: 284.05 E-value: 6.92e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 52 ISKLRQVADAMAVEMHAGLA--SDGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQDRVAKQEFEEV 129
Cdd:cd24091 4 HDQLLEVKARMRAEMERGLRkeTHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHNKIY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 130 SIPPHLMTGGSDELFNFIAEALAKFVATEGedfhlPEGRQRELGFTFSFPVRQTSLSSGSLIKWTKGFSIDEAVGEDVVG 209
Cdd:cd24091 84 AIPQEIMQGTGEELFDHIVQCIADFLEYMG-----LKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 210 ALKKAMERVG-LDMRVAALVNDTVGTLAGGRYYNPDVAAAVILGTGTNAAYVERATAIPKWHGplpKSGEMVINMEWGNF 288
Cdd:cd24091 159 LLREAIKRREeFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEG---EEGRMCINMEWGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 289 RSS----HLpLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPSKLRIPFIIRTPHMSAMH 364
Cdd:cd24091 236 GDNgcldDI-RTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 365 NDTSPDLKIvgSKIKDILEVPTTSlKMRKVVISLCDIIATRGARLSAAGIYGILKKLgRDTTSKEEVQKSViAMDGGLFE 444
Cdd:cd24091 315 SDRLALLQV--RAILQQLGLDSTC-DDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKI-RENRGLDHLNVTV-GVDGTLYK 389
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 727550411 445 HYKQFSECMESSLKELlgdEASGTIEVIHSNDGSGIGAALLAA 487
Cdd:cd24091 390 LHPHFSRVMHETVKEL---APKCDVTFLQSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
55-487 |
3.23e-89 |
|
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: 279.43 E-value: 3.23e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 55 LRQVADAMAVEMHAGLASDGGSK--LKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQDRVAKQEFEEVSIP 132
Cdd:cd24126 7 LLDIMTRFRAEMEKGLAKDTNPTaaVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMESQFYPTP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 133 PHLMTGGSDELFNFIAEALAKFVATEG-EDFHLPegrqreLGFTFSFPVRQTSLSSGSLIKWTKGFSIDEAVGEDVVGAL 211
Cdd:cd24126 87 EEIIHGTGTELFDYVAECLADFMKKKGiKHKKLP------LGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 212 KKAMERVG-LDMRVAALVNDTVGTLAGGRYYNPDVAAAVILGTGTNAAYVERATAIPKWHGplpKSGEMVINMEWGNFRS 290
Cdd:cd24126 161 RKAIRKHKdVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEG---DEGRMCINTEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 291 SHLP---LTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPSKLRIPFIIRTPHMSAMHNdt 367
Cdd:cd24126 238 DGSLediRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEK-- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 368 spdLKIVGSKIKDILevptTSLKMRK------VVISLCDIIATRGARLSAAGIYGILKKLGRDttSKEEVQKSVIAMDGG 441
Cdd:cd24126 316 ---YKEGLYNTREIL----SDLGLEPseedciAVQHVCTIVSFRSANLCAAALAAILTRLREN--KKLERLRTTVGMDGT 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 727550411 442 LFEHYKQFSECMESSLKELLgdeASGTIEVIHSNDGSGIGAALLAA 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-88 |
|
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: 277.92 E-value: 1.27e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 54 KLRQVADAMAVEMHAGLASD--GGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQDRVAKQEFeevSI 131
Cdd:cd24129 6 QLAAVQAQMRKEMAKGLRGEthAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTAGVQITSEIY---SI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 132 PPHLMTGGSDELFNFIAEALAKFVATEGEdfhlpEGRQRELGFTFSFPVRQTSLSSGSLIKWTKGFSIDEAVGEDVVGAL 211
Cdd:cd24129 83 PETVAQGTGQQLFDHIVDCIVDFQQKQGL-----SGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 212 KKAMER-VGLDMRVAALVNDTVGTLAGGRYYNPDVAAAVILGTGTNAAYVERATAIPKWHGplpKSGEMVINMEWGNF-- 288
Cdd:cd24129 158 REAATRkQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPG---DSGRMCINMEWGAFgd 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 289 -RSSHLPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPSKLRIPFIIRTPHMSAMHNDT 367
Cdd:cd24129 235 nGCLAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 368 SPdLKIVGSKIKDiLEVPTT---SLKMRKVvislCDIIATRGARLSAAGIYGILKKLgRDTTSKEEVQKSViAMDGGLFE 444
Cdd:cd24129 315 LA-LRQVRAILED-LGLPLTsddALLVLEV----CQTVSQRAAQLCAAGVAAVVEKM-RENRGLDELAVTV-GVDGTLYK 386
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 727550411 445 HYKQFSECMESSLKELlgdEASGTIEVIHSNDGSGIGAALLAA 487
Cdd:cd24129 387 LHPRFSSLVQATVREL---APRCVVTFLQSEDGSGKGAALVTA 426
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
54-487 |
2.93e-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: 264.45 E-value: 2.93e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 54 KLRQVADAMAVEMHAGLA--SDGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQDRVAKQEFEEVSI 131
Cdd:cd24128 6 QLLEVKRRMKVEMERGLSkeTHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHNKIYAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 132 PPHLMTGGSDELFNFIAEALAKFVATEGEdfhlpEGRQRELGFTFSFPVRQTSLSSGSLIKWTKGFSIDEAVGEDVVGAL 211
Cdd:cd24128 86 PQEVMHGTGEELFDHIVHCIADFLEYMGM-----KGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 212 KKAMERV-GLDMRVAALVNDTVGTLAGGRYYNPDVAAAVILGTGTNAAYVERATAIPKWHGplpKSGEMVINMEWGNFRS 290
Cdd:cd24128 161 KEAIHRReEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEG---EEGRMCVNMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 291 SHLP---LTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPSKLRIPFIIRTPHMSAMHNDt 367
Cdd:cd24128 238 NGCLddfRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESD- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 368 spdlKIVGSKIKDILEV--PTTSLKMRKVVISLCDIIATRGARLSAAGIYGILKKLgRDTTSKEEVqKSVIAMDGGLFEH 445
Cdd:cd24128 317 ----RLALLQVRAILQHlgLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKI-RENRGLDAL-KVTVGVDGTLYKL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 727550411 446 YKQFSECMESSLKELlgdEASGTIEVIHSNDGSGIGAALLAA 487
Cdd:cd24128 391 HPHFAKVMHETVKDL---APKCDVSFLQSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
55-487 |
7.38e-83 |
|
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: 262.91 E-value: 7.38e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 55 LRQVADAMAVEMHAGLASDGG--SKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQDRVAKQEFEEVSIP 132
Cdd:cd24125 7 LLEISKRFRKEMEKGLGATTHptAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMENQIYAIP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 133 PHLMTGGSDELFNFIAEALAKFVATEG-EDFHLPegrqreLGFTFSFPVRQTSLSSGSLIKWTKGFSIDEAVGEDVVGAL 211
Cdd:cd24125 87 EDIMRGSGTQLFDHIAECLANFMDKLQiKDKKLP------LGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 212 KKAMERVG-LDMRVAALVNDTVGTLAGGRYYNPDVAAAVILGTGTNAAYVERATAIPKWHGplpKSGEMVINMEWGNFRS 290
Cdd:cd24125 161 RKAIQKRGdFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEG---DEGRMCINMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 291 SHL---PLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPSKLRIPFIIRTPHMSAMHNDT 367
Cdd:cd24125 238 DGSlddIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 368 SPDLKIVGSKIKDILE-VPTTSLKMRKVvislCDIIATRGARLSAAGIYGILKKLgRDTTSKEEVqKSVIAMDGGLFEHY 446
Cdd:cd24125 318 DGIRKAREVLMRLGLDpTQEDCVATHRI----CQIVSTRSASLCAATLAAVLQRI-KENKGEERL-RSTIGVDGSVYKKH 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 727550411 447 KQFSECMESSLKELLGDeasGTIEVIHSNDGSGIGAALLAA 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 |
1.84e-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: 1.84e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 54 KLRQVADAMAVEMHAGL--ASDGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQDRVAKQEFEEVSI 131
Cdd:cd24127 6 MLLEVKKRMRAEMELGLrkQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 132 PPHLMTGGSDELFNFIAEALAKFVategeDFHLPEGRQRELGFTFSFPVRQTSLSSGSLIKWTKGFSIDEAVGEDVVGAL 211
Cdd:cd24127 86 PIEIMQGTGEELFDHIVSCISDFL-----DYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 212 KKAMERVG-LDMRVAALVNDTVGTLAGGRYYNPDVAAAVILGTGTNAAYVERATAIPKWHGplpKSGEMVINMEWGNFRS 290
Cdd:cd24127 161 RDAIKRREeFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEG---DQGQMCINMEWGAFGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 291 SHL---PLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPSKLRIPFIIRTPHMSAMHNDt 367
Cdd:cd24127 238 NGClddIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESD- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 368 spdlKIVGSKIKDILEV--PTTSLKMRKVVISLCDIIATRGARLSAAGIYGILKKLgRDTTSKEEVQKSViAMDGGLFEH 445
Cdd:cd24127 317 ----RLALLQVRAILQQlgLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKI-RENRGLDHLNVTV-GVDGTLYKL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 727550411 446 YKQFSECMESSLKELlgdEASGTIEVIHSNDGSGIGAALLAA 487
Cdd:cd24127 391 HPHFSRIMHQTVKEL---SPKCNVSFLLSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
54-487 |
2.19e-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: 259.48 E-value: 2.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 54 KLRQVADAMAVEMHAGLA--SDGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLggKQDRVAKQEFEEV-S 130
Cdd:cd24130 6 QLQEVKQKMRTELEYGLKkeTHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKI--RSGRRSVRMYNKIfA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 131 IPPHLMTGGSDELFNFIAEALAKFVategeDFHLPEGRQRELGFTFSFPVRQTSLSSGSLIKWTKGFSIDEAVGEDVVGA 210
Cdd:cd24130 84 IPLEIMQGTGEELFDHIVQCIADFL-----DYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 211 LKKAMERVG-LDMRVAALVNDTVGTLAGGRYYNPDVAAAVILGTGTNAAYVERATAIPKWHGplpKSGEMVINMEWGNFR 289
Cdd:cd24130 159 LREAIKRRNeFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEG---DEGRMCINTEWGGFG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 290 SSHLP---LTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPSKLRIPFIIRTPHMSAMHND 366
Cdd:cd24130 236 DNGCIddiRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 367 TSPDLKIvgSKIKDILEVPTTSlKMRKVVISLCDIIATRGARLSAAGIYGILKKLgRDTTSKEEVQKSViAMDGGLFEHY 446
Cdd:cd24130 316 RLALLQV--RRILQQLGLDSTC-EDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKI-RENQGLDRLDITV-GVDGTLYKLH 390
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 727550411 447 KQFSECMESSLKELlgdEASGTIEVIHSNDGSGIGAALLAA 487
Cdd:cd24130 391 PHFSRILQETVKEL---APQCDVTFMLSEDGSGKGAALITA 428
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
55-487 |
2.56e-80 |
|
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: 258.01 E-value: 2.56e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 55 LRQVADAMAVEMHAGLASDGG--SKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVMRVLLGGKQDRVAKQEFEEVSIP 132
Cdd:cd24124 35 LIDIMTRFRKEMKNGLSRDFNptATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 133 PHLMTGGSDELFNFIAEALAKFVATEG-EDFHLPegrqreLGFTFSFPVRQTSLSSGSLIKWTKGFSIDEAVGEDVVGAL 211
Cdd:cd24124 115 ENIVHGSGSQLFDHVAECLGDFMEKRKiKDKKLP------VGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 212 KKAMERVG-LDMRVAALVNDTVGTLAGGRYYNPDVAAAVILGTGTNAAYVERATAIPKWHGplpKSGEMVINMEWGNFR- 289
Cdd:cd24124 189 NKAIKKRGdYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEG---DEGRMCINTEWGAFGd 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 290 --SSHLPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPSKLRIPFIIRTPHMSAMHNDt 367
Cdd:cd24124 266 dgSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKN- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 368 spdlKIVGSKIKDILevptTSLKMRK------VVISLCDIIATRGARLSAAGIYGILKKLgRDTTSKEEVQKSViAMDGG 441
Cdd:cd24124 345 ----KEGLHNAKEIL----TRLGVEPsdddcvSVQHVCTIVSFRSANLVAATLGAILNRL-RDNKGTPRLRTTV-GVDGS 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 727550411 442 LFEHYKQFSECMESSLKELLGDEasgTIEVIHSNDGSGIGAALLAA 487
Cdd:cd24124 415 LYKTHPQYSRRFHKTLRRLVPDS---DVRFLLSESGSGKGAAMVTA 457
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
36-487 |
7.81e-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: 255.58 E-value: 7.81e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 36 RVSAILKAF---EEDcatpiskLRQVADAMAVEMHAGL--ASDGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVM 110
Cdd:cd24092 1 LVEQILAEFqlqEED-------LKKVMRRMQKEMDRGLrlETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 111 RVLLGGKQDRVAKQEFEE--VSIPPHLMTGGSDELFNFIAEALAKFVategeDFHLPEGRQRELGFTFSFPVRQTSLSSG 188
Cdd:cd24092 74 LVKVGEGEEGQWSVKTKHqmYSIPEDAMTGTAEMLFDYISECISDFL-----DKHQMKHKKLPLGFTFSFPVRHEDIDKG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 189 SLIKWTKGFSIDEAVGEDVVGALKKAMERVG-LDMRVAALVNDTVGTLAGGRYYNPDVAAAVILGTGTNAAYVERATAIP 267
Cdd:cd24092 149 ILLNWTKGFKASGAEGNNVVGLLRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 268 KWHGplpKSGEMVINMEWGNF-RSSHLP--LTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDT 344
Cdd:cd24092 229 LVEG---DEGRMCVNTEWGAFgDSGELDefLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 345 VPSKLRIPFIIRTPHMSAMHNDTSpDLKivgsKIKDILevptTSLKMR------KVVISLCDIIATRGARLSAAGIYGIL 418
Cdd:cd24092 306 ASEQLRTRGAFETRFVSQVESDTG-DRK----QIYNIL----STLGLRpsttdcDIVRRACESVSTRAAHMCSAGLAGVI 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727550411 419 KKLgRDTTSKEEVqKSVIAMDGGLFEHYKQFSECMESSLKELlgdEASGTIEVIHSNDGSGIGAALLAA 487
Cdd:cd24092 377 NRM-RESRSEDVM-RITVGVDGSVYKLHPSFKERFHASVRRL---TPSCEITFIESEEGSGRGAALVSA 440
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
51-487 |
1.29e-74 |
|
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: 241.75 E-value: 1.29e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 51 PISKLRQVADAMAVEMHAGLASDGG--SKLKMLISYVDNLPSGDEKGLFYALDLG--GTNFRVMRVLLGGKQDRVAKQEF 126
Cdd:cd24090 3 TRAQLQQIQASLLGSMEQALRGQASpaPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 127 EEVSIPPHLMTGGSDELFNFIAEALAKFVATegedfhLPEGRQR-ELGFTFSFPVRQTSLSSGSLIKWTKGFSIDEAVGE 205
Cdd:cd24090 83 QEFVIPQEVMLGAGQQLFDFAAHCLSEFLDG------QPVPKQGlQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 206 DVVGALKKAMERVGL-DMRVAALVNDTVGTLAGGRYYNPDVAAAVILGTGTNAAYVERATAIPKWHgplPKSGEMVINME 284
Cdd:cd24090 157 DVVQLLRDAIQRQGAyNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLD---EDRGRVCVSVE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 285 WGNFR---SSHLPLTEFDHTLDFESLNPGEQILEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPSKLRIPFIIRTPHMS 361
Cdd:cd24090 234 WGSFSddgALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 362 AMHnDTSPDLKIVGSKIKDILEVPTTSLKMRkvVISLCDIIATRGARLSAAGIYGILKKLgRDTTSKEEVQKSViAMDGG 441
Cdd:cd24090 314 EME-DPSAGAARVRAILQDLGLSPSASDVEL--VQHVCRAVCTRAAQLCAAALAAVLSHL-QHSREQQTLQVAV-ATGGR 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 727550411 442 LFEHYKQFSECMESSLKeLLGDEAsgTIEVIHSNDGSGIGAALLAA 487
Cdd:cd24090 389 VCERHPRFCSILQGTVM-LLAPEC--DVSFIPSVDGGGRGVAMVTA 431
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
210-263 |
1.08e-03 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 41.02 E-value: 1.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 727550411 210 ALKKAMERVGLDMRVAaLVNDTVGTLAGGryYNPDVAAAVILGTGTNAAYVERA 263
Cdd:COG2971 82 ALEAALRELFPFARVV-VVNDALAALAGA--LGGEDGIVVIAGTGSIAAGRDGD 132
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
93-260 |
1.50e-03 |
|
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: 40.65 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 93 EKGLFYALDLGGTNFRVMRVLLGGKQdrVAKQEFeevsipPHLMTGGSDELFNFIAEALAKFVATEGEDFHLPEGrqreL 172
Cdd:COG1940 3 DAGYVIGIDIGGTKIKAALVDLDGEV--LARERI------PTPAGAGPEAVLEAIAELIEELLAEAGISRGRILG----I 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727550411 173 GFTFSFPV---RQTSLSSGSLIKWTkgfsideavGEDVVGALKkamERVGLDMRVAalvND-TVGTLA-----GGRYYnp 243
Cdd:COG1940 71 GIGVPGPVdpeTGVVLNAPNLPGWR---------GVPLAELLE---ERLGLPVFVE---NDaNAAALAeawfgAGRGA-- 133
|
170
....*....|....*..
gi 727550411 244 DVAAAVILGTGTNAAYV 260
Cdd:COG1940 134 DNVVYLTLGTGIGGGIV 150
|
|
| |
