|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02362 |
PLN02362 |
hexokinase |
1-502 |
0e+00 |
|
hexokinase
Pssm-ID: 215206 [Multi-domain] Cd Length: 509 Bit Score: 866.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 1 MGKVLVMLTAAAAVVACSVATVMVRRRMKGRRKWRRVVGLLKDLEEACETPLGRLRQMVDAIAVEMQAGLVSEGGSKLKM 80
Cdd:PLN02362 1 MGKVAVGLAAAAAVAACAVAAVMVGRRVKSRRKWRRVVGVLKELEEACETPVGRLRQVVDAMAVEMHAGLASEGGSKLKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 81 LLTFVDDLPNGSETGTYYALHLGGSYFRIIKVHLGGQRSSLEVQDVERHSIPTSLMNSTSEVLFDFLASSLQRFIEKEGN 160
Cdd:PLN02362 81 LLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRSSILSQDVERHPIPQHLMNSTSEVLFDFIASSLKQFVEKEEN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 161 DFSLSQPLKRELAFTFSFPVKQTSISSGVLIKWTKGFAISEMAGEDIAECLQGALNKRGLDIRVAALVNDTVGALSFGHF 240
Cdd:PLN02362 161 GSEFSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRRGLDMRVAALVNDTVGTLALGHY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 241 HDPDTIAAVVFGTGSNACYLERTDAIIKCQNPRTTSGSMVVNMEWGNFWSSRLPRTSYDLELDAESMNSNDMGFEKMIGG 320
Cdd:PLN02362 241 HDPDTVAAVIIGTGTNACYLERTDAIIKCQGLLTTSGSMVVNMEWGNFWSSHLPRTSYDIDLDAESPNPNDQGFEKMISG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 321 MYLGDIVRRVILRMSQESDIFGPISSILSTPFVLRTNSVSAMHEDDTSELQEVARILKD-LGVSEVPMKVRKLVVKICDV 399
Cdd:PLN02362 321 MYLGDIVRRVILRMSQESDIFGPVSSRLSTPFVLRTPSVAAMHEDDSPELQEVARILKEtLGISEVPLKVRKLVVKICDV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 400 VTRRAARLAAAGIAGILKKV----GRDGSGGGRRSDKQIMRRTVVAVEGGLYLNYRMFREYMDEALRDILGEDVAQHVVV 475
Cdd:PLN02362 401 VTRRAARLAAAGIVGILKKIgrdgSGGITSGRSRSDIQIMRRTVVAVEGGLYTNYTMFREYLHEALNEILGEDVAQHVIL 480
|
490 500
....*....|....*....|....*....
gi 332626974 476 KAMEDGSSIGSALLLASSQS--VQTIPSV 502
Cdd:PLN02362 481 KATEDGSGIGSALLAASYSSysVDTVQLL 509
|
|
| ASKHA_NBD_HK_plant |
cd24020 |
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
50-493 |
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: 638.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 50 TPLGRLRQMVDAIAVEMQAGLVSEGGSKLKMLLTFVDDLPNGSETGTYYALHLGGSYFRIIKVHLGGQRSSLEVQDVERH 129
Cdd:cd24020 1 TPVSRLRQVADAMVVEMEAGLASEGGSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 130 SIPTSLMNSTSEVLFDFLASSLQRFIEKEGNDFSlSQPLKRELAFTFSFPVKQTSISSGVLIKWTKGFAISEMAGEDIAE 209
Cdd:cd24020 81 PIPPELMVGTSEELFDFIAGELAKFVATEGEGFH-PEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 210 CLQGALNKRGLDIRVAALVNDTVGALSFGHFHDPDTIAAVVFGTGSNACYLERTDAIIKCQNPRTTSGSMVVNMEWGNFW 289
Cdd:cd24020 160 LLEEALERQGLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGLPRSGEMVINTEWGNFR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 290 SSRLPRTSYDLELDAESMNSNDMGFEKMIGGMYLGDIVRRVILRMSQESDIFG-PISSILSTPFVLRTNSVSAMHEDDTS 368
Cdd:cd24020 240 SSHLPRTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGdTVPSKLEIPFILRTPDMSAMHEDDSP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 369 ELQEVARILKD-LGVSEVPMKVRKLVVKICDVVTRRAARLAAAGIAGILKKVGRDGSGGGRRsdkqimRRTVVAVEGGLY 447
Cdd:cd24020 320 DLETVARILKDaLGIDDTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLGRDGGGSSPA------QRTVVAVDGGLY 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 332626974 448 LNYRMFREYMDEALRDILGEDVAQHVVVKAMEDGSSIGSALLLASS 493
Cdd:cd24020 394 EHYPKFREYMQQALVELLGDEAADSVELELSNDGSGIGAALLAAAH 439
|
|
| PLN02405 |
PLN02405 |
hexokinase |
1-492 |
1.02e-179 |
|
hexokinase
Pssm-ID: 215226 [Multi-domain] Cd Length: 497 Bit Score: 513.61 E-value: 1.02e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 1 MGKVLVMLTAAAAVVACSVATVMVRRRMKGRRKWRRVVGLLKDLEEACETPLGRLRQMVDAIAVEMQAGLVSEGGSKLKM 80
Cdd:PLN02405 1 MGKVAVGAAVVCAAAVCAAAALVVRRRMKSSGKWARAMEILKEFEEDCATPIGKLRQVADAMTVEMHAGLASEGGSKLKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 81 LLTFVDDLPNGSETGTYYALHLGGSYFRIIKVHLGGQRSSLEVQDVERHSIPTSLMNSTSEVLFDFLASSLQRFIEKEGN 160
Cdd:PLN02405 81 LISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVSIPPHLMTGSSDALFDFIAAALAKFVATEGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 161 DFSLSQPLKRELAFTFSFPVKQTSISSGVLIKWTKGFAISEMAGEDIAECLQGALNKRGLDIRVAALVNDTVGALSFGHF 240
Cdd:PLN02405 161 DFHLPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMERVGLDMRVSALVNDTIGTLAGGRY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 241 HDPDTIAAVVFGTGSNACYLERTDAIIKCQNPRTTSGSMVVNMEWGNFWSSRLPRTSYDLELDAESMNSNDMGFEKMIGG 320
Cdd:PLN02405 241 YNPDVVAAVILGTGTNAAYVERAQAIPKWHGLLPKSGEMVINMEWGNFRSSHLPLTEYDHALDVESLNPGEQIFEKIISG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 321 MYLGDIVRRVILRMSQESDIFGPI-SSILSTPFVLRTNSVSAMHEDDTSELQEVARILKD-LGVSEVPMKVRKLVVKICD 398
Cdd:PLN02405 321 MYLGEILRRVLLKMAEEAAFFGDTvPPKLKIPFILRTPDMSAMHHDTSPDLKVVGSKLKDiLEIPNTSLKMRKVVVELCN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 399 VVTRRAARLAAAGIAGILKKVGRDGSGGGRRsdkqimRRTVVAVEGGLYLNYRMFREYMDEALRDILGEDVAQHVVVKAM 478
Cdd:PLN02405 401 IVATRGARLSAAGIYGILKKLGRDTVKDGEK------QKSVIAMDGGLFEHYTEFSKCMESTLKELLGEEVSESIEVEHS 474
|
490
....*....|....
gi 332626974 479 EDGSSIGSALLLAS 492
Cdd:PLN02405 475 NDGSGIGAALLAAS 488
|
|
| PLN02914 |
PLN02914 |
hexokinase |
25-493 |
1.07e-165 |
|
hexokinase
Pssm-ID: 178502 [Multi-domain] Cd Length: 490 Bit Score: 477.84 E-value: 1.07e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 25 RRRMKGRRKWRRVVGLLKDLEEACETPLGRLRQMVDAIAVEMQAGLVSEGGSKLKMLLTFVDDLPNGSETGTYYALHLGG 104
Cdd:PLN02914 25 RSRMAVRSNAVSVAPILTKLQKDCATPLPVLRHVADAMAADMRAGLAVDGGGDLKMILSYVDSLPSGNEKGLFYALDLGG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 105 SYFRIIKVHLGGQRSSLEVQDVERHSIPTSLMNSTSEVLFDFLASSLQRFIEKEGNDFSLSQPLKRELAFTFSFPVKQTS 184
Cdd:PLN02914 105 TNFRVLRVQLGGKDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFVAKEGGKFHLPEGRKREIGFTFSFPVKQTS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 185 ISSGVLIKWTKGFAISEMAGEDIAECLQGALNKRGLDIRVAALVNDTVGALSFGHFHDPDTIAAVVFGTGSNACYLERTD 264
Cdd:PLN02914 185 IDSGILMKWTKGFAVSGTAGKDVVACLNEAMERQGLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 265 AIIKCQNPRTTSGSMVVNMEWGNFwSSRLPRTSYDLELDAESMNSNDMGFEKMIGGMYLGDIVRRVILRMSQESDIFGP- 343
Cdd:PLN02914 265 AIPKLQGQKSSSGRTIINTEWGAF-SDGLPLTEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHf 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 344 ISSILSTPFVLRTNSVSAMHEDDTSELQEVARILKDLGVSEVPMKVRKLVVKICDVVTRRAARLAAAGIAGILKKVGRDG 423
Cdd:PLN02914 344 VPEKLSTPFALRTPHLCAMQQDNSDDLQAVGSILYDVLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDS 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 424 SGGGRRsdkqimRRTVVAVEGGLYLNYRMFREYMDEALRDILGEDVAQHVVVKAMEDGSSIGSALLLASS 493
Cdd:PLN02914 424 KGMIFG------KRTVVAMDGGLYEKYPQYRRYMQDAVTELLGLELSKNIAIEHTKDGSGIGAALLAATN 487
|
|
| ASKHA_NBD_HK_fungi |
cd24018 |
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ... |
54-489 |
7.15e-132 |
|
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: 389.30 E-value: 7.15e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 54 RLRQMVDAIAVEMQAGLVSEGGSkLKMLLTFVDDLPNGSETGTYYALHLGGSYFRIIKVHLGGQRSSLEVQdVERHSIPT 133
Cdd:cd24018 3 KLEEIVKHFLSEMEKGLEGDGGS-LPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNGGIFIIV-QRKYKIPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 134 SLMNSTSEVLFDFLASSLQRFIEKegNDFSLSQPLKRELAFTFSFPVKQTSISSGVLIKWTKGFAISEMAGEDIAECLQG 213
Cdd:cd24018 81 EAKTGTGEELFDFIAECIAEFLEE--HNLDLQSDKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 214 ALNKRGLDIRVAALVNDTVGALSFGHFHDPDTIAAVVFGTGSNACYLERTDAIIKCQNP---RTTSGSMVVNMEWGNFWS 290
Cdd:cd24018 159 ALDRRGVNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTSPsgsVTKSDEMIINTEWGAFDN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 291 SR--LPRTSYDLELDAESMNSNDMGFEKMIGGMYLGDIVRRVILRMSQESDIF-GPISSILSTPFVLRTNSVSAMHEDDT 367
Cdd:cd24018 239 ERevLPLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFsGKSSELLNEPYSLDTAFLSRIEADTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 368 SELQEVARILKDLGVSEVPMKV-RKLVVKICDVVTRRAARLAAAGIAGILKKVGRDGSgggrrsdkqimRRTVVAVEGGL 446
Cdd:cd24018 319 PDLDAVRDILKELLAIDNTTLEdRKLIKRICELVSTRAARLSAAAIAAILLKRGSLLP-----------EPVTVGIDGSV 387
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 332626974 447 YLNYRMFREYMDEALRDILGEDVAQHVVVKAMEDGSSIGSALL 489
Cdd:cd24018 388 YEKYPGFKDRLSEALRELFGPEVKANISLVLAKDGSGLGAAII 430
|
|
| ASKHA_NBD_HK_meta |
cd24019 |
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ... |
55-491 |
6.73e-120 |
|
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: 358.39 E-value: 6.73e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 55 LRQMVDAIAVEMQAGLVSEG--GSKLKMLLTFVDDLPNGSETGTYYALHLGGSYFRIIKVHLGGQRSslEVQDVERHSIP 132
Cdd:cd24019 7 LEEIMDRLLKEMEKGLSKDThpTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGGSQ--VKMESEIYAIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 133 TSLMNSTSEVLFDFLASSLQRFIEKEGndfslsqpLKRE---LAFTFSFPVKQTSISSGVLIKWTKGFAISEMAGEDIAE 209
Cdd:cd24019 85 EEIMTGTGEQLFDYIAECLAEFLEKNG--------LKDKklpLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 210 CLQGALNKRGL-DIRVAALVNDTVGALSFGHFHDPDTIAAVVFGTGSNACYLERTDAIIKCQNPRTTSGSMVVNMEWGNF 288
Cdd:cd24019 157 LLQEAIKRRGDiKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKWDGDEGDPGQVIINTEWGAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 289 W---SSRLPRTSYDLELDAESMNSNDMGFEKMIGGMYLGDIVRRVILRMSQESDIF-GPISSILSTPFVLRTNSVSAMHE 364
Cdd:cd24019 237 GdngVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFrGQLSEELLTRGSFETKYVSEIES 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 365 DDTSELQEVARILKDLGVSEVPMKVRKLVVKICDVVTRRAARLAAAGIAGILKKVGRdgsgggrrsdkqimRRTVVAVEG 444
Cdd:cd24019 317 DNEGDFSNTREILKELGLEDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNR--------------KEVTVGVDG 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 332626974 445 GLYLNYRMFREYMDEALRDILGEDVAqhvvVKAM--EDGSSIGSALLLA 491
Cdd:cd24019 383 SLYKYHPKFHKRMHETLKELVPPGCK----FKLMlsEDGSGKGAALVAA 427
|
|
| PLN02596 |
PLN02596 |
hexokinase-like |
1-495 |
5.46e-119 |
|
hexokinase-like
Pssm-ID: 178206 [Multi-domain] Cd Length: 490 Bit Score: 358.42 E-value: 5.46e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 1 MGKVLVMLTAAAAVVACSVATVMVRRRMKGRRKWRRVVGLLKDLEEACETPLGRLRQMVDAIAVEMQAGLVSEGGSKLKM 80
Cdd:PLN02596 2 MRKEVVVAATVATVAAVAAAVLMGRWKRRKERQWKHTQRILRKFARECATPVSKLWEVADALVSDMTASLTAEETTTLNM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 81 LLTFVDDLPNGSETGTYYALHLGGSYFRIIKVHLGGQRSSLEVQDVERHSIPTSLMNSTSEVLFDFLASSLQRFIEKEGN 160
Cdd:PLN02596 82 LVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNEPISDLYREEISIPSNVLNGTSQELFDYIALELAKFVAEHPG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 161 DFSLSQPLKRELAFTFSFPVKQTSISSGVLIKWtKGFAISEMAGEDIAECLQGALNKRGLDIRVAALVNDTVGALSFGHF 240
Cdd:PLN02596 162 DEADTPERVKKLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDINRALEKHGLKIRVFALVDDTIGNLAGGRY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 241 HDPDTIAAVVFGTGSNACYLERTDAIIKCQNPRTTSGSMVVNMEWGNFWSSRLPRTSYDLELDAESMNSNDMGFEKMIGG 320
Cdd:PLN02596 241 YNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSPSPESQEIVISTEWGNFNSCHLPITEFDASLDAESSNPGSRIFEKLTSG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 321 MYLGDIVRRVILRMSQESDIFGP-ISSILSTPFVLRTNSVSAMHEDDTSELQEVARILKD-LGVSEVPMKVRKLVVKICD 398
Cdd:PLN02596 321 MYLGEIVRRVLLKMAEETALFGDtLPPKLTTPYLLRSPDMAAMHQDTSEDHEVVNEKLKEiFGITDSTPMAREVVAEVCD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 399 VVTRRAARLAAAGIAGILKKVGRDGSgggrrsdkqimRRTVVAVEGGLYLNYRMFREYMDEALRDILGEDVAQHVVVKAM 478
Cdd:PLN02596 401 IVAERGARLAGAGIVGIIKKLGRIEN-----------KKSVVTVEGGLYEHYRVFRNYLHSSVWEMLGSELSDNVVIEHS 469
|
490
....*....|....*..
gi 332626974 479 EDGSSIGsALLLASSQS 495
Cdd:PLN02596 470 HGGSGAG-ALFLAACQT 485
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
54-489 |
1.27e-102 |
|
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: 311.52 E-value: 1.27e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 54 RLRQMVDAIAVEMQAGLvSEGGSKLKMLLTFVDDLPNGSETGTYYALHLGGSYFRIIKVHLGGQRSslEVQDVERHSIPT 133
Cdd:cd24000 3 DLKEITDAFLEELEKGL-AGEPSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGKGI--EVTISKKYEIPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 134 SLMNSTSEVLFDFLASSLQRFIEKEGNDFSLSqplkreLAFTFSFPVKQTSISSGVLIKWTKGFAISEMAGEDIAECLQG 213
Cdd:cd24000 80 EIKTASAEEFFDFIADCIAEFLKENGLKKPLP------LGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLND 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 214 ALNKRGLDIRVAALVNDTVGALSFGHFHDPDTIAAVVFGTGSNACYLERTDAIIkcqnprTTSGSMVVNMEWGNFWSSRL 293
Cdd:cd24000 154 ALKKRGLPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNIL------LGDGGMIINTEWGNFGKNSL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 294 PRTSYDLELDAESMNSNDMGFEKMIGGMYLGDIVRRVILRMSQEsdifgpissilstpfvlrtnsvsamheddtselqev 373
Cdd:cd24000 228 PRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------------------------ 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 374 arilkdlgvsevpmkvrkLVVKICDVVTRRAARLAAAGIAGILKKVGRDGsgggrrsdkqiMRRTVVAVEGGLYLNYRMF 453
Cdd:cd24000 272 ------------------ILRKICELVAERSARLAAAAIAALLRKTGDSP-----------EKKITIAVDGSLFEKYPGY 322
|
410 420 430
....*....|....*....|....*....|....*.
gi 332626974 454 REYMDEALRDILGEdvAQHVVVKAMEDGSSIGSALL 489
Cdd:cd24000 323 RERLEEYLKELLGR--GIRIELVLVEDGSLIGAALA 356
|
|
| ASKHA_NBD_GLK1-2_fungi |
cd24088 |
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ... |
65-488 |
1.53e-101 |
|
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: 312.02 E-value: 1.53e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 65 EMQAGLvSEGGSKLKMLLTFVDDLPNGSETGTYYALHLGGSYFRIIKVHLGGQRSSLEVQdvERHSIPTSLMNS-TSEVL 143
Cdd:cd24088 14 QMEKGL-AKHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHGDGTFSLRQ--EKSKIPDELKTGvTAKDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 144 FDFLASSLQRFIEKEGND-FSLSQPLKR-ELAFTFSFPVKQTSISSGVLIKWTKGFAISEMAGEDIAECLQGALNKRGLD 221
Cdd:cd24088 91 FDYLAKSVEAFLTKHHGDsFAAGKDDDRlKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVVKLLQDELDRQGIP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 222 IRVAALVNDTVGAL---SFGHFHDPDTIAAVVFGTGSNACYLERTDAIIKCQNP---RTTSGSMVVNMEWGNFWSSR--L 293
Cdd:cd24088 171 VKVVALVNDTVGTLlarSYTSPEISGAVLGAIFGTGTNGAYLEDLEKIKKLDDSsrvGKGKTHMVINTEWGSFDNELkvL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 294 PRTSYDLELDAESMNSNDMGFEKMIGGMYLGDIVRRVILRMSQESDIF----GPISSILSTPFVLRTNSVSAMHEDDTSE 369
Cdd:cd24088 251 PTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFLiqynDKSPSALNTPYGLDTAVLSAIEIDSEAE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 370 LQEVARILKDLGVSEVPMKV-RKLVVKICDVVTRRAARLAAAGIAGILKKVGRDGSGGGRRSDkqimrrtvVAVEGGLYL 448
Cdd:cd24088 331 LRATRKVLLDDLGLPAPSLEdAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSYDGEIN--------IGVDGSVIE 402
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 332626974 449 NYRMFREYMDEALRDIL-GEDVAQHVVVKAMEDGSSIGSAL 488
Cdd:cd24088 403 FYPGFESMLREALRLLLiGAEGEKRIKIGIAKDGSGVGAAL 443
|
|
| ASKHA_NBD_HK1-2_fungi |
cd24087 |
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ... |
54-494 |
9.16e-101 |
|
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: 309.31 E-value: 9.16e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 54 RLRQMVDAIAVEMQAGLVSEGGSkLKMLLTFVDDLPNGSETGTYYALHLGGSYFRIIKVHLGGQRSSLEVQdvERHSIPT 133
Cdd:cd24087 3 RLRKITDHFISELEKGLSKKGGN-IPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNGKFDITQ--SKYRLPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 134 SLMNSTSEVLFDFLASSLQRFIEKEGNDfSLSQPLkrELAFTFSFPVKQTSISSGVLIKWTKGFAISEMAGEDIAECLQG 213
Cdd:cd24087 80 ELKTGTGEELWDFIADCLKKFVEEHFPG-GKSEPL--PLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 214 ALNKRGLDIRVAALVNDTVGALSFGHFHDPDTIAAVVFGTGSNACYLERTDAIIKCQNPRTTSGS-MVVNMEWGNFWSSR 292
Cdd:cd24087 157 ALKKRNVPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEHDDIPPDSpMAINCEYGAFDNEH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 293 --LPRTSYDLELDAESMNSNDMGFEKMIGGMYLGDIVRRVILRMSQESDIF-GPISSILSTPFVLRTNSVSAMHEDDTSE 369
Cdd:cd24087 237 lvLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFkGQDTSKLEKPYVMDTSFLSRIEEDPFEN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 370 LQEVARI-LKDLGVsEVPMKVRKLVVKICDVVTRRAARLAAAGIAGILKKVGrdgsgggrrsdkqiMRRTVVAVEGGLYL 448
Cdd:cd24087 317 LEDTDDLfQHFFGL-ETTVPERKFIRRLAELIGTRAARLSACGIAAICKKRG--------------YKTCHVAADGSVYN 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 332626974 449 NYRMFREYMDEALRDILGEDVAQH-VVVKAMEDGSSIGSALLLASSQ 494
Cdd:cd24087 382 KYPGFKERAAQALKDIFGWDGEDDpIKTVPAEDGSGVGAAIIAALTK 428
|
|
| PTZ00107 |
PTZ00107 |
hexokinase; Provisional |
55-491 |
2.68e-85 |
|
hexokinase; Provisional
Pssm-ID: 240270 [Multi-domain] Cd Length: 464 Bit Score: 270.78 E-value: 2.68e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 55 LRQMVDAIAVEMQAGLVSEGG---------SKLKMLLTFVDDLPNGSETGTYYALHLGGSYFRIIKVHLGGQRSSLEVQD 125
Cdd:PTZ00107 25 LKELVDYFLYELVEGLEAHRRhrnlwipneCSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFRAVRVSLRGGGKMERTQS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 126 V-----ERHSIPTSLMN--STSEVLFDFLASSLQRFIEKEGNDFSLSQPLKreLAFTFSFPVKQTSISSGVLIKWTKGFA 198
Cdd:PTZ00107 105 KfslpkSALLGEKGLLDkkATATDLFDHIAKSIKKMMEENGDPEDLNKPVP--VGFTFSFPCTQLSVNNAILIDWTKGFE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 199 ISEMA-----GEDIAECLQGALNKRGLDIRVAALVNDTVGALSFGHFHD----PDTIAAVVFGTGSNACYLErtDAIIKc 269
Cdd:PTZ00107 183 TGRATndpveGKDVGELLNDAFKRNNVPANVVAVLNDTVGTLISCAYQKpkntPPCQVGVIIGTGSNACYFE--PEVSA- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 270 qnpRTTSGSmVVNMEWGNFwSSRLPRTSYDLELDAESMNSNDMGFEKMIGGMYLGDIVRRVILRMSQE--SDIFGPISSI 347
Cdd:PTZ00107 260 ---YGYAGT-PINMECGNF-DSKLPITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLLQLkaPPKMWQSGSF 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 348 lstpfvlrtNSVSA-MHEDDTSE-LQEVARILKDLGVSEVPMKVRKLVVKICDVVTRRAARLAAAGIAGILKKVgrdgsg 425
Cdd:PTZ00107 335 ---------ESEDAsMILNDQSPdLQFSRQVIKEAWDVDLTDEDLYTIRKICELVRGRAAQLAAAFIAAPAKKT------ 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332626974 426 ggrrsdKQIMRRTVVAVEGGLYLNYRMFREYMDEALRDILGEDvAQHVVVKAMEDGSSIGSALLLA 491
Cdd:PTZ00107 400 ------RTVQGKATVAIDGSVYVKNPWFRRLLQEYINSILGPD-AGNVVFYLADDGSGKGAAIIAA 458
|
|
| COG5026 |
COG5026 |
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ... |
55-494 |
7.29e-81 |
|
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 444044 [Multi-domain] Cd Length: 434 Bit Score: 258.35 E-value: 7.29e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 55 LRQMVDAIAVEMQAGLvSEGGSKLKMLLTFVDdLPNGS-ETGTYYALHLGGSYFRIIKVHLGGQRSsLEVQDVERHSIPT 133
Cdd:COG5026 22 LEEIAAKFQEEMEKGL-EGKKSSLKMLPSYLG-LPTGVkETGPVIALDAGGTNFRVALVRFDGEGT-FEIENFKSFPLPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 134 SLMNSTSEVLFDFLASSLQRFIEKegndfslsqplKRELAFTFSFPVKQTSISSGVLIKWTKGFAISEMAGEDIAECLQG 213
Cdd:COG5026 99 TSSEITAEEFFDFIADYIEPLLDE-----------SYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNIGELLEA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 214 ALNKRGLD-IRVAALVNDTVGALSFGHFHDPDTI----AAVVFGTGSNACYLERTDAIIKCQNPrttSGSMVVNMEWGNF 288
Cdd:COG5026 168 ALARKGLDnVKPVAILNDTVATLLAGAYADPDDGysgyIGSILGTGHNTCYLEPNAPIGKLPAY---EGPMIINMESGNF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 289 wsSRLPRTSYDLELDAESMNSNDMGFEKMIGGMYLGDIVRRVILRMSQESDIFGPISSILSTPFVLRTNSVSAMHEDDTS 368
Cdd:COG5026 245 --NKLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEGLFSPGFSEVFETPYSLTTVDMSRFLADPSD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 369 ELQEVARILKDLGVSEvpmkvRKLVVKICDVVTRRAARLAAAGIAGILKKvgrdgsgggRRSDKQIMRRTVVAVEGGLYL 448
Cdd:COG5026 323 EKEILSQCLEAGSEED-----REILREIADAIVERAARLVAATLAGILLH---------LGPGKTPLKPHCIAIDGSTYE 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 332626974 449 NYRMFREYMDEALRDILGEDVAQHVVVKAMEDGSSIGSALLLASSQ 494
Cdd:COG5026 389 KMPGLAEKIEYALQEYLLGEKGRYVEFVLVENASLLGAAIAAALNE 434
|
|
| Hexokinase_1 |
pfam00349 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
41-240 |
9.06e-81 |
|
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: 249.73 E-value: 9.06e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 41 LKDLEEACETPLGRLRQMVDAIAVEMQAGLVSEGGSKLKMLLTFVDDLPNGSETGTYYALHLGGSYFRIIKVHLGGQRSS 120
Cdd:pfam00349 2 LEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGGDGKF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 121 LEVQdvERHSIPTSLMNSTSEVLFDFLASSLQRFIEKEGNDFSLSQPLKreLAFTFSFPVKQTSISSGVLIKWTKGFAIS 200
Cdd:pfam00349 82 EITQ--EKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDFEEKELP--LGFTFSFPVEQTSLDSGTLIRWTKGFDIP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 332626974 201 EMAGEDIAECLQGALNKRGLDIRVAALVNDTVGALSFGHF 240
Cdd:pfam00349 158 GVVGKDVVQLLQEALERRGLPVKVVALVNDTVGTLMAGAY 197
|
|
| Hexokinase_2 |
pfam03727 |
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ... |
246-492 |
1.04e-77 |
|
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: 243.17 E-value: 1.04e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 246 IAAVVFGTGSNACYLERTDAIIKCQNPRTTSGSMVVNMEWGNFWSSR---LPRTSYDLELDAESMNSNDMGFEKMIGGMY 322
Cdd:pfam03727 1 RIGLILGTGTNAAYVEKVSNIPKLEGKLPKSGEMIINTEWGAFGDNGllpLPRTEYDKELDAESPNPGFQPFEKMISGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 323 LGDIVRRVILRMSQESDIFGPISSILSTPFVLRTNSVSAMHEDDTSELQEVARILKD-LGVSEVPMKVRKLVVKICDVVT 401
Cdd:pfam03727 81 LGELVRLVLLDLAEEGLLFKGQSEKLKTPYSLDTSFLSAIESDPSEDLETTREILEElLGIETVTEEDRKIVRRICEAVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 402 RRAARLAAAGIAGILKKVGRDgsgggrrsdkqimRRTVVAVEGGLYLNYRMFREYMDEALRDILGedVAQHVVVKAMEDG 481
Cdd:pfam03727 161 TRAARLVAAGIAAILKKIGRD-------------KKVTVGVDGSVYEKYPGFRERLQEALRELLG--PGDKVVLVLAEDG 225
|
250
....*....|.
gi 332626974 482 SSIGSALLLAS 492
Cdd:pfam03727 226 SGVGAALIAAV 236
|
|
| ASKHA_NBD_HK1-2_meta_rpt1 |
cd24089 |
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ... |
54-491 |
1.68e-77 |
|
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: 249.31 E-value: 1.68e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 54 RLRQMVDAIAVEMQAGLVSEGG--SKLKMLLTFVDDLPNGSETGTYYALHLGGSYFRIIKVHLGGQRSSLEVQDVERHSI 131
Cdd:cd24089 6 TLLDISRRFRKEMEKGLGKDTHptATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMESQVYAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 132 PTSLMNSTSEVLFDFLASSLQRFIEKegndfslsQPLKRE---LAFTFSFPVKQTSISSGVLIKWTKGFAISEMAGEDIA 208
Cdd:cd24089 86 PEEIMHGSGTQLFDHVAECLADFMDK--------QKIKDKklpLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 209 ECLQGALNKRG-LDIRVAALVNDTVGALSFGHFHDPDTIAAVVFGTGSNACYLERTDAIIKCQNprtTSGSMVVNMEWGN 287
Cdd:cd24089 158 KLLRKAIRRRGdYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEG---DEGRMCINTEWGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 288 F---WSSRLPRTSYDLELDAESMNSNDMGFEKMIGGMYLGDIVRRVILRMSQESDIF-GPISSILSTPFVLRTNSVSAMh 363
Cdd:cd24089 235 FgddGSLEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFgGKISPELLTRGKFETKDVSAI- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 364 EDDTSELQEVARILKDLGVSevPMKVRKLVVK-ICDVVTRRAARLAAAGIAGILKKVGRDGSGGGRrsdkqimrRTVVAV 442
Cdd:cd24089 314 EKEKEGLANAKEILTRLGLD--PSEDDCVNVQhVCTIVSFRSANLCAATLAAILTRLRENKGLERL--------RTTVGV 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 332626974 443 EGGLYLNYRMFREYMDEALRDIlgedvAQHVVVKAM--EDGSSIGSALLLA 491
Cdd:cd24089 384 DGSVYKKHPQFSKRLHKAVRRL-----VPDCDVRFLlsEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1-3_meta_rpt2 |
cd24091 |
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ... |
54-491 |
5.15e-75 |
|
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: 242.84 E-value: 5.15e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 54 RLRQMVDAIAVEMQAGLVSE--GGSKLKMLLTFVDDLPNGSETGTYYALHLGGSYFRI--IKVHLGGQRSSLEVQDVerH 129
Cdd:cd24091 6 QLLEVKARMRAEMERGLRKEthASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVllVKVRSGKWRGVEMHNKI--Y 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 130 SIPTSLMNSTSEVLFDFLASSLQRFIEKEGNDfSLSQPLkrelAFTFSFPVKQTSISSGVLIKWTKGFAISEMAGEDIAE 209
Cdd:cd24091 84 AIPQEIMQGTGEELFDHIVQCIADFLEYMGLK-GVSLPL----GFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 210 CLQGALNKRG-LDIRVAALVNDTVGALSFGHFHDPDTIAAVVFGTGSNACYLERTDAIIKCQNprtTSGSMVVNMEWGNF 288
Cdd:cd24091 159 LLREAIKRREeFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEG---EEGRMCINMEWGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 289 ---WSSRLPRTSYDLELDAESMNSNDMGFEKMIGGMYLGDIVRRVILRMSQESDIF-GPISSILSTPFVLRTNSVSAMhE 364
Cdd:cd24091 236 gdnGCLDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFrGQISERLKTRGIFETKFLSQI-E 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 365 DDTSELQEVARILKDLGVsEVPMKVRKLVVKICDVVTRRAARLAAAGIAGILKKVGRDGSGGGRrsdkqimrRTVVAVEG 444
Cdd:cd24091 315 SDRLALLQVRAILQQLGL-DSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHL--------NVTVGVDG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 332626974 445 GLYLNYRMFREYMDEALRDIlgedvAQHVVVKAM--EDGSSIGSALLLA 491
Cdd:cd24091 386 TLYKLHPHFSRVMHETVKEL-----APKCDVTFLqsEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt1 |
cd24126 |
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ... |
55-491 |
2.80e-72 |
|
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: 235.90 E-value: 2.80e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 55 LRQMVDAIAVEMQAGLVSEGGSK--LKMLLTFVDDLPNGSETGTYYALHLGGSYFRIIKVHL---GGQRSSLEVQdveRH 129
Cdd:cd24126 7 LLDIMTRFRAEMEKGLAKDTNPTaaVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVsedGKQKVQMESQ---FY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 130 SIPTSLMNSTSEVLFDFLASSLQRFIEKEGndfslSQPLKRELAFTFSFPVKQTSISSGVLIKWTKGFAISEMAGEDIAE 209
Cdd:cd24126 84 PTPEEIIHGTGTELFDYVAECLADFMKKKG-----IKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 210 CLQGALNKRG-LDIRVAALVNDTVGALSFGHFHDPDTIAAVVFGTGSNACYLERTDAIIKCQNprtTSGSMVVNMEWGNF 288
Cdd:cd24126 159 SLRKAIRKHKdVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEG---DEGRMCINTEWGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 289 WSSRLP---RTSYDLELDAESMNSNDMGFEKMIGGMYLGDIVRRVILRMSQESDIF-GPISSILSTPFVLRTNSVSAMhE 364
Cdd:cd24126 236 GDDGSLediRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFkGQISPALRTKGKIETKHVAAI-E 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 365 DDTSELQEVARILKDLGVSevPMKVRKLVVK-ICDVVTRRAARLAAAGIAGILKKVgrdgsgggRRSDKQIMRRTVVAVE 443
Cdd:cd24126 315 KYKEGLYNTREILSDLGLE--PSEEDCIAVQhVCTIVSFRSANLCAAALAAILTRL--------RENKKLERLRTTVGMD 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 332626974 444 GGLYLNYRMFREYMDEALRDILGEdvaQHVVVKAMEDGSSIGSALLLA 491
Cdd:cd24126 385 GTVYKTHPQYAKRLHKVVRRLVPS---CDVRFLLSESGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK1_meta_rpt2 |
cd24127 |
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ... |
64-491 |
3.91e-69 |
|
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: 227.49 E-value: 3.91e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 64 VEMQAGLVSE--GGSKLKMLLTFVDDLPNGSETGTYYALHLGGSYFRIIKVHL-GGQRSSLEVQDvERHSIPTSLMNSTS 140
Cdd:cd24127 16 AEMELGLRKQthNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIrSGKKRTVEMHN-KIYAIPIEIMQGTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 141 EVLFDFLASSLQRFIekegnDFSLSQPLKRELAFTFSFPVKQTSISSGVLIKWTKGFAISEMAGEDIAECLQGALNKRG- 219
Cdd:cd24127 95 EELFDHIVSCISDFL-----DYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLLRDAIKRREe 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 220 LDIRVAALVNDTVGALSFGHFHDPDTIAAVVFGTGSNACYLERTDAIikcQNPRTTSGSMVVNMEWGNFWSSRL---PRT 296
Cdd:cd24127 170 FDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNV---EMVEGDQGQMCINMEWGAFGDNGClddIRT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 297 SYDLELDAESMNSNDMGFEKMIGGMYLGDIVRRVILRMSQESDIF-GPISSILSTPFVLRTNSVSAMHEDDTSELQeVAR 375
Cdd:cd24127 247 HYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFrGQISETLKTRGIFETKFLSQIESDRLALLQ-VRA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 376 ILKDLGVSEVpMKVRKLVVKICDVVTRRAARLAAAGIAGILKKVGRDGSGGGRrsdkqimrRTVVAVEGGLYLNYRMFRE 455
Cdd:cd24127 326 ILQQLGLNST-CDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHL--------NVTVGVDGTLYKLHPHFSR 396
|
410 420 430
....*....|....*....|....*....|....*.
gi 332626974 456 YMDEALRDILGEdvaQHVVVKAMEDGSSIGSALLLA 491
Cdd:cd24127 397 IMHQTVKELSPK---CNVSFLLSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HK3_meta_rpt2 |
cd24129 |
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ... |
65-491 |
3.17e-68 |
|
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: 225.15 E-value: 3.17e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 65 EMQAGLVSE--GGSKLKMLLTFVDDLPNGSETGTYYALHLGGSYFRIIKVHLGgqRSSLEVQDvERHSIPTSLMNSTSEV 142
Cdd:cd24129 17 EMAKGLRGEthAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVG--TAGVQITS-EIYSIPETVAQGTGQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 143 LFDFLASSLQRFIEKEGndfSLSQPLKreLAFTFSFPVKQTSISSGVLIKWTKGFAISEMAGEDIAECL-QGALNKRGLD 221
Cdd:cd24129 94 LFDHIVDCIVDFQQKQG---LSGQSLP--LGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLLrEAATRKQAVE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 222 IRVAALVNDTVGALSFGHFHDPDTIAAVVFGTGSNACYLERTDAIIKCQNprtTSGSMVVNMEWGNFWSS---RLPRTSY 298
Cdd:cd24129 169 LNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPG---DSGRMCINMEWGAFGDNgclAMISTRF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 299 DLELDAESMNSNDMGFEKMIGGMYLGDIVRRVILRMSQESDIF-GPISSILSTPFVLRTNSVSAMhEDDTSELQEVARIL 377
Cdd:cd24129 246 DASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFrGKQIQRLQTRDIFKTKFLSEI-ESDSLALRQVRAIL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 378 KDLGVsEVPMKVRKLVVKICDVVTRRAARLAAAGIAGILKKVGRDGSGGGRrsdkqimrRTVVAVEGGLYLNYRMFREYM 457
Cdd:cd24129 325 EDLGL-PLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDEL--------AVTVGVDGTLYKLHPRFSSLV 395
|
410 420 430
....*....|....*....|....*....|....*.
gi 332626974 458 DEALRDIlgedvAQHVVVKAM--EDGSSIGSALLLA 491
Cdd:cd24129 396 QATVREL-----APRCVVTFLqsEDGSGKGAALVTA 426
|
|
| ASKHA_NBD_HK2_meta_rpt2 |
cd24128 |
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ... |
64-491 |
6.46e-68 |
|
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: 224.39 E-value: 6.46e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 64 VEMQAGLVSE--GGSKLKMLLTFVDDLPNGSETGTYYALHLGGSYFRIIKVHL-GGQRSSLEVQDvERHSIPTSLMNSTS 140
Cdd:cd24128 16 VEMERGLSKEthASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVrNGKWRGVEMHN-KIYAIPQEVMHGTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 141 EVLFDFLASSLQRFIEKEGNDfSLSQPLkrelAFTFSFPVKQTSISSGVLIKWTKGFAISEMAGEDIAECLQGALNKR-G 219
Cdd:cd24128 95 EELFDHIVHCIADFLEYMGMK-GVSLPL----GFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLLKEAIHRReE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 220 LDIRVAALVNDTVGALSFGHFHDPDTIAAVVFGTGSNACYLERTDAIIKCQNprtTSGSMVVNMEWGNFWSSRLP---RT 296
Cdd:cd24128 170 FDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEG---EEGRMCVNMEWGAFGDNGCLddfRT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 297 SYDLELDAESMNSNDMGFEKMIGGMYLGDIVRRVILRMSQESDIF-GPISSILSTPFVLRTNSVSAMhEDDTSELQEVAR 375
Cdd:cd24128 247 EFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFrGRISERLKTRGIFETKFLSQI-ESDRLALLQVRA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 376 ILKDLGVsEVPMKVRKLVVKICDVVTRRAARLAAAGIAGILKKVGRDGSGGGRrsdkqimrRTVVAVEGGLYLNYRMFRE 455
Cdd:cd24128 326 ILQHLGL-ESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDAL--------KVTVGVDGTLYKLHPHFAK 396
|
410 420 430
....*....|....*....|....*....|....*.
gi 332626974 456 YMDEALRDILGEdvaQHVVVKAMEDGSSIGSALLLA 491
Cdd:cd24128 397 VMHETVKDLAPK---CDVSFLQSEDGSGKGAALITA 429
|
|
| ASKHA_NBD_HKDC1_meta_rpt2 |
cd24130 |
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ... |
54-491 |
3.09e-67 |
|
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: 222.50 E-value: 3.09e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 54 RLRQMVDAIAVEMQAGLVSE--GGSKLKMLLTFVDDLPNGSETGTYYALHLGGSYFRIIKVHLGGQRSSLEVQDvERHSI 131
Cdd:cd24130 6 QLQEVKQKMRTELEYGLKKEthPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGRRSVRMYN-KIFAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 132 PTSLMNSTSEVLFDFLASSLQRFIEKEGndfslSQPLKRELAFTFSFPVKQTSISSGVLIKWTKGFAISEMAGEDIAECL 211
Cdd:cd24130 85 PLEIMQGTGEELFDHIVQCIADFLDYMG-----LKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 212 QGALNKRG-LDIRVAALVNDTVGALSFGHFHDPDTIAAVVFGTGSNACYLERTDAIIKCQNprtTSGSMVVNMEWGNFWS 290
Cdd:cd24130 160 REAIKRRNeFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEG---DEGRMCINTEWGGFGD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 291 SRLP---RTSYDLELDAESMNSNDMGFEKMIGGMYLGDIVRRVILRMSQESDIF-GPISSILSTPFVLRTNSVSAMHEDD 366
Cdd:cd24130 237 NGCIddiRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFrGQISERLRTRGIFETKFLSQIESDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 367 TSELQeVARILKDLGVSEVPMKvrKLVVK-ICDVVTRRAARLAAAGIAGILKKVGRDGSGGGRrsdkqimrRTVVAVEGG 445
Cdd:cd24130 317 LALLQ-VRRILQQLGLDSTCED--SIIVKeVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRL--------DITVGVDGT 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 332626974 446 LYLNYRMFREYMDEALRDIlgedvAQHVVVKAM--EDGSSIGSALLLA 491
Cdd:cd24130 386 LYKLHPHFSRILQETVKEL-----APQCDVTFMlsEDGSGKGAALITA 428
|
|
| ASKHA_NBD_HK1_meta_rpt1 |
cd24124 |
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ... |
65-491 |
6.56e-67 |
|
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: 222.96 E-value: 6.56e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 65 EMQAGLVSEGG--SKLKMLLTFVDDLPNGSETGTYYALHLGGSYFRIIKVHLGGQRSSLEVQDVERHSIPTSLMNSTSEV 142
Cdd:cd24124 45 EMKNGLSRDFNptATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVHGSGSQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 143 LFDFLASSLQRFIEKEGndfslSQPLKRELAFTFSFPVKQTSISSGVLIKWTKGFAISEMAGEDIAECLQGALNKRG-LD 221
Cdd:cd24124 125 LFDHVAECLGDFMEKRK-----IKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLNKAIKKRGdYD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 222 IRVAALVNDTVGALSFGHFHDPDTIAAVVFGTGSNACYLERTDAIIKCQNprtTSGSMVVNMEWGNF---WSSRLPRTSY 298
Cdd:cd24124 200 ANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEG---DEGRMCINTEWGAFgddGSLEDIRTEF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 299 DLELDAESMNSNDMGFEKMIGGMYLGDIVRRVILRMSQESDIF-GPISSILSTPFVLRTNSVSAMhEDDTSELQEVARIL 377
Cdd:cd24124 277 DREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFeGRITPELLTRGKFNTSDVSAI-EKNKEGLHNAKEIL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 378 KDLGVSevPMKVRKLVVK-ICDVVTRRAARLAAAGIAGILKKVgrdgsgggrRSDKQIMR-RTVVAVEGGLYLNYRMFRE 455
Cdd:cd24124 356 TRLGVE--PSDDDCVSVQhVCTIVSFRSANLVAATLGAILNRL---------RDNKGTPRlRTTVGVDGSLYKTHPQYSR 424
|
410 420 430
....*....|....*....|....*....|....*.
gi 332626974 456 YMDEALRDILGEDVAQHVVvkaMEDGSSIGSALLLA 491
Cdd:cd24124 425 RFHKTLRRLVPDSDVRFLL---SESGSGKGAAMVTA 457
|
|
| ASKHA_NBD_HK2_meta_rpt1 |
cd24125 |
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ... |
64-491 |
2.41e-66 |
|
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: 220.15 E-value: 2.41e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 64 VEMQAGLVSEGG--SKLKMLLTFVDDLPNGSETGTYYALHLGGSYFRIIKVHL---GGQRSSLEVQdveRHSIPTSLMNS 138
Cdd:cd24125 16 KEMEKGLGATTHptAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVsdnGLQKVEMENQ---IYAIPEDIMRG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 139 TSEVLFDFLASSLQRFIEKEGndfslSQPLKRELAFTFSFPVKQTSISSGVLIKWTKGFAISEMAGEDIAECLQGALNKR 218
Cdd:cd24125 93 SGTQLFDHIAECLANFMDKLQ-----IKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALLRKAIQKR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 219 G-LDIRVAALVNDTVGALSFGHFHDPDTIAAVVFGTGSNACYLERTDAIIKCQNprtTSGSMVVNMEWGNFWSSRL---P 294
Cdd:cd24125 168 GdFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEG---DEGRMCINMEWGAFGDDGSlddI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 295 RTSYDLELDAESMNSNDMGFEKMIGGMYLGDIVRRVILRMSQESDIF-GPISSILSTPFVLRTNSVSAMhEDDTSELQEV 373
Cdd:cd24125 245 RTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFgGKLSPELLNTGHFETKDVSDI-EGEKDGIRKA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 374 ARILKDLGVSEVPMKVRKlVVKICDVVTRRAARLAAAGIAGILKKVgrdgsgggrRSDKQIMR-RTVVAVEGGLYLNYRM 452
Cdd:cd24125 324 REVLMRLGLDPTQEDCVA-THRICQIVSTRSASLCAATLAAVLQRI---------KENKGEERlRSTIGVDGSVYKKHPH 393
|
410 420 430
....*....|....*....|....*....|....*....
gi 332626974 453 FREYMDEALRDILGEdvaQHVVVKAMEDGSSIGSALLLA 491
Cdd:cd24125 394 FARRLHKTVRRLVPG---CDVRFLRSEDGSGKGAAMVTA 429
|
|
| ASKHA_NBD_HK4_meta |
cd24092 |
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ... |
55-491 |
1.97e-59 |
|
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: 202.42 E-value: 1.97e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 55 LRQMVDAIAVEMQAGLVSEG--GSKLKMLLTFVDDLPNGSETGTYYALHLGGSYFRIIKVHLG-GQRSSLEVQDVER-HS 130
Cdd:cd24092 16 LKKVMRRMQKEMDRGLRLETheEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGeGEEGQWSVKTKHQmYS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 131 IPTSLMNSTSEVLFDFLASSLQRFIEKEGndfslSQPLKRELAFTFSFPVKQTSISSGVLIKWTKGFAISEMAGEDIAEC 210
Cdd:cd24092 96 IPEDAMTGTAEMLFDYISECISDFLDKHQ-----MKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVGL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 211 LQGALNKRG-LDIRVAALVNDTVGALSFGHFHDPDTIAAVVFGTGSNACYLERtdaIIKCQNPRTTSGSMVVNMEWGNFW 289
Cdd:cd24092 171 LRDAIKRRGdFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEE---MQNVELVEGDEGRMCVNTEWGAFG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 290 -SSRLP--RTSYDLELDAESMNSNDMGFEKMIGGMYLGDIVRRVILRMSQESDIF-GPISSILSTPFVLRTNSVSAMhED 365
Cdd:cd24092 248 dSGELDefLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFhGEASEQLRTRGAFETRFVSQV-ES 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 366 DTSELQEVARILKDLGV--SEVPMKVRKLVvkiCDVVTRRAARLAAAGIAGILKKVgrdgsggGRRSDKQIMRRTvVAVE 443
Cdd:cd24092 327 DTGDRKQIYNILSTLGLrpSTTDCDIVRRA---CESVSTRAAHMCSAGLAGVINRM-------RESRSEDVMRIT-VGVD 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 332626974 444 GGLYLNYRMFREYMDEALRDILGedvAQHVVVKAMEDGSSIGSALLLA 491
Cdd:cd24092 396 GSVYKLHPSFKERFHASVRRLTP---SCEITFIESEEGSGRGAALVSA 440
|
|
| ASKHA_NBD_HK3_meta_rpt1 |
cd24090 |
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ... |
51-459 |
1.77e-55 |
|
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: 191.67 E-value: 1.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 51 PLGRLRQMVDAIAVEMQAGLVSEGG--SKLKMLLTFVDDLPNGSETGTYYALHLG--GSYFRIIKVHLGG-QRSSLEVQD 125
Cdd:cd24090 3 TRAQLQQIQASLLGSMEQALRGQASpaPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGiEGHRVEPRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 126 VErHSIPTSLMNSTSEVLFDFLASSLQRFIEKEGNDfslSQPLkrELAFTFSFPVKQTSISSGVLIKWTKGFAISEMAGE 205
Cdd:cd24090 83 QE-FVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVP---KQGL--QLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 206 DIAECLQGALNKRGL-DIRVAALVNDTVGALSFGHFHDPDTIAAVVFGTGSNACYLERTDAIIKCQNprtTSGSMVVNME 284
Cdd:cd24090 157 DVVQLLRDAIQRQGAyNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDE---DRGRVCVSVE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 285 WGNF---WSSRLPRTSYDLELDAESMNSNDMGFEKMIGGMYLGDIVRRVILRMSQESDIF-GPISSILSTPFVLRTNSVS 360
Cdd:cd24090 234 WGSFsddGALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFgGSTSPALRSQGSILLEHVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332626974 361 AMhEDDTSELQEVARILKDLGVSEVPMKVrKLVVKICDVVTRRAARLAAAGIAGILKKVgrdgsgggRRSDKQIMRRTVV 440
Cdd:cd24090 314 EM-EDPSAGAARVRAILQDLGLSPSASDV-ELVQHVCRAVCTRAAQLCAAALAAVLSHL--------QHSREQQTLQVAV 383
|
410
....*....|....*....
gi 332626974 441 AVEGGLYLNYRMFREYMDE 459
Cdd:cd24090 384 ATGGRVCERHPRFCSILQG 402
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
202-269 |
3.79e-03 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 39.48 E-value: 3.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332626974 202 MAG---EDIAECLQGALNKRGLDIRVAaLVNDTVGALSFGHFHDPDtiAAVVFGTGSNACYLERTDAIIKC 269
Cdd:COG2971 71 LAGagtPEDAEALEAALRELFPFARVV-VVNDALAALAGALGGEDG--IVVIAGTGSIAAGRDGDGRTARV 138
|
|
| |
