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Conserved domains on  [gi|19113860|ref|NP_592948|]
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hexokinase 1 [Schizosaccharomyces pombe]

Protein Classification

hexokinase family protein( domain architecture ID 11472104)

hexokinase family protein similar to Saccharomyces cerevisiae glucokinase and hexokinase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 42-468 0e+00

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


The actual alignment was detected with superfamily member cd24087:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 428  Bit Score: 787.72  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  42 TELLHRVTDRFVSELYKGLTTNPGDVPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEVQGNGKFDITQSKYRLPQE 121
Cdd:cd24087   1 TERLRKITDHFISELEKGLSKKGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNGKFDITQSKYRLPEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 122 LKVGTREALFDYIADCIKKFVEEVHP-GKSQNLEIGFTFSYPCVQRSINDASLVAWTKGFDIDGVEGESVGPLLSAALKR 200
Cdd:cd24087  81 LKTGTGEELWDFIADCLKKFVEEHFPgGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQKALKK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 201 VGCNnVRLNAILSDTTGTLVASNYASPGTEIGVIFGTGCNACYIEKFSEIPKLHKYDFPEDMNMIINCEWCDFDNQHVVL 280
Cdd:cd24087 161 RNVP-IELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEHDDIPPDSPMAINCEYGAFDNEHLVL 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 281 PRTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGALFNGQDVTKIRDPLAMDTSVLSAIEVDPFENLDE 360
Cdd:cd24087 240 PRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDPFENLED 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 361 TQTLFEETYGLKTTEEERQFIRRACELIGTRSARLSACGVCALVRKMNKPSMIVGTDGSVYNLYPRFKDRLAQAFKDILG 440
Cdd:cd24087 320 TDDLFQHFFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKKRGYKTCHVAADGSVYNKYPGFKERAAQALKDIFG 399

                       410       420
                ....*....|....*....|....*....
gi 19113860 441 EEIG-SKVVTIPAEDGSGVGAALVSALEA 468
Cdd:cd24087 400 WDGEdDPIKTVPAEDGSGVGAAIIAALTK 428
 
Name Accession Description Interval E-value
ASKHA_NBD_HK1-2_fungi cd24087
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ...
 42-468 0e+00

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: 787.72  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  42 TELLHRVTDRFVSELYKGLTTNPGDVPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEVQGNGKFDITQSKYRLPQE 121
Cdd:cd24087   1 TERLRKITDHFISELEKGLSKKGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNGKFDITQSKYRLPEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 122 LKVGTREALFDYIADCIKKFVEEVHP-GKSQNLEIGFTFSYPCVQRSINDASLVAWTKGFDIDGVEGESVGPLLSAALKR 200
Cdd:cd24087  81 LKTGTGEELWDFIADCLKKFVEEHFPgGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQKALKK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 201 VGCNnVRLNAILSDTTGTLVASNYASPGTEIGVIFGTGCNACYIEKFSEIPKLHKYDFPEDMNMIINCEWCDFDNQHVVL 280
Cdd:cd24087 161 RNVP-IELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEHDDIPPDSPMAINCEYGAFDNEHLVL 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 281 PRTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGALFNGQDVTKIRDPLAMDTSVLSAIEVDPFENLDE 360
Cdd:cd24087 240 PRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDPFENLED 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 361 TQTLFEETYGLKTTEEERQFIRRACELIGTRSARLSACGVCALVRKMNKPSMIVGTDGSVYNLYPRFKDRLAQAFKDILG 440
Cdd:cd24087 320 TDDLFQHFFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKKRGYKTCHVAADGSVYNKYPGFKERAAQALKDIFG 399

                       410       420
                ....*....|....*....|....*....
gi 19113860 441 EEIG-SKVVTIPAEDGSGVGAALVSALEA 468
Cdd:cd24087 400 WDGEdDPIKTVPAEDGSGVGAAIIAALTK 428
PTZ00107 PTZ00107
hexokinase; Provisional
 21-471 3.39e-115

hexokinase; Provisional


Pssm-ID: 240270 [Multi-domain]  Cd Length: 464  Bit Score: 347.05  E-value: 3.39e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860   21 IKLNKTLQDHLDELEEQFTIPTELLHRVTDRFVSELYKGL----------TTNPGDVPMVPTWIIGTPDGNEHGSYLALD 90
Cdd:PTZ00107   1 EMRYIKQRVRLASLVNQFTMSKEKLKELVDYFLYELVEGLeahrrhrnlwIPNECSFKMLDSCVYNLPTGKEKGVYYAID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860   91 LGGTNLRVCAVEVQGNGKFDITQSKYRLPQE---------LKVGTREALFDYIADCIKKFVEE--VHPGKSQNLEIGFTF 159
Cdd:PTZ00107  81 FGGTNFRAVRVSLRGGGKMERTQSKFSLPKSallgekgllDKKATATDLFDHIAKSIKKMMEEngDPEDLNKPVPVGFTF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  160 SYPCVQRSINDASLVAWTKGFD-----IDGVEGESVGPLLSAALKRVGCnNVRLNAILSDTTGTLVASNY----ASPGTE 230
Cdd:PTZ00107 161 SFPCTQLSVNNAILIDWTKGFEtgratNDPVEGKDVGELLNDAFKRNNV-PANVVAVLNDTVGTLISCAYqkpkNTPPCQ 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  231 IGVIFGTGCNACYIEkfseiPKLHKYDFpedMNMIINCEWCDFDNQhvvLPRTKYDVAIDEESPRPGLQTYEKMIAGCYL 310
Cdd:PTZ00107 240 VGVIIGTGSNACYFE-----PEVSAYGY---AGTPINMECGNFDSK---LPITPYDLEMDWYTPNRGRQQFEKMISGAYL 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  311 GDILRRILLDLYEQGAL--------FNGQDVTKIRDplamDTSvlsaievdpfENLDETQTLFEETYGLKTTEEERQFIR 382
Cdd:PTZ00107 309 GEISRRLIVHLLQLKAPpkmwqsgsFESEDASMILN----DQS----------PDLQFSRQVIKEAWDVDLTDEDLYTIR 374

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  383 RACELIGTRSARLSACGVCALVRKMNKPS--MIVGTDGSVYNLYPRFKDRLAQAFKDILGEEIGSkVVTIPAEDGSGVGA 460
Cdd:PTZ00107 375 KICELVRGRAAQLAAAFIAAPAKKTRTVQgkATVAIDGSVYVKNPWFRRLLQEYINSILGPDAGN-VVFYLADDGSGKGA 453

                        490
                 ....*....|.
gi 19113860  461 ALVSALEAKGK 471
Cdd:PTZ00107 454 AIIAAMVANDK 464
Hexokinase_2 pfam03727
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 230-466 2.22e-110

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: 326.37  E-value: 2.22e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860   230 EIGVIFGTGCNACYIEKFSEIPKLHKyDFPEDMNMIINCEWCDFDNQHV-VLPRTKYDVAIDEESPRPGLQTYEKMIAGC 308
Cdd:pfam03727   1 RIGLILGTGTNAAYVEKVSNIPKLEG-KLPKSGEMIINTEWGAFGDNGLlPLPRTEYDKELDAESPNPGFQPFEKMISGM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860   309 YLGDILRRILLDLYEQGALFNGQDVtKIRDPLAMDTSVLSAIEVDPFENLDETQTLFEETYGLKT-TEEERQFIRRACEL 387
Cdd:pfam03727  80 YLGELVRLVLLDLAEEGLLFKGQSE-KLKTPYSLDTSFLSAIESDPSEDLETTREILEELLGIETvTEEDRKIVRRICEA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860   388 IGTRSARLSACGVCALVRKMNK-PSMIVGTDGSVYNLYPRFKDRLAQAFKDILGEEIgsKVVTIPAEDGSGVGAALVSAL 466
Cdd:pfam03727 159 VSTRAARLVAAGIAAILKKIGRdKKVTVGVDGSVYEKYPGFRERLQEALRELLGPGD--KVVLVLAEDGSGVGAALIAAV 236
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 33-466 7.80e-110

Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 332.31  E-value: 7.80e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  33 ELEEQFTIPTELLHRVTDRFVSELYKGLTTNPGDVPMVPTWIiGTPDG-NEHGSYLALDLGGTNLRVCAVEVQGNGKFDI 111
Cdd:COG5026  10 LKRHGFDLSSIDLEEIAAKFQEEMEKGLEGKKSSLKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRFDGEGTFEI 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 112 TQ-SKYRLPQELKVGTREALFDYIADCIKKFVEEVHPgksqnleIGFTFSYPCVQRSINDASLVAWTKGFDIDGVEGESV 190
Cdd:COG5026  89 ENfKSFPLPGTSSEITAEEFFDFIADYIEPLLDESYK-------LGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNI 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 191 GPLLSAALKRVGCNNVRLNAILSDTTGTLVASNYASP----GTEIGVIFGTGCNACYIEKFSEIPKLHKYDFPedmnMII 266
Cdd:COG5026 162 GELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPddgySGYIGSILGTGHNTCYLEPNAPIGKLPAYEGP----MII 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 267 NCEWCDFDnqhvVLPRTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGaLFNGQDVTKIRDPLAMDTSV 346
Cdd:COG5026 238 NMESGNFN----KLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTVD 312

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 347 LSAIEVDPFENLDETQTLFEEtyglkTTEEERQFIRRACELIGTRSARLSACGVCALVRKM------NKPSMIVgTDGSV 420
Cdd:COG5026 313 MSRFLADPSDEKEILSQCLEA-----GSEEDREILREIADAIVERAARLVAATLAGILLHLgpgktpLKPHCIA-IDGST 386

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 19113860 421 YNLYPRFKDRLAQAFKDILGEEIGSKVVTIPAEDGSGVGAALVSAL 466
Cdd:COG5026 387 YEKMPGLAEKIEYALQEYLLGEKGRYVEFVLVENASLLGAAIAAAL 432
 
Name Accession Description Interval E-value
ASKHA_NBD_HK1-2_fungi cd24087
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ...
 42-468 0e+00

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: 787.72  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  42 TELLHRVTDRFVSELYKGLTTNPGDVPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEVQGNGKFDITQSKYRLPQE 121
Cdd:cd24087   1 TERLRKITDHFISELEKGLSKKGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNGKFDITQSKYRLPEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 122 LKVGTREALFDYIADCIKKFVEEVHP-GKSQNLEIGFTFSYPCVQRSINDASLVAWTKGFDIDGVEGESVGPLLSAALKR 200
Cdd:cd24087  81 LKTGTGEELWDFIADCLKKFVEEHFPgGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQKALKK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 201 VGCNnVRLNAILSDTTGTLVASNYASPGTEIGVIFGTGCNACYIEKFSEIPKLHKYDFPEDMNMIINCEWCDFDNQHVVL 280
Cdd:cd24087 161 RNVP-IELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEHDDIPPDSPMAINCEYGAFDNEHLVL 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 281 PRTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGALFNGQDVTKIRDPLAMDTSVLSAIEVDPFENLDE 360
Cdd:cd24087 240 PRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDPFENLED 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 361 TQTLFEETYGLKTTEEERQFIRRACELIGTRSARLSACGVCALVRKMNKPSMIVGTDGSVYNLYPRFKDRLAQAFKDILG 440
Cdd:cd24087 320 TDDLFQHFFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKKRGYKTCHVAADGSVYNKYPGFKERAAQALKDIFG 399

                       410       420
                ....*....|....*....|....*....
gi 19113860 441 EEIG-SKVVTIPAEDGSGVGAALVSALEA 468
Cdd:cd24087 400 WDGEdDPIKTVPAEDGSGVGAAIIAALTK 428
ASKHA_NBD_HK_fungi cd24018
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ...
 45-464 0e+00

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: 524.89  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  45 LHRVTDRFVSELYKGLTTNPGDVPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEVQGNGK-FDITQSKYRLPQELK 123
Cdd:cd24018   4 LEEIVKHFLSEMEKGLEGDGGSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNGGiFIIVQRKYKIPDEAK 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 124 VGTREALFDYIADCIKKFVEE--VHPGKSQNLEIGFTFSYPCVQRSINDASLVAWTKGFDIDGVEGESVGPLLSAALKRV 201
Cdd:cd24018  84 TGTGEELFDFIAECIAEFLEEhnLDLQSDKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQNALDRR 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 202 GCNnVRLNAILSDTTGTLVASNYASPGTEIGVIFGTGCNACYIEKFSEIPKLHKY--DFPEDMNMIINCEWCDFDNQHVV 279
Cdd:cd24018 164 GVN-VKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTSPsgSVTKSDEMIINTEWGAFDNEREV 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 280 LPRTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGALFNGQDVTKIRDPLAMDTSVLSAIEVDPFENLD 359
Cdd:cd24018 243 LPLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEADTSPDLD 322

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 360 ETQTLFEETYGLK-TTEEERQFIRRACELIGTRSARLSACGVCALVRKMNKPS---MIVGTDGSVYNLYPRFKDRLAQAF 435
Cdd:cd24018 323 AVRDILKELLAIDnTTLEDRKLIKRICELVSTRAARLSAAAIAAILLKRGSLLpepVTVGIDGSVYEKYPGFKDRLSEAL 402

                       410       420
                ....*....|....*....|....*....
gi 19113860 436 KDILGEEIGSKVVTIPAEDGSGVGAALVS 464
Cdd:cd24018 403 RELFGPEVKANISLVLAKDGSGLGAAIIA 431
ASKHA_NBD_HK_meta cd24019
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ...
 43-465 2.98e-162

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: 465.86  E-value: 2.98e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  43 ELLHRVTDRFVSELYKGL--TTNPG-DVPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEVQGNGKFDITQSKYRLP 119
Cdd:cd24019   5 EQLEEIMDRLLKEMEKGLskDTHPTaSVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGGSQVKMESEIYAIP 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 120 QELKVGTREALFDYIADCIKKFVEEvHPGKSQNLEIGFTFSYPCVQRSINDASLVAWTKGFDIDGVEGESVGPLLSAALK 199
Cdd:cd24019  85 EEIMTGTGEQLFDYIAECLAEFLEK-NGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLLQEAIK 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 200 RVGCNNVRLNAILSDTTGTLVASNYASPGTEIGVIFGTGCNACYIEKFSEIPKLhKYDFPEDMNMIINCEWCDF-DNQHV 278
Cdd:cd24019 164 RRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKW-DGDEGDPGQVIINTEWGAFgDNGVL 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 279 VLPRTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGALFNGQDVTKIRDPLAMDTSVLSAIEVDPFENL 358
Cdd:cd24019 243 DFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDNEGDF 322

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 359 DETQTLFEETYGLKTTEEERQFIRRACELIGTRSARLSACGVCALVRKMNKPSMIVGTDGSVYNLYPRFKDRLAQAFKDI 438
Cdd:cd24019 323 SNTREILKELGLEDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNRKEVTVGVDGSLYKYHPKFHKRMHETLKEL 402

                       410       420
                ....*....|....*....|....*..
gi 19113860 439 LGeeIGSKVVTIPAEDGSGVGAALVSA 465
Cdd:cd24019 403 VP--PGCKFKLMLSEDGSGKGAALVAA 427
ASKHA_NBD_GLK1-2_fungi cd24088
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ...
 42-463 2.73e-143

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: 418.34  E-value: 2.73e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  42 TELLHRVTDRFVSELYKGLTTNPGDVPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEVQGNGKFDITQSKYRLPQE 121
Cdd:cd24088   1 DEKLDKLTAEFQRQMEKGLAKHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHGDGTFSLRQEKSKIPDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 122 LKVG-TREALFDYIADCIKKFVEEVHP-----GKSQN-LEIGFTFSYPCVQRSINDASLVAWTKGFDIDGVEGESVGPLL 194
Cdd:cd24088  81 LKTGvTAKDLFDYLAKSVEAFLTKHHGdsfaaGKDDDrLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVVKLL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 195 SAALKRVGCnNVRLNAILSDTTGTLVASNYASP---GTEIGVIFGTGCNACYIEKFSEIPKL--HKYDFPEDMNMIINCE 269
Cdd:cd24088 161 QDELDRQGI-PVKVVALVNDTVGTLLARSYTSPeisGAVLGAIFGTGTNGAYLEDLEKIKKLddSSRVGKGKTHMVINTE 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 270 WCDFDNQHVVLPRTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGAL---FNGQDVTKIRDPLAMDTSV 346
Cdd:cd24088 240 WGSFDNELKVLPTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFliqYNDKSPSALNTPYGLDTAV 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 347 LSAIEVDPFENLDETQTLFEETYGLKT-TEEERQFIRRACELIGTRSARLSACGVCALVRKMNKPS------MIVGTDGS 419
Cdd:cd24088 320 LSAIEIDSEAELRATRKVLLDDLGLPApSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNksydgeINIGVDGS 399

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 19113860 420 VYNLYPRFKDRLAQAFKDILGEEIGSKVVTIP-AEDGSGVGAALV 463
Cdd:cd24088 400 VIEFYPGFESMLREALRLLLIGAEGEKRIKIGiAKDGSGVGAALC 444
ASKHA_NBD_HK_plant cd24020
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 40-465 2.82e-138

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: 405.12  E-value: 2.82e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  40 IPTELLHRVTDRFVSELYKGLTTNPG-DVPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEVQGN-GKFDITQS-KY 116
Cdd:cd24020   1 TPVSRLRQVADAMVVEMEAGLASEGGsKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKeGRVDKQEYeEV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 117 RLPQELKVGTREALFDYIADCIKKFVEEVHPG---KSQNLEIGFTFSYPCVQRSINDASLVAWTKGFDIDGVEGESVGPL 193
Cdd:cd24020  81 PIPPELMVGTSEELFDFIAGELAKFVATEGEGfhpEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVEL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 194 LSAALKRVGCNnVRLNAILSDTTGTLVASNYASPGTEIGVIFGTGCNACYIEKFSEIPKLHKyDFPEDMNMIINCEWCDF 273
Cdd:cd24020 161 LEEALERQGLD-MRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSG-GLPRSGEMVINTEWGNF 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 274 DNQHvvLPRTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGALFNGQDVTKIRDPLAMDTSVLSAIEVD 353
Cdd:cd24020 239 RSSH--LPRTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMHED 316

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 354 PFENLDETQTLFEETYGL-KTTEEERQFIRRACELIGTRSARLSACGVCALVRK---------MNKPSmIVGTDGSVYNL 423
Cdd:cd24020 317 DSPDLETVARILKDALGIdDTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKlgrdgggssPAQRT-VVAVDGGLYEH 395

                       410       420       430       440
                ....*....|....*....|....*....|....*....|..
gi 19113860 424 YPRFKDRLAQAFKDILGEEIGSKVVTIPAEDGSGVGAALVSA 465
Cdd:cd24020 396 YPKFREYMQQALVELLGDEAADSVELELSNDGSGIGAALLAA 437
ASKHA_NBD_HK cd24000
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 42-463 9.50e-131

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: 382.78  E-value: 9.50e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  42 TELLHRVTDRFVSELYKGLTTNPGDVPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEVQGNGKFDITQSKYRLPQE 121
Cdd:cd24000   1 DEDLKEITDAFLEELEKGLAGEPSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGKGIEVTISKKYEIPDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 122 LKVGTREALFDYIADCIKKFVEEvhPGKSQNLEIGFTFSYPCVQRSINDASLVAWTKGFDIDGVEGESVGPLLSAALKRV 201
Cdd:cd24000  81 IKTASAEEFFDFIADCIAEFLKE--NGLKKPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDALKKR 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 202 GCnNVRLNAILSDTTGTLVASNYASPGTEIGVIFGTGCNACYIEKFSEIPklhkydfPEDMNMIINCEWCDFDnqHVVLP 281
Cdd:cd24000 159 GL-PVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNIL-------LGDGGMIINTEWGNFG--KNSLP 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 282 RTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYeqgalfngqdvtkirdplamdtsvlsaievdpfenldet 361
Cdd:cd24000 229 RTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLA--------------------------------------- 269

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 362 qtlfeetyglktteeeRQFIRRACELIGTRSARLSACGVCALVRKMNK---PSMIVGTDGSVYNLYPRFKDRLAQAFKDI 438
Cdd:cd24000 270 ----------------DEILRKICELVAERSARLAAAAIAALLRKTGDspeKKITIAVDGSLFEKYPGYRERLEEYLKEL 333

                       410       420
                ....*....|....*....|....*
gi 19113860 439 LGEEIGSKVVtiPAEDGSGVGAALV 463
Cdd:cd24000 334 LGRGIRIELV--LVEDGSLIGAALA 356
PTZ00107 PTZ00107
hexokinase; Provisional
 21-471 3.39e-115

hexokinase; Provisional


Pssm-ID: 240270 [Multi-domain]  Cd Length: 464  Bit Score: 347.05  E-value: 3.39e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860   21 IKLNKTLQDHLDELEEQFTIPTELLHRVTDRFVSELYKGL----------TTNPGDVPMVPTWIIGTPDGNEHGSYLALD 90
Cdd:PTZ00107   1 EMRYIKQRVRLASLVNQFTMSKEKLKELVDYFLYELVEGLeahrrhrnlwIPNECSFKMLDSCVYNLPTGKEKGVYYAID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860   91 LGGTNLRVCAVEVQGNGKFDITQSKYRLPQE---------LKVGTREALFDYIADCIKKFVEE--VHPGKSQNLEIGFTF 159
Cdd:PTZ00107  81 FGGTNFRAVRVSLRGGGKMERTQSKFSLPKSallgekgllDKKATATDLFDHIAKSIKKMMEEngDPEDLNKPVPVGFTF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  160 SYPCVQRSINDASLVAWTKGFD-----IDGVEGESVGPLLSAALKRVGCnNVRLNAILSDTTGTLVASNY----ASPGTE 230
Cdd:PTZ00107 161 SFPCTQLSVNNAILIDWTKGFEtgratNDPVEGKDVGELLNDAFKRNNV-PANVVAVLNDTVGTLISCAYqkpkNTPPCQ 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  231 IGVIFGTGCNACYIEkfseiPKLHKYDFpedMNMIINCEWCDFDNQhvvLPRTKYDVAIDEESPRPGLQTYEKMIAGCYL 310
Cdd:PTZ00107 240 VGVIIGTGSNACYFE-----PEVSAYGY---AGTPINMECGNFDSK---LPITPYDLEMDWYTPNRGRQQFEKMISGAYL 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  311 GDILRRILLDLYEQGAL--------FNGQDVTKIRDplamDTSvlsaievdpfENLDETQTLFEETYGLKTTEEERQFIR 382
Cdd:PTZ00107 309 GEISRRLIVHLLQLKAPpkmwqsgsFESEDASMILN----DQS----------PDLQFSRQVIKEAWDVDLTDEDLYTIR 374

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  383 RACELIGTRSARLSACGVCALVRKMNKPS--MIVGTDGSVYNLYPRFKDRLAQAFKDILGEEIGSkVVTIPAEDGSGVGA 460
Cdd:PTZ00107 375 KICELVRGRAAQLAAAFIAAPAKKTRTVQgkATVAIDGSVYVKNPWFRRLLQEYINSILGPDAGN-VVFYLADDGSGKGA 453

                        490
                 ....*....|.
gi 19113860  461 ALVSALEAKGK 471
Cdd:PTZ00107 454 AIIAAMVANDK 464
Hexokinase_2 pfam03727
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 230-466 2.22e-110

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: 326.37  E-value: 2.22e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860   230 EIGVIFGTGCNACYIEKFSEIPKLHKyDFPEDMNMIINCEWCDFDNQHV-VLPRTKYDVAIDEESPRPGLQTYEKMIAGC 308
Cdd:pfam03727   1 RIGLILGTGTNAAYVEKVSNIPKLEG-KLPKSGEMIINTEWGAFGDNGLlPLPRTEYDKELDAESPNPGFQPFEKMISGM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860   309 YLGDILRRILLDLYEQGALFNGQDVtKIRDPLAMDTSVLSAIEVDPFENLDETQTLFEETYGLKT-TEEERQFIRRACEL 387
Cdd:pfam03727  80 YLGELVRLVLLDLAEEGLLFKGQSE-KLKTPYSLDTSFLSAIESDPSEDLETTREILEELLGIETvTEEDRKIVRRICEA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860   388 IGTRSARLSACGVCALVRKMNK-PSMIVGTDGSVYNLYPRFKDRLAQAFKDILGEEIgsKVVTIPAEDGSGVGAALVSAL 466
Cdd:pfam03727 159 VSTRAARLVAAGIAAILKKIGRdKKVTVGVDGSVYEKYPGFRERLQEALRELLGPGD--KVVLVLAEDGSGVGAALIAAV 236
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 33-466 7.80e-110

Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 332.31  E-value: 7.80e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  33 ELEEQFTIPTELLHRVTDRFVSELYKGLTTNPGDVPMVPTWIiGTPDG-NEHGSYLALDLGGTNLRVCAVEVQGNGKFDI 111
Cdd:COG5026  10 LKRHGFDLSSIDLEEIAAKFQEEMEKGLEGKKSSLKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRFDGEGTFEI 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 112 TQ-SKYRLPQELKVGTREALFDYIADCIKKFVEEVHPgksqnleIGFTFSYPCVQRSINDASLVAWTKGFDIDGVEGESV 190
Cdd:COG5026  89 ENfKSFPLPGTSSEITAEEFFDFIADYIEPLLDESYK-------LGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEGKNI 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 191 GPLLSAALKRVGCNNVRLNAILSDTTGTLVASNYASP----GTEIGVIFGTGCNACYIEKFSEIPKLHKYDFPedmnMII 266
Cdd:COG5026 162 GELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPddgySGYIGSILGTGHNTCYLEPNAPIGKLPAYEGP----MII 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 267 NCEWCDFDnqhvVLPRTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGaLFNGQDVTKIRDPLAMDTSV 346
Cdd:COG5026 238 NMESGNFN----KLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTVD 312

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 347 LSAIEVDPFENLDETQTLFEEtyglkTTEEERQFIRRACELIGTRSARLSACGVCALVRKM------NKPSMIVgTDGSV 420
Cdd:COG5026 313 MSRFLADPSDEKEILSQCLEA-----GSEEDREILREIADAIVERAARLVAATLAGILLHLgpgktpLKPHCIA-IDGST 386

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 19113860 421 YNLYPRFKDRLAQAFKDILGEEIGSKVVTIPAEDGSGVGAALVSAL 466
Cdd:COG5026 387 YEKMPGLAEKIEYALQEYLLGEKGRYVEFVLVENASLLGAAIAAAL 432
ASKHA_NBD_HK1-3_meta_rpt2 cd24091
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ...
 43-469 9.25e-104

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: 316.79  E-value: 9.25e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  43 ELLHRVTDRFVSELYKGL---TTNPGDVPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEVQgNGKF---DITQSKY 116
Cdd:cd24091   5 DQLLEVKARMRAEMERGLrkeTHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVR-SGKWrgvEMHNKIY 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 117 RLPQELKVGTREALFDYIADCIKKFVEEVHPgKSQNLEIGFTFSYPCVQRSINDASLVAWTKGFDIDGVEGESVGPLLSA 196
Cdd:cd24091  84 AIPQEIMQGTGEELFDHIVQCIADFLEYMGL-KGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLLRE 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 197 ALKRVGCNNVRLNAILSDTTGTLVASNYASPGTEIGVIFGTGCNACYIEKFSEIPKLHKydfpEDMNMIINCEWCDF-DN 275
Cdd:cd24091 163 AIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEG----EEGRMCINMEWGAFgDN 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 276 QHVVLPRTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGALFNGQDVTKIRDPLAMDTSVLSAIEVDPF 355
Cdd:cd24091 239 GCLDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRL 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 356 ENLDETQTLfeETYGLKTTEEERQFIRRACELIGTRSARLSACGVCALV------RKMNKPSMIVGTDGSVYNLYPRFKD 429
Cdd:cd24091 319 ALLQVRAIL--QQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVdkirenRGLDHLNVTVGVDGTLYKLHPHFSR 396

                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 19113860 430 RLAQAFKDILGEeigSKVVTIPAEDGSGVGAALVSALEAK 469
Cdd:cd24091 397 VMHETVKELAPK---CDVTFLQSEDGSGKGAALITAVACR 433
PLN02405 PLN02405
hexokinase
 31-465 7.35e-103

hexokinase


Pssm-ID: 215226 [Multi-domain]  Cd Length: 497  Bit Score: 316.39  E-value: 7.35e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860   31 LDELEEQFTIPTELLHRVTDRFVSELYKGLTTNPGD-VPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEVQGNGKF 109
Cdd:PLN02405  41 LKEFEEDCATPIGKLRQVADAMTVEMHAGLASEGGSkLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGR 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  110 DITQ--SKYRLPQELKVGTREALFDYIADCIKKFV----EEVHPGKSQNLEIGFTFSYPCVQRSINDASLVAWTKGFDID 183
Cdd:PLN02405 121 VVKQefEEVSIPPHLMTGSSDALFDFIAAALAKFVategEDFHLPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSID 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  184 GVEGESVGPLLSAALKRVGCNnVRLNAILSDTTGTLVASNYASPGTEIGVIFGTGCNACYIEKFSEIPKLHKyDFPEDMN 263
Cdd:PLN02405 201 DAVGQDVVGELTKAMERVGLD-MRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHG-LLPKSGE 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  264 MIINCEWCDFDNQHvvLPRTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGALFNGQDVTKIRDPLAMD 343
Cdd:PLN02405 279 MVINMEWGNFRSSH--LPLTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILR 356

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  344 TSVLSAIEVDPFENLDETQTLFEETYGLKTTE-EERQFIRRACELIGTRSARLSACGVCALVRKMNKPSM--------IV 414
Cdd:PLN02405 357 TPDMSAMHHDTSPDLKVVGSKLKDILEIPNTSlKMRKVVVELCNIVATRGARLSAAGIYGILKKLGRDTVkdgekqksVI 436

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 19113860  415 GTDGSVYNLYPRFKDRLAQAFKDILGEEIGSKVVTIPAEDGSGVGAALVSA 465
Cdd:PLN02405 437 AMDGGLFEHYTEFSKCMESTLKELLGEEVSESIEVEHSNDGSGIGAALLAA 487
PLN02914 PLN02914
hexokinase
 31-469 1.05e-101

hexokinase


Pssm-ID: 178502 [Multi-domain]  Cd Length: 490  Bit Score: 313.36  E-value: 1.05e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860   31 LDELEEQFTIPTELLHRVTDRFVSELYKGLTTNPG-DVPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEVQGNGK- 108
Cdd:PLN02914  41 LTKLQKDCATPLPVLRHVADAMAADMRAGLAVDGGgDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKDEr 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  109 -FDITQSKYRLPQELKVGTREALFDYIADCIKKFVEE----VHPGKSQNLEIGFTFSYPCVQRSINDASLVAWTKGFDID 183
Cdd:PLN02914 121 vIATEFEQVSIPQELMFGTSEELFDFIASGLANFVAKeggkFHLPEGRKREIGFTFSFPVKQTSIDSGILMKWTKGFAVS 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  184 GVEGESVGPLLSAALKRVGCNnVRLNAILSDTTGTLVASNYASPGTEIGVIFGTGCNACYIEKFSEIPKLHKYDfPEDMN 263
Cdd:PLN02914 201 GTAGKDVVACLNEAMERQGLD-MRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQK-SSSGR 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  264 MIINCEWCDFDNqhvVLPRTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGALFNGQDVTKIRDPLAMD 343
Cdd:PLN02914 279 TIINTEWGAFSD---GLPLTEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALR 355

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  344 TSVLSAIEVDPFENLDETQTLFEETYGLKTTEEERQFIRRACELIGTRSARLSACGVCALVRKMNKPS--------MIVG 415
Cdd:PLN02914 356 TPHLCAMQQDNSDDLQAVGSILYDVLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDSkgmifgkrTVVA 435

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 19113860  416 TDGSVYNLYPRFKDRLAQAFKDILGEEIGSKVVTIPAEDGSGVGAALVSALEAK 469
Cdd:PLN02914 436 MDGGLYEKYPQYRRYMQDAVTELLGLELSKNIAIEHTKDGSGIGAALLAATNSK 489
ASKHA_NBD_HK1-2_meta_rpt1 cd24089
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ...
 43-465 2.19e-101

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: 310.55  E-value: 2.19e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  43 ELLHRVTDRFVSELYKGL---TTNPGDVPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEV--QGNGKFDITQSKYR 117
Cdd:cd24089   5 ETLLDISRRFRKEMEKGLgkdTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVndEKNQKVEMESQVYA 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 118 LPQELKVGTREALFDYIADCIKKFVEEVHPgKSQNLEIGFTFSYPCVQRSINDASLVAWTKGFDIDGVEGESVGPLLSAA 197
Cdd:cd24089  85 IPEEIMHGSGTQLFDHVAECLADFMDKQKI-KDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLLRKA 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 198 LKRVGCNNVRLNAILSDTTGTLVASNYASPGTEIGVIFGTGCNACYIEKFSEIPKLHKydfpEDMNMIINCEWCDF-DNQ 276
Cdd:cd24089 164 IRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEG----DEGRMCINTEWGAFgDDG 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 277 HVVLPRTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGALFNGQDVTKIRDPLAMDTSVLSAIEvDPFE 356
Cdd:cd24089 240 SLEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIE-KEKE 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 357 NLDETQTLFEEtYGLKTTEEERQFIRRACELIGTRSARLSACGVCALV------RKMNKPSMIVGTDGSVYNLYPRFKDR 430
Cdd:cd24089 319 GLANAKEILTR-LGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILtrlrenKGLERLRTTVGVDGSVYKKHPQFSKR 397

                       410       420       430
                ....*....|....*....|....*....|....*
gi 19113860 431 LAQAFKDILGEeigSKVVTIPAEDGSGVGAALVSA 465
Cdd:cd24089 398 LHKAVRRLVPD---CDVRFLLSEDGSGKGAAMVTA 429
ASKHA_NBD_HK3_meta_rpt2 cd24129
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ...
 45-466 6.14e-98

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: 301.80  E-value: 6.14e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  45 LHRVTDRFVSELYKGL---TTNPGDVPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEVqGNGKFDITQSKYRLPQE 121
Cdd:cd24129   7 LAAVQAQMRKEMAKGLrgeTHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHV-GTAGVQITSEIYSIPET 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 122 LKVGTREALFDYIADCIKKFVEEvHPGKSQNLEIGFTFSYPCVQRSINDASLVAWTKGFDIDGVEGESVGPLLSAALKRV 201
Cdd:cd24129  86 VAQGTGQQLFDHIVDCIVDFQQK-QGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLLREAATRK 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 202 GCNNVRLNAILSDTTGTLVASNYASPGTEIGVIFGTGCNACYIEKFSEIPKLHKydfpEDMNMIINCEWCDF-DNQHVVL 280
Cdd:cd24129 165 QAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPG----DSGRMCINMEWGAFgDNGCLAM 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 281 PRTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGALFNGQDVTKIRDPLAMDTSVLSAIEVDPFeNLDE 360
Cdd:cd24129 241 ISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSL-ALRQ 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 361 TQTLFEEtYGLKTTEEERQFIRRACELIGTRSARLSACGVCALVRKM------NKPSMIVGTDGSVYNLYPRFKDRLAQA 434
Cdd:cd24129 320 VRAILED-LGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMrenrglDELAVTVGVDGTLYKLHPRFSSLVQAT 398

                       410       420       430
                ....*....|....*....|....*....|..
gi 19113860 435 FKDILGEeigSKVVTIPAEDGSGVGAALVSAL 466
Cdd:cd24129 399 VRELAPR---CVVTFLQSEDGSGKGAALVTAV 427
ASKHA_NBD_HK4_meta cd24092
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ...
 31-469 1.93e-97

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: 300.64  E-value: 1.93e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  31 LDELEEQFTIPTELLHRVTDRFVSELYKGL---TTNPGDVPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEV---- 103
Cdd:cd24092   2 VEQILAEFQLQEEDLKKVMRRMQKEMDRGLrleTHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVgege 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 104 QGNGKFDITQSKYRLPQELKVGTREALFDYIADCIKKFVEEvHPGKSQNLEIGFTFSYPCVQRSINDASLVAWTKGFDID 183
Cdd:cd24092  82 EGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDK-HQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKAS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 184 GVEGESVGPLLSAALKRVGCNNVRLNAILSDTTGTLVASNYASPGTEIGVIFGTGCNACYIEKFSEIPKLHKydfpEDMN 263
Cdd:cd24092 161 GAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEG----DEGR 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 264 MIINCEWCDF-DNQHVVLPRTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGALFNGQDVTKIRDPLAM 342
Cdd:cd24092 237 MCVNTEWGAFgDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAF 316

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 343 DTSVLSAIEVDpfeNLDETQTL-FEETYGLKTTEEERQFIRRACELIGTRSARLSACGVCALVRKMNKP------SMIVG 415
Cdd:cd24092 317 ETRFVSQVESD---TGDRKQIYnILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESrsedvmRITVG 393

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....
gi 19113860 416 TDGSVYNLYPRFKDRLAQAFKDILGeeiGSKVVTIPAEDGSGVGAALVSALEAK 469
Cdd:cd24092 394 VDGSVYKLHPSFKERFHASVRRLTP---SCEITFIESEEGSGRGAALVSAVACK 444
ASKHA_NBD_HK2_meta_rpt2 cd24128
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ...
 43-469 1.92e-96

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: 297.97  E-value: 1.92e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  43 ELLHRVTDRFVSELYKGL---TTNPGDVPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEVQGN--GKFDITQSKYR 117
Cdd:cd24128   5 DQLLEVKRRMKVEMERGLskeTHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGkwRGVEMHNKIYA 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 118 LPQELKVGTREALFDYIADCIKKFVEEVHPgKSQNLEIGFTFSYPCVQRSINDASLVAWTKGFDIDGVEGESVGPLLSAA 197
Cdd:cd24128  85 IPQEVMHGTGEELFDHIVHCIADFLEYMGM-KGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLLKEA 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 198 LKRVGCNNVRLNAILSDTTGTLVASNYASPGTEIGVIFGTGCNACYIEKFSEIPKLHKydfpEDMNMIINCEWCDF-DNQ 276
Cdd:cd24128 164 IHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEG----EEGRMCVNMEWGAFgDNG 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 277 HVVLPRTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGALFNGQDVTKIRDPLAMDTSVLSAIEVDPFE 356
Cdd:cd24128 240 CLDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLA 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 357 NLDETQTLfeETYGLKTTEEERQFIRRACELIGTRSARLSACGVCALV------RKMNKPSMIVGTDGSVYNLYPRFKDR 430
Cdd:cd24128 320 LLQVRAIL--QHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVdkirenRGLDALKVTVGVDGTLYKLHPHFAKV 397

                       410       420       430
                ....*....|....*....|....*....|....*....
gi 19113860 431 LAQAFKDILGEeigSKVVTIPAEDGSGVGAALVSALEAK 469
Cdd:cd24128 398 MHETVKDLAPK---CDVSFLQSEDGSGKGAALITAVACR 433
ASKHA_NBD_HKDC1_meta_rpt2 cd24130
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ...
 43-466 2.87e-96

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: 297.61  E-value: 2.87e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  43 ELLHRVTDRFVSELYKGL---TTNPGDVPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEVQ-GNGKFDITQSKYRL 118
Cdd:cd24130   5 DQLQEVKQKMRTELEYGLkkeTHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRsGRRSVRMYNKIFAI 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 119 PQELKVGTREALFDYIADCIKKFVEEVHPgKSQNLEIGFTFSYPCVQRSINDASLVAWTKGFDIDGVEGESVGPLLSAAL 198
Cdd:cd24130  85 PLEIMQGTGEELFDHIVQCIADFLDYMGL-KGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDMLREAI 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 199 KRVGCNNVRLNAILSDTTGTLVASNYASPGTEIGVIFGTGCNACYIEKFSEIPKLHKydfpEDMNMIINCEWCDF-DNQH 277
Cdd:cd24130 164 KRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEG----DEGRMCINTEWGGFgDNGC 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 278 VVLPRTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGALFNGQDVTKIRDPLAMDTSVLSAIEVDPFEN 357
Cdd:cd24130 240 IDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLAL 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 358 LDETQTLfeETYGLKTTEEERQFIRRACELIGTRSARLSACGVCALVRK------MNKPSMIVGTDGSVYNLYPRFKDRL 431
Cdd:cd24130 320 LQVRRIL--QQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKirenqgLDRLDITVGVDGTLYKLHPHFSRIL 397

                       410       420       430
                ....*....|....*....|....*....|....*
gi 19113860 432 AQAFKDILGEeigSKVVTIPAEDGSGVGAALVSAL 466
Cdd:cd24130 398 QETVKELAPQ---CDVTFMLSEDGSGKGAALITAV 429
ASKHA_NBD_HKDC1_meta_rpt1 cd24126
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ...
 43-465 2.16e-95

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: 295.22  E-value: 2.16e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  43 ELLHRVTDRFVSELYKGLT--TNP-GDVPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEVQGNGKFDI-TQSK-YR 117
Cdd:cd24126   5 DTLLDIMTRFRAEMEKGLAkdTNPtAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVqMESQfYP 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 118 LPQELKVGTREALFDYIADCIKKFVEEVHPgKSQNLEIGFTFSYPCVQRSINDASLVAWTKGFDIDGVEGESVGPLLSAA 197
Cdd:cd24126  85 TPEEIIHGTGTELFDYVAECLADFMKKKGI-KHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSLRKA 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 198 LKRVGCNNVRLNAILSDTTGTLVASNYASPGTEIGVIFGTGCNACYIEKFSEIpklhkyDFPE--DMNMIINCEWCDF-D 274
Cdd:cd24126 164 IRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHI------DLVEgdEGRMCINTEWGAFgD 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 275 NQHVVLPRTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGALFNGQDVTKIRDPLAMDTSVLSAIEvDP 354
Cdd:cd24126 238 DGSLEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIE-KY 316

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 355 FENLDETQTLFEEtYGLKTTEEERQFIRRACELIGTRSARLSACGVCALV------RKMNKPSMIVGTDGSVYNLYPRFK 428
Cdd:cd24126 317 KEGLYNTREILSD-LGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILtrlrenKKLERLRTTVGMDGTVYKTHPQYA 395

                       410       420       430
                ....*....|....*....|....*....|....*..
gi 19113860 429 DRLAQAFKDILGEeigSKVVTIPAEDGSGVGAALVSA 465
Cdd:cd24126 396 KRLHKVVRRLVPS---CDVRFLLSESGSGKGAAMVTA 429
Hexokinase_1 pfam00349
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 30-224 2.65e-95

Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by this family and pfam03727. Some members of the family have two copies of each of these domains.


Pssm-ID: 459774 [Multi-domain]  Cd Length: 197  Bit Score: 286.32  E-value: 2.65e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860    30 HLDELEEQFTIPTELLHRVTDRFVSELYKGLTTNP-GDVPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEVQGNGK 108
Cdd:pfam00349   1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGsSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGGDGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860   109 FDITQSKYRLPQELKVGTREALFDYIADCIKKFVEEVHPGKSQN--LEIGFTFSYPCVQRSINDASLVAWTKGFDIDGVE 186
Cdd:pfam00349  81 FEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDFEEkeLPLGFTFSFPVEQTSLDSGTLIRWTKGFDIPGVV 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 19113860   187 GESVGPLLSAALKRVGCnNVRLNAILSDTTGTLVASNY 224
Cdd:pfam00349 161 GKDVVQLLQEALERRGL-PVKVVALVNDTVGTLMAGAY 197
PLN02362 PLN02362
hexokinase
 31-465 5.71e-95

hexokinase


Pssm-ID: 215206 [Multi-domain]  Cd Length: 509  Bit Score: 296.41  E-value: 5.71e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860   31 LDELEEQFTIPTELLHRVTDRFVSELYKGLTTNPGD-VPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEVQGNGKF 109
Cdd:PLN02362  41 LKELEEACETPVGRLRQVVDAMAVEMHAGLASEGGSkLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRSS 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  110 DITQSKYR--LPQELKVGTREALFDYIADCIKKFVE------EVHPGKSQnlEIGFTFSYPCVQRSINDASLVAWTKGFD 181
Cdd:PLN02362 121 ILSQDVERhpIPQHLMNSTSEVLFDFIASSLKQFVEkeengsEFSQVRRR--ELGFTFSFPVKQTSISSGILIKWTKGFA 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  182 IDGVEGESVGPLLSAALKRVGCNnVRLNAILSDTTGTLVASNYASPGTEIGVIFGTGCNACYIEKFSEIPKLHKYdFPED 261
Cdd:PLN02362 199 ISDMVGKDVAECLQGALNRRGLD-MRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQGL-LTTS 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  262 MNMIINCEWCDFDNQHvvLPRTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGALFnGQDVTKIRDPLA 341
Cdd:PLN02362 277 GSMVVNMEWGNFWSSH--LPRTSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIF-GPVSSRLSTPFV 353

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  342 MDTSVLSAIEVDPFENLDETQTLFEETYGLKTTE-EERQFIRRACELIGTRSARLSACGVCALVRKMNKPS--------- 411
Cdd:PLN02362 354 LRTPSVAAMHEDDSPELQEVARILKETLGISEVPlKVRKLVVKICDVVTRRAARLAAAGIVGILKKIGRDGsggitsgrs 433

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113860  412 ---------MIVGTDGSVYNLYPRFKDRLAQAFKDILGEEIGSKVVTIPAEDGSGVGAALVSA 465
Cdd:PLN02362 434 rsdiqimrrTVVAVEGGLYTNYTMFREYLHEALNEILGEDVAQHVILKATEDGSGIGSALLAA 496
ASKHA_NBD_HK2_meta_rpt1 cd24125
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ...
 43-465 1.21e-94

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: 292.95  E-value: 1.21e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  43 ELLHRVTDRFVSELYKGL--TTNP-GDVPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEVQGNG--KFDITQSKYR 117
Cdd:cd24125   5 ETLLEISKRFRKEMEKGLgaTTHPtAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGlqKVEMENQIYA 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 118 LPQELKVGTREALFDYIADCIKKFVEEVHPgKSQNLEIGFTFSYPCVQRSINDASLVAWTKGFDIDGVEGESVGPLLSAA 197
Cdd:cd24125  85 IPEDIMRGSGTQLFDHIAECLANFMDKLQI-KDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALLRKA 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 198 LKRVGCNNVRLNAILSDTTGTLVASNYASPGTEIGVIFGTGCNACYIEKFSEIPKLHKydfpEDMNMIINCEWCDFDNQH 277
Cdd:cd24125 164 IQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEG----DEGRMCINMEWGAFGDDG 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 278 VVLP-RTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGALFNGQDVTKIRDPLAMDTSVLSAIEVDPfE 356
Cdd:cd24125 240 SLDDiRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEK-D 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 357 NLDETQTLFEEtYGLKTTEEERQFIRRACELIGTRSARLSACGVCALVRKM--NKPS----MIVGTDGSVYNLYPRFKDR 430
Cdd:cd24125 319 GIRKAREVLMR-LGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIkeNKGEerlrSTIGVDGSVYKKHPHFARR 397

                       410       420       430
                ....*....|....*....|....*....|....*
gi 19113860 431 LAQAFKDILGEeigSKVVTIPAEDGSGVGAALVSA 465
Cdd:cd24125 398 LHKTVRRLVPG---CDVRFLRSEDGSGKGAAMVTA 429
ASKHA_NBD_HK1_meta_rpt2 cd24127
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ...
 39-466 4.38e-91

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: 284.11  E-value: 4.38e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  39 TIPTELLHRVTDRFVSELYKGL---TTNPGDVPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEVQGNGK--FDITQ 113
Cdd:cd24127   1 HLTKDMLLEVKKRMRAEMELGLrkqTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKrtVEMHN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 114 SKYRLPQELKVGTREALFDYIADCIKKFVEEVHPgKSQNLEIGFTFSYPCVQRSINDASLVAWTKGFDIDGVEGESVGPL 193
Cdd:cd24127  81 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGI-KGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 194 LSAALKRVGCNNVRLNAILSDTTGTLVASNYASPGTEIGVIFGTGCNACYIEKFSEIPKLHKydfpEDMNMIINCEWCDF 273
Cdd:cd24127 160 LRDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEG----DQGQMCINMEWGAF 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 274 -DNQHVVLPRTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGALFNGQDVTKIRDPLAMDTSVLSAIEV 352
Cdd:cd24127 236 gDNGCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIES 315

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 353 DPFENLDETQTLfeETYGLKTTEEERQFIRRACELIGTRSARLSACGVCALV------RKMNKPSMIVGTDGSVYNLYPR 426
Cdd:cd24127 316 DRLALLQVRAIL--QQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVdkirenRGLDHLNVTVGVDGTLYKLHPH 393

                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 19113860 427 FKDRLAQAFKDILGEeigSKVVTIPAEDGSGVGAALVSAL 466
Cdd:cd24127 394 FSRIMHQTVKELSPK---CNVSFLLSEDGSGKGAALITAV 430
ASKHA_NBD_HK1_meta_rpt1 cd24124
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ...
 43-466 4.04e-85

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: 269.95  E-value: 4.04e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  43 ELLHRVTDRFVSELYKGLT--TNP-GDVPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEVQGNGKFDITQSK--YR 117
Cdd:cd24124  33 ETLIDIMTRFRKEMKNGLSrdFNPtATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESevYD 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 118 LPQELKVGTREALFDYIADCIKKFVEEvHPGKSQNLEIGFTFSYPCVQRSINDASLVAWTKGFDIDGVEGESVGPLLSAA 197
Cdd:cd24124 113 TPENIVHGSGSQLFDHVAECLGDFMEK-RKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLNKA 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 198 LKRVGCNNVRLNAILSDTTGTLVASNYASPGTEIGVIFGTGCNACYIEKFSEIPKLHKydfpEDMNMIINCEWCDF-DNQ 276
Cdd:cd24124 192 IKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEG----DEGRMCINTEWGAFgDDG 267

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 277 HVVLPRTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGALFNGQDVTKIRDPLAMDTSVLSAIEVDPfE 356
Cdd:cd24124 268 SLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNK-E 346

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 357 NLDETQTLFEEtYGLKTTEEERQFIRRACELIGTRSARLSACGVCALVRKM--NK--PSM--IVGTDGSVYNLYPRFKDR 430
Cdd:cd24124 347 GLHNAKEILTR-LGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLrdNKgtPRLrtTVGVDGSLYKTHPQYSRR 425

                       410       420       430
                ....*....|....*....|....*....|....*.
gi 19113860 431 LAQAFKDILGEeigSKVVTIPAEDGSGVGAALVSAL 466
Cdd:cd24124 426 FHKTLRRLVPD---SDVRFLLSESGSGKGAAMVTAV 458
ASKHA_NBD_HK3_meta_rpt1 cd24090
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ...
 39-465 5.27e-79

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: 252.92  E-value: 5.27e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  39 TIPTELLHRVTDRFVSELYKGLTTNPGDVP---MVPTWIIGTPDGNEHGSYLALDLG--GTNLRVCAVEVQGNG--KFDI 111
Cdd:cd24090   1 KVTRAQLQQIQASLLGSMEQALRGQASPAPavrMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEghRVEP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 112 TQSKYRLPQELKVGTREALFDYIADCIKKFVEeVHPGKSQNLEIGFTFSYPCVQRSINDASLVAWTKGFDIDGVEGESVG 191
Cdd:cd24090  81 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLD-GQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVV 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 192 PLLSAALKRVGCNNVRLNAILSDTTGTLVASNYASPGTEIGVIFGTGCNACYIEKFSEIPKLHkydfpEDM-NMIINCEW 270
Cdd:cd24090 160 QLLRDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLD-----EDRgRVCVSVEW 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 271 CDFDNQHVVLP-RTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGALFNGQDVTKIRDPLAMDTSVLSA 349
Cdd:cd24090 235 GSFSDDGALGPvLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAE 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860 350 IEvDPFENLDETQTLFEEtYGLKTTEEERQFIRRACELIGTRSARLSACGVCALV------RKMNKPSMIVGTDGSVYNL 423
Cdd:cd24090 315 ME-DPSAGAARVRAILQD-LGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLshlqhsREQQTLQVAVATGGRVCER 392

                       410       420       430       440
                ....*....|....*....|....*....|....*....|..
gi 19113860 424 YPRFKDRLaQAFKDILGEEigSKVVTIPAEDGSGVGAALVSA 465
Cdd:cd24090 393 HPRFCSIL-QGTVMLLAPE--CDVSFIPSVDGGGRGVAMVTA 431
PLN02596 PLN02596
hexokinase-like
 41-465 5.33e-60

hexokinase-like


Pssm-ID: 178206 [Multi-domain]  Cd Length: 490  Bit Score: 204.73  E-value: 5.33e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860   41 PTELLHRVTDRFVSELYKGLTTNP-GDVPMVPTWIIGTPDGNEHGSYLALDLGGTNLRVCAVEVQGNGK--FDITQSKYR 117
Cdd:PLN02596  52 PVSKLWEVADALVSDMTASLTAEEtTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNEpiSDLYREEIS 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  118 LPQELKVGTREALFDYIADCIKKFVEEvHPGKSQNL-----EIGFTFSYPCVQRSINDASLVAWtKGFDIDGVEGESVGP 192
Cdd:PLN02596 132 IPSNVLNGTSQELFDYIALELAKFVAE-HPGDEADTpervkKLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVN 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  193 LLSAALKRVGCNnVRLNAILSDTTGTLVASNYASPGTEIGVIFGTGCNACYIEKFSEIPKLHKyDFPEDMNMIINCEWCD 272
Cdd:PLN02596 210 DINRALEKHGLK-IRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQS-PSPESQEIVISTEWGN 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  273 FDNQHvvLPRTKYDVAIDEESPRPGLQTYEKMIAGCYLGDILRRILLDLYEQGALFNGQDVTKIRDPLAMDTSVLSAIEV 352
Cdd:PLN02596 288 FNSCH--LPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAAMHQ 365

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113860  353 DPFENLDETQTLFEETYGL-KTTEEERQFIRRACELIGTRSARLSACGVCALVRKM----NKPSmIVGTDGSVYNLYPRF 427
Cdd:PLN02596 366 DTSEDHEVVNEKLKEIFGItDSTPMAREVVAEVCDIVAERGARLAGAGIVGIIKKLgrieNKKS-VVTVEGGLYEHYRVF 444

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 19113860  428 KDRLAQAFKDILGEEIGSKVVTIPAEDGSGVGAALVSA 465
Cdd:PLN02596 445 RNYLHSSVWEMLGSELSDNVVIEHSHGGSGAGALFLAA 482
ASKHA_NBD_ROK-like cd24152
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ...
 86-145 4.83e-04

nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This subfamily is composed of uncharacterized proteins belonging to the the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Members of this subfamily lack the cysteine-rich zinc-binding motif, which presents in other ROK families.


Pssm-ID: 466988 [Multi-domain]  Cd Length: 286  Bit Score: 42.17  E-value: 4.83e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113860  86 YLALDLGGTNLRVCAVEVQGN----GKFDITQSkyrlpqelkvgTREALFDYIADCIKKFVEEV 145
Cdd:cd24152   2 YLVFDIGGTFIKYALVDENGNiikkGKIPTPKD-----------SLEEFLDYIKKIIKRYDEEI 54
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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