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Conserved domains on  [gi|767938343|ref|XP_011532842|]
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hexokinase-3 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASKHA_NBD_HK3_meta_rpt1 cd24090
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ...
 41-471 0e+00

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: 822.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  41 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGATGASLRVLWVTLTGIEGHRVEP 120
Cdd:cd24090    1 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGATGASLRVLWVTLTGIEGHRVEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 121 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24090   81 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 201 LLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 280
Cdd:cd24090  161 LLRDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 281 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST 360
Cdd:cd24090  241 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 361 GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCERHPRFCSVL 440
Cdd:cd24090  321 GAARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSIL 400

                        410       420       430
                 ....*....|....*....|....*....|.
gi 767938343 441 QGTVMLLAPECDVSLIPSVDGGGRGVAMVTA 471
Cdd:cd24090  401 QGTVMLLAPECDVSFIPSVDGGGRGVAMVTA 431
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 491-626 4.45e-72

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 cd24129:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 430  Bit Score: 239.02  E-value: 4.45e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 491 RLNHDQLAAVQAQMRKAMAKGLRGE---ASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTT-GVQITSEIY 566
Cdd:cd24129    1 QLSHDQLAAVQAQMRKEMAKGLRGEthaAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTaGVQITSEIY 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 567 SIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQwASLAAW 626
Cdd:cd24129   81 SIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQ-GILLNW 139
 
Name Accession Description Interval E-value
ASKHA_NBD_HK3_meta_rpt1 cd24090
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ...
 41-471 0e+00

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: 822.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  41 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGATGASLRVLWVTLTGIEGHRVEP 120
Cdd:cd24090    1 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGATGASLRVLWVTLTGIEGHRVEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 121 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24090   81 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 201 LLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 280
Cdd:cd24090  161 LLRDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 281 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST 360
Cdd:cd24090  241 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 361 GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCERHPRFCSVL 440
Cdd:cd24090  321 GAARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSIL 400

                        410       420       430
                 ....*....|....*....|....*....|.
gi 767938343 441 QGTVMLLAPECDVSLIPSVDGGGRGVAMVTA 471
Cdd:cd24090  401 QGTVMLLAPECDVSFIPSVDGGGRGVAMVTA 431
Hexokinase_1 pfam00349
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 33-230 4.12e-80

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: 251.65  E-value: 4.12e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343   33 VQECLQQFKVTRAQLQQIQASLLGSMEQALrgQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGATgaSLRVLWVTLTG 112
Cdd:pfam00349   2 LEELLKQFALSDEKLKEIVDRFVEEMEKGL--AKEGSSSLKMLPTYVTSLPTGTEKGTFLALDLGGT--NFRVCLVELGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  113 ieGHRVEPRSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQG---LQLGFSFSFPCHQTGLDRSTLISWTKGFR 189
Cdd:pfam00349  78 --DGKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDFEekeLPLGFTFSFPVEQTSLDSGTLIRWTKGFD 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767938343  190 CSGVEGQDVVQLLRDAIRRQGaYNIDVVAVVNDTVGTMMGC 230
Cdd:pfam00349 156 IPGVVGKDVVQLLQEALERRG-LPVKVVALVNDTVGTLMAG 195
ASKHA_NBD_HK3_meta_rpt2 cd24129
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ...
 491-626 4.45e-72

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: 239.02  E-value: 4.45e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 491 RLNHDQLAAVQAQMRKAMAKGLRGE---ASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTT-GVQITSEIY 566
Cdd:cd24129    1 QLSHDQLAAVQAQMRKEMAKGLRGEthaAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTaGVQITSEIY 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 567 SIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQwASLAAW 626
Cdd:cd24129   81 SIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQ-GILLNW 139
PLN02914 PLN02914
hexokinase
 72-471 3.93e-71

hexokinase


Pssm-ID: 178502 [Multi-domain]  Cd Length: 490  Bit Score: 238.25  E-value: 3.93e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  72 VRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRSQEFVIPQEVMLGAGQQLFDFAAHCLSEFL 151
Cdd:PLN02914  78 LKMILSYVDSLPSGNEKGLFYALDLG--GTNFRVLRVQLGGKDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFV 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 152 DAQ------PVNKQgLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIRRQGaYNIDVVAVVNDTVG 225
Cdd:PLN02914 156 AKEggkfhlPEGRK-REIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLNEAMERQG-LDMRVSALVNDTVG 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 226 TMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDR---GRVCVSVEWGSFSDdgalGPVLTTFDHTLDHESLNPG 302
Cdd:PLN02914 234 TLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKsssGRTIINTEWGAFSD----GLPLTEFDREMDAASINPG 309

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 303 AQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEM-EDPSTGAARVHAILQD-LGLSPGASD 380
Cdd:PLN02914 310 EQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALRTPHLCAMqQDNSDDLQAVGSILYDvLGVEASLSA 389

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 381 VELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTL--QVAVATGGRVCERHPRFCSVLQGTVM-LLAPEC--DVSL 455
Cdd:PLN02914 390 RRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDSKGMIFgkRTVVAMDGGLYEKYPQYRRYMQDAVTeLLGLELskNIAI 469

                        410
                 ....*....|....*.
gi 767938343 456 IPSVDGGGRGVAMVTA 471
Cdd:PLN02914 470 EHTKDGSGIGAALLAA 485
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 38-394 5.18e-66

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


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 222.91  E-value: 5.18e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  38 QQFKVTRAQLQQIQASLLGSMEQALRGQASpapAVRMLPTYVGSTPHGTEQGDFVVLELGATgaSLRVLWVTLTGIEGHR 117
Cdd:COG5026   13 HGFDLSSIDLEEIAAKFQEEMEKGLEGKKS---SLKMLPSYLGLPTGVKETGPVIALDAGGT--NFRVALVRFDGEGTFE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 118 VEpRSQEFVIP---QEVmlgAGQQLFDFAAHCLSEFLDaqpvnkQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVE 194
Cdd:COG5026   88 IE-NFKSFPLPgtsSEI---TAEEFFDFIADYIEPLLD------ESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 195 GQDVVQLLRDAIRRQGAYNIDVVAVVNDTVGTMMG---CEP-GVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCV 270
Cdd:COG5026  158 GKNIGELLEAALARKGLDNVKPVAILNDTVATLLAgayADPdDGYSGYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMII 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 271 SVEWGSFSddgalGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGvLFGGCTSPALLSQGSILLE 350
Cdd:COG5026  238 NMESGNFN-----KLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTV 311

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 767938343 351 HVAE-MEDPSTGAARVHAILQdlglSPGASDVELVQHVCAAVCTR 394
Cdd:COG5026  312 DMSRfLADPSDEKEILSQCLE----AGSEEDREILREIADAIVER 352
Hexokinase_1 pfam00349
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 483-626 9.24e-57

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: 190.41  E-value: 9.24e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  483 LEETLAPFRLNHDQLAAVQAQMRKAMAKGLRGE-ASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVT--TGV 559
Cdd:pfam00349   2 LEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEgSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGgdGKF 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  560 QITSEIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLS---GQSLPLGFTFSFPCRQLGLDQwASLAAW 626
Cdd:pfam00349  82 EITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEdfeEKELPLGFTFSFPVEQTSLDS-GTLIRW 150
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 490-626 1.61e-24

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


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 106.58  E-value: 1.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 490 FRLNHDQLAAVQAQMRKAMAKGLRGEASSLRMLPTFVrATPDGS-ERGDFLALDLGGTNFRVLLVRVT-TGVQITSEI-- 565
Cdd:COG5026   15 FDLSSIDLEEIAAKFQEEMEKGLEGKKSSLKMLPSYL-GLPTGVkETGPVIALDAGGTNFRVALVRFDgEGTFEIENFks 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767938343 566 YSIPETVAQGSGQQLFDHIVDCIVDfqqkqgLSGQSLPLGFTFSFPCRQLGLDQwASLAAW 626
Cdd:COG5026   94 FPLPGTSSEITAEEFFDFIADYIEP------LLDESYKLGFCFSFPAEQLPDKD-GRLIQW 147
PTZ00107 PTZ00107
hexokinase; Provisional
 480-626 7.75e-22

hexokinase; Provisional


Pssm-ID: 240270 [Multi-domain]  Cd Length: 464  Bit Score: 98.98  E-value: 7.75e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 480 RRLLEETLAPFRLNHDQLAAVQAQMRKAMAKGLRG----------EASSLRMLPTFVRATPDGSERGDFLALDLGGTNFR 549
Cdd:PTZ00107   8 RVRLASLVNQFTMSKEKLKELVDYFLYELVEGLEAhrrhrnlwipNECSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 550 VLLVRVTTG--VQITSEIYSIPETVAQG---------SGQQLFDHIVDCIVDFQQKQGL---SGQSLPLGFTFSFPCRQL 615
Cdd:PTZ00107  88 AVRVSLRGGgkMERTQSKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDpedLNKPVPVGFTFSFPCTQL 167

                        170
                 ....*....|.
gi 767938343 616 GLDQwASLAAW 626
Cdd:PTZ00107 168 SVNN-AILIDW 177
 
Name Accession Description Interval E-value
ASKHA_NBD_HK3_meta_rpt1 cd24090
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ...
 41-471 0e+00

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: 822.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  41 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGATGASLRVLWVTLTGIEGHRVEP 120
Cdd:cd24090    1 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGATGASLRVLWVTLTGIEGHRVEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 121 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24090   81 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 201 LLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 280
Cdd:cd24090  161 LLRDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 281 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST 360
Cdd:cd24090  241 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 361 GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCERHPRFCSVL 440
Cdd:cd24090  321 GAARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSIL 400

                        410       420       430
                 ....*....|....*....|....*....|.
gi 767938343 441 QGTVMLLAPECDVSLIPSVDGGGRGVAMVTA 471
Cdd:cd24090  401 QGTVMLLAPECDVSFIPSVDGGGRGVAMVTA 431
ASKHA_NBD_HK_meta cd24019
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ...
 41-471 0e+00

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: 591.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  41 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGieGHRVEP 120
Cdd:cd24019    1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLG--GTNFRVLLVTLNG--GSQVKM 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 121 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24019   77 ESEIYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 201 LLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDR---GRVCVSVEWGSF 277
Cdd:cd24019  157 LLQEAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKWDGDEgdpGQVIINTEWGAF 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 278 SDDGALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEME- 356
Cdd:cd24019  237 GDNGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIEs 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 357 DPSTGAARVHAILQDLGLSP-GASDVELVQHVCAAVCTRAAQLCAAALAAVLsclqhsREQQTLQVAVATGGRVCERHPR 435
Cdd:cd24019  317 DNEGDFSNTREILKELGLEDaSDEDCEIVRYVCEAVSTRAAQLVAAGIAALL------NRMNRKEVTVGVDGSLYKYHPK 390

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 767938343 436 FCSVLQGTVMLLAP-ECDVSLIPSVDGGGRGVAMVTA 471
Cdd:cd24019  391 FHKRMHETLKELVPpGCKFKLMLSEDGSGKGAALVAA 427
ASKHA_NBD_HK1-2_meta_rpt1 cd24089
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ...
 41-471 1.77e-177

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: 510.86  E-value: 1.77e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  41 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGIEGHRVEP 120
Cdd:cd24089    1 RLSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLG--GSNFRVLWVQVNDEKNQKVEM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 121 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24089   79 ESQVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 201 LLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 280
Cdd:cd24089  159 LLRKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDD 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 281 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST 360
Cdd:cd24089  239 GSLEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKE 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 361 GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCERHPRFCSVL 440
Cdd:cd24089  319 GLANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRL 398

                        410       420       430
                 ....*....|....*....|....*....|.
gi 767938343 441 QGTVMLLAPECDVSLIPSVDGGGRGVAMVTA 471
Cdd:cd24089  399 HKAVRRLVPDCDVRFLLSEDGSGKGAAMVTA 429
ASKHA_NBD_HKDC1_meta_rpt1 cd24126
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ...
 46-471 1.33e-150

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: 441.98  E-value: 1.33e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  46 QLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRSQEF 125
Cdd:cd24126    6 TLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLG--GSKFRVLRVKVSEDGKQKVQMESQFY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 126 VIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDA 205
Cdd:cd24126   84 PTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSLRKA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 206 IRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDDGALGP 285
Cdd:cd24126  164 IRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGSLED 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 286 VLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPSTGAARV 365
Cdd:cd24126  244 IRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGLYNT 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 366 HAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCERHPRFCSVLQGTVM 445
Cdd:cd24126  324 REILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHKVVR 403

                        410       420
                 ....*....|....*....|....*.
gi 767938343 446 LLAPECDVSLIPSVDGGGRGVAMVTA 471
Cdd:cd24126  404 RLVPSCDVRFLLSESGSGKGAAMVTA 429
ASKHA_NBD_HK2_meta_rpt1 cd24125
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ...
 41-471 5.22e-150

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: 440.48  E-value: 5.22e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  41 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGIEGHRVEP 120
Cdd:cd24125    1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLG--GTNFRVLWVKVSDNGLQKVEM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 121 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24125   79 ENQIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 201 LLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 280
Cdd:cd24125  159 LLRKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDD 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 281 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST 360
Cdd:cd24125  239 GSLDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKD 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 361 GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCERHPRFCSVL 440
Cdd:cd24125  319 GIRKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRL 398

                        410       420       430
                 ....*....|....*....|....*....|.
gi 767938343 441 QGTVMLLAPECDVSLIPSVDGGGRGVAMVTA 471
Cdd:cd24125  399 HKTVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
ASKHA_NBD_HK1-3_meta_rpt2 cd24091
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ...
 41-475 1.27e-147

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: 434.67  E-value: 1.27e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  41 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGIEGHRVEP 120
Cdd:cd24091    1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLG--GTNFRVLLVKVRSGKWRGVEM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 121 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24091   79 HNKIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 201 LLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 280
Cdd:cd24091  159 LLREAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDN 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 281 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST 360
Cdd:cd24091  239 GCLDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRL 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 361 GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCERHPRFCSVL 440
Cdd:cd24091  319 ALLQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVM 398

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 767938343 441 QGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAAR 475
Cdd:cd24091  399 HETVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
ASKHA_NBD_HK1_meta_rpt1 cd24124
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ...
 28-487 3.15e-143

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: 424.80  E-value: 3.15e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  28 DSSELVQECLQQFKVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLW 107
Cdd:cd24124   16 DQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLG--GSSFRILR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 108 VTLTGIEGHRVEPRSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKG 187
Cdd:cd24124   94 VQVNHEKNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKR 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 188 FRCSGVEGQDVVQLLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGR 267
Cdd:cd24124  174 FKASGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGR 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 268 VCVSVEWGSFSDDGALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSI 347
Cdd:cd24124  254 MCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKF 333

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 348 LLEHVAEMEDPSTGAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGG 427
Cdd:cd24124  334 NTSDVSAIEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDG 413

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 428 RVCERHPRFCSVLQGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAARLAAHRRLLEETL 487
Cdd:cd24124  414 SLYKTHPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETL 473
ASKHA_NBD_HK3_meta_rpt2 cd24129
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ...
 41-475 5.74e-141

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: 417.36  E-value: 5.74e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  41 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLtGIEGHRVEp 120
Cdd:cd24129    1 QLSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLG--GTNFRVLLVHV-GTAGVQIT- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 121 rSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24129   77 -SEIYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 201 LLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 280
Cdd:cd24129  156 LLREAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDN 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 281 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST 360
Cdd:cd24129  236 GCLAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSL 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 361 GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCERHPRFCSVL 440
Cdd:cd24129  316 ALRQVRAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLV 395

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 767938343 441 QGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAAR 475
Cdd:cd24129  396 QATVRELAPRCVVTFLQSEDGSGKGAALVTAVACR 430
ASKHA_NBD_HK2_meta_rpt2 cd24128
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ...
 41-476 1.14e-135

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: 404.28  E-value: 1.14e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  41 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGIEGHRVEP 120
Cdd:cd24128    1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLG--GTNFRVLLVRVRNGKWRGVEM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 121 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24128   79 HNKIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 201 LLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 280
Cdd:cd24128  159 LLKEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDN 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 281 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST 360
Cdd:cd24128  239 GCLDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRL 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 361 GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCERHPRFCSVL 440
Cdd:cd24128  319 ALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVM 398

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 767938343 441 QGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAARL 476
Cdd:cd24128  399 HETVKDLAPKCDVSFLQSEDGSGKGAALITAVACRI 434
ASKHA_NBD_HK1_meta_rpt2 cd24127
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ...
 41-476 6.08e-134

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: 399.67  E-value: 6.08e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  41 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGIEGHRVEP 120
Cdd:cd24127    1 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLG--GTNFRVLLVKIRSGKKRTVEM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 121 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24127   79 HNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 201 LLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 280
Cdd:cd24127  159 LLRDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDN 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 281 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST 360
Cdd:cd24127  239 GCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRL 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 361 GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCERHPRFCSVL 440
Cdd:cd24127  319 ALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIM 398

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 767938343 441 QGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAARL 476
Cdd:cd24127  399 HQTVKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 434
ASKHA_NBD_HKDC1_meta_rpt2 cd24130
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ...
 41-476 3.47e-130

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: 390.06  E-value: 3.47e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  41 KVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGIEgHRVEP 120
Cdd:cd24130    1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLG--GTNFRVLLVKIRSGR-RSVRM 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 121 RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24130   78 YNKIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 201 LLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDD 280
Cdd:cd24130  158 MLREAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDN 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 281 GALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST 360
Cdd:cd24130  238 GCIDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRL 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 361 GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCERHPRFCSVL 440
Cdd:cd24130  318 ALLQVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRIL 397

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 767938343 441 QGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAARL 476
Cdd:cd24130  398 QETVKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 433
ASKHA_NBD_HK4_meta cd24092
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ...
 33-475 7.00e-128

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: 384.62  E-value: 7.00e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  33 VQECLQQFKVTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTL-T 111
Cdd:cd24092    2 VEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLG--GTNFRVMLVKVgE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 112 GIEGH-RVEPRSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRC 190
Cdd:cd24092   80 GEEGQwSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 191 SGVEGQDVVQLLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCV 270
Cdd:cd24092  160 SGAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 271 SVEWGSFSDDGALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLE 350
Cdd:cd24092  240 NTEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETR 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 351 HVAEMEDPSTGAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQVAVATGGRVC 430
Cdd:cd24092  320 FVSQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVY 399

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 767938343 431 ERHPRFCSVLQGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAAR 475
Cdd:cd24092  400 KLHPSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 444
ASKHA_NBD_HK_fungi cd24018
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ...
 45-469 1.57e-118

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: 360.03  E-value: 1.57e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  45 AQLQQIQASLLGSMEQALRGQASpapAVRMLPTYVGSTPHGTEQGDFVVLELGATgaSLRVLWVTLTGiEGHRVEPRSQE 124
Cdd:cd24018    2 SKLEEIVKHFLSEMEKGLEGDGG---SLPMLPSFVTERPTGKETGTYLALDLGGT--NLRVCLVTLDG-NGGIFIIVQRK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 125 FVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPV---NKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQL 201
Cdd:cd24018   76 YKIPDEAKTGTGEELFDFIAECIAEFLEEHNLdlqSDKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVEL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 202 LRDAIRRQGaYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLD------EDRGRVCVSVEWG 275
Cdd:cd24018  156 LQNALDRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTspsgsvTKSDEMIINTEWG 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 276 SFSDDGALGPvLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEM 355
Cdd:cd24018  235 AFDNEREVLP-LTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRI 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 356 E-DPSTGAARVHAILQDLGLSPGAS--DVELVQHVCAAVCTRaaqLCAAALAAVLSCLQHSREQQTLQVAVATGGRVCER 432
Cdd:cd24018  314 EaDTSPDLDAVRDILKELLAIDNTTleDRKLIKRICELVSTR---AARLSAAAIAAILLKRGSLLPEPVTVGIDGSVYEK 390

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 767938343 433 HPRFCSVLQGTV-MLLAPEC--DVSLIPSVDGGGRGVAMV 469
Cdd:cd24018  391 YPGFKDRLSEALrELFGPEVkaNISLVLAKDGSGLGAAII 430
ASKHA_NBD_HK_plant cd24020
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 45-478 4.67e-92

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: 291.49  E-value: 4.67e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  45 AQLQQIQASLLGSMEQALRgqASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRSQE 124
Cdd:cd24020    4 SRLRQVADAMVVEMEAGLA--SEGGSKLKMLPSYVDNLPSGDEKGLFYALDLG--GTNFRVLRVQLGGKEGRVDKQEYEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 125 FVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQG----LQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24020   80 VPIPPELMVGTSEELFDFIAGELAKFVATEGEGFHPegekRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 201 LLRDAIRRQGaYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGR---VCVSVEWGSF 277
Cdd:cd24020  160 LLEEALERQG-LDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGLPRsgeMVINTEWGNF 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 278 sdDGALGPvLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEM-E 356
Cdd:cd24020  239 --RSSHLP-RTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMhE 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 357 DPSTGAARVHAILQDLGLSPGAS--DVELVQHVCAAVCTRAAQLCAAALAAVLSCLQH--SREQQTLQVAVATGGRVCER 432
Cdd:cd24020  316 DDSPDLETVARILKDALGIDDTSleARKVVVEVCDLVAERGARLAAAGIVGILKKLGRdgGGSSPAQRTVVAVDGGLYEH 395

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 767938343 433 HPRFCSVLQGTVM-LLAPEC--DVSLIPSVDGGGRGvamvtavAARLAA 478
Cdd:cd24020  396 YPKFREYMQQALVeLLGDEAadSVELELSNDGSGIG-------AALLAA 437
ASKHA_NBD_HK cd24000
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 44-470 3.25e-91

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: 286.48  E-value: 3.25e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  44 RAQLQQIQASLLGSMEQALRGQASPapaVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGieGHRVEPRSQ 123
Cdd:cd24000    1 DEDLKEITDAFLEELEKGLAGEPSS---LKMLPSYVSPLPTGLESGEFLAIDLG--GTNLRVALVSLDG--KGIEVTISK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 124 EFVIPQEVMLGAGQQLFDFAAHCLSEFLDaQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLR 203
Cdd:cd24000   74 KYEIPDEIKTASAEEFFDFIADCIAEFLK-ENGLKKPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLN 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 204 DAIRRQGaYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVavlDEDRGRVCVSVEWGSFSDDGAl 283
Cdd:cd24000  153 DALKKRG-LPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNI---LLGDGGMIINTEWGNFGKNSL- 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 284 gpVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARcgvlfggctspallsqgsILLEHVAEMedPSTGAA 363
Cdd:cd24000  228 --PRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLAD------------------EILRKICEL--VAERSA 285

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 364 RVHAILqdlglspgasdvelvqhvCAAVCtraaqlcaaalaavlsclQHSREQQTLQVAVATGGRVCERHPRFCSVLQGT 443
Cdd:cd24000  286 RLAAAA------------------IAALL------------------RKTGDSPEKKITIAVDGSLFEKYPGYRERLEEY 329

                        410       420
                 ....*....|....*....|....*...
gi 767938343 444 V-MLLAPECDVSLIPSVDGGGRGVAMVT 470
Cdd:cd24000  330 LkELLGRGIRIELVLVEDGSLIGAALAA 357
Hexokinase_1 pfam00349
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 33-230 4.12e-80

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: 251.65  E-value: 4.12e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343   33 VQECLQQFKVTRAQLQQIQASLLGSMEQALrgQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGATgaSLRVLWVTLTG 112
Cdd:pfam00349   2 LEELLKQFALSDEKLKEIVDRFVEEMEKGL--AKEGSSSLKMLPTYVTSLPTGTEKGTFLALDLGGT--NFRVCLVELGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  113 ieGHRVEPRSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQG---LQLGFSFSFPCHQTGLDRSTLISWTKGFR 189
Cdd:pfam00349  78 --DGKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDFEekeLPLGFTFSFPVEQTSLDSGTLIRWTKGFD 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767938343  190 CSGVEGQDVVQLLRDAIRRQGaYNIDVVAVVNDTVGTMMGC 230
Cdd:pfam00349 156 IPGVVGKDVVQLLQEALERRG-LPVKVVALVNDTVGTLMAG 195
ASKHA_NBD_GLK1-2_fungi cd24088
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ...
 45-469 1.52e-78

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: 256.55  E-value: 1.52e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  45 AQLQQIQASLLGSMEQALrgqASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGATgaSLRVLWVTLTGieGHRVEPRSQE 124
Cdd:cd24088    2 EKLDKLTAEFQRQMEKGL---AKHGKGMAMIPTYVTGVPDGTETGTYLALDLGGT--NFRVCSVELHG--DGTFSLRQEK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 125 FVIPQEVMLGA-GQQLFDFAAHCLSEFL-----DAQPVNKQG--LQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQ 196
Cdd:cd24088   75 SKIPDELKTGVtAKDLFDYLAKSVEAFLtkhhgDSFAAGKDDdrLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 197 DVVQLLRDAIRRQGAyNIDVVAVVNDTVGTMMG---CEPGVRPCEVGLVVDTGTNACYMEEARHVAVLD------EDRGR 267
Cdd:cd24088  155 DVVKLLQDELDRQGI-PVKVVALVNDTVGTLLArsyTSPEISGAVLGAIFGTGTNGAYLEDLEKIKKLDdssrvgKGKTH 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 268 VCVSVEWGSFSDDGALGPVlTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCT--SPALLSQG 345
Cdd:cd24088  234 MVINTEWGSFDNELKVLPT-TPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFLIQYNdkSPSALNTP 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 346 SIL----LEHVAEMEDPSTGAARvHAILQDLGL-SPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQ 420
Cdd:cd24088  313 YGLdtavLSAIEIDSEAELRATR-KVLLDDLGLpAPSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSYDGE 391

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767938343 421 VAVATGGRVCERHPRFCSVLQGTVMLLAP----ECDVSLIPSVDGGGRGVAMV 469
Cdd:cd24088  392 INIGVDGSVIEFYPGFESMLREALRLLLIgaegEKRIKIGIAKDGSGVGAALC 444
ASKHA_NBD_HK3_meta_rpt2 cd24129
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ...
 491-626 4.45e-72

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: 239.02  E-value: 4.45e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 491 RLNHDQLAAVQAQMRKAMAKGLRGE---ASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTT-GVQITSEIY 566
Cdd:cd24129    1 QLSHDQLAAVQAQMRKEMAKGLRGEthaAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTaGVQITSEIY 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 567 SIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQwASLAAW 626
Cdd:cd24129   81 SIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQ-GILLNW 139
PLN02914 PLN02914
hexokinase
 72-471 3.93e-71

hexokinase


Pssm-ID: 178502 [Multi-domain]  Cd Length: 490  Bit Score: 238.25  E-value: 3.93e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  72 VRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRSQEFVIPQEVMLGAGQQLFDFAAHCLSEFL 151
Cdd:PLN02914  78 LKMILSYVDSLPSGNEKGLFYALDLG--GTNFRVLRVQLGGKDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFV 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 152 DAQ------PVNKQgLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIRRQGaYNIDVVAVVNDTVG 225
Cdd:PLN02914 156 AKEggkfhlPEGRK-REIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLNEAMERQG-LDMRVSALVNDTVG 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 226 TMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDR---GRVCVSVEWGSFSDdgalGPVLTTFDHTLDHESLNPG 302
Cdd:PLN02914 234 TLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKsssGRTIINTEWGAFSD----GLPLTEFDREMDAASINPG 309

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 303 AQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEM-EDPSTGAARVHAILQD-LGLSPGASD 380
Cdd:PLN02914 310 EQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALRTPHLCAMqQDNSDDLQAVGSILYDvLGVEASLSA 389

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 381 VELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTL--QVAVATGGRVCERHPRFCSVLQGTVM-LLAPEC--DVSL 455
Cdd:PLN02914 390 RRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDSKGMIFgkRTVVAMDGGLYEKYPQYRRYMQDAVTeLLGLELskNIAI 469

                        410
                 ....*....|....*.
gi 767938343 456 IPSVDGGGRGVAMVTA 471
Cdd:PLN02914 470 EHTKDGSGIGAALLAA 485
ASKHA_NBD_HK1-3_meta_rpt2 cd24091
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ...
 491-626 1.27e-69

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: 232.44  E-value: 1.27e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 491 RLNHDQLAAVQAQMRKAMAKGLRGEA---SSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTG----VQITS 563
Cdd:cd24091    1 QLSHDQLLEVKARMRAEMERGLRKEThasAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGkwrgVEMHN 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767938343 564 EIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQwASLAAW 626
Cdd:cd24091   81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDE-GILLKW 142
PTZ00107 PTZ00107
hexokinase; Provisional
 39-474 3.40e-69

hexokinase; Provisional


Pssm-ID: 240270 [Multi-domain]  Cd Length: 464  Bit Score: 232.26  E-value: 3.40e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  39 QFKVTRAQLQQIQASLLGSMEQALRGQASPAPA-------VRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLt 111
Cdd:PTZ00107  17 QFTMSKEKLKELVDYFLYELVEGLEAHRRHRNLwipnecsFKMLDSCVYNLPTGKEKGVYYAIDFG--GTNFRAVRVSL- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 112 giEGHRVEPRSQE-FVIPQEVMLGA---------GQQLFDFAAHCLSEFLD--AQPVN-KQGLQLGFSFSFPCHQTGLDR 178
Cdd:PTZ00107  94 --RGGGKMERTQSkFSLPKSALLGEkglldkkatATDLFDHIAKSIKKMMEenGDPEDlNKPVPVGFTFSFPCTQLSVNN 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 179 STLISWTKGFRCS-----GVEGQDVVQLLRDAIRRQGAyNIDVVAVVNDTVGTMMGC----EPGVRPCEVGLVVDTGTNA 249
Cdd:PTZ00107 172 AILIDWTKGFETGratndPVEGKDVGELLNDAFKRNNV-PANVVAVLNDTVGTLISCayqkPKNTPPCQVGVIIGTGSNA 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 250 CYME-EARHvavldedRGR--VCVSVEWGSFSDDgaLgPVlTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHL 326
Cdd:PTZ00107 251 CYFEpEVSA-------YGYagTPINMECGNFDSK--L-PI-TPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHL 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 327 ARCGvlfggcTSPALLSQGSILLEHVAEM-EDPSTGAARVHAILQDL-GLSPGASDVELVQHVCAAVCTRAAQLCAAALA 404
Cdd:PTZ00107 320 LQLK------APPKMWQSGSFESEDASMIlNDQSPDLQFSRQVIKEAwDVDLTDEDLYTIRKICELVRGRAAQLAAAFIA 393

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767938343 405 AVLSCLQHSREQQTlqvaVATGGRVCERHPRFCSVLQGTV-MLLAPE-CDVSLIPSVDGGGRGVAMVTAVAA 474
Cdd:PTZ00107 394 APAKKTRTVQGKAT----VAIDGSVYVKNPWFRRLLQEYInSILGPDaGNVVFYLADDGSGKGAAIIAAMVA 461
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 38-394 5.18e-66

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


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 222.91  E-value: 5.18e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  38 QQFKVTRAQLQQIQASLLGSMEQALRGQASpapAVRMLPTYVGSTPHGTEQGDFVVLELGATgaSLRVLWVTLTGIEGHR 117
Cdd:COG5026   13 HGFDLSSIDLEEIAAKFQEEMEKGLEGKKS---SLKMLPSYLGLPTGVKETGPVIALDAGGT--NFRVALVRFDGEGTFE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 118 VEpRSQEFVIP---QEVmlgAGQQLFDFAAHCLSEFLDaqpvnkQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVE 194
Cdd:COG5026   88 IE-NFKSFPLPgtsSEI---TAEEFFDFIADYIEPLLD------ESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 195 GQDVVQLLRDAIRRQGAYNIDVVAVVNDTVGTMMG---CEP-GVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCV 270
Cdd:COG5026  158 GKNIGELLEAALARKGLDNVKPVAILNDTVATLLAgayADPdDGYSGYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMII 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 271 SVEWGSFSddgalGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGvLFGGCTSPALLSQGSILLE 350
Cdd:COG5026  238 NMESGNFN-----KLPRTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTV 311

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 767938343 351 HVAE-MEDPSTGAARVHAILQdlglSPGASDVELVQHVCAAVCTR 394
Cdd:COG5026  312 DMSRfLADPSDEKEILSQCLE----AGSEEDREILREIADAIVER 352
ASKHA_NBD_HK1-2_fungi cd24087
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ...
 45-335 7.06e-66

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: 222.64  E-value: 7.06e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  45 AQLQQIQASLLGSMEQAL--RGQASPapavrMLPTYVGSTPHGTEQGDFVVLELGATgaSLRVLWVTLTGieGHRVEPRS 122
Cdd:cd24087    2 ERLRKITDHFISELEKGLskKGGNIP-----MIPTWVMGFPTGKETGDYLALDLGGT--NLRVCLVKLGG--NGKFDITQ 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 123 QEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVN--KQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQ 200
Cdd:cd24087   73 SKYRLPEELKTGTGEELWDFIADCLKKFVEEHFPGgkSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVP 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 201 LLRDAIRRQGAyNIDVVAVVNDTVGTMMG---CEPGVrpcEVGLVVDTGTNACYMEEARHVAVLDED----RGRVCVSVE 273
Cdd:cd24087  153 MLQKALKKRNV-PIELVALINDTTGTLIAsnyTDPET---KIGVIFGTGCNAAYMEVVSNIPKLEHDdippDSPMAINCE 228

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767938343 274 WGSFsDDGALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGG 335
Cdd:cd24087  229 YGAF-DNEHLVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKG 289
Hexokinase_2 pfam03727
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 238-472 1.98e-63

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: 209.66  E-value: 1.98e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  238 EVGLVVDTGTNACYMEEARHVAVLDEDR---GRVCVSVEWGSFSDDGALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLY 314
Cdd:pfam03727   1 RIGLILGTGTNAAYVEKVSNIPKLEGKLpksGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  315 LGELVRLVLAHLARCGVLFGGcTSPALLSQGSILLEHVAEME-DPSTGAARVHAILQD-LGLSPGAS-DVELVQHVCAAV 391
Cdd:pfam03727  81 LGELVRLVLLDLAEEGLLFKG-QSEKLKTPYSLDTSFLSAIEsDPSEDLETTREILEElLGIETVTEeDRKIVRRICEAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  392 CTRaaqlcaaalaavlsclqhS-------------REQQTLQVAVATGGRVCERHPRFCSVLQGTV-MLLAPECDVSLIP 457
Cdd:pfam03727 160 STR------------------AarlvaagiaailkKIGRDKKVTVGVDGSVYEKYPGFRERLQEALrELLGPGDKVVLVL 221

                         250
                  ....*....|....*
gi 767938343  458 SVDGGGRGVAMVTAV 472
Cdd:pfam03727 222 AEDGSGVGAALIAAV 236
ASKHA_NBD_HK_meta cd24019
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ...
 491-626 5.27e-63

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: 214.71  E-value: 5.27e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 491 RLNHDQLAAVQAQMRKAMAKGLRGE---ASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTG--VQITSEI 565
Cdd:cd24019    1 RLSDEQLEEIMDRLLKEMEKGLSKDthpTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGGsqVKMESEI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767938343 566 YSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQwASLAAW 626
Cdd:cd24019   81 YAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDS-ATLVRW 140
Hexokinase_1 pfam00349
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 483-626 9.24e-57

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: 190.41  E-value: 9.24e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  483 LEETLAPFRLNHDQLAAVQAQMRKAMAKGLRGE-ASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVT--TGV 559
Cdd:pfam00349   2 LEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEgSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGgdGKF 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  560 QITSEIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLS---GQSLPLGFTFSFPCRQLGLDQwASLAAW 626
Cdd:pfam00349  82 EITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEdfeEKELPLGFTFSFPVEQTSLDS-GTLIRW 150
PLN02405 PLN02405
hexokinase
 45-471 1.51e-55

hexokinase


Pssm-ID: 215226 [Multi-domain]  Cd Length: 497  Bit Score: 196.59  E-value: 1.51e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  45 AQLQQIQASLLGSMEQALRGQAspAPAVRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRSQE 124
Cdd:PLN02405  53 GKLRQVADAMTVEMHAGLASEG--GSKLKMLISYVDNLPSGDEKGLFYALDLG--GTNFRVLRVLLGGKDGRVVKQEFEE 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 125 FVIPQEVMLGAGQQLFDFAAHCLSEFL-----DAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVV 199
Cdd:PLN02405 129 VSIPPHLMTGSSDALFDFIAAALAKFVategeDFHLPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVV 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 200 QLLRDAIRRQGAyNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAV---LDEDRGRVCVSVEWGS 276
Cdd:PLN02405 209 GELTKAMERVGL-DMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKwhgLLPKSGEMVINMEWGN 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 277 FSDDGAlgpVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEM- 355
Cdd:PLN02405 288 FRSSHL---PLTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMh 364

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 356 EDPSTGAARVHAILQDLGLSPGAS--DVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHS--REQQTLQVAVATGGRVCE 431
Cdd:PLN02405 365 HDTSPDLKVVGSKLKDILEIPNTSlkMRKVVVELCNIVATRGARLSAAGIYGILKKLGRDtvKDGEKQKSVIAMDGGLFE 444

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 767938343 432 RHPRFCSVLQGTVM-LLAPEC--DVSLIPSVDGGGRGVAMVTA 471
Cdd:PLN02405 445 HYTEFSKCMESTLKeLLGEEVseSIEVEHSNDGSGIGAALLAA 487
ASKHA_NBD_HK1-2_meta_rpt1 cd24089
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ...
 491-626 1.22e-50

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: 181.51  E-value: 1.22e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 491 RLNHDQLAAVQAQMRKAMAKGLRGEA---SSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTG----VQITS 563
Cdd:cd24089    1 RLSDETLLDISRRFRKEMEKGLGKDThptATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEknqkVEMES 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767938343 564 EIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQwASLAAW 626
Cdd:cd24089   81 QVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDE-SILISW 142
ASKHA_NBD_HK2_meta_rpt2 cd24128
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ...
 491-619 2.24e-50

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: 180.87  E-value: 2.24e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 491 RLNHDQLAAVQAQMRKAMAKGLRGE---ASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTG----VQITS 563
Cdd:cd24128    1 QLSHDQLLEVKRRMKVEMERGLSKEthaSAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGkwrgVEMHN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767938343 564 EIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQ 619
Cdd:cd24128   81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDE 136
ASKHA_NBD_HKDC1_meta_rpt1 cd24126
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ...
 491-626 9.25e-48

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: 173.50  E-value: 9.25e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 491 RLNHDQLAAVQAQMRKAMAKGLRGEASS---LRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTT----GVQITS 563
Cdd:cd24126    1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPtaaVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEdgkqKVQMES 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767938343 564 EIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQwASLAAW 626
Cdd:cd24126   81 QFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDE-GVLISW 142
ASKHA_NBD_HK1_meta_rpt2 cd24127
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ...
 491-618 3.82e-47

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: 172.02  E-value: 3.82e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 491 RLNHDQLAAVQAQMRKAMAKGLRG---EASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTG----VQITS 563
Cdd:cd24127    1 HLTKDMLLEVKKRMRAEMELGLRKqthNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGkkrtVEMHN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767938343 564 EIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLD 618
Cdd:cd24127   81 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLD 135
PLN02362 PLN02362
hexokinase
 72-394 1.58e-46

hexokinase


Pssm-ID: 215206 [Multi-domain]  Cd Length: 509  Bit Score: 171.99  E-value: 1.58e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  72 VRMLPTYVGSTPHGTEQGDFVVLELGatGASLRVLWVTLTG----IEGHRVEPRSqefvIPQEVMLGAGQQLFDFAAHCL 147
Cdd:PLN02362  78 LKMLLTFVDDLPTGSEIGTYYALDLG--GTNFRVLRVQLGGqrssILSQDVERHP----IPQHLMNSTSEVLFDFIASSL 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 148 SEFL-----DAQPVNKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSGVEGQDVVQLLRDAIRRQGaYNIDVVAVVND 222
Cdd:PLN02362 152 KQFVekeenGSEFSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRRG-LDMRVAALVND 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 223 TVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAV---LDEDRGRVCVSVEWGSFSDDGAlgpVLTTFDHTLDHESL 299
Cdd:PLN02362 231 TVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKcqgLLTTSGSMVVNMEWGNFWSSHL---PRTSYDIDLDAESP 307

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 300 NPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTS----PALLSQGSILLEHvaemEDPSTGAARVHAILQD-LGL 374
Cdd:PLN02362 308 NPNDQGFEKMISGMYLGDIVRRVILRMSQESDIFGPVSSrlstPFVLRTPSVAAMH----EDDSPELQEVARILKEtLGI 383

                        330       340
                 ....*....|....*....|.
gi 767938343 375 SPGASDV-ELVQHVCAAVCTR 394
Cdd:PLN02362 384 SEVPLKVrKLVVKICDVVTRR 404
ASKHA_NBD_HKDC1_meta_rpt2 cd24130
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ...
 491-626 4.60e-46

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: 168.96  E-value: 4.60e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 491 RLNHDQLAAVQAQMRKAMAKGLRGEA---SSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTG---VQITSE 564
Cdd:cd24130    1 QLTRDQLQEVKQKMRTELEYGLKKEThptASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGrrsVRMYNK 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767938343 565 IYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQwASLAAW 626
Cdd:cd24130   81 IFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDK-GTLVGW 141
ASKHA_NBD_HK2_meta_rpt1 cd24125
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ...
 491-626 4.32e-45

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: 166.22  E-value: 4.32e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 491 RLNHDQLAAVQAQMRKAMAKGLRGEA---SSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTG----VQITS 563
Cdd:cd24125    1 RLSDETLLEISKRFRKEMEKGLGATThptAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNglqkVEMEN 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767938343 564 EIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQwASLAAW 626
Cdd:cd24125   81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDE-SFLVSW 142
ASKHA_NBD_HK1_meta_rpt1 cd24124
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ...
 483-626 1.63e-43

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: 162.86  E-value: 1.63e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 483 LEETLAPFRLNHDQLAAVQAQMRKAMAKGLRGE---ASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVT--- 556
Cdd:cd24124   21 IDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDfnpTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNhek 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767938343 557 -TGVQITSEIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQwASLAAW 626
Cdd:cd24124  101 nQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDE-AILITW 170
ASKHA_NBD_HK4_meta cd24092
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ...
 483-619 7.14e-41

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: 154.65  E-value: 7.14e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 483 LEETLAPFRLNHDQLAAVQAQMRKAMAKGLR---GEASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTG- 558
Cdd:cd24092    2 VEQILAEFQLQEEDLKKVMRRMQKEMDRGLRletHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGe 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767938343 559 -----VQITSEIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQ 619
Cdd:cd24092   82 egqwsVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDK 147
ASKHA_NBD_HK_fungi cd24018
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ...
 495-619 4.99e-39

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: 148.94  E-value: 4.99e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 495 DQLAAVQAQMRKAMAKGLRGEASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRV---TTGVQITSEIYSIPET 571
Cdd:cd24018    2 SKLEEIVKHFLSEMEKGLEGDGGSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLdgnGGIFIIVQRKYKIPDE 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767938343 572 VAQGSGQQLFDHIVDCIVDFQQKQGLSGQS---LPLGFTFSFPCRQLGLDQ 619
Cdd:cd24018   82 AKTGTGEELFDFIAECIAEFLEEHNLDLQSdktIPLGFTFSFPVQQTSIDS 132
PLN02596 PLN02596
hexokinase-like
 46-394 1.34e-37

hexokinase-like


Pssm-ID: 178206 [Multi-domain]  Cd Length: 490  Bit Score: 146.17  E-value: 1.34e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343  46 QLQQIQASLLGSMEQALRGQASPApaVRMLPTYVGSTPHGTEQGDFVVLELgaTGASLRVLWVTLTGIEGHRVEPRSQEF 125
Cdd:PLN02596  55 KLWEVADALVSDMTASLTAEETTT--LNMLVSYVASLPSGDEKGLYYGLNL--RGSNFLLLRARLGGKNEPISDLYREEI 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 126 VIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNK-----QGLQLGFSFSFPCHQTGLDRSTLISWtKGFRCSGVEGQDVVQ 200
Cdd:PLN02596 131 SIPSNVLNGTSQELFDYIALELAKFVAEHPGDEadtpeRVKKLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVN 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 201 LLRDAIRRQGAyNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDE---DRGRVCVSVEWGSF 277
Cdd:PLN02596 210 DINRALEKHGL-KIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSpspESQEIVISTEWGNF 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 278 SddgALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEM-E 356
Cdd:PLN02596 289 N---SCHLPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAAMhQ 365

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 767938343 357 DPSTGAARVHAILQD-LGL---SPGASdvELVQHVCAAVCTR 394
Cdd:PLN02596 366 DTSEDHEVVNEKLKEiFGItdsTPMAR--EVVAEVCDIVAER 405
ASKHA_NBD_HK cd24000
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 494-618 9.59e-37

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: 140.87  E-value: 9.59e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 494 HDQLAAVQAQMRKAMAKGLRGEASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTG--VQITSEIYSIPET 571
Cdd:cd24000    1 DEDLKEITDAFLEELEKGLAGEPSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGKgiEVTISKKYEIPDE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767938343 572 VAQGSGQQLFDHIVDCIVDFQQKQGLSgQSLPLGFTFSFPCRQLGLD 618
Cdd:cd24000   81 IKTASAEEFFDFIADCIAEFLKENGLK-KPLPLGFTFSFPLEQTSLN 126
ASKHA_NBD_HK3_meta_rpt1 cd24090
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ...
 496-626 2.01e-30

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: 124.26  E-value: 2.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 496 QLAAVQAQMRKAMAKGLRGE---ASSLRMLPTFVRATPDGSERGDFLALDLG--GTNFRVLLVRVTT----GVQITSEIY 566
Cdd:cd24090    6 QLQQIQASLLGSMEQALRGQaspAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGieghRVEPRSQEF 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 567 SIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQwASLAAW 626
Cdd:cd24090   86 VIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDR-STLISW 144
ASKHA_NBD_HK1-2_fungi cd24087
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ...
 510-626 1.31e-28

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: 119.02  E-value: 1.31e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 510 KGLRGEASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTG--VQITSEIYSIPETVAQGSGQQLFDHIVDC 587
Cdd:cd24087   17 KGLSKKGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNgkFDITQSKYRLPEELKTGTGEELWDFIADC 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767938343 588 IVDF---QQKQGLSGQsLPLGFTFSFPCRQLGLDQwASLAAW 626
Cdd:cd24087   97 LKKFveeHFPGGKSEP-LPLGFTFSYPASQDKINH-GILQRW 136
ASKHA_NBD_HK_plant cd24020
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 495-618 7.88e-28

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: 116.61  E-value: 7.88e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 495 DQLAAVQAQMRKAMAKGLRGEA-SSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLlvRVTTG-----VQIT-SEIYS 567
Cdd:cd24020    4 SRLRQVADAMVVEMEAGLASEGgSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVL--RVQLGgkegrVDKQeYEEVP 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767938343 568 IPETVAQGSGQQLFDHIVDCIVDFQQKQG----LSGQSLPLGFTFSFPCRQLGLD 618
Cdd:cd24020   82 IPPELMVGTSEELFDFIAGELAKFVATEGegfhPEGEKRELGFTFSFPVKQTSID 136
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 490-626 1.61e-24

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


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 106.58  E-value: 1.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 490 FRLNHDQLAAVQAQMRKAMAKGLRGEASSLRMLPTFVrATPDGS-ERGDFLALDLGGTNFRVLLVRVT-TGVQITSEI-- 565
Cdd:COG5026   15 FDLSSIDLEEIAAKFQEEMEKGLEGKKSSLKMLPSYL-GLPTGVkETGPVIALDAGGTNFRVALVRFDgEGTFEIENFks 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767938343 566 YSIPETVAQGSGQQLFDHIVDCIVDfqqkqgLSGQSLPLGFTFSFPCRQLGLDQwASLAAW 626
Cdd:COG5026   94 FPLPGTSSEITAEEFFDFIADYIEP------LLDESYKLGFCFSFPAEQLPDKD-GRLIQW 147
ASKHA_NBD_GLK1-2_fungi cd24088
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ...
 496-618 5.42e-23

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: 102.47  E-value: 5.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 496 QLAAVQAQMRKAMAKGLRGEASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVT--TGVQITSEIYSIPETVA 573
Cdd:cd24088    3 KLDKLTAEFQRQMEKGLAKHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELHgdGTFSLRQEKSKIPDELK 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767938343 574 QG-SGQQLFDHIVDCIVDFQQK-------QGLSGQSLPLGFTFSFPCRQLGLD 618
Cdd:cd24088   83 TGvTAKDLFDYLAKSVEAFLTKhhgdsfaAGKDDDRLKLGFTFSFPVDQTAIN 135
PTZ00107 PTZ00107
hexokinase; Provisional
 480-626 7.75e-22

hexokinase; Provisional


Pssm-ID: 240270 [Multi-domain]  Cd Length: 464  Bit Score: 98.98  E-value: 7.75e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 480 RRLLEETLAPFRLNHDQLAAVQAQMRKAMAKGLRG----------EASSLRMLPTFVRATPDGSERGDFLALDLGGTNFR 549
Cdd:PTZ00107   8 RVRLASLVNQFTMSKEKLKELVDYFLYELVEGLEAhrrhrnlwipNECSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 550 VLLVRVTTG--VQITSEIYSIPETVAQG---------SGQQLFDHIVDCIVDFQQKQGL---SGQSLPLGFTFSFPCRQL 615
Cdd:PTZ00107  88 AVRVSLRGGgkMERTQSKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDpedLNKPVPVGFTFSFPCTQL 167

                        170
                 ....*....|.
gi 767938343 616 GLDQwASLAAW 626
Cdd:PTZ00107 168 SVNN-AILIDW 177
PLN02914 PLN02914
hexokinase
 497-626 6.65e-19

hexokinase


Pssm-ID: 178502 [Multi-domain]  Cd Length: 490  Bit Score: 90.33  E-value: 6.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 497 LAAVQAQMRKAMAKGLRGE-ASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLlvRVTTG------VQITSEIYSIP 569
Cdd:PLN02914  55 LRHVADAMAADMRAGLAVDgGGDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVL--RVQLGgkdervIATEFEQVSIP 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767938343 570 ETVAQGSGQQLFDHIVDCIVDFQQKQG-----LSGQSLPLGFTFSFPCRQLGLDQwASLAAW 626
Cdd:PLN02914 133 QELMFGTSEELFDFIASGLANFVAKEGgkfhlPEGRKREIGFTFSFPVKQTSIDS-GILMKW 193
PLN02405 PLN02405
hexokinase
 496-626 8.09e-18

hexokinase


Pssm-ID: 215226 [Multi-domain]  Cd Length: 497  Bit Score: 86.81  E-value: 8.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 496 QLAAVQAQMRKAMAKGLRGEA-SSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLlvRVTTG------VQITSEIYSI 568
Cdd:PLN02405  54 KLRQVADAMTVEMHAGLASEGgSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVL--RVLLGgkdgrvVKQEFEEVSI 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767938343 569 PETVAQGSGQQLFDHIVDCIVDFQQKQG-----LSGQSLPLGFTFSFPCRQLGLDQwASLAAW 626
Cdd:PLN02405 132 PPHLMTGSSDALFDFIAAALAKFVATEGedfhlPPGRQRELGFTFSFPVKQTSISS-GTLIKW 193
PLN02362 PLN02362
hexokinase
 503-617 2.37e-16

hexokinase


Pssm-ID: 215206 [Multi-domain]  Cd Length: 509  Bit Score: 82.24  E-value: 2.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 503 QMRKAMA----KGLRGEA-SSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLlvRVTTGVQITS------EIYSIPET 571
Cdd:PLN02362  57 QVVDAMAvemhAGLASEGgSKLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVL--RVQLGGQRSSilsqdvERHPIPQH 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767938343 572 VAQGSGQQLFDHIVDCIVDFQQKQGLSGQSLP-----LGFTFSFPCRQLGL 617
Cdd:PLN02362 135 LMNSTSEVLFDFIASSLKQFVEKEENGSEFSQvrrreLGFTFSFPVKQTSI 185
PLN02596 PLN02596
hexokinase-like
 515-625 1.39e-09

hexokinase-like


Pssm-ID: 178206 [Multi-domain]  Cd Length: 490  Bit Score: 60.66  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938343 515 EASSLRMLPTFVRATPDGSERGDFLALDLGGTNFRVLLVRVTTGVQITSEIY----SIPETVAQGSGQQLFDHIVDCIVD 590
Cdd:PLN02596  75 ETTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNEPISDLYreeiSIPSNVLNGTSQELFDYIALELAK 154

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767938343 591 FQQKQGLSGQSLP-----LGFTFSFPCRQLGLD-----QWASLAA 625
Cdd:PLN02596 155 FVAEHPGDEADTPervkkLGFTVSYPVDQAAASsgsaiKWKSFSA 199
 
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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