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Conserved domains on  [gi|1705100392|ref|NP_001358454|]
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hexokinase-2 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASKHA_NBD_HK2_meta_rpt2 cd24128
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ...
 450-884 0e+00

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: 906.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 450 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWGGVEMHN 529
Cdd:cd24128     1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 530 KIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLL 609
Cdd:cd24128    81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 610 KEAIHRREEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 689
Cdd:cd24128   161 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 690 LDDFRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLAL 769
Cdd:cd24128   241 LDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLAL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 770 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 849
Cdd:cd24128   321 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 400

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1705100392 850 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACRIR 884
Cdd:cd24128   401 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACRIR 435
ASKHA_NBD_HK2_meta_rpt1 cd24125
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ...
 2-430 0e+00

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: 883.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   2 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMEN 81
Cdd:cd24125     1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  82 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALI 161
Cdd:cd24125    81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 162 RKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGS 241
Cdd:cd24125   161 RKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 242 LNDIRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGI 321
Cdd:cd24125   241 LDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 322 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHK 401
Cdd:cd24125   321 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHK 400

                         410       420
                  ....*....|....*....|....*....
gi 1705100392 402 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 430
Cdd:cd24125   401 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
 
Name Accession Description Interval E-value
ASKHA_NBD_HK2_meta_rpt2 cd24128
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ...
 450-884 0e+00

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: 906.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 450 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWGGVEMHN 529
Cdd:cd24128     1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 530 KIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLL 609
Cdd:cd24128    81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 610 KEAIHRREEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 689
Cdd:cd24128   161 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 690 LDDFRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLAL 769
Cdd:cd24128   241 LDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLAL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 770 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 849
Cdd:cd24128   321 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 400

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1705100392 850 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACRIR 884
Cdd:cd24128   401 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACRIR 435
ASKHA_NBD_HK2_meta_rpt1 cd24125
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ...
 2-430 0e+00

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: 883.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   2 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMEN 81
Cdd:cd24125     1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  82 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALI 161
Cdd:cd24125    81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 162 RKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGS 241
Cdd:cd24125   161 RKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 242 LNDIRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGI 321
Cdd:cd24125   241 LDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 322 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHK 401
Cdd:cd24125   321 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHK 400

                         410       420
                  ....*....|....*....|....*....
gi 1705100392 402 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 430
Cdd:cd24125   401 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
PTZ00107 PTZ00107
hexokinase; Provisional
 1-432 2.07e-116

hexokinase; Provisional


Pssm-ID: 240270 [Multi-domain]  Cd Length: 464  Bit Score: 362.84  E-value: 2.07e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   1 MRLSDETLLEISKRFRKEMEKGL-GATTHPTA------AVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNG 73
Cdd:PTZ00107   18 FTMSKEKLKELVDYFLYELVEGLeAHRRHRNLwipnecSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFRAVRVSLRGGG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  74 lqKVEMENQIYAIPEDIMRG---------SGTQLFDHIAECLANFMDKLQIKD---KKLPLGFTFSFPCHQTKLDESFLV 141
Cdd:PTZ00107   98 --KMERTQSKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDPEdlnKPVPVGFTFSFPCTQLSVNNAILI 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 142 SWTKGFKSS-----GVEGRDVVALIRKAIQRRGdFDIDIVAVVNDTVGTMMTCGYDDH----NCEIGLIVGTGSNACYME 212
Cdd:PTZ00107  176 DWTKGFETGratndPVEGKDVGELLNDAFKRNN-VPANVVAVLNDTVGTLISCAYQKPkntpPCQVGVIIGTGSNACYFE 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 213 emrhiDMVE--GDEGRMcINMEWGAFgdDGSLNdiRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEel 290
Cdd:PTZ00107  255 -----PEVSayGYAGTP-INMECGNF--DSKLP--ITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLLQL-- 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 291 lfggKLSPELLNTGRFETKDISDIEGEK-DGIRKAREVLMRL-GLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQR 368
Cdd:PTZ00107  323 ----KAPPKMWQSGSFESEDASMILNDQsPDLQFSRQVIKEAwDVDLTDEDLYTIRKICELVRGRAAQLAAAFIAAPAKK 398

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1705100392 369 IKENKGeerlRSTIGVDGSVYKKHPHFAKRLHKTVRRLV--PGCDVRFLRSEDGSGKGAAMVTAVA 432
Cdd:PTZ00107  399 TRTVQG----KATVAIDGSVYVKNPWFRRLLQEYINSILgpDAGNVVFYLADDGSGKGAAIIAAMV 460
Hexokinase_2 pfam03727
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 645-879 1.26e-107

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: 331.38  E-value: 1.26e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 645 EVGLIVGTGSNACYMEEMRNVELVEG---EEGRMCVNMEWGAFGDNGCLDDFRTEFDVAVDELSLNPGKQRFEKMISGMY 721
Cdd:pfam03727   1 RIGLILGTGTNAAYVEKVSNIPKLEGklpKSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 722 LGEIVRNILIDFTKRGLLFRGRiSERLKTRGIFETKFLSQIESD-CLALLQVRAILQ-HLGLES-TCDDSIIVKEVCTVV 798
Cdd:pfam03727  81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDpSEDLETTREILEeLLGIETvTEEDRKIVRRICEAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 799 ARRAAQLCGAGMAAVVDRIRENRgldalKVTVGVDGTLYKLHPHFAKVMHETVKD-LAPKCDVSFLQSEDGSGKGAALIT 877
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-----KVTVGVDGSVYEKYPGFRERLQEALRElLGPGDKVVLVLAEDGSGVGAALIA 234


                  ..
gi 1705100392 878 AV 879
Cdd:pfam03727 235 AV 236
PTZ00107 PTZ00107
hexokinase; Provisional
 434-880 5.16e-105

hexokinase; Provisional


Pssm-ID: 240270 [Multi-domain]  Cd Length: 464  Bit Score: 333.18  E-value: 5.16e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 434 RLADQHRARQKTLEHLQLSHDQLLEVKRRMKVEMERGL-SKETHASA------PVKMLPTYVCATPDGTEKGDFLALDLG 506
Cdd:PTZ00107    3 RYIKQRVRLASLVNQFTMSKEKLKELVDYFLYELVEGLeAHRRHRNLwipnecSFKMLDSCVYNLPTGKEKGVYYAIDFG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 507 GTNFRVLLVRVRNGkwGGVEMHNKIYAIPQEVM---------HGTGDELFDHIVQCIADFLEYMGMK---GVSLPLGFTF 574
Cdd:PTZ00107   83 GTNFRAVRVSLRGG--GKMERTQSKFSLPKSALlgekglldkKATATDLFDHIAKSIKKMMEENGDPedlNKPVPVGFTF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 575 SFPCQQNSLDESILLKWTKGFKAS-----GCEGEDVVTLLKEAIhRREEFDLDVVAVVNDTVGTMMTCGFED----PHCE 645
Cdd:PTZ00107  161 SFPCTQLSVNNAILIDWTKGFETGratndPVEGKDVGELLNDAF-KRNNVPANVVAVLNDTVGTLISCAYQKpkntPPCQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 646 VGLIVGTGSNACYMEEMrnvELVEGEEGRMcVNMEWGAFgdngCLDDFRTEFDVAVDELSLNPGKQRFEKMISGMYLGEI 725
Cdd:PTZ00107  240 VGVIIGTGSNACYFEPE---VSAYGYAGTP-INMECGNF----DSKLPITPYDLEMDWYTPNRGRQQFEKMISGAYLGEI 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 726 VRNILIdftkrgLLFRGRISERLKTRGIFETKFLSQIESDCLALLQV--RAILQHLGLESTCDDSIIVKEVCTVVARRAA 803
Cdd:PTZ00107  312 SRRLIV------HLLQLKAPPKMWQSGSFESEDASMILNDQSPDLQFsrQVIKEAWDVDLTDEDLYTIRKICELVRGRAA 385

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1705100392 804 QLCGAGMAAVVDRIRENRGldalKVTVGVDGTLYKLHPHFAKVMHETVKD-LAPK-CDVSFLQSEDGSGKGAALITAVA 880
Cdd:PTZ00107  386 QLAAAFIAAPAKKTRTVQG----KATVAIDGSVYVKNPWFRRLLQEYINSiLGPDaGNVVFYLADDGSGKGAAIIAAMV 460
Hexokinase_2 pfam03727
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 197-431 4.79e-103

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: 319.44  E-value: 4.79e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 197 EIGLIVGTGSNACYMEEMRHIDMVEGD---EGRMCINMEWGAFGDDGSLNDIRTEFDQEIDMGSLNPGKQLFEKMISGMY 273
Cdd:pfam03727   1 RIGLILGTGTNAAYVEKVSNIPKLEGKlpkSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 274 MGELVRLILVKMAKEELLFGGKlSPELLNTGRFETKDISDIEGEK-DGIRKAREVLMR-LGL-DPTQEDCVATHRICQIV 350
Cdd:pfam03727  81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDPsEDLETTREILEElLGIeTVTEEDRKIVRRICEAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 351 STRSASLCAATLAAVLQRIKENKgeerlRSTIGVDGSVYKKHPHFAKRLHKTVRRLV-PGCDVRFLRSEDGSGKGAAMVT 429
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-----KVTVGVDGSVYEKYPGFRERLQEALRELLgPGDKVVLVLAEDGSGVGAALIA 234


                  ..
gi 1705100392 430 AV 431
Cdd:pfam03727 235 AV 236
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 1-432 5.00e-102

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


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 324.22  E-value: 5.00e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   1 MRLSDETLLEISKRFRKEMEKGLgatTHPTAAVKMLPTFVrSTPDG-TEHGEFLALDLGGTNFRVLWVKVTDNGlqKVEM 79
Cdd:COG5026    15 FDLSSIDLEEIAAKFQEEMEKGL---EGKKSSLKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRFDGEG--TFEI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  80 ENQIyAIPediMRGSG-----TQLFDHIAECLAnfmdklQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEG 154
Cdd:COG5026    89 ENFK-SFP---LPGTSseitaEEFFDFIADYIE------PLLDESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 155 RDVVALIRKAIQRRGDFDIDIVAVVNDTVGTMMTCGY----DDHNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCIN 230
Cdd:COG5026   159 KNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYadpdDGYSGYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMIIN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 231 MEWGAFgdDGSLndiRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEElLFGGKLSPELLNTGRFETKD 310
Cdd:COG5026   239 MESGNF--NKLP---RTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTVD 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 311 ISDIEGEKDGirkAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERlRSTIGVDGSVYK 390
Cdd:COG5026   313 MSRFLADPSD---EKEILSQCLEAGSEEDREILREIADAIVERAARLVAATLAGILLHLGPGKTPLK-PHCIAIDGSTYE 388

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1705100392 391 KHPHFAKRLHKTVRRLVPGCD---VRFLRSEDGSGKGAAMVTAVA 432
Cdd:COG5026   389 KMPGLAEKIEYALQEYLLGEKgryVEFVLVENASLLGAAIAAALN 433
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 448-881 5.49e-99

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


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 316.13  E-value: 5.49e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 448 HLQLSHDQLLEVKRRMKVEMERGLSketHASAPVKMLPTYVcATPDG-TEKGDFLALDLGGTNFRVLLVRVrNGKwGGVE 526
Cdd:COG5026    14 GFDLSSIDLEEIAAKFQEEMEKGLE---GKKSSLKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRF-DGE-GTFE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 527 MHN-KIYAIP---QEVmhgTGDELFDHIVQCIADFLEYmgmkgvSLPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEG 602
Cdd:COG5026    88 IENfKSFPLPgtsSEI---TAEEFFDFIADYIEPLLDE------SYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 603 EDVVTLLKEAIHRREEFDLDVVAVVNDTVGTMMTCGFEDP----HCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVN 678
Cdd:COG5026   159 KNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPddgySGYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMIIN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 679 MEWGAFgdNGCLddfRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGlLFRGRISERLKTRGIFETKF 758
Cdd:COG5026   239 MESGNF--NKLP---RTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTVD 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 759 LSQI---ESDclALLQVRAILQhlglESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVdrIRENRGLDALK-VTVGVDG 834
Cdd:COG5026   313 MSRFladPSD--EKEILSQCLE----AGSEEDREILREIADAIVERAARLVAATLAGIL--LHLGPGKTPLKpHCIAIDG 384

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1705100392 835 TLYKLHPHFAKVMHETVKD-LAPKCD--VSFLQSEDGSGKGAALITAVAC 881
Cdd:COG5026   385 STYEKMPGLAEKIEYALQEyLLGEKGryVEFVLVENASLLGAAIAAALNE 434
 
Name Accession Description Interval E-value
ASKHA_NBD_HK2_meta_rpt2 cd24128
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ...
 450-884 0e+00

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: 906.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 450 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWGGVEMHN 529
Cdd:cd24128     1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 530 KIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLL 609
Cdd:cd24128    81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 610 KEAIHRREEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 689
Cdd:cd24128   161 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 690 LDDFRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLAL 769
Cdd:cd24128   241 LDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLAL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 770 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 849
Cdd:cd24128   321 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 400

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1705100392 850 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACRIR 884
Cdd:cd24128   401 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACRIR 435
ASKHA_NBD_HK1-3_meta_rpt2 cd24091
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ...
 450-882 0e+00

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: 902.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 450 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWGGVEMHN 529
Cdd:cd24091     1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 530 KIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLL 609
Cdd:cd24091    81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 610 KEAIHRREEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 689
Cdd:cd24091   161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 690 LDDFRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLAL 769
Cdd:cd24091   241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 770 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 849
Cdd:cd24091   321 LQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHE 400

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1705100392 850 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACR 882
Cdd:cd24091   401 TVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
ASKHA_NBD_HK2_meta_rpt1 cd24125
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ...
 2-430 0e+00

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: 883.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   2 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMEN 81
Cdd:cd24125     1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  82 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALI 161
Cdd:cd24125    81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 162 RKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGS 241
Cdd:cd24125   161 RKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 242 LNDIRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGI 321
Cdd:cd24125   241 LDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 322 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHK 401
Cdd:cd24125   321 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHK 400

                         410       420
                  ....*....|....*....|....*....
gi 1705100392 402 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 430
Cdd:cd24125   401 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
ASKHA_NBD_HK1-2_meta_rpt1 cd24089
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ...
 2-430 0e+00

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: 859.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   2 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMEN 81
Cdd:cd24089     1 RLSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  82 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALI 161
Cdd:cd24089    81 QVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 162 RKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGS 241
Cdd:cd24089   161 RKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 242 LNDIRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGI 321
Cdd:cd24089   241 LEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 322 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHK 401
Cdd:cd24089   321 ANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLHK 400

                         410       420
                  ....*....|....*....|....*....
gi 1705100392 402 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 430
Cdd:cd24089   401 AVRRLVPDCDVRFLLSEDGSGKGAAMVTA 429
ASKHA_NBD_HK1_meta_rpt2 cd24127
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ...
 451-883 0e+00

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: 815.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 451 LSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWGGVEMHNK 530
Cdd:cd24127     2 LTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 531 IYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLLK 610
Cdd:cd24127    82 IYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLLR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 611 EAIHRREEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGCL 690
Cdd:cd24127   162 DAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 691 DDFRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLALL 770
Cdd:cd24127   242 DDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLALL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 771 QVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHET 850
Cdd:cd24127   322 QVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQT 401

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1705100392 851 VKDLAPKCDVSFLQSEDGSGKGAALITAVACRI 883
Cdd:cd24127   402 VKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 434
ASKHA_NBD_HKDC1_meta_rpt2 cd24130
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ...
 450-883 0e+00

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: 766.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 450 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKwGGVEMHN 529
Cdd:cd24130     1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGR-RSVRMYN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 530 KIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLL 609
Cdd:cd24130    80 KIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDML 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 610 KEAIHRREEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 689
Cdd:cd24130   160 REAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDNGC 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 690 LDDFRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLAL 769
Cdd:cd24130   240 IDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLAL 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 770 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 849
Cdd:cd24130   320 LQVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRILQE 399

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1705100392 850 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACRI 883
Cdd:cd24130   400 TVKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 433
ASKHA_NBD_HK1_meta_rpt1 cd24124
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ...
 1-446 0e+00

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: 762.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   1 MRLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEME 80
Cdd:cd24124    28 MRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHME 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  81 NQIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVAL 160
Cdd:cd24124   108 SEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKL 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 161 IRKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDG 240
Cdd:cd24124   188 LNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDG 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 241 SLNDIRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDG 320
Cdd:cd24124   268 SLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEG 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 321 IRKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLH 400
Cdd:cd24124   348 LHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFH 427

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1705100392 401 KTVRRLVPGCDVRFLRSEDGSGKGAAMVTAVAYRLADQHRARQKTL 446
Cdd:cd24124   428 KTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETL 473
ASKHA_NBD_HKDC1_meta_rpt1 cd24126
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ...
 2-430 0e+00

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: 751.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   2 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMEN 81
Cdd:cd24126     1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  82 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALI 161
Cdd:cd24126    81 QFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 162 RKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGS 241
Cdd:cd24126   161 RKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 242 LNDIRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGI 321
Cdd:cd24126   241 LEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 322 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHK 401
Cdd:cd24126   321 YNTREILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHK 400

                         410       420
                  ....*....|....*....|....*....
gi 1705100392 402 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 430
Cdd:cd24126   401 VVRRLVPSCDVRFLLSESGSGKGAAMVTA 429
ASKHA_NBD_HK_meta cd24019
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ...
 2-430 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: 745.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   2 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNglQKVEMEN 81
Cdd:cd24019     1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGG--SQVKMES 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  82 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALI 161
Cdd:cd24019    79 EIYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 162 RKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHI---DMVEGDEGRMCINMEWGAFGD 238
Cdd:cd24019   159 QEAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVekwDGDEGDPGQVIINTEWGAFGD 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 239 DGSLNDIRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEK 318
Cdd:cd24019   239 NGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDN 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 319 -DGIRKAREVLMRLGL-DPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIkenkgeERLRSTIGVDGSVYKKHPHFA 396
Cdd:cd24019   319 eGDFSNTREILKELGLeDASDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRM------NRKEVTVGVDGSLYKYHPKFH 392

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1705100392 397 KRLHKTVRRLVP-GCDVRFLRSEDGSGKGAAMVTA 430
Cdd:cd24019   393 KRMHETLKELVPpGCKFKLMLSEDGSGKGAALVAA 427
ASKHA_NBD_HK_meta cd24019
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ...
 450-878 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: 739.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 450 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKwgGVEMHN 529
Cdd:cd24019     1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGGS--QVKMES 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 530 KIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLL 609
Cdd:cd24019    79 EIYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 610 KEAIHRREEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVEL---VEGEEGRMCVNMEWGAFGD 686
Cdd:cd24019   159 QEAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKwdgDEGDPGQVIINTEWGAFGD 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 687 NGCLDDFRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDC 766
Cdd:cd24019   239 NGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDN 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 767 L-ALLQVRAILQHLGLES-TCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRIREnrgldaLKVTVGVDGTLYKLHPHFA 844
Cdd:cd24019   319 EgDFSNTREILKELGLEDaSDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMNR------KEVTVGVDGSLYKYHPKFH 392

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1705100392 845 KVMHETVKDLAPK-CDVSFLQSEDGSGKGAALITA 878
Cdd:cd24019   393 KRMHETLKELVPPgCKFKLMLSEDGSGKGAALVAA 427
ASKHA_NBD_HK3_meta_rpt2 cd24129
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ...
 450-882 0e+00

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: 718.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 450 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVrnGKwGGVEMHN 529
Cdd:cd24129     1 QLSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHV--GT-AGVQITS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 530 KIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLL 609
Cdd:cd24129    78 EIYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 610 KEAIHRREEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 689
Cdd:cd24129   158 REAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDNGC 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 690 LDDFRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLAL 769
Cdd:cd24129   238 LAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSLAL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 770 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 849
Cdd:cd24129   318 RQVRAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLVQA 397

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1705100392 850 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACR 882
Cdd:cd24129   398 TVRELAPRCVVTFLQSEDGSGKGAALVTAVACR 430
ASKHA_NBD_HK1-2_meta_rpt1 cd24089
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ...
 450-878 0e+00

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: 668.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 450 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWGGVEMHN 529
Cdd:cd24089     1 RLSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 530 KIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLL 609
Cdd:cd24089    81 QVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 610 KEAIHRREEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 689
Cdd:cd24089   161 RKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 690 LDDFRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLAL 769
Cdd:cd24089   241 LEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 770 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 849
Cdd:cd24089   321 ANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLHK 400

                         410       420
                  ....*....|....*....|....*....
gi 1705100392 850 TVKDLAPKCDVSFLQSEDGSGKGAALITA 878
Cdd:cd24089   401 AVRRLVPDCDVRFLLSEDGSGKGAAMVTA 429
ASKHA_NBD_HK1-3_meta_rpt2 cd24091
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ...
 2-434 0e+00

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: 631.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   2 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMEN 81
Cdd:cd24091     1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  82 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALI 161
Cdd:cd24091    81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 162 RKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGS 241
Cdd:cd24091   161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 242 LNDIRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGI 321
Cdd:cd24091   241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 322 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHK 401
Cdd:cd24091   321 LQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHE 400

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1705100392 402 TVRRLVPGCDVRFLRSEDGSGKGAAMVTAVAYR 434
Cdd:cd24091   401 TVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
ASKHA_NBD_HK2_meta_rpt1 cd24125
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ...
 450-878 0e+00

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: 616.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 450 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWGGVEMHN 529
Cdd:cd24125     1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 530 KIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLL 609
Cdd:cd24125    81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 610 KEAIHRREEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 689
Cdd:cd24125   161 RKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 690 LDDFRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLAL 769
Cdd:cd24125   241 LDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 770 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 849
Cdd:cd24125   321 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHK 400

                         410       420
                  ....*....|....*....|....*....
gi 1705100392 850 TVKDLAPKCDVSFLQSEDGSGKGAALITA 878
Cdd:cd24125   401 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
ASKHA_NBD_HKDC1_meta_rpt1 cd24126
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ...
 450-878 0e+00

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: 607.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 450 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRV-RNGKwGGVEMH 528
Cdd:cd24126     1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVsEDGK-QKVQME 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 529 NKIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTL 608
Cdd:cd24126    80 SQFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 609 LKEAIHRREEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNG 688
Cdd:cd24126   160 LRKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 689 CLDDFRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLA 768
Cdd:cd24126   240 SLEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 769 LLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMH 848
Cdd:cd24126   320 LYNTREILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLH 399

                         410       420       430
                  ....*....|....*....|....*....|
gi 1705100392 849 ETVKDLAPKCDVSFLQSEDGSGKGAALITA 878
Cdd:cd24126   400 KVVRRLVPSCDVRFLLSESGSGKGAAMVTA 429
ASKHA_NBD_HK2_meta_rpt2 cd24128
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ...
 2-435 0e+00

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: 605.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   2 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMEN 81
Cdd:cd24128     1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  82 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALI 161
Cdd:cd24128    81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 162 RKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGS 241
Cdd:cd24128   161 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 242 LNDIRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGI 321
Cdd:cd24128   241 LDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLAL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 322 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHK 401
Cdd:cd24128   321 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 400

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1705100392 402 TVRRLVPGCDVRFLRSEDGSGKGAAMVTAVAYRL 435
Cdd:cd24128   401 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACRI 434
ASKHA_NBD_HK1_meta_rpt2 cd24127
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ...
 2-435 0e+00

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: 600.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   2 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMEN 81
Cdd:cd24127     1 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  82 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALI 161
Cdd:cd24127    81 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 162 RKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGS 241
Cdd:cd24127   161 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 242 LNDIRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGI 321
Cdd:cd24127   241 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 322 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHK 401
Cdd:cd24127   321 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 400

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1705100392 402 TVRRLVPGCDVRFLRSEDGSGKGAAMVTAVAYRL 435
Cdd:cd24127   401 TVKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 434
ASKHA_NBD_HK1_meta_rpt1 cd24124
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ...
 437-885 0e+00

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: 598.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 437 DQHRARQKTLEHLQLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVR 516
Cdd:cd24124    16 DQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQ 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 517 VRNGKWGGVEMHNKIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDESILLKWTKGFK 596
Cdd:cd24124    96 VNHEKNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFK 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 597 ASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMC 676
Cdd:cd24124   176 ASGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMC 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 677 VNMEWGAFGDNGCLDDFRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFET 756
Cdd:cd24124   256 INTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNT 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 757 KFLSQIESDCLALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRIRENRGLDALKVTVGVDGTL 836
Cdd:cd24124   336 SDVSAIEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSL 415

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1705100392 837 YKLHPHFAKVMHETVKDLAPKCDVSFLQSEDGSGKGAALITAVACRIRE 885
Cdd:cd24124   416 YKTHPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAE 464
ASKHA_NBD_HKDC1_meta_rpt2 cd24130
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ...
 2-435 0e+00

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: 584.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   2 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTdNGLQKVEMEN 81
Cdd:cd24130     1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIR-SGRRSVRMYN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  82 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALI 161
Cdd:cd24130    80 KIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDML 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 162 RKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGS 241
Cdd:cd24130   160 REAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDNGC 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 242 LNDIRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGI 321
Cdd:cd24130   240 IDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLAL 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 322 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHK 401
Cdd:cd24130   320 LQVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRILQE 399

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1705100392 402 TVRRLVPGCDVRFLRSEDGSGKGAAMVTAVAYRL 435
Cdd:cd24130   400 TVKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 433
ASKHA_NBD_HK4_meta cd24092
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ...
 443-882 0e+00

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: 583.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 443 QKTLEHLQLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKW 522
Cdd:cd24092     3 EQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 523 GG--VEMHNKIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDESILLKWTKGFKASGC 600
Cdd:cd24092    83 GQwsVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 601 EGEDVVTLLKEAIHRREEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNME 680
Cdd:cd24092   163 EGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTE 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 681 WGAFGDNGCLDDFRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLS 760
Cdd:cd24092   243 WGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVS 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 761 QIESDCLALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRIRENRGLDALKVTVGVDGTLYKLH 840
Cdd:cd24092   323 QVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLH 402

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1705100392 841 PHFAKVMHETVKDLAPKCDVSFLQSEDGSGKGAALITAVACR 882
Cdd:cd24092   403 PSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 444
ASKHA_NBD_HK3_meta_rpt2 cd24129
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ...
 2-434 0e+00

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: 577.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   2 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQkveMEN 81
Cdd:cd24129     1 QLSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTAGVQ---ITS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  82 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALI 161
Cdd:cd24129    78 EIYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 162 RKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGS 241
Cdd:cd24129   158 REAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDNGC 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 242 LNDIRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGI 321
Cdd:cd24129   238 LAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSLAL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 322 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHK 401
Cdd:cd24129   318 RQVRAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLVQA 397

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1705100392 402 TVRRLVPGCDVRFLRSEDGSGKGAAMVTAVAYR 434
Cdd:cd24129   398 TVRELAPRCVVTFLQSEDGSGKGAALVTAVACR 430
ASKHA_NBD_HK4_meta cd24092
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ...
 2-434 0e+00

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: 570.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   2 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDN--GLQKVEM 79
Cdd:cd24092    10 QLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGeeGQWSVKT 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  80 ENQIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVA 159
Cdd:cd24092    90 KHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 160 LIRKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDD 239
Cdd:cd24092   170 LLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGDS 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 240 GSLNDIRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKD 319
Cdd:cd24092   250 GELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTG 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 320 GIRKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFAKRL 399
Cdd:cd24092   330 DRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERF 409

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1705100392 400 HKTVRRLVPGCDVRFLRSEDGSGKGAAMVTAVAYR 434
Cdd:cd24092   410 HASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 444
ASKHA_NBD_HK3_meta_rpt1 cd24090
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ...
 6-430 3.33e-174

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: 511.00  E-value: 3.33e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   6 ETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLG--GTNFRVLWVKVTDNGLQKVEMENQI 83
Cdd:cd24090     5 AQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRSQE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  84 YAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALIRK 163
Cdd:cd24090    85 FVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQLLRD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 164 AIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGSLN 243
Cdd:cd24090   165 AIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDDGALG 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 244 DIRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGIRK 323
Cdd:cd24090   245 PVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSAGAAR 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 324 AREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHKTV 403
Cdd:cd24090   325 VRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSILQGTV 404

                         410       420
                  ....*....|....*....|....*..
gi 1705100392 404 RRLVPGCDVRFLRSEDGSGKGAAMVTA 430
Cdd:cd24090   405 MLLAPECDVSFIPSVDGGGRGVAMVTA 431
ASKHA_NBD_HK3_meta_rpt1 cd24090
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ...
 455-878 8.64e-162

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: 479.03  E-value: 8.64e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 455 QLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLG--GTNFRVLLVRVRNGKWGGVEMHNKIY 532
Cdd:cd24090     6 QLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRSQEF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 533 AIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLLKEA 612
Cdd:cd24090    86 VIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQLLRDA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 613 IHRREEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGCLDD 692
Cdd:cd24090   166 IQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDDGALGP 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 693 FRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLALLQV 772
Cdd:cd24090   246 VLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSAGAARV 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 773 RAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHETVK 852
Cdd:cd24090   326 RAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSILQGTVM 405

                         410       420
                  ....*....|....*....|....*.
gi 1705100392 853 DLAPKCDVSFLQSEDGSGKGAALITA 878
Cdd:cd24090   406 LLAPECDVSFIPSVDGGGRGVAMVTA 431
ASKHA_NBD_HK_fungi cd24018
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ...
 5-428 1.23e-160

nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. It is a putative glucokinase that functions in phosphorylation of aldohexoses and glucose uptake. It is involved in sporulation and required for the full activation of the early meiotic inducer IME1. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar.


Pssm-ID: 466868 [Multi-domain]  Cd Length: 431  Bit Score: 475.97  E-value: 1.23e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   5 DETLLEISKRFRKEMEKGLgatTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQkVEMENQIY 84
Cdd:cd24018     1 VSKLEEIVKHFLSEMEKGL---EGDGGSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNGGI-FIIVQRKY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  85 AIPEDIMRGSGTQLFDHIAECLANFMDK---LQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALI 161
Cdd:cd24018    77 KIPDEAKTGTGEELFDFIAECIAEFLEEhnlDLQSDKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 162 RKAIQRRGdFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHI---DMVEG---DEGRMCINMEWGA 235
Cdd:cd24018   157 QNALDRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIkklTSPSGsvtKSDEMIINTEWGA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 236 FgdDGSLNDI-RTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDI 314
Cdd:cd24018   236 F--DNEREVLpLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRI 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 315 EGEKDG-IRKAREVLMRLG--LDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEerlRSTIGVDGSVYKK 391
Cdd:cd24018   314 EADTSPdLDAVRDILKELLaiDNTTLEDRKLIKRICELVSTRAARLSAAAIAAILLKRGSLLPE---PVTVGIDGSVYEK 390

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1705100392 392 HPHFAKRLHKTVRRLVPGC---DVRFLRSEDGSGKGAAMV 428
Cdd:cd24018   391 YPGFKDRLSEALRELFGPEvkaNISLVLAKDGSGLGAAII 430
ASKHA_NBD_HK_fungi cd24018
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ...
 454-876 8.86e-159

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: 471.35  E-value: 8.86e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 454 DQLLEVKRRMKVEMERGLSKEThasAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVrNGKWGGVEMHNKIYA 533
Cdd:cd24018     2 SKLEEIVKHFLSEMEKGLEGDG---GSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTL-DGNGGIFIIVQRKYK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 534 IPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVS---LPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLLK 610
Cdd:cd24018    78 IPDEAKTGTGEELFDFIAECIAEFLEEHNLDLQSdktIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELLQ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 611 EAIHRREeFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNV------ELVEGEEGRMCVNMEWGAF 684
Cdd:cd24018   158 NALDRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIkkltspSGSVTKSDEMIINTEWGAF 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 685 GDNGCLDDFrTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIES 764
Cdd:cd24018   237 DNEREVLPL-TKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIEA 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 765 DCLALLQ-VRAILQHLG--LESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVdrirENRGLDAL-KVTVGVDGTLYKLH 840
Cdd:cd24018   316 DTSPDLDaVRDILKELLaiDNTTLEDRKLIKRICELVSTRAARLSAAAIAAIL----LKRGSLLPePVTVGIDGSVYEKY 391

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1705100392 841 PHFAKVMHETVKDLAP---KCDVSFLQSEDGSGKGAALI 876
Cdd:cd24018   392 PGFKDRLSEALRELFGpevKANISLVLAKDGSGLGAAII 430
ASKHA_NBD_HK cd24000
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 5-429 2.50e-144

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: 431.31  E-value: 2.50e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   5 DETLLEISKRFRKEMEKGLGATTHPtaaVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGlqKVEMENQIY 84
Cdd:cd24000     1 DEDLKEITDAFLEELEKGLAGEPSS---LKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDGKG--IEVTISKKY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  85 AIPEDIMRGSGTQLFDHIAECLANFMDKLQIKdKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALIRKA 164
Cdd:cd24000    76 EIPDEIKTASAEEFFDFIADCIAEFLKENGLK-KPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 165 IQRRGDfDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHIDmveGDEGRMCINMEWGAFGDDgslND 244
Cdd:cd24000   155 LKKRGL-PVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNIL---LGDGGMIINTEWGNFGKN---SL 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 245 IRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELlfggklspellntgrfetkdisdiegekdgirka 324
Cdd:cd24000   228 PRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADEIL---------------------------------- 273

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 325 revlmrlgldptqedcvatHRICQIVSTRSASLCAATLAAVLQRIKENKGEerlRSTIGVDGSVYKKHPHFAKRLHKTVR 404
Cdd:cd24000   274 -------------------RKICELVAERSARLAAAAIAALLRKTGDSPEK---KITIAVDGSLFEKYPGYRERLEEYLK 331

                         410       420
                  ....*....|....*....|....*.
gi 1705100392 405 RLV-PGCDVRFLRSEDGSGKGAAMVT 429
Cdd:cd24000   332 ELLgRGIRIELVLVEDGSLIGAALAA 357
ASKHA_NBD_HK cd24000
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 453-877 4.17e-139

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: 417.83  E-value: 4.17e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 453 HDQLLEVKRRMKVEMERGLSKEthaSAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVrNGKwGGVEMHNKIY 532
Cdd:cd24000     1 DEDLKEITDAFLEELEKGLAGE---PSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSL-DGK-GIEVTISKKY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 533 AIPQEVMHGTGDELFDHIVQCIADFLEYMGMKgVSLPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLLKEA 612
Cdd:cd24000    76 EIPDEIKTASAEEFFDFIADCIAEFLKENGLK-KPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 613 IHRReEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNvelVEGEEGRMCVNMEWGAFGDNgclDD 692
Cdd:cd24000   155 LKKR-GLPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSN---ILLGDGGMIINTEWGNFGKN---SL 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 693 FRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRgllfrgriserlktrgifetkflsqiesdclallqv 772
Cdd:cd24000   228 PRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------------------------ 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 773 railqhlglestcddsiIVKEVCTVVARRAAQLCGAGMAAVVDRIRENrglDALKVTVGVDGTLYKLHPHFAKVMHETVK 852
Cdd:cd24000   272 -----------------ILRKICELVAERSARLAAAAIAALLRKTGDS---PEKKITIAVDGSLFEKYPGYRERLEEYLK 331

                         410       420
                  ....*....|....*....|....*.
gi 1705100392 853 DLAPK-CDVSFLQSEDGSGKGAALIT 877
Cdd:cd24000   332 ELLGRgIRIELVLVEDGSLIGAALAA 357
ASKHA_NBD_HK_plant cd24020
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 454-880 2.18e-122

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: 377.39  E-value: 2.18e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 454 DQLLEVKRRMKVEMERGLSKETHAsaPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWGGVEMHNKIYA 533
Cdd:cd24020     4 SRLRQVADAMVVEMEAGLASEGGS--KLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 534 IPQEVMHGTGDELFDHIVQCIADFLEYMG----MKGVSLPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLL 609
Cdd:cd24020    82 IPPELMVGTSEELFDFIAGELAKFVATEGegfhPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVELL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 610 KEAIHRReEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEG---EEGRMCVNMEWGAFgD 686
Cdd:cd24020   162 EEALERQ-GLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGglpRSGEMVINTEWGNF-R 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 687 NGCLDdfRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDC 766
Cdd:cd24020   240 SSHLP--RTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMHEDD 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 767 LA-LLQVRAILQH-LGLE-STCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRI--RENRGLDALKVTVGVDGTLYKLHP 841
Cdd:cd24020   318 SPdLETVARILKDaLGIDdTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLgrDGGGSSPAQRTVVAVDGGLYEHYP 397

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1705100392 842 HFAKVMHETVKDLAPKC---DVSFLQSEDGSGKGAALITAVA 880
Cdd:cd24020   398 KFREYMQQALVELLGDEaadSVELELSNDGSGIGAALLAAAH 439
ASKHA_NBD_HK1-2_fungi cd24087
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ...
 455-880 3.35e-119

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: 369.01  E-value: 3.35e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 455 QLLEVKRRMKVEMERGLSKETHAsapVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVR-NGKWggvEMHNKIYA 533
Cdd:cd24087     3 RLRKITDHFISELEKGLSKKGGN---IPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGgNGKF---DITQSKYR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 534 IPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVS--LPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLLKE 611
Cdd:cd24087    77 LPEELKTGTGEELWDFIADCLKKFVEEHFPGGKSepLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 612 AIHRREeFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVE----GEEGRMCVNMEWGAFgDN 687
Cdd:cd24087   157 ALKKRN-VPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEhddiPPDSPMAINCEYGAF-DN 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 688 GCLDDFRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCL 767
Cdd:cd24087   235 EHLVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDPF 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 768 A-LLQVRAILQH-LGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRirenRGLDalKVTVGVDGTLYKLHPHFAK 845
Cdd:cd24087   315 EnLEDTDDLFQHfFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKK----RGYK--TCHVAADGSVYNKYPGFKE 388

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1705100392 846 VMHETVKDL----APKCDVSFLQSEDGSGKGAALITAVA 880
Cdd:cd24087   389 RAAQALKDIfgwdGEDDPIKTVPAEDGSGVGAAIIAALT 427
ASKHA_NBD_HK_plant cd24020
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 6-432 1.96e-118

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: 367.37  E-value: 1.96e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   6 ETLLEISKRFRKEMEKGLGATTHptAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMENQIYA 85
Cdd:cd24020     4 SRLRQVADAMVVEMEAGLASEGG--SKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  86 IPEDIMRGSGTQLFDHIAECLANFMDK----LQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALI 161
Cdd:cd24020    82 IPPELMVGTSEELFDFIAGELAKFVATegegFHPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVELL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 162 RKAIQRRGdFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVEGD---EGRMCINMEWGAFGd 238
Cdd:cd24020   162 EEALERQG-LDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGlprSGEMVINTEWGNFR- 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 239 dgSLNDIRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEG-E 317
Cdd:cd24020   240 --SSHLPRTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMHEdD 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 318 KDGIRKAREVLMR-LGLDPTQ-EDCVATHRICQIVSTRSASLCAATLAAVLQRI--KENKGEERLRSTIGVDGSVYKKHP 393
Cdd:cd24020   318 SPDLETVARILKDaLGIDDTSlEARKVVVEVCDLVAERGARLAAAGIVGILKKLgrDGGGSSPAQRTVVAVDGGLYEHYP 397

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1705100392 394 HFAKRLHKTVRRLV---PGCDVRFLRSEDGSGKGAAMVTAVA 432
Cdd:cd24020   398 KFREYMQQALVELLgdeAADSVELELSNDGSGIGAALLAAAH 439
PTZ00107 PTZ00107
hexokinase; Provisional
 1-432 2.07e-116

hexokinase; Provisional


Pssm-ID: 240270 [Multi-domain]  Cd Length: 464  Bit Score: 362.84  E-value: 2.07e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   1 MRLSDETLLEISKRFRKEMEKGL-GATTHPTA------AVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNG 73
Cdd:PTZ00107   18 FTMSKEKLKELVDYFLYELVEGLeAHRRHRNLwipnecSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFRAVRVSLRGGG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  74 lqKVEMENQIYAIPEDIMRG---------SGTQLFDHIAECLANFMDKLQIKD---KKLPLGFTFSFPCHQTKLDESFLV 141
Cdd:PTZ00107   98 --KMERTQSKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDPEdlnKPVPVGFTFSFPCTQLSVNNAILI 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 142 SWTKGFKSS-----GVEGRDVVALIRKAIQRRGdFDIDIVAVVNDTVGTMMTCGYDDH----NCEIGLIVGTGSNACYME 212
Cdd:PTZ00107  176 DWTKGFETGratndPVEGKDVGELLNDAFKRNN-VPANVVAVLNDTVGTLISCAYQKPkntpPCQVGVIIGTGSNACYFE 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 213 emrhiDMVE--GDEGRMcINMEWGAFgdDGSLNdiRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEel 290
Cdd:PTZ00107  255 -----PEVSayGYAGTP-INMECGNF--DSKLP--ITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLLQL-- 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 291 lfggKLSPELLNTGRFETKDISDIEGEK-DGIRKAREVLMRL-GLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQR 368
Cdd:PTZ00107  323 ----KAPPKMWQSGSFESEDASMILNDQsPDLQFSRQVIKEAwDVDLTDEDLYTIRKICELVRGRAAQLAAAFIAAPAKK 398

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1705100392 369 IKENKGeerlRSTIGVDGSVYKKHPHFAKRLHKTVRRLV--PGCDVRFLRSEDGSGKGAAMVTAVA 432
Cdd:PTZ00107  399 TRTVQG----KATVAIDGSVYVKNPWFRRLLQEYINSILgpDAGNVVFYLADDGSGKGAAIIAAMV 460
ASKHA_NBD_HK1-2_fungi cd24087
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ...
 6-432 1.15e-111

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: 348.98  E-value: 1.15e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   6 ETLLEISKRFRKEMEKGLgatTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGlqKVEMENQIYA 85
Cdd:cd24087     2 ERLRKITDHFISELEKGL---SKKGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNG--KFDITQSKYR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  86 IPEDIMRGSGTQLFDHIAECLANFMDK--LQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALIRK 163
Cdd:cd24087    77 LPEELKTGTGEELWDFIADCLKKFVEEhfPGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 164 AIQRRGdFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVE----GDEGRMCINMEWGAFgDD 239
Cdd:cd24087   157 ALKKRN-VPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEhddiPPDSPMAINCEYGAF-DN 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 240 GSLNDIRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEG--- 316
Cdd:cd24087   235 EHLVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEdpf 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 317 ----EKDGIrkareVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEerlrstIGVDGSVYKKH 392
Cdd:cd24087   315 enleDTDDL-----FQHFFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKKRGYKTCH------VAADGSVYNKY 383

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1705100392 393 PHFAKRLHKTVRRLV--PGCD--VRFLRSEDGSGKGAAMVTAVA 432
Cdd:cd24087   384 PGFKERAAQALKDIFgwDGEDdpIKTVPAEDGSGVGAAIIAALT 427
ASKHA_NBD_GLK1-2_fungi cd24088
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ...
 5-428 8.82e-111

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: 347.46  E-value: 8.82e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   5 DETLLEISKRFRKEMEKGLgatTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVlwVKVTDNGLQKVEMENQIY 84
Cdd:cd24088     1 DEKLDKLTAEFQRQMEKGL---AKHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRV--CSVELHGDGTFSLRQEKS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  85 AIPEDIMRG-SGTQLFDHIAECLANFMDK-------LQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRD 156
Cdd:cd24088    76 KIPDELKTGvTAKDLFDYLAKSVEAFLTKhhgdsfaAGKDDDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 157 VVALIRKAIQRRGdFDIDIVAVVNDTVGTMMTCGYDDHNCE---IGLIVGTGSNACYMEEMRHI---DMVEGDE---GRM 227
Cdd:cd24088   156 VVKLLQDELDRQG-IPVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIkklDDSSRVGkgkTHM 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 228 CINMEWGAFgdDGSLNDI-RTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKL--SPELLNTG 304
Cdd:cd24088   235 VINTEWGSF--DNELKVLpTTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFLIQYNdkSPSALNTP 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 305 -RFETKDISDIEG-EKDGIRKAREVLMR-LGL-DPTQEDCVATHRICQIVSTRSASLCAATLAAVLqrIKENK--GEERL 378
Cdd:cd24088   313 yGLDTAVLSAIEIdSEAELRATRKVLLDdLGLpAPSLEDAEAVRKISRAIGRRAARLSAVAIAAIL--IKTGAlnKSYDG 390

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1705100392 379 RSTIGVDGSVYKKHPHFAKRLHKTVRRLVPGC----DVRFLRSEDGSGKGAAMV 428
Cdd:cd24088   391 EINIGVDGSVIEFYPGFESMLREALRLLLIGAegekRIKIGIAKDGSGVGAALC 444
ASKHA_NBD_GLK1-2_fungi cd24088
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ...
 455-876 8.57e-110

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: 344.76  E-value: 8.57e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 455 QLLEVKRRMKVEMERGLSketHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVrNGKwGGVEMHNKIYAI 534
Cdd:cd24088     3 KLDKLTAEFQRQMEKGLA---KHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVEL-HGD-GTFSLRQEKSKI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 535 PQEVMHG-TGDELFDHIVQCIADFL-EYMGMKGVS------LPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEGEDVV 606
Cdd:cd24088    78 PDELKTGvTAKDLFDYLAKSVEAFLtKHHGDSFAAgkdddrLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 607 TLLKEAIHRREeFDLDVVAVVNDTVGTMMTCGFEDPHCE---VGLIVGTGSNACYMEEMRNV------ELVEGEEGRMCV 677
Cdd:cd24088   158 KLLQDELDRQG-IPVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIkklddsSRVGKGKTHMVI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 678 NMEWGAFgdngclDDFR-----TEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLL---FRGRISERLK 749
Cdd:cd24088   237 NTEWGSF------DNELkvlptTPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFliqYNDKSPSALN 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 750 TRGIFETKFLSQIESDCLALLQV--RAILQHLGLES-TCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRIRENRGLDAL 826
Cdd:cd24088   311 TPYGLDTAVLSAIEIDSEAELRAtrKVLLDDLGLPApSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSYDG 390

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1705100392 827 KVTVGVDGTLYKLHPHFAKVMHETVKDLAP----KCDVSFLQSEDGSGKGAALI 876
Cdd:cd24088   391 EINIGVDGSVIEFYPGFESMLREALRLLLIgaegEKRIKIGIAKDGSGVGAALC 444
Hexokinase_2 pfam03727
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 645-879 1.26e-107

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: 331.38  E-value: 1.26e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 645 EVGLIVGTGSNACYMEEMRNVELVEG---EEGRMCVNMEWGAFGDNGCLDDFRTEFDVAVDELSLNPGKQRFEKMISGMY 721
Cdd:pfam03727   1 RIGLILGTGTNAAYVEKVSNIPKLEGklpKSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 722 LGEIVRNILIDFTKRGLLFRGRiSERLKTRGIFETKFLSQIESD-CLALLQVRAILQ-HLGLES-TCDDSIIVKEVCTVV 798
Cdd:pfam03727  81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDpSEDLETTREILEeLLGIETvTEEDRKIVRRICEAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 799 ARRAAQLCGAGMAAVVDRIRENRgldalKVTVGVDGTLYKLHPHFAKVMHETVKD-LAPKCDVSFLQSEDGSGKGAALIT 877
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-----KVTVGVDGSVYEKYPGFRERLQEALRElLGPGDKVVLVLAEDGSGVGAALIA 234


                  ..
gi 1705100392 878 AV 879
Cdd:pfam03727 235 AV 236
PTZ00107 PTZ00107
hexokinase; Provisional
 434-880 5.16e-105

hexokinase; Provisional


Pssm-ID: 240270 [Multi-domain]  Cd Length: 464  Bit Score: 333.18  E-value: 5.16e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 434 RLADQHRARQKTLEHLQLSHDQLLEVKRRMKVEMERGL-SKETHASA------PVKMLPTYVCATPDGTEKGDFLALDLG 506
Cdd:PTZ00107    3 RYIKQRVRLASLVNQFTMSKEKLKELVDYFLYELVEGLeAHRRHRNLwipnecSFKMLDSCVYNLPTGKEKGVYYAIDFG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 507 GTNFRVLLVRVRNGkwGGVEMHNKIYAIPQEVM---------HGTGDELFDHIVQCIADFLEYMGMK---GVSLPLGFTF 574
Cdd:PTZ00107   83 GTNFRAVRVSLRGG--GKMERTQSKFSLPKSALlgekglldkKATATDLFDHIAKSIKKMMEENGDPedlNKPVPVGFTF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 575 SFPCQQNSLDESILLKWTKGFKAS-----GCEGEDVVTLLKEAIhRREEFDLDVVAVVNDTVGTMMTCGFED----PHCE 645
Cdd:PTZ00107  161 SFPCTQLSVNNAILIDWTKGFETGratndPVEGKDVGELLNDAF-KRNNVPANVVAVLNDTVGTLISCAYQKpkntPPCQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 646 VGLIVGTGSNACYMEEMrnvELVEGEEGRMcVNMEWGAFgdngCLDDFRTEFDVAVDELSLNPGKQRFEKMISGMYLGEI 725
Cdd:PTZ00107  240 VGVIIGTGSNACYFEPE---VSAYGYAGTP-INMECGNF----DSKLPITPYDLEMDWYTPNRGRQQFEKMISGAYLGEI 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 726 VRNILIdftkrgLLFRGRISERLKTRGIFETKFLSQIESDCLALLQV--RAILQHLGLESTCDDSIIVKEVCTVVARRAA 803
Cdd:PTZ00107  312 SRRLIV------HLLQLKAPPKMWQSGSFESEDASMILNDQSPDLQFsrQVIKEAWDVDLTDEDLYTIRKICELVRGRAA 385

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1705100392 804 QLCGAGMAAVVDRIRENRGldalKVTVGVDGTLYKLHPHFAKVMHETVKD-LAPK-CDVSFLQSEDGSGKGAALITAVA 880
Cdd:PTZ00107  386 QLAAAFIAAPAKKTRTVQG----KATVAIDGSVYVKNPWFRRLLQEYINSiLGPDaGNVVFYLADDGSGKGAAIIAAMV 460
Hexokinase_2 pfam03727
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 197-431 4.79e-103

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: 319.44  E-value: 4.79e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 197 EIGLIVGTGSNACYMEEMRHIDMVEGD---EGRMCINMEWGAFGDDGSLNDIRTEFDQEIDMGSLNPGKQLFEKMISGMY 273
Cdd:pfam03727   1 RIGLILGTGTNAAYVEKVSNIPKLEGKlpkSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 274 MGELVRLILVKMAKEELLFGGKlSPELLNTGRFETKDISDIEGEK-DGIRKAREVLMR-LGL-DPTQEDCVATHRICQIV 350
Cdd:pfam03727  81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDPsEDLETTREILEElLGIeTVTEEDRKIVRRICEAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 351 STRSASLCAATLAAVLQRIKENKgeerlRSTIGVDGSVYKKHPHFAKRLHKTVRRLV-PGCDVRFLRSEDGSGKGAAMVT 429
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-----KVTVGVDGSVYEKYPGFRERLQEALRELLgPGDKVVLVLAEDGSGVGAALIA 234


                  ..
gi 1705100392 430 AV 431
Cdd:pfam03727 235 AV 236
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 1-432 5.00e-102

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


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 324.22  E-value: 5.00e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   1 MRLSDETLLEISKRFRKEMEKGLgatTHPTAAVKMLPTFVrSTPDG-TEHGEFLALDLGGTNFRVLWVKVTDNGlqKVEM 79
Cdd:COG5026    15 FDLSSIDLEEIAAKFQEEMEKGL---EGKKSSLKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRFDGEG--TFEI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  80 ENQIyAIPediMRGSG-----TQLFDHIAECLAnfmdklQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEG 154
Cdd:COG5026    89 ENFK-SFP---LPGTSseitaEEFFDFIADYIE------PLLDESYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 155 RDVVALIRKAIQRRGDFDIDIVAVVNDTVGTMMTCGY----DDHNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCIN 230
Cdd:COG5026   159 KNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYadpdDGYSGYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMIIN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 231 MEWGAFgdDGSLndiRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEElLFGGKLSPELLNTGRFETKD 310
Cdd:COG5026   239 MESGNF--NKLP---RTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTVD 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 311 ISDIEGEKDGirkAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERlRSTIGVDGSVYK 390
Cdd:COG5026   313 MSRFLADPSD---EKEILSQCLEAGSEEDREILREIADAIVERAARLVAATLAGILLHLGPGKTPLK-PHCIAIDGSTYE 388

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1705100392 391 KHPHFAKRLHKTVRRLVPGCD---VRFLRSEDGSGKGAAMVTAVA 432
Cdd:COG5026   389 KMPGLAEKIEYALQEYLLGEKgryVEFVLVENASLLGAAIAAALN 433
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 448-881 5.49e-99

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


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 316.13  E-value: 5.49e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 448 HLQLSHDQLLEVKRRMKVEMERGLSketHASAPVKMLPTYVcATPDG-TEKGDFLALDLGGTNFRVLLVRVrNGKwGGVE 526
Cdd:COG5026    14 GFDLSSIDLEEIAAKFQEEMEKGLE---GKKSSLKMLPSYL-GLPTGvKETGPVIALDAGGTNFRVALVRF-DGE-GTFE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 527 MHN-KIYAIP---QEVmhgTGDELFDHIVQCIADFLEYmgmkgvSLPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEG 602
Cdd:COG5026    88 IENfKSFPLPgtsSEI---TAEEFFDFIADYIEPLLDE------SYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 603 EDVVTLLKEAIHRREEFDLDVVAVVNDTVGTMMTCGFEDP----HCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVN 678
Cdd:COG5026   159 KNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPddgySGYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMIIN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 679 MEWGAFgdNGCLddfRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGlLFRGRISERLKTRGIFETKF 758
Cdd:COG5026   239 MESGNF--NKLP---RTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTVD 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 759 LSQI---ESDclALLQVRAILQhlglESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVdrIRENRGLDALK-VTVGVDG 834
Cdd:COG5026   313 MSRFladPSD--EKEILSQCLE----AGSEEDREILREIADAIVERAARLVAATLAGIL--LHLGPGKTPLKpHCIAIDG 384

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1705100392 835 TLYKLHPHFAKVMHETVKD-LAPKCD--VSFLQSEDGSGKGAALITAVAC 881
Cdd:COG5026   385 STYEKMPGLAEKIEYALQEyLLGEKGryVEFVLVENASLLGAAIAAALNE 434
PLN02914 PLN02914
hexokinase
 446-878 7.51e-97

hexokinase


Pssm-ID: 178502 [Multi-domain]  Cd Length: 490  Bit Score: 312.20  E-value: 7.51e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 446 LEHLQLSHDQLLEVKRR----MKVEMERGLSKEthASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGK 521
Cdd:PLN02914   41 LTKLQKDCATPLPVLRHvadaMAADMRAGLAVD--GGGDLKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKD 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 522 WGGVEMHNKIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMK-----GVSLPLGFTFSFPCQQNSLDESILLKWTKGFK 596
Cdd:PLN02914  119 ERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFVAKEGGKfhlpeGRKREIGFTFSFPVKQTSIDSGILMKWTKGFA 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 597 ASGCEGEDVVTLLKEAIHRrEEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEG---EEG 673
Cdd:PLN02914  199 VSGTAGKDVVACLNEAMER-QGLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGqksSSG 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 674 RMCVNMEWGAFGDNGCLddfrTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGI 753
Cdd:PLN02914  278 RTIINTEWGAFSDGLPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFA 353

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 754 FETKFLSQIESDCLALLQ-VRAILQH-LGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRIREN-RGLDALKVT- 829
Cdd:PLN02914  354 LRTPHLCAMQQDNSDDLQaVGSILYDvLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDsKGMIFGKRTv 433

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1705100392 830 VGVDGTLYKLHPHFAKVMHETVKD-LAPKC--DVSFLQSEDGSGKGAALITA 878
Cdd:PLN02914  434 VAMDGGLYEKYPQYRRYMQDAVTElLGLELskNIAIEHTKDGSGIGAALLAA 485
Hexokinase_1 pfam00349
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 443-639 2.55e-92

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: 289.40  E-value: 2.55e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 443 QKTLEHLQLSHDQLLEVKRRMKVEMERGLSKETHASapVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVrnGKW 522
Cdd:pfam00349   3 EELLKQFALSDEKLKEIVDRFVEEMEKGLAKEGSSS--LKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVEL--GGD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 523 GGVEMHNKIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMK---GVSLPLGFTFSFPCQQNSLDESILLKWTKGFKASG 599
Cdd:pfam00349  79 GKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEdfeEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDIPG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1705100392 600 CEGEDVVTLLKEAIHRREEfDLDVVAVVNDTVGTMMTCGF 639
Cdd:pfam00349 159 VVGKDVVQLLQEALERRGL-PVKVVALVNDTVGTLMAGAY 197
Hexokinase_1 pfam00349
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 1-191 3.75e-92

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: 289.02  E-value: 3.75e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   1 MRLSDETLLEISKRFRKEMEKGLGAttHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGlqKVEME 80
Cdd:pfam00349   9 FALSDEKLKEIVDRFVEEMEKGLAK--EGSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELGGDG--KFEIT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  81 NQIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKD---KKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDV 157
Cdd:pfam00349  85 QEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDfeeKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDIPGVVGKDV 164

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1705100392 158 VALIRKAIQRRGDfDIDIVAVVNDTVGTMMTCGY 191
Cdd:pfam00349 165 VQLLQEALERRGL-PVKVVALVNDTVGTLMAGAY 197
PLN02914 PLN02914
hexokinase
 33-430 8.84e-89

hexokinase


Pssm-ID: 178502 [Multi-domain]  Cd Length: 490  Bit Score: 291.02  E-value: 8.84e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  33 VKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMENQIYAIPEDIMRGSGTQLFDHIAECLANFMDK 112
Cdd:PLN02914   78 LKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFVAK 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 113 LQIK-----DKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALIRKAIQRRGdFDIDIVAVVNDTVGTMM 187
Cdd:PLN02914  158 EGGKfhlpeGRKREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLNEAMERQG-LDMRVSALVNDTVGTLA 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 188 TCGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVEGDE---GRMCINMEWGAFGDDGSLndirTEFDQEIDMGSLNPGKQL 264
Cdd:PLN02914  237 GARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKsssGRTIINTEWGAFSDGLPL----TEFDREMDAASINPGEQI 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 265 FEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGE-KDGIRKAREVLMR-LGLDPTQEDCVA 342
Cdd:PLN02914  313 FEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALRTPHLCAMQQDnSDDLQAVGSILYDvLGVEASLSARRR 392

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 343 THRICQIVSTRSASLCAATLAAVLQRIKENKgeERL----RSTIGVDGSVYKKHPHFAKRLHKTVRRLVP---GCDVRFL 415
Cdd:PLN02914  393 VVEVCDTIVKRGGRLAGAGIVGILEKMEEDS--KGMifgkRTVVAMDGGLYEKYPQYRRYMQDAVTELLGlelSKNIAIE 470

                         410
                  ....*....|....*
gi 1705100392 416 RSEDGSGKGAAMVTA 430
Cdd:PLN02914  471 HTKDGSGIGAALLAA 485
PLN02362 PLN02362
hexokinase
 455-878 2.47e-79

hexokinase


Pssm-ID: 215206 [Multi-domain]  Cd Length: 509  Bit Score: 265.98  E-value: 2.47e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 455 QLLEVKRRMKVEMERGLSKEthASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVrNGKWGGVEMHN-KIYA 533
Cdd:PLN02362   54 RLRQVVDAMAVEMHAGLASE--GGSKLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQL-GGQRSSILSQDvERHP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 534 IPQEVMHGTGDELFDHIVQCIADFLEYMG-----MKGVSLPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTL 608
Cdd:PLN02362  131 IPQHLMNSTSEVLFDFIASSLKQFVEKEEngsefSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAEC 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 609 LKEAIHRReEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEG---EEGRMCVNMEWGAFG 685
Cdd:PLN02362  211 LQGALNRR-GLDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQGlltTSGSMVVNMEWGNFW 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 686 DNGCLddfRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFrGRISERLKTRGIFETKFLSQI-ES 764
Cdd:PLN02362  290 SSHLP---RTSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVAAMhED 365

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 765 DCLALLQVRAILQH-LGL-ESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRI-RENRGLDAL-----------KVTV 830
Cdd:PLN02362  366 DSPELQEVARILKEtLGIsEVPLKVRKLVVKICDVVTRRAARLAAAGIVGILKKIgRDGSGGITSgrsrsdiqimrRTVV 445

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1705100392 831 GVDGTLYKLHPHFAKVMHETVKDLAPKcDVS----FLQSEDGSGKGAALITA 878
Cdd:PLN02362  446 AVEGGLYTNYTMFREYLHEALNEILGE-DVAqhviLKATEDGSGIGSALLAA 496
PLN02405 PLN02405
hexokinase
 18-430 2.58e-79

hexokinase


Pssm-ID: 215226 [Multi-domain]  Cd Length: 497  Bit Score: 265.54  E-value: 2.58e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  18 EMEKGLGatTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKV--TDNGLQKVEMENQiyAIPEDIMRGSG 95
Cdd:PLN02405   65 EMHAGLA--SEGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLggKDGRVVKQEFEEV--SIPPHLMTGSS 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  96 TQLFDHIAECLANFMDKlQIKDKKLP------LGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALIRKAIQRRG 169
Cdd:PLN02405  141 DALFDFIAAALAKFVAT-EGEDFHLPpgrqreLGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTKAMERVG 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 170 dFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVEGD---EGRMCINMEWGAFGddgSLNDIR 246
Cdd:PLN02405  220 -LDMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGLlpkSGEMVINMEWGNFR---SSHLPL 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 247 TEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDIS-------------- 312
Cdd:PLN02405  296 TEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSamhhdtspdlkvvg 375

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 313 ----DIEGEKDGIRKAREVLMRLgldptqedcvathriCQIVSTRSASLCAATLAAVLQRIKEN--KGEERLRSTIGVDG 386
Cdd:PLN02405  376 sklkDILEIPNTSLKMRKVVVEL---------------CNIVATRGARLSAAGIYGILKKLGRDtvKDGEKQKSVIAMDG 440

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1705100392 387 SVYKKHPHFAKRLHKTVRRLVpGCDVR----FLRSEDGSGKGAAMVTA 430
Cdd:PLN02405  441 GLFEHYTEFSKCMESTLKELL-GEEVSesieVEHSNDGSGIGAALLAA 487
PLN02405 PLN02405
hexokinase
 455-878 7.35e-79

hexokinase


Pssm-ID: 215226 [Multi-domain]  Cd Length: 497  Bit Score: 264.39  E-value: 7.35e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 455 QLLEVKRRMKVEMERGLSKEthASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVrNGKWGG-VEMHNKIYA 533
Cdd:PLN02405   54 KLRQVADAMTVEMHAGLASE--GGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLL-GGKDGRvVKQEFEEVS 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 534 IPQEVMHGTGDELFDHIVQCIADFLEYMGmKGVSLP------LGFTFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVT 607
Cdd:PLN02405  131 IPPHLMTGSSDALFDFIAAALAKFVATEG-EDFHLPpgrqreLGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVG 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 608 LLKEAIhRREEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEG---EEGRMCVNMEWGaf 684
Cdd:PLN02405  210 ELTKAM-ERVGLDMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGllpKSGEMVINMEWG-- 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 685 gdngcldDFR------TEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKF 758
Cdd:PLN02405  287 -------NFRsshlplTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPD 359

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 759 LSQIESDCLALLQVRAILQHLGLE---STCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRIREN--RGLDALKVTVGVD 833
Cdd:PLN02405  360 MSAMHHDTSPDLKVVGSKLKDILEipnTSLKMRKVVVELCNIVATRGARLSAAGIYGILKKLGRDtvKDGEKQKSVIAMD 439

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1705100392 834 GTLYKLHPHFAKVMHETVKDLAPK---CDVSFLQSEDGSGKGAALITA 878
Cdd:PLN02405  440 GGLFEHYTEFSKCMESTLKELLGEevsESIEVEHSNDGSGIGAALLAA 487
PLN02362 PLN02362
hexokinase
 18-430 4.76e-70

hexokinase


Pssm-ID: 215206 [Multi-domain]  Cd Length: 509  Bit Score: 240.94  E-value: 4.76e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  18 EMEKGLgaTTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTD--NGLQKVEMENQiyAIPEDIMRGSG 95
Cdd:PLN02362   65 EMHAGL--ASEGGSKLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGGqrSSILSQDVERH--PIPQHLMNSTS 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  96 TQLFDHIAECLANFMDKLQ-----IKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALIRKAIQRRGd 170
Cdd:PLN02362  141 EVLFDFIASSLKQFVEKEEngsefSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRRG- 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 171 FDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVEG---DEGRMCINMEWGAFGddgSLNDIRT 247
Cdd:PLN02362  220 LDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQGlltTSGSMVVNMEWGNFW---SSHLPRT 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 248 EFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFG---GKLS-PELLNTGRF---------ETKDISDI 314
Cdd:PLN02362  297 SYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIFGpvsSRLStPFVLRTPSVaamheddspELQEVARI 376

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 315 EGEKDGIR----KAREVLMrlgldptqedcvathRICQIVSTRSASLCAATLAAVLQRIKE----------NKGEERL-- 378
Cdd:PLN02362  377 LKETLGISevplKVRKLVV---------------KICDVVTRRAARLAAAGIVGILKKIGRdgsggitsgrSRSDIQImr 441

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1705100392 379 RSTIGVDGSVYKKHPHFAKRLHKTVRRLVpGCDVR----FLRSEDGSGKGAAMVTA 430
Cdd:PLN02362  442 RTVVAVEGGLYTNYTMFREYLHEALNEIL-GEDVAqhviLKATEDGSGIGSALLAA 496
PLN02596 PLN02596
hexokinase-like
 8-430 3.51e-52

hexokinase-like


Pssm-ID: 178206 [Multi-domain]  Cd Length: 490  Bit Score: 190.47  E-value: 3.51e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392   8 LLEISKRFRKEMEKGLgaTTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMENQIYAIP 87
Cdd:PLN02596   56 LWEVADALVSDMTASL--TAEETTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNEPISDLYREEISIP 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392  88 EDIMRGSGTQLFDHIAECLANFM-----DKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWtKGFKSSGVEGRDVVALIR 162
Cdd:PLN02596  134 SNVLNGTSQELFDYIALELAKFVaehpgDEADTPERVKKLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDIN 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 163 KAIQRRGdFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVEG---DEGRMCINMEWGAFGdd 239
Cdd:PLN02596  213 RALEKHG-LKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSpspESQEIVISTEWGNFN-- 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 240 gSLNDIRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDIS----DIE 315
Cdd:PLN02596  290 -SCHLPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAamhqDTS 368

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 316 GEKDGI-RKAREVLMRLGLDPTQEDCVAthRICQIVSTRSASLCAATLAAVLQRIK--ENKgeerlRSTIGVDGSVYKKH 392
Cdd:PLN02596  369 EDHEVVnEKLKEIFGITDSTPMAREVVA--EVCDIVAERGARLAGAGIVGIIKKLGriENK-----KSVVTVEGGLYEHY 441

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1705100392 393 PHFAKRLHKTVRRLVpGCD----VRFLRSEDGSGKGAAMVTA 430
Cdd:PLN02596  442 RVFRNYLHSSVWEML-GSElsdnVVIEHSHGGSGAGALFLAA 482
PLN02596 PLN02596
hexokinase-like
 455-878 5.06e-50

hexokinase-like


Pssm-ID: 178206 [Multi-domain]  Cd Length: 490  Bit Score: 184.31  E-value: 5.06e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 455 QLLEVKRRMKVEMERGLSKETHASapVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWGGVEMHNKIYAI 534
Cdd:PLN02596   55 KLWEVADALVSDMTASLTAEETTT--LNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNEPISDLYREEISI 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 535 PQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLP-----LGFTFSFPCQQNSLDESILLKWtKGFKASGCEGEDVVTLL 609
Cdd:PLN02596  133 PSNVLNGTSQELFDYIALELAKFVAEHPGDEADTPervkkLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDI 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 610 KEAIHRrEEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEG---EEGRMCVNMEWGAFGd 686
Cdd:PLN02596  212 NRALEK-HGLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSpspESQEIVISTEWGNFN- 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 687 ngCLDDFRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDC 766
Cdd:PLN02596  290 --SCHLPITEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAAMHQDT 367

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 767 LALLQV--RAILQHLGL-ESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRIR--ENRgldalKVTVGVDGTLYKLHP 841
Cdd:PLN02596  368 SEDHEVvnEKLKEIFGItDSTPMAREVVAEVCDIVAERGARLAGAGIVGIIKKLGriENK-----KSVVTVEGGLYEHYR 442

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1705100392 842 HFAKVMHETV-----KDLAPkcDVSFLQSEDGSGKGAALITA 878
Cdd:PLN02596  443 VFRNYLHSSVwemlgSELSD--NVVIEHSHGGSGAGALFLAA 482
ASKHA_NBD_NAGK_meta cd24078
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ...
 579-655 4.40e-04

nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; NAGK (EC 2.7.1.59), also called N-acetylglucosamine kinase, or GlcNAc kinase, converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. It is involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. NAGK also has ManNAc kinase activity. Members in this family are mainly from metazoa.


Pssm-ID: 466928 [Multi-domain]  Cd Length: 314  Bit Score: 43.34  E-value: 4.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 579 QQNSLDESILLKwTKGFKASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVGTMMTCgfedphCEVG---LIVGTGSN 655
Cdd:cd24078    55 KKAGLDPDTPLK-SLGLSLSGAEQEEAQEELIEGLRSRYPNLSESYYVTSDTVGAIATA------FENGgivLISGTGSN 127
BadF COG2971
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ...
 150-241 9.64e-04

BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];


Pssm-ID: 442210 [Multi-domain]  Cd Length: 298  Bit Score: 42.18  E-value: 9.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705100392 150 SGVEGRDVVALIRKAIQRRGDFDIdiVAVVNDTVGTMMtCGYDDHNCeIGLIVGTGSNACYMEEMRHIDMVEGdegrmci 229
Cdd:COG2971    72 AGAGTPEDAEALEAALRELFPFAR--VVVVNDALAALA-GALGGEDG-IVVIAGTGSIAAGRDGDGRTARVGG------- 140

                          90
                  ....*....|...
gi 1705100392 230 nmeWG-AFGDDGS 241
Cdd:COG2971   141 ---WGyLLGDEGS 150
 
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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