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Conserved domains on  [gi|8572069|gb|AAF76986|]
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fructose-6-phosphate 2-kinase/fructose-2,6-bisphosphatase [Arabidopsis thaliana]

Protein Classification

6PF2K and HP_PGM_like domain-containing protein (domain architecture ID 11279677)

protein containing domains CBM_2, 6PF2K, and HP_PGM_like

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
6PF2K pfam01591
6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2, ...
335-551 7.90e-102

6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2,6-bisphosphatase. The bifunctional enzyme catalyzes both the synthesis and degradation of fructose-2,6-bisphosphate, a potent regulator of glycolysis. This enzyme contains a P-loop motif.


:

Pssm-ID: 334602  Cd Length: 219  Bit Score: 311.58  E-value: 7.90e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069    335 MLGPK-EDRHLAIVLVGLPARGKTFTAAKLTRYLRWLGHDTKHFNVGKYRRLKHGVNMSADFFRADNPEGVEARTEVAAL 413
Cdd:pfam01591   1 STGPNfTNSKTLIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRRSAVKAYSDYEFFRPDNEEGMKIREQCALA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069    414 AMEDMIAWMQ-EGGQVGIFDATNSTRVRRNMLMKMAEG-KCKIIFLETLCNDERIIERNIRLKIQQSPDYSEEMDFEAgV 491
Cdd:pfam01591  81 ALNDVLAYLNeESGQVAIFDATNTTRERRKMILDFAEEnGLKVFFLESICDDPEIIARNIKLVKFSSPDYKGKPPEEA-I 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8572069    492 RDFRDRLANYEKVYEPVEE-GSYIKMIDMVSGnGGQIQVNNISGYLPGRIVFFLVNTHLTP 551
Cdd:pfam01591 160 DDFMKRIECYEKQYEPLDEhDEDLSYIKVIDV-GQSIVVNNVQGYLQSRIVYYLMNIHVTP 219
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
554-729 3.81e-43

Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so named because catalysis centers on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches. The larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members.


:

Pssm-ID: 333990 [Multi-domain]  Cd Length: 193  Bit Score: 154.28  E-value: 3.81e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069    554 ILLTRHGESMDNVRGRIGG--DSVISDSGKLYAKKLAsfveKRLKSEKAASIWTSTLQRTNLTASSI---VGFPKVQWRA 628
Cdd:pfam00300   1 LYLVRHGETEWNLEGRLQGrtDSPLTERGREQAEALA----ERLAGEPFDAIYSSPLKRARQTAEIIaeaLGLPVEIDER 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069    629 LDEINAGVCDGMTYEEVKKNMPEEYESRKKDKLRYRYPRGESYLDVIQRLEPVIIELERQRAP--VVVISHQAVLRALYA 706
Cdd:pfam00300  77 LREIDFGDWEGLTFAEIRERYPEEYAAWLADPADYRPPGGESLADVQARVRAALEELAARHPGktVLVVSHGGVIRALLA 156
                         170       180
                  ....*....|....*....|...
gi 8572069    707 YFADRPLKEIPQIEMPLHTIIEI 729
Cdd:pfam00300 157 HLLGLPLEELRRFELDNASLTIL 179
CBM_2 smart01065
Starch binding domain;
25-110 4.86e-16

Starch binding domain;


:

Pssm-ID: 215006  Cd Length: 88  Bit Score: 73.54  E-value: 4.86e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069      25 VSLKMENSKVEGELTPHVYGSLPLIGSWDPSKALPMQRESA--LMSELSFVVPPDHETLDFKFLLKPKNRNtpCIVEEGE 102
Cdd:smart01065   3 VTFKVRNGYTQPGESVYVVGSVPELGNWNPKKAVPLSPDTDgyPLWKGTVSLPPAGTTIEYKYVKVDEDGS--VTWESGP 80

                   ....*...
gi 8572069     103 NRLLTGGS 110
Cdd:smart01065  81 NRRLTVPE 88
 
Name Accession Description Interval E-value
6PF2K pfam01591
6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2, ...
335-551 7.90e-102

6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2,6-bisphosphatase. The bifunctional enzyme catalyzes both the synthesis and degradation of fructose-2,6-bisphosphate, a potent regulator of glycolysis. This enzyme contains a P-loop motif.


Pssm-ID: 334602  Cd Length: 219  Bit Score: 311.58  E-value: 7.90e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069    335 MLGPK-EDRHLAIVLVGLPARGKTFTAAKLTRYLRWLGHDTKHFNVGKYRRLKHGVNMSADFFRADNPEGVEARTEVAAL 413
Cdd:pfam01591   1 STGPNfTNSKTLIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRRSAVKAYSDYEFFRPDNEEGMKIREQCALA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069    414 AMEDMIAWMQ-EGGQVGIFDATNSTRVRRNMLMKMAEG-KCKIIFLETLCNDERIIERNIRLKIQQSPDYSEEMDFEAgV 491
Cdd:pfam01591  81 ALNDVLAYLNeESGQVAIFDATNTTRERRKMILDFAEEnGLKVFFLESICDDPEIIARNIKLVKFSSPDYKGKPPEEA-I 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8572069    492 RDFRDRLANYEKVYEPVEE-GSYIKMIDMVSGnGGQIQVNNISGYLPGRIVFFLVNTHLTP 551
Cdd:pfam01591 160 DDFMKRIECYEKQYEPLDEhDEDLSYIKVIDV-GQSIVVNNVQGYLQSRIVYYLMNIHVTP 219
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
335-738 7.57e-51

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 188.57  E-value: 7.57e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069   335 MLGPkedrhLAIVLVGLPARGKTFTAAKLTRYLRWLGHDTKHFNVGKYRR---LKHGVNMSAdffradnPEGVEARTEVA 411
Cdd:PTZ00322 212 MMGS-----LIVIMVGLPGRGKTYVARQIQRYFQWNGLQSRIFIHQAYRRrleRRGGAVSSP-------TGAAEVEFRIA 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069   412 ALAMEDMIAWMQEGGQVGIFDATNSTRVRRNMLMK--MAEGKC---KIIFLETLCNDERIIERNIRLKIQQSPDYSEemD 486
Cdd:PTZ00322 280 KAIAHDMTTFICKTDGVAVLDGTNTTHARRMALLRaiRETGLIrmtRVVFVEVVNNNSETIRRNVLRAKEMFPGAPE--D 357
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069   487 FeagVRDFRDRLANYEKVYE---PVEEG--SYIKMIDmvsgnGGQIQVNNISGYLPGRIVFFLVNTHLTPRPILLTRHGE 561
Cdd:PTZ00322 358 F---VDRYYEVIEQLEAVYKslnPVTDCdlTYIRIED-----TQTFSLNNISGWMPSRLAYMLHNLNPTPMNLYLTRAGE 429
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069   562 SMDNVRGRIGGDSVISDSGKLYAKKLASFVEKRLkSEKAASIWTS----------------TLQRTNLTASSIVGfPKVQ 625
Cdd:PTZ00322 430 YVDLLSGRIGGNSRLTERGRAYSRALFEYFQKEI-STTSFTVMSScakrctetvhyfaeesILQQSTASAASSQS-PSLN 507
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069   626 WR-----ALDEINAGVCDGMTYEEVKKNMPEEYESRKKDKLRYRYPRGESYLDVIQ-RLEPVIIELERQRAPVVVISHQA 699
Cdd:PTZ00322 508 CRvlyfpTLDDINHGDCEGQLLSDVRRTMPNTLQSMKADPYYTAWPNGECIHQVFNaRLEPHIHDIQASTTPVLVVSHLH 587
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 8572069   700 VLRALYAYFADRPLKEI-PQ----IEMPLHTIIEIQM-GVSGVQE 738
Cdd:PTZ00322 588 LLQGLYSYFVTDGDNIVaPQnaykIDIPFEHVIKIRMvGFNRVAE 632
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
554-729 3.81e-43

Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so named because catalysis centers on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches. The larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members.


Pssm-ID: 333990 [Multi-domain]  Cd Length: 193  Bit Score: 154.28  E-value: 3.81e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069    554 ILLTRHGESMDNVRGRIGG--DSVISDSGKLYAKKLAsfveKRLKSEKAASIWTSTLQRTNLTASSI---VGFPKVQWRA 628
Cdd:pfam00300   1 LYLVRHGETEWNLEGRLQGrtDSPLTERGREQAEALA----ERLAGEPFDAIYSSPLKRARQTAEIIaeaLGLPVEIDER 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069    629 LDEINAGVCDGMTYEEVKKNMPEEYESRKKDKLRYRYPRGESYLDVIQRLEPVIIELERQRAP--VVVISHQAVLRALYA 706
Cdd:pfam00300  77 LREIDFGDWEGLTFAEIRERYPEEYAAWLADPADYRPPGGESLADVQARVRAALEELAARHPGktVLVVSHGGVIRALLA 156
                         170       180
                  ....*....|....*....|...
gi 8572069    707 YFADRPLKEIPQIEMPLHTIIEI 729
Cdd:pfam00300 157 HLLGLPLEELRRFELDNASLTIL 179
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
554-732 3.60e-33

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 223483 [Multi-domain]  Cd Length: 208  Bit Score: 126.83  E-value: 3.60e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069  554 ILLTRHGESMDNVRGRIGG--DSVISDSGKLYAKKLASFVEKRLKSEKAasIWTSTLQRTNLTA---SSIVGFPKVQWRA 628
Cdd:COG0406   5 LYLVRHGETEWNVEGRLQGwtDSPLTEEGRAQAEALAERLAARDIGFDA--IYSSPLKRAQQTAeplAEELGLPLEVDDR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069  629 LDEINAGVCDGMTYEEVKKNMPEEYESRKKDKLRYRYPRGESYLDVIQRLEPVIIELER--QRAPVVVISHQAVLRALYA 706
Cdd:COG0406  83 LREIDFGDWEGLTIDELAEEPPEELAAWLADPYLAPPPGGESLADVSKRVVAALAELLRspPGNNVLVVSHGGVIRALLA 162
                       170       180
                ....*....|....*....|....*...
gi 8572069  707 YFADRPLKEIPQIEMPLH--TIIEIQMG 732
Cdd:COG0406 163 YLLGLDLEELWRLRLDNAsvTVLEFDDG 190
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
554-704 5.54e-31

Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase (BPGM) are structurally related enzymes that catalyse reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate... Both enzymes can catalyse three different reactions with different specificities, the isomerization of 2-phosphoglycerate (2-PGA) to 3-phosphoglycerate (3-PGA) with 2,3-diphosphoglycerate (2,3-DPG) as the primer of the reaction, the synthesis of 2,3-DPG from 1,3-DPG with 3-PGA as a primer and the degradation of 2,3-DPG to 3-PGA (phosphatase activity). In mammals, PGAM is a dimeric protein with two isoforms, the M (muscle) and B (brain) forms. In yeast, PGAM is a tetrameric protein.


Pssm-ID: 214859 [Multi-domain]  Cd Length: 158  Bit Score: 118.72  E-value: 5.54e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069     554 ILLTRHGESMDNVRGRIGG--DSVISDSGKLYAKKLASFVeKRLKSEKAASIWTSTLQRTNLTASsIVGFPKVQWRaLDE 631
Cdd:smart00855   2 LYLIRHGETEWNREGRLYGdtDVPLTELGRAQAEALGRLL-ASLLLPRFDVVYSSPLKRARQTAE-ALAIALGLPG-LRE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069     632 INAGVCDGMTYEEVKKNMPEEYESRKKDKLRYRYPR---GESYLDVIQRLEPVIIELERQRA----PVVVISHQAVLRAL 704
Cdd:smart00855  79 RDFGAWEGLTWDEIAAKYPEEYLAAWRDPYDPAPPAppgGESLADLVERVEPALDELIATADasgqNVLIVSHGGVIRAL 158
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
554-731 3.66e-21

Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Subgroup of the catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This subgroup contains cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example, F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG.


Pssm-ID: 132718  Cd Length: 153  Bit Score: 90.46  E-value: 3.66e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069  554 ILLTRHGESMDNVRGRIGG--DSVISDSGKLYAKKLAsfveKRLKSE--KAASIWTSTLQRTNLTASSIV----GFPKVQ 625
Cdd:cd07067   2 LYLVRHGESEWNAEGRFQGwtDVPLTEKGREQARALG----KRLKELgiKFDRIYSSPLKRAIQTAEIILeelpGLPVEV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069  626 WRALDEinagvcdgmtyeevkknmpeeyesrkkdklryryprgesyldviQRLEPVIIELERQRAP--VVVISHQAVLRA 703
Cdd:cd07067  78 DPRLRE--------------------------------------------ARVLPALEELIAPHDGknVLIVSHGGVLRA 113
                       170       180
                ....*....|....*....|....*...
gi 8572069  704 LYAYFADRPLKEIPQIEMPLHTIIEIQM 731
Cdd:cd07067 114 LLAYLLGLSDEDILRLNLPNGSISVLEL 141
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
554-722 7.40e-20

alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of Salmonella and Eschichia coli species, and homologous proteins found in cobalamin biosynthesis regions in other bacteria. This protein is alpha-ribazole phosphatase (EC 3.1.3.73) and, like many phosphatases, can be closely related in sequence to other phosphatases with different functions. Close homologs excluded from this model include proteins with duplications, so this model is built in -g mode to suppress hits to those proteins. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274461 [Multi-domain]  Cd Length: 177  Bit Score: 87.29  E-value: 7.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069    554 ILLTRHGESMDNVRGRIG-GDSVISDSGKLYAKKLAsfveKRLKSEKAASIWTSTLQRTNLTASSI---VGFPKVQWRAL 629
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCYGqTDVPLAESGEEQAAALR----EKLADVPFDAVYSSPLSRCRELAEILaerRGLPIIKDDRL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069    630 DEINAGVCDGMTYEEVKKNMPEeYESRKKDKLRYRYPRGESYLDVIQRLEPVIIEL--ERQRAPVVVISHQAVLRALYAY 707
Cdd:TIGR03162  77 REMDFGDWEGRSWDEIPEAYPE-LDAWAADWQHARPPGGESFADFYQRVSEFLEELlkAHEGDNVLIVTHGGVIRALLAH 155
                         170
                  ....*....|....*
gi 8572069    708 FADRPLKEIPQIEMP 722
Cdd:TIGR03162 156 LLGLPLEQWWSFAVE 170
CBM_2 smart01065
Starch binding domain;
25-110 4.86e-16

Starch binding domain;


Pssm-ID: 215006  Cd Length: 88  Bit Score: 73.54  E-value: 4.86e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069      25 VSLKMENSKVEGELTPHVYGSLPLIGSWDPSKALPMQRESA--LMSELSFVVPPDHETLDFKFLLKPKNRNtpCIVEEGE 102
Cdd:smart01065   3 VTFKVRNGYTQPGESVYVVGSVPELGNWNPKKAVPLSPDTDgyPLWKGTVSLPPAGTTIEYKYVKVDEDGS--VTWESGP 80

                   ....*...
gi 8572069     103 NRLLTGGS 110
Cdd:smart01065  81 NRRLTVPE 88
PRK13463 PRK13463
phosphatase PhoE; Provisional
554-738 9.41e-15

phosphatase PhoE; Provisional


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 73.54  E-value: 9.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069   554 ILLTRHGESMDNVRGRIGG--DSVISDSGKLYAKKLAsfveKRLKSEKAASIWTSTLQRTNLTASSIVG---FPKVQWRA 628
Cdd:PRK13463   5 VYVTRHGETEWNVAKRMQGrkNSALTENGILQAKQLG----ERMKDLSIHAIYSSPSERTLHTAELIKGerdIPIIADEH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069   629 LDEINAGVCDGMTYEEVKKNMPEEYESRKKDKLRYRYPRGESYLDVIQR-LEPVIIELERQRAP-VVVISHQAVLRALYA 706
Cdd:PRK13463  81 FYEINMGIWEGQTIDDIERQYPDDIQLFWNEPHLFQSTSGENFEAVHKRvIEGMQLLLEKHKGEsILIVSHAAAAKLLVG 160
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 8572069   707 YFADRPLKEI---PQIEMPLHTIIEIQMGVSGVQE 738
Cdd:PRK13463 161 HFAGIEIENVwddPFMHSASLSIIEFEDGKGEVKQ 195
CBM20 cd05467
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
41-107 1.99e-08

The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 119437  Cd Length: 96  Bit Score: 52.30  E-value: 1.99e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8572069   41 HVY--GSLPLIGSWDPSKALPMQRESAL---MSELSFVVPPDhETLDFKFLLKPKNRNTpcIVEEGENRLLT 107
Cdd:cd05467  15 SVYvvGSHPELGNWDPAKALRLNTSNSYplwTGEIPLPAPEG-QVIEYKYVIVDDDGNV--QWESGSNRVLT 83
CBM_20 pfam00686
Starch binding domain;
41-107 5.28e-05

Starch binding domain;


Pssm-ID: 307023  Cd Length: 96  Bit Score: 42.29  E-value: 5.28e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8572069     41 HVY--GSLPLIGSWDPSKALPMQRESALMSELSFVVP---PDHETLDFKFLLKPKNRNTpcIVEEGENRLLT 107
Cdd:pfam00686  16 NVYivGSIPELGNWNPKKAVALSASEYTSSYPLWSGTvdlPAGTTIEYKYIKKDSDGNV--TWESGPNRSYT 85
 
Name Accession Description Interval E-value
6PF2K pfam01591
6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2, ...
335-551 7.90e-102

6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2,6-bisphosphatase. The bifunctional enzyme catalyzes both the synthesis and degradation of fructose-2,6-bisphosphate, a potent regulator of glycolysis. This enzyme contains a P-loop motif.


Pssm-ID: 334602  Cd Length: 219  Bit Score: 311.58  E-value: 7.90e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069    335 MLGPK-EDRHLAIVLVGLPARGKTFTAAKLTRYLRWLGHDTKHFNVGKYRRLKHGVNMSADFFRADNPEGVEARTEVAAL 413
Cdd:pfam01591   1 STGPNfTNSKTLIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRRSAVKAYSDYEFFRPDNEEGMKIREQCALA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069    414 AMEDMIAWMQ-EGGQVGIFDATNSTRVRRNMLMKMAEG-KCKIIFLETLCNDERIIERNIRLKIQQSPDYSEEMDFEAgV 491
Cdd:pfam01591  81 ALNDVLAYLNeESGQVAIFDATNTTRERRKMILDFAEEnGLKVFFLESICDDPEIIARNIKLVKFSSPDYKGKPPEEA-I 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8572069    492 RDFRDRLANYEKVYEPVEE-GSYIKMIDMVSGnGGQIQVNNISGYLPGRIVFFLVNTHLTP 551
Cdd:pfam01591 160 DDFMKRIECYEKQYEPLDEhDEDLSYIKVIDV-GQSIVVNNVQGYLQSRIVYYLMNIHVTP 219
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
335-738 7.57e-51

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 188.57  E-value: 7.57e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069   335 MLGPkedrhLAIVLVGLPARGKTFTAAKLTRYLRWLGHDTKHFNVGKYRR---LKHGVNMSAdffradnPEGVEARTEVA 411
Cdd:PTZ00322 212 MMGS-----LIVIMVGLPGRGKTYVARQIQRYFQWNGLQSRIFIHQAYRRrleRRGGAVSSP-------TGAAEVEFRIA 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069   412 ALAMEDMIAWMQEGGQVGIFDATNSTRVRRNMLMK--MAEGKC---KIIFLETLCNDERIIERNIRLKIQQSPDYSEemD 486
Cdd:PTZ00322 280 KAIAHDMTTFICKTDGVAVLDGTNTTHARRMALLRaiRETGLIrmtRVVFVEVVNNNSETIRRNVLRAKEMFPGAPE--D 357
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069   487 FeagVRDFRDRLANYEKVYE---PVEEG--SYIKMIDmvsgnGGQIQVNNISGYLPGRIVFFLVNTHLTPRPILLTRHGE 561
Cdd:PTZ00322 358 F---VDRYYEVIEQLEAVYKslnPVTDCdlTYIRIED-----TQTFSLNNISGWMPSRLAYMLHNLNPTPMNLYLTRAGE 429
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069   562 SMDNVRGRIGGDSVISDSGKLYAKKLASFVEKRLkSEKAASIWTS----------------TLQRTNLTASSIVGfPKVQ 625
Cdd:PTZ00322 430 YVDLLSGRIGGNSRLTERGRAYSRALFEYFQKEI-STTSFTVMSScakrctetvhyfaeesILQQSTASAASSQS-PSLN 507
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069   626 WR-----ALDEINAGVCDGMTYEEVKKNMPEEYESRKKDKLRYRYPRGESYLDVIQ-RLEPVIIELERQRAPVVVISHQA 699
Cdd:PTZ00322 508 CRvlyfpTLDDINHGDCEGQLLSDVRRTMPNTLQSMKADPYYTAWPNGECIHQVFNaRLEPHIHDIQASTTPVLVVSHLH 587
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 8572069   700 VLRALYAYFADRPLKEI-PQ----IEMPLHTIIEIQM-GVSGVQE 738
Cdd:PTZ00322 588 LLQGLYSYFVTDGDNIVaPQnaykIDIPFEHVIKIRMvGFNRVAE 632
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
554-729 3.81e-43

Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so named because catalysis centers on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches. The larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members.


Pssm-ID: 333990 [Multi-domain]  Cd Length: 193  Bit Score: 154.28  E-value: 3.81e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069    554 ILLTRHGESMDNVRGRIGG--DSVISDSGKLYAKKLAsfveKRLKSEKAASIWTSTLQRTNLTASSI---VGFPKVQWRA 628
Cdd:pfam00300   1 LYLVRHGETEWNLEGRLQGrtDSPLTERGREQAEALA----ERLAGEPFDAIYSSPLKRARQTAEIIaeaLGLPVEIDER 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069    629 LDEINAGVCDGMTYEEVKKNMPEEYESRKKDKLRYRYPRGESYLDVIQRLEPVIIELERQRAP--VVVISHQAVLRALYA 706
Cdd:pfam00300  77 LREIDFGDWEGLTFAEIRERYPEEYAAWLADPADYRPPGGESLADVQARVRAALEELAARHPGktVLVVSHGGVIRALLA 156
                         170       180
                  ....*....|....*....|...
gi 8572069    707 YFADRPLKEIPQIEMPLHTIIEI 729
Cdd:pfam00300 157 HLLGLPLEELRRFELDNASLTIL 179
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
554-732 3.60e-33

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 223483 [Multi-domain]  Cd Length: 208  Bit Score: 126.83  E-value: 3.60e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069  554 ILLTRHGESMDNVRGRIGG--DSVISDSGKLYAKKLASFVEKRLKSEKAasIWTSTLQRTNLTA---SSIVGFPKVQWRA 628
Cdd:COG0406   5 LYLVRHGETEWNVEGRLQGwtDSPLTEEGRAQAEALAERLAARDIGFDA--IYSSPLKRAQQTAeplAEELGLPLEVDDR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069  629 LDEINAGVCDGMTYEEVKKNMPEEYESRKKDKLRYRYPRGESYLDVIQRLEPVIIELER--QRAPVVVISHQAVLRALYA 706
Cdd:COG0406  83 LREIDFGDWEGLTIDELAEEPPEELAAWLADPYLAPPPGGESLADVSKRVVAALAELLRspPGNNVLVVSHGGVIRALLA 162
                       170       180
                ....*....|....*....|....*...
gi 8572069  707 YFADRPLKEIPQIEMPLH--TIIEIQMG 732
Cdd:COG0406 163 YLLGLDLEELWRLRLDNAsvTVLEFDDG 190
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
554-704 5.54e-31

Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase (BPGM) are structurally related enzymes that catalyse reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate... Both enzymes can catalyse three different reactions with different specificities, the isomerization of 2-phosphoglycerate (2-PGA) to 3-phosphoglycerate (3-PGA) with 2,3-diphosphoglycerate (2,3-DPG) as the primer of the reaction, the synthesis of 2,3-DPG from 1,3-DPG with 3-PGA as a primer and the degradation of 2,3-DPG to 3-PGA (phosphatase activity). In mammals, PGAM is a dimeric protein with two isoforms, the M (muscle) and B (brain) forms. In yeast, PGAM is a tetrameric protein.


Pssm-ID: 214859 [Multi-domain]  Cd Length: 158  Bit Score: 118.72  E-value: 5.54e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069     554 ILLTRHGESMDNVRGRIGG--DSVISDSGKLYAKKLASFVeKRLKSEKAASIWTSTLQRTNLTASsIVGFPKVQWRaLDE 631
Cdd:smart00855   2 LYLIRHGETEWNREGRLYGdtDVPLTELGRAQAEALGRLL-ASLLLPRFDVVYSSPLKRARQTAE-ALAIALGLPG-LRE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069     632 INAGVCDGMTYEEVKKNMPEEYESRKKDKLRYRYPR---GESYLDVIQRLEPVIIELERQRA----PVVVISHQAVLRAL 704
Cdd:smart00855  79 RDFGAWEGLTWDEIAAKYPEEYLAAWRDPYDPAPPAppgGESLADLVERVEPALDELIATADasgqNVLIVSHGGVIRAL 158
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
554-731 3.66e-21

Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Subgroup of the catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This subgroup contains cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example, F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG.


Pssm-ID: 132718  Cd Length: 153  Bit Score: 90.46  E-value: 3.66e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069  554 ILLTRHGESMDNVRGRIGG--DSVISDSGKLYAKKLAsfveKRLKSE--KAASIWTSTLQRTNLTASSIV----GFPKVQ 625
Cdd:cd07067   2 LYLVRHGESEWNAEGRFQGwtDVPLTEKGREQARALG----KRLKELgiKFDRIYSSPLKRAIQTAEIILeelpGLPVEV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069  626 WRALDEinagvcdgmtyeevkknmpeeyesrkkdklryryprgesyldviQRLEPVIIELERQRAP--VVVISHQAVLRA 703
Cdd:cd07067  78 DPRLRE--------------------------------------------ARVLPALEELIAPHDGknVLIVSHGGVLRA 113
                       170       180
                ....*....|....*....|....*...
gi 8572069  704 LYAYFADRPLKEIPQIEMPLHTIIEIQM 731
Cdd:cd07067 114 LLAYLLGLSDEDILRLNLPNGSISVLEL 141
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
554-722 7.40e-20

alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of Salmonella and Eschichia coli species, and homologous proteins found in cobalamin biosynthesis regions in other bacteria. This protein is alpha-ribazole phosphatase (EC 3.1.3.73) and, like many phosphatases, can be closely related in sequence to other phosphatases with different functions. Close homologs excluded from this model include proteins with duplications, so this model is built in -g mode to suppress hits to those proteins. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274461 [Multi-domain]  Cd Length: 177  Bit Score: 87.29  E-value: 7.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069    554 ILLTRHGESMDNVRGRIG-GDSVISDSGKLYAKKLAsfveKRLKSEKAASIWTSTLQRTNLTASSI---VGFPKVQWRAL 629
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCYGqTDVPLAESGEEQAAALR----EKLADVPFDAVYSSPLSRCRELAEILaerRGLPIIKDDRL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069    630 DEINAGVCDGMTYEEVKKNMPEeYESRKKDKLRYRYPRGESYLDVIQRLEPVIIEL--ERQRAPVVVISHQAVLRALYAY 707
Cdd:TIGR03162  77 REMDFGDWEGRSWDEIPEAYPE-LDAWAADWQHARPPGGESFADFYQRVSEFLEELlkAHEGDNVLIVTHGGVIRALLAH 155
                         170
                  ....*....|....*
gi 8572069    708 FADRPLKEIPQIEMP 722
Cdd:TIGR03162 156 LLGLPLEQWWSFAVE 170
CBM_2 smart01065
Starch binding domain;
25-110 4.86e-16

Starch binding domain;


Pssm-ID: 215006  Cd Length: 88  Bit Score: 73.54  E-value: 4.86e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069      25 VSLKMENSKVEGELTPHVYGSLPLIGSWDPSKALPMQRESA--LMSELSFVVPPDHETLDFKFLLKPKNRNtpCIVEEGE 102
Cdd:smart01065   3 VTFKVRNGYTQPGESVYVVGSVPELGNWNPKKAVPLSPDTDgyPLWKGTVSLPPAGTTIEYKYVKVDEDGS--VTWESGP 80

                   ....*...
gi 8572069     103 NRLLTGGS 110
Cdd:smart01065  81 NRRLTVPE 88
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
554-731 2.36e-15

Histidine phosphatase domain found in a functionally diverse set of proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This set of proteins includes cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, histidine acid phosphatases, phytases, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system; phytases scavenge phosphate from extracellular sources. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG. Clinical applications include the use of prostatic acid phosphatase (PAP) as a serum marker for prostate cancer. Agricultural applications include the addition of phytases to animal feed.


Pssm-ID: 132716  Cd Length: 153  Bit Score: 73.60  E-value: 2.36e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069  554 ILLTRHGESMDNVRGRIGG--DSVISDSGKLYAKKLASFVEKRLKSEKAasIWTSTLQRTNLTASSIVgfpkvqwralde 631
Cdd:cd07040   2 LYLVRHGEREPNAEGRFTGwgDGPLTEKGRQQARELGKALRERYIKFDR--IYSSPLKRAIQTAEIIL------------ 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069  632 inagvcdgmtyEEVKKNMPEEYESRkkdklryryprgesyldviQRLEPVIIELERQRAP----VVVISHQAVLRALYAY 707
Cdd:cd07040  68 -----------EGLFEGLPVEVDPR-------------------ARVLNALLELLARHLLdgknVLIVSHGGTIRALLAA 117
                       170       180
                ....*....|....*....|....
gi 8572069  708 FADRPLKEIPQIEMPLHTIIEIQM 731
Cdd:cd07040 118 LLGLSDEEILSLNLPNGSILVLEL 141
PRK13463 PRK13463
phosphatase PhoE; Provisional
554-738 9.41e-15

phosphatase PhoE; Provisional


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 73.54  E-value: 9.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069   554 ILLTRHGESMDNVRGRIGG--DSVISDSGKLYAKKLAsfveKRLKSEKAASIWTSTLQRTNLTASSIVG---FPKVQWRA 628
Cdd:PRK13463   5 VYVTRHGETEWNVAKRMQGrkNSALTENGILQAKQLG----ERMKDLSIHAIYSSPSERTLHTAELIKGerdIPIIADEH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069   629 LDEINAGVCDGMTYEEVKKNMPEEYESRKKDKLRYRYPRGESYLDVIQR-LEPVIIELERQRAP-VVVISHQAVLRALYA 706
Cdd:PRK13463  81 FYEINMGIWEGQTIDDIERQYPDDIQLFWNEPHLFQSTSGENFEAVHKRvIEGMQLLLEKHKGEsILIVSHAAAAKLLVG 160
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 8572069   707 YFADRPLKEI---PQIEMPLHTIIEIQMGVSGVQE 738
Cdd:PRK13463 161 HFAGIEIENVwddPFMHSASLSIIEFEDGKGEVKQ 195
CBM20 cd05467
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
41-107 1.99e-08

The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 119437  Cd Length: 96  Bit Score: 52.30  E-value: 1.99e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8572069   41 HVY--GSLPLIGSWDPSKALPMQRESAL---MSELSFVVPPDhETLDFKFLLKPKNRNTpcIVEEGENRLLT 107
Cdd:cd05467  15 SVYvvGSHPELGNWDPAKALRLNTSNSYplwTGEIPLPAPEG-QVIEYKYVIVDDDGNV--QWESGSNRVLT 83
CBM20_DPE2_repeat2 cd05816
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
42-116 1.66e-07

Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) domain, repeat 2. DPE2 is a transglucosidase that is essential for the cytosolic metabolism of maltose in plant leaves at night. Maltose is an intermediate on the pathway from starch to sucrose and DPE2 is thought to metabolize the maltose that is exported from the chloroplast. DPE2 has two N-terminal CBM20 domains as well as a C-terminal amylomaltase (4-alpha-glucanotransferase) catalytic domain. DPE1, the plastid version of this enzyme, has a transglucosidase domain that is similar to that of DPE2 but lacks the N-terminal CBM20 domains. Included in this group are PDE2-like proteins from Dictyostelium, Entamoeba, and Bacteroides. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99890  Cd Length: 99  Bit Score: 49.63  E-value: 1.66e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8572069   42 VYGSLPLIGSWDPSKALPMQRESALMSELSFVVPPDHETLDFKFLLKPKNRNTPCiVEEGENRLLTGGSLQGDAR 116
Cdd:cd05816  19 VTGSSPELGNWDPQKALKLSDVGFPIWEADIDISKDSFPFEYKYIIANKDSGVVS-WENGPNRELSAPSLKGESS 92
GpmA COG0588
Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism];
556-722 1.10e-06

Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism];


Pssm-ID: 223661  Cd Length: 230  Bit Score: 49.97  E-value: 1.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069  556 LTRHGESMDNVRGRIGG--DSVISDSGKLYAKKLAsfveKRLKSEKAASI--WTSTLQRTN------LTASSIVGFPKV- 624
Cdd:COG0588   6 LLRHGQSEWNKENLFTGwvDVDLTEKGISEAKAAG----KLLKEEGLEFDiaYTSVLKRAIktlnivLEESDQLWIPVIk 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069  625 QWRaLDEINAGVCDGMTYEEVKKNMPEEY-------------------ESRKKDKLRYRY------PRGESYLDVIQRLE 679
Cdd:COG0588  82 SWR-LNERHYGALQGLNKAETAAKYGEEQvliwrrsydipppklekddERSPHRDRRYAHldigglPLTESLKDTVERVL 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 8572069  680 P----VIIELERQRAPVVVISHQAVLRALYAYFADRPLKEIPQIEMP 722
Cdd:COG0588 161 PywedDIAPNLKSGKNVLIVAHGNSLRALIKYLEGISDEDILDLNIP 207
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
550-697 1.55e-05

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 47.67  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069   550 TPRPILLTRHGESMDNVRGRIGG--DSVISDSGKLYAKKLAsfveKRLKSEKA-ASIWTSTLQRTNLTASSI---VGFPK 623
Cdd:PRK07238 170 TPTRLLLLRHGQTELSVQRRYSGrgNPELTEVGRRQAAAAA----RYLAARGGiDAVVSSPLQRARDTAAAAakaLGLDV 245
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8572069   624 VQWRALDEINAGVCDGMTYEEVKKNMPEEYESRKKDKlRYRYPRGESYLDVIQRLEPVIIELER--QRAPVVVISH 697
Cdd:PRK07238 246 TVDDDLIETDFGAWEGLTFAEAAERDPELHRAWLADT-SVAPPGGESFDAVARRVRRARDRLIAeyPGATVLVVSH 320
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteristic of the ...
346-502 2.07e-05

AAA domain; This family of domains contain only a P-loop motif, that is characteristic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 338887 [Multi-domain]  Cd Length: 143  Bit Score: 44.97  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069    346 IVLVGLPARGKTFTAAKLTRYLRW--LGHDTkhfnvgkYRRlkhgvNMSADffRADNPEGVEARTEVAALAMEDMIAWMQ 423
Cdd:pfam13671   2 ILLVGLPGSGKSTLAERLLRELGAvrLSSDT-------LRK-----RLYGD--GRPSISYSADASDRTYQRLHELARIAL 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069    424 EGGQVGIFDATNSTRVRRNMLMKMAEG---KCKIIFLETlcnDERIIERNIRLKIQQSPDYSeEMDFEAgvrdFRDRLAN 500
Cdd:pfam13671  68 RAGRPVILDATNLTRAERARLLALARRygvPVRIVVFEA---PEEVLRERLAARARAGGDPS-EVPEEV----LDRQKAR 139

                  ..
gi 8572069    501 YE 502
Cdd:pfam13671 140 FE 141
CBM_20 pfam00686
Starch binding domain;
41-107 5.28e-05

Starch binding domain;


Pssm-ID: 307023  Cd Length: 96  Bit Score: 42.29  E-value: 5.28e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8572069     41 HVY--GSLPLIGSWDPSKALPMQRESALMSELSFVVP---PDHETLDFKFLLKPKNRNTpcIVEEGENRLLT 107
Cdd:pfam00686  16 NVYivGSIPELGNWNPKKAVALSASEYTSSYPLWSGTvdlPAGTTIEYKYIKKDSDGNV--TWESGPNRSYT 85
PRK15004 PRK15004
alpha-ribazole phosphatase; Provisional
556-733 7.61e-05

alpha-ribazole phosphatase; Provisional


Pssm-ID: 184966  Cd Length: 199  Bit Score: 44.27  E-value: 7.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069   556 LTRHGESMDNVRGRIGG--DSVISDSGKLYAKKLASfvekRLKSEKAASIWTSTLQRTNLTASSIVGFPKVQWR---ALD 630
Cdd:PRK15004   5 LVRHGETQANVDGLYSGhaPTPLTARGIEQAQNLHT----LLRDVPFDLVLCSELERAQHTARLVLSDRQLPVHiipELN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069   631 EINAGVCDGMTYEEVKKNMPEEYESRKKDKLRYRYPRGESYLDVIQRLEPVIIELERQR--APVVVISHQAVLRALYAYF 708
Cdd:PRK15004  81 EMFFGDWEMRHHRDLMQEDAENYAAWCNDWQHAIPTNGEGFQAFSQRVERFIARLSAFQhyQNLLIVSHQGVLSLLIARL 160
                        170       180
                 ....*....|....*....|....*..
gi 8572069   709 ADRPLKEIPQ--IEMPLHTIIEIQMGV 733
Cdd:PRK15004 161 LGMPAEAMWHfrVEQGCWSAIDINQGF 187
PRK03482 PRK03482
phosphoglycerate mutase; Provisional
556-704 1.39e-04

phosphoglycerate mutase; Provisional


Pssm-ID: 179583  Cd Length: 215  Bit Score: 43.56  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069   556 LTRHGESMDNVRGRIGG--DSVISDSGklyaKKLASFVEKRLKSEKAASIWTSTLQRTNLTASSIV---GFPKVQWRALD 630
Cdd:PRK03482   6 LVRHGETQWNAERRIQGqsDSPLTAKG----EQQAMQVAERAKELGITHIISSDLGRTRRTAEIIAqacGCDIIFDPRLR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8572069   631 EINAGVCDGMTYEEVKknmPEEYESRKK---DKLRYRYPRGESYLDVIQRLEPVI---IELERQRAPVVViSHQAVLRAL 704
Cdd:PRK03482  82 ELNMGVLEKRHIDSLT---EEEEGWRRQlvnGTVDGRIPEGESMQELSDRMHAALescLELPQGSRPLLV-SHGIALGCL 157
CBM20_Prei4 cd05814
Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation ...
25-63 9.18e-03

Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation protein 4 (Prei4) is a protein of unknown function that is expressed during mouse preimplantation embryogenesis. In addition to the N-terminal CBM20 domain, Prei4 contains a C-terminal glycerophosphoryl diester phosphodiesterase (GDPD) domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99888  Cd Length: 120  Bit Score: 36.53  E-value: 9.18e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 8572069   25 VSLKMENSKVEGELTPHVYGSLPLIGSWDPSKALPMQRE 63
Cdd:cd05814   3 VTFRVFASELAPGEVVAVVGSLPVLGNWQPEKAVPLEKE 41
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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