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Conserved domains on  [gi|1958648956|ref|XP_038944421|]
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amino acid transporter heavy chain SLC3A2 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AmyAc_family super family cl38930
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
100-430 1.57e-142

Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; and C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost this catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


The actual alignment was detected with superfamily member cd11345:

Pssm-ID: 476817 [Multi-domain]  Cd Length: 326  Bit Score: 413.37  E-value: 1.57e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 100 APRCRELPVQRWWHKGALYRIGDLQAFvgPEARGIAGLKNHLEYLSTLKVKGLVLGPIHKNQKDEVNETDLKQIDPDLGS 179
Cdd:cd11345     1 APRCKPIPEMNWWNEGPLYQIGDLQAF--SEAGGLKGVEGKLDYLSQLKVKGLVLGPIHVVQADQPGELNLTEIDPDLGT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 180 QEDFKDLLQSAKKKSIHIILDLTPNYKGQNAWFlPPQADIVATKMKEALSSWLQDGVDGFQVRDVGKLANASLYlaEWQN 259
Cdd:cd11345    79 LEDFTSLLTAAHKKGISVVLDLTPNYRGESSWA-FSDAENVAEKVKEALEFWLNQGVDGIQVSDLENVASSASS--EWSN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 260 ITKNFSE-----DRLLIAGTASSDLQQIVNIL-ESTSDLLLTSSYLSQPVFTGEHAelLVIKYLNATGSRWCSWSVSQAG 333
Cdd:cd11345   156 LTAIVQKntdgkKRVLIGVTSSSSLSEISLLLnTSGVDLLLSGALLSASNRPSFGT--LVTQLLSTTGQRSLAWGIGARQ 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 334 LLTSF--IPAQFLRLYQLLLFTLPGTPVFSYGDELGLQAVALPGQPMEAP--FMLWNESsnsqtsspVSLNMTVKGQNED 409
Cdd:cd11345   234 GGHLAslVPAALVRLYQLLLFTLPGTPVFNYGDEIGLQDAQGKSPKMLRPnnEPEIAEE--------VNANMTAKAQKED 305
                         330       340
                  ....*....|....*....|.
gi 1958648956 410 PGSLLTQFRRLSDLRGKERSL 430
Cdd:cd11345   306 RGSLRSFFRSLSDLRGKERSL 326
SLC3A2_N pfam16028
Solute carrier family 3 member 2 N-terminus; This domain is found at the N-terminus of solute ...
42-118 3.11e-27

Solute carrier family 3 member 2 N-terminus; This domain is found at the N-terminus of solute carrier family 3 member 2 proteins (4F2 cell-surface antigen heavy chain).


:

Pssm-ID: 464983  Cd Length: 77  Bit Score: 104.33  E-value: 3.11e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958648956  42 KVAEDEAEAGVKFTGLSKEELLKVAGSPGWVRTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPVQRWWHKGALY 118
Cdd:pfam16028   1 DAKIDIEAEKVKFTGLTKEELLKYANDPFWVRVRWALFVLFWLGWLGMLVGAIVIIVQAPKCKPPPPLSWWEKGPLY 77
 
Name Accession Description Interval E-value
AmyAc_SLC3A2 cd11345
Alpha amylase catalytic domain found in solute carrier family 3 member 2 proteins; 4F2 ...
100-430 1.57e-142

Alpha amylase catalytic domain found in solute carrier family 3 member 2 proteins; 4F2 cell-surface antigen heavy chain (hc) is a protein that in humans is encoded by the SLC3A2 gene. 4F2hc is a multifunctional type II membrane glycoprotein involved in amino acid transport and cell fusion, adhesion, and transformation. It is related to bacterial alpha-glycosidases, but lacks alpha-glycosidase activity. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200483 [Multi-domain]  Cd Length: 326  Bit Score: 413.37  E-value: 1.57e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 100 APRCRELPVQRWWHKGALYRIGDLQAFvgPEARGIAGLKNHLEYLSTLKVKGLVLGPIHKNQKDEVNETDLKQIDPDLGS 179
Cdd:cd11345     1 APRCKPIPEMNWWNEGPLYQIGDLQAF--SEAGGLKGVEGKLDYLSQLKVKGLVLGPIHVVQADQPGELNLTEIDPDLGT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 180 QEDFKDLLQSAKKKSIHIILDLTPNYKGQNAWFlPPQADIVATKMKEALSSWLQDGVDGFQVRDVGKLANASLYlaEWQN 259
Cdd:cd11345    79 LEDFTSLLTAAHKKGISVVLDLTPNYRGESSWA-FSDAENVAEKVKEALEFWLNQGVDGIQVSDLENVASSASS--EWSN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 260 ITKNFSE-----DRLLIAGTASSDLQQIVNIL-ESTSDLLLTSSYLSQPVFTGEHAelLVIKYLNATGSRWCSWSVSQAG 333
Cdd:cd11345   156 LTAIVQKntdgkKRVLIGVTSSSSLSEISLLLnTSGVDLLLSGALLSASNRPSFGT--LVTQLLSTTGQRSLAWGIGARQ 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 334 LLTSF--IPAQFLRLYQLLLFTLPGTPVFSYGDELGLQAVALPGQPMEAP--FMLWNESsnsqtsspVSLNMTVKGQNED 409
Cdd:cd11345   234 GGHLAslVPAALVRLYQLLLFTLPGTPVFNYGDEIGLQDAQGKSPKMLRPnnEPEIAEE--------VNANMTAKAQKED 305
                         330       340
                  ....*....|....*....|.
gi 1958648956 410 PGSLLTQFRRLSDLRGKERSL 430
Cdd:cd11345   306 RGSLRSFFRSLSDLRGKERSL 326
SLC3A2_N pfam16028
Solute carrier family 3 member 2 N-terminus; This domain is found at the N-terminus of solute ...
42-118 3.11e-27

Solute carrier family 3 member 2 N-terminus; This domain is found at the N-terminus of solute carrier family 3 member 2 proteins (4F2 cell-surface antigen heavy chain).


Pssm-ID: 464983  Cd Length: 77  Bit Score: 104.33  E-value: 3.11e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958648956  42 KVAEDEAEAGVKFTGLSKEELLKVAGSPGWVRTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPVQRWWHKGALY 118
Cdd:pfam16028   1 DAKIDIEAEKVKFTGLTKEELLKYANDPFWVRVRWALFVLFWLGWLGMLVGAIVIIVQAPKCKPPPPLSWWEKGPLY 77
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
111-424 3.03e-25

Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 108.03  E-value: 3.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 111 WWHKGALYRI-------------GDLQafvgpeargiaGLKNHLEYLSTLKVKGLVLGPIHKN-QKD---EVneTDLKQI 173
Cdd:COG0366     5 WWKDAVIYQIypdsfadsngdggGDLK-----------GIIEKLDYLKDLGVDAIWLSPFFPSpMSDhgyDI--SDYRDV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 174 DPDLGSQEDFKDLLQSAKKKSIHIILDLTPN----------------------------------------YKGQNAW-- 211
Cdd:COG0366    72 DPRFGTLADFDELVAEAHARGIKVILDLVLNhtsdehpwfqearagpdspyrdwyvwrdgkpdlppnnwfsIFGGSAWtw 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 212 -----------FLPPQADI------VATKMKEALSSWLQDGVDGFQV-------RDVGKLAN---ASLYLAEWQNITKNF 264
Cdd:COG0366   152 dpedgqyylhlFFSSQPDLnwenpeVREELLDVLRFWLDRGVDGFRLdavnhldKDEGLPENlpeVHEFLRELRAAVDEY 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 265 SEDRLLIAGTASSDLQQIVNILESTS-------DLLLTSSYLSQPVFTGEHAELLVIKYLNATGSRWCSWSVS---QAGL 334
Cdd:COG0366   232 YPDFFLVGEAWVDPPEDVARYFGGDEldmafnfPLMPALWDALAPEDAAELRDALAQTPALYPEGGWWANFLRnhdQPRL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 335 LTSFIPAQFLRLYQL---LLFTLPGTPVFSYGDELGlqavaLPGQPMEAPF--------MLWNESSN---SQTSSPVSLN 400
Cdd:COG0366   312 ASRLGGDYDRRRAKLaaaLLLTLPGTPYIYYGDEIG-----MTGDKLQDPEgrdgcrtpMPWSDDRNagfSTGWLPVPPN 386
                         410       420
                  ....*....|....*....|....*..
gi 1958648956 401 ---MTVKGQNEDPGSLLTQFRRLSDLR 424
Cdd:COG0366   387 ykaINVEAQEADPDSLLNFYRKLIALR 413
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
121-368 7.74e-16

Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.


Pssm-ID: 395077 [Multi-domain]  Cd Length: 334  Bit Score: 78.55  E-value: 7.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 121 GDLQafvgpeargiaGLKNHLEYLSTLKVKGLVLGPIHKNQKDE--VNETDLKQIDPDLGSQEDFKDLLQSAKKKSIHII 198
Cdd:pfam00128   1 GDLQ-----------GIIEKLDYLKELGVTAIWLSPIFDSPQADhgYDIADYYKIDPHYGTMEDFKELISKAHERGIKVI 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 199 LDLTPN----------------------------------------YKGQNAW-------------FLPPQADI------ 219
Cdd:pfam00128  70 LDLVVNhtsdehawfqesrsskdnpyrdyyfwrpgggpippnnwrsYFGGSAWtydekgqeyylhlFVAGQPDLnwenpe 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 220 VATKMKEALSSWLQDGVDGFQVrDVGKL---------ANASLYLAEW---QNITKNFSEDRLL---IAGTASSDLQQIVN 284
Cdd:pfam00128 150 VRNELYDVVRFWLDKGIDGFRI-DVVKHiskvpglpfENNGPFWHEFtqaMNETVFGYKDVMTvgeVFHGDGEWARVYTT 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 285 ilESTSDLLLTSSYLSQPVFTGEHAELLVIKY----LNATGSRWCSWSVSQAGLLTSFI--------------PAQFLRL 346
Cdd:pfam00128 229 --EARMELEMGFNFPHNDVALKPFIKWDLAPIsarkLKEMITDWLDALPDTNGWNFTFLgnhdqprflsrfgdDRASAKL 306
                         330       340
                  ....*....|....*....|..
gi 1958648956 347 YQLLLFTLPGTPVFSYGDELGL 368
Cdd:pfam00128 307 LAVFLLTLRGTPYIYQGEEIGM 328
Aamy smart00642
Alpha-amylase domain;
120-211 1.73e-11

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 62.73  E-value: 1.73e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956  120 IGDLQafvgpeargiaGLKNHLEYLSTLKVKGLVLGPIHKN-QKDEVNE----TDLKQIDPDLGSQEDFKDLLQSAKKKS 194
Cdd:smart00642  15 GGDLQ-----------GIIEKLDYLKDLGVTAIWLSPIFESpQGYPSYHgydiSDYKQIDPRFGTMEDFKELVDAAHARG 83
                           90
                   ....*....|....*..
gi 1958648956  195 IHIILDLTPNYKGQNAW 211
Cdd:smart00642  84 IKVILDVVINHTSDGGF 100
PRK10933 PRK10933
trehalose-6-phosphate hydrolase; Provisional
111-212 2.74e-10

trehalose-6-phosphate hydrolase; Provisional


Pssm-ID: 182849 [Multi-domain]  Cd Length: 551  Bit Score: 62.84  E-value: 2.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 111 WWHKGALYRI--GDLQAFVGPEARGIAGLKNHLEYLSTLKVKGLVLGPIH-----KNQKDEVNETdlkQIDPDLGSQEDF 183
Cdd:PRK10933    7 WWQNGVIYQIypKSFQDTTGSGTGDLRGVTQRLDYLQKLGVDAIWLTPFYvspqvDNGYDVANYT---AIDPTYGTLDDF 83
                          90       100       110
                  ....*....|....*....|....*....|
gi 1958648956 184 KDLLQSAKKKSIHIILDLTPNYKG-QNAWF 212
Cdd:PRK10933   84 DELVAQAKSRGIRIILDMVFNHTStQHAWF 113
 
Name Accession Description Interval E-value
AmyAc_SLC3A2 cd11345
Alpha amylase catalytic domain found in solute carrier family 3 member 2 proteins; 4F2 ...
100-430 1.57e-142

Alpha amylase catalytic domain found in solute carrier family 3 member 2 proteins; 4F2 cell-surface antigen heavy chain (hc) is a protein that in humans is encoded by the SLC3A2 gene. 4F2hc is a multifunctional type II membrane glycoprotein involved in amino acid transport and cell fusion, adhesion, and transformation. It is related to bacterial alpha-glycosidases, but lacks alpha-glycosidase activity. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200483 [Multi-domain]  Cd Length: 326  Bit Score: 413.37  E-value: 1.57e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 100 APRCRELPVQRWWHKGALYRIGDLQAFvgPEARGIAGLKNHLEYLSTLKVKGLVLGPIHKNQKDEVNETDLKQIDPDLGS 179
Cdd:cd11345     1 APRCKPIPEMNWWNEGPLYQIGDLQAF--SEAGGLKGVEGKLDYLSQLKVKGLVLGPIHVVQADQPGELNLTEIDPDLGT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 180 QEDFKDLLQSAKKKSIHIILDLTPNYKGQNAWFlPPQADIVATKMKEALSSWLQDGVDGFQVRDVGKLANASLYlaEWQN 259
Cdd:cd11345    79 LEDFTSLLTAAHKKGISVVLDLTPNYRGESSWA-FSDAENVAEKVKEALEFWLNQGVDGIQVSDLENVASSASS--EWSN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 260 ITKNFSE-----DRLLIAGTASSDLQQIVNIL-ESTSDLLLTSSYLSQPVFTGEHAelLVIKYLNATGSRWCSWSVSQAG 333
Cdd:cd11345   156 LTAIVQKntdgkKRVLIGVTSSSSLSEISLLLnTSGVDLLLSGALLSASNRPSFGT--LVTQLLSTTGQRSLAWGIGARQ 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 334 LLTSF--IPAQFLRLYQLLLFTLPGTPVFSYGDELGLQAVALPGQPMEAP--FMLWNESsnsqtsspVSLNMTVKGQNED 409
Cdd:cd11345   234 GGHLAslVPAALVRLYQLLLFTLPGTPVFNYGDEIGLQDAQGKSPKMLRPnnEPEIAEE--------VNANMTAKAQKED 305
                         330       340
                  ....*....|....*....|.
gi 1958648956 410 PGSLLTQFRRLSDLRGKERSL 430
Cdd:cd11345   306 RGSLRSFFRSLSDLRGKERSL 326
AmyAc_maltase-like cd11329
Alpha amylase catalytic domain family found in maltase; Maltase (EC 3.2.1.20) hydrolyzes the ...
54-493 1.00e-34

Alpha amylase catalytic domain family found in maltase; Maltase (EC 3.2.1.20) hydrolyzes the terminal, non-reducing (1->4)-linked alpha-D-glucose residues in maltose, releasing alpha-D-glucose. The catalytic triad (DED) which is highly conserved in the other maltase group is not present in this subfamily. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200468 [Multi-domain]  Cd Length: 477  Bit Score: 136.36  E-value: 1.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956  54 FTGLSKEELLKVAGSPGWVRTRWALLLLFWLGWLGMLAGAVVIIVRAPRCrELPVQR-WWHKGALYRIGDLQAFvgpear 132
Cdd:cd11329     8 FSGMGKEELMKYANDPFWVRLRWLLFVLFWLLWVAMLLGAVAIIVLAPKC-AAPVPLkWWQKGPLVELDTESFF------ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 133 giagLKNHLEYLSTLKVKGLVL-GPIHknqkdevnETDLKqidPDLGSQEDFKDLLQSAKKKSIHIILDLTPNYKG-QNA 210
Cdd:cd11329    81 ----KEEHVEAISKLGAKGVIYeLPAD--------ETYLN---NSYGVESDLKELVKTAKQKDIKVILDLTPNHSSkQHP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 211 WF----------------------LPP----------------------------QAD------IVATKMKEALSSWLQD 234
Cdd:cd11329   146 LFkdsvlkeppyrsafvwadgkghTPPnnwlsvtggsawkwvedrqyylhqfgpdQPDlnlnnpAVVDELKDVLKHWLDL 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 235 GVDGFQVRDVGKL-------------ANASL---------------------YLAEWQNITKNFSEDR-LLIAG-TASSD 278
Cdd:cd11329   226 GVRGFRLANAKYLledpnlkdeeissNTKGVtpndygfythikttnlpelgeLLREWRSVVKNYTDGGgLSVAEdIIRPD 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 279 LQQIVNILESTSDLLLTSSYLS-QPVFTGEHAELLVIKYLNATGS--RWCSWSvsqagLLTSFIPAQFLRLYQLLLFTLP 355
Cdd:cd11329   306 VYQVNGTLDLLIDLPLYGNFLAkLSKAITANALHKILASISTVSAttSWPQWN-----LRYRDTKVVASDALTLFTSLLP 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 356 GTPVFSYGDELGLqavalpgqpmeapfmlwNESSNSqtsspvslnmtvkgqnedpGSLLTQFRRlsdlrgkERSLLHGDF 435
Cdd:cd11329   381 GTPVVPLDSELYA-----------------NVSKPT-------------------ISTLEKFRA-------TPSIQHGSF 417
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958648956 436 DA-LSSSSGLFSYVRHWDQNERYLVVLNfqdvgLSARVGASNLPAGISLPASANLLLST 493
Cdd:cd11329   418 NAyLLNNDTVFAYTRIKSGNPGYLVALN-----LSENPTVVDFSSDDGIPEEVTVVLTS 471
AmyAc_SLC3A1 cd11359
Alpha amylase catalytic domain found in Solute Carrier family 3 member 1 proteins; SLC3A1, ...
110-433 3.15e-29

Alpha amylase catalytic domain found in Solute Carrier family 3 member 1 proteins; SLC3A1, also called Neutral and basic amino acid transport protein rBAT or NBAT, plays a role in amino acid and cystine absorption. Mutations in the gene encoding SLC3A1 causes cystinuria, an autosomal recessive disorder characterized by the failure of proximal tubules to reabsorb filtered cystine and dibasic amino acids. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200494 [Multi-domain]  Cd Length: 456  Bit Score: 120.16  E-value: 3.15e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 110 RWWHKGALYRI-------------GDLqafvgpeargiAGLKNHLEYLSTLKVKGLVLGPIHKN-QKD---EVneTDLKQ 172
Cdd:cd11359     1 PWWQTSVIYQIyprsfkdsngdgnGDL-----------KGIREKLDYLKYLGVKTVWLSPIYKSpMKDfgyDV--SDFTD 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 173 IDPDLGSQEDFKDLLQSAKKKSIHIILDLTPN------------------YK------------------------GQNA 210
Cdd:cd11359    68 IDPMFGTMEDFERLLAAMHDRGMKLIMDFVPNhtsdkhewfqlsrnstnpYTdyyiwadctadgpgtppnnwvsvfGNSA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 211 W-------------FLPPQADI------VATKMKEALSSWLQDGVDGFQVRDVGKLANA--------------------- 250
Cdd:cd11359   148 WeydekrnqcylhqFLKEQPDLnfrnpdVQQEMDDVLRFWLDKGVDGFRVDAVKHLLEAthlrdepqvnptqppetqyny 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 251 -SLY-------------LAEWQNITKNFSED----RLLIaGTASSDLQQIV----NILESTSDLLLTSSYLSQPV-FTGE 307
Cdd:cd11359   228 sELYhdyttnqegvhdiIRDWRQTMDKYSSEpgryRFMI-TEVYDDIDTTMryygTSFKQEADFPFNFYLLDLGAnLSGN 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 308 HAELLVIKYL-NATGSRWCSWSV---SQAGLLTSFIPaQFLRLYQLLLFTLPGTPVFSYGDELGLQAVALP--------- 374
Cdd:cd11359   307 SINELVESWMsNMPEGKWPNWVLgnhDNSRIASRLGP-QYVRAMNMLLLTLPGTPTTYYGEEIGMEDVDISvdkekdpyt 385
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958648956 375 ---GQPMEAPfMLWNESSNSQTSS------PVSLN---MTVKGQNEDPGSLLTQFRRLSDLRGKERSLLHG 433
Cdd:cd11359   386 fesRDPERTP-MQWNNSNNAGFSDanktwlPVNSDyktVNVEVQKTDPTSMLNLYRELLLLRSSELALHRG 455
SLC3A2_N pfam16028
Solute carrier family 3 member 2 N-terminus; This domain is found at the N-terminus of solute ...
42-118 3.11e-27

Solute carrier family 3 member 2 N-terminus; This domain is found at the N-terminus of solute carrier family 3 member 2 proteins (4F2 cell-surface antigen heavy chain).


Pssm-ID: 464983  Cd Length: 77  Bit Score: 104.33  E-value: 3.11e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958648956  42 KVAEDEAEAGVKFTGLSKEELLKVAGSPGWVRTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPVQRWWHKGALY 118
Cdd:pfam16028   1 DAKIDIEAEKVKFTGLTKEELLKYANDPFWVRVRWALFVLFWLGWLGMLVGAIVIIVQAPKCKPPPPLSWWEKGPLY 77
AmyAc_OligoGlu_like cd11331
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
110-434 7.39e-27

Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins; Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200470 [Multi-domain]  Cd Length: 450  Bit Score: 113.19  E-value: 7.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 110 RWWHKGALYRI-------------GDLqafvgpeargiAGLKNHLEYLSTLKVKGLVLGPIHKN-QKD---EVneTDLKQ 172
Cdd:cd11331     1 LWWQTGVIYQIyprsfqdsngdgvGDL-----------RGIISRLDYLSDLGVDAVWLSPIYPSpMADfgyDV--SDYCG 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 173 IDPDLGSQEDFKDLLQSAKKKSIHIILDLTPNYK-----------------------------------------GQNAW 211
Cdd:cd11331    68 IDPLFGTLEDFDRLVAEAHARGLKVILDFVPNHTsdqhpwflesrssrdnpkrdwyiwrdpapdggppnnwrsefGGSAW 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 212 -------------FLPPQADI------VATKMKEALSSWLQDGVDGFQV------------RD-----------VGKLAN 249
Cdd:cd11331   148 twdertgqyylhaFLPEQPDLnwrnpeVRAAMHDVLRFWLDRGVDGFRVdvlwllikdpqfRDnppnpdwrggmPPHERL 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 250 ASLY----------LAEWQNITKNFSeDRLLIaGTASSDLQQIVNILESTSD---------LLLT---SSYLSQPVFTGE 307
Cdd:cd11331   228 LHIYtadqpetheiVREMRRVVDEFG-DRVLI-GEIYLPLDRLVAYYGAGRDglhlpfnfhLISLpwdAAALARAIEEYE 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 308 HAellvikyLNATGsrWCSWSVS---QAGLLTSFIPAQfLRLYQLLLFTLPGTPVFSYGDELGLQAVALPGQPMEAPF-- 382
Cdd:cd11331   306 AA-------LPAGA--WPNWVLGnhdQPRIASRVGPAQ-ARVAAMLLLTLRGTPTLYYGDELGMEDVPIPPERVQDPAel 375
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958648956 383 ---------------MLWNESSNSQTSS-----PVSLN---MTVKGQNEDPGSLLTQFRRLSDLRGKERSLLHGD 434
Cdd:cd11331   376 nqpggglgrdpertpMPWDASPNAGFSAadpwlPLSPDarqRNVATQEADPGSMLSLYRRLLALRRAHPALSAGS 450
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
111-424 3.03e-25

Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 108.03  E-value: 3.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 111 WWHKGALYRI-------------GDLQafvgpeargiaGLKNHLEYLSTLKVKGLVLGPIHKN-QKD---EVneTDLKQI 173
Cdd:COG0366     5 WWKDAVIYQIypdsfadsngdggGDLK-----------GIIEKLDYLKDLGVDAIWLSPFFPSpMSDhgyDI--SDYRDV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 174 DPDLGSQEDFKDLLQSAKKKSIHIILDLTPN----------------------------------------YKGQNAW-- 211
Cdd:COG0366    72 DPRFGTLADFDELVAEAHARGIKVILDLVLNhtsdehpwfqearagpdspyrdwyvwrdgkpdlppnnwfsIFGGSAWtw 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 212 -----------FLPPQADI------VATKMKEALSSWLQDGVDGFQV-------RDVGKLAN---ASLYLAEWQNITKNF 264
Cdd:COG0366   152 dpedgqyylhlFFSSQPDLnwenpeVREELLDVLRFWLDRGVDGFRLdavnhldKDEGLPENlpeVHEFLRELRAAVDEY 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 265 SEDRLLIAGTASSDLQQIVNILESTS-------DLLLTSSYLSQPVFTGEHAELLVIKYLNATGSRWCSWSVS---QAGL 334
Cdd:COG0366   232 YPDFFLVGEAWVDPPEDVARYFGGDEldmafnfPLMPALWDALAPEDAAELRDALAQTPALYPEGGWWANFLRnhdQPRL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 335 LTSFIPAQFLRLYQL---LLFTLPGTPVFSYGDELGlqavaLPGQPMEAPF--------MLWNESSN---SQTSSPVSLN 400
Cdd:COG0366   312 ASRLGGDYDRRRAKLaaaLLLTLPGTPYIYYGDEIG-----MTGDKLQDPEgrdgcrtpMPWSDDRNagfSTGWLPVPPN 386
                         410       420
                  ....*....|....*....|....*..
gi 1958648956 401 ---MTVKGQNEDPGSLLTQFRRLSDLR 424
Cdd:COG0366   387 ykaINVEAQEADPDSLLNFYRKLIALR 413
AmyAc_bac2_AmyA cd11316
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
120-433 4.65e-23

Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase); AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes Chloroflexi, Dictyoglomi, and Fusobacteria. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200455 [Multi-domain]  Cd Length: 403  Bit Score: 101.12  E-value: 4.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 120 IGDLQafvgpeargiaGLKNHLEYLSTLKVKGLVLGPIHKNQKD---EVneTDLKQIDPDLGSQEDFKDLLQSAKKKSIH 196
Cdd:cd11316    19 IGDLN-----------GLTEKLDYLNDLGVNGIWLMPIFPSPSYhgyDV--TDYYAIEPDYGTMEDFERLIAEAHKRGIK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 197 IILDLTPN-----------------------------------YKGQNAWFLPP------------QADI------VATK 223
Cdd:cd11316    86 VIIDLVINhtssehpwfqeaasspdspyrdyyiwadddpggwsSWGGNVWHKAGdggyyygafwsgMPDLnldnpaVREE 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 224 MKEALSSWLQDGVDGFQVrdvgklaNASLYLAE----WQNITKNF-------------SEDRLLIaGTASSDLQQIV--- 283
Cdd:cd11316   166 IKKIAKFWLDKGVDGFRL-------DAAKHIYEngegQADQEENIefwkefrdyvksvKPDAYLV-GEVWDDPSTIApyy 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 284 --------------NILESTSDLLLTSSYLSQPVFTGEHAELLVIKYLNAT---------GSRWCSWSVSQAglltsfip 340
Cdd:cd11316   238 asgldsafnfdlaeAIIDSVKNGGSGAGLAKALLRVYELYAKYNPDYIDAPflsnhdqdrVASQLGGDEAKA-------- 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 341 aqflRLYQLLLFTLPGTPVFSYGDELGLQAvalpGQPME---APfMLWNESSNSQTSSP----VSLNMTVKG---QNEDP 410
Cdd:cd11316   310 ----KLAAALLLTLPGNPFIYYGEEIGMLG----SKPDEnirTP-MSWDADSGAGFTTWipprPNTNATTASveaQEADP 380
                         410       420
                  ....*....|....*....|...
gi 1958648956 411 GSLLTQFRRLSDLRGKERSLLHG 433
Cdd:cd11316   381 DSLLNHYKRLIALRNEYPALARG 403
AmyAc_family cd00551
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
134-366 1.33e-22

Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; and C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost this catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200451 [Multi-domain]  Cd Length: 260  Bit Score: 97.24  E-value: 1.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 134 IAGLKNHLEYLSTLKVKGLVLGPIHKNQ-----KDEVNETDLKQIDPDLGSQEDFKDLLQSAKKKSIHIILDLTPNYkgq 208
Cdd:cd00551    24 LKGIIDKLDYLKDLGVTAIWLTPIFESPeydgyDKDDGYLDYYEIDPRLGTEEDFKELVKAAHKRGIKVILDLVFNH--- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 209 nawflppqadivatkmkEALSSWLQDGVDGFQVRDVGKLANASL--YLAEWQNITKNFSEDRLLIAGT-ASSDLQQIVNI 285
Cdd:cd00551   101 -----------------DILRFWLDEGVDGFRLDAAKHVPKPEPveFLREIRKDAKLAKPDTLLLGEAwGGPDELLAKAG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 286 LESTSDLLL--TSSYLSQPVFTGEHAELLVIK--YLNATGSRWCSWSV---------SQAGLLTSFIPAQFLRLYQLLLF 352
Cdd:cd00551   164 FDDGLDSVFdfPLLEALRDALKGGEGALAILAalLLLNPEGALLVNFLgnhdtfrlaDLVSYKIVELRKARLKLALALLL 243
                         250
                  ....*....|....
gi 1958648956 353 TLPGTPVFSYGDEL 366
Cdd:cd00551   244 TLPGTPMIYYIKKL 257
AmyAc_maltase cd11328
Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related ...
111-436 1.10e-19

Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related proteins; Maltase (EC 3.2.1.20) hydrolyzes the terminal, non-reducing (1->4)-linked alpha-D-glucose residues in maltose, releasing alpha-D-glucose. In most cases, maltase is equivalent to alpha-glucosidase, but the term "maltase" emphasizes the disaccharide nature of the substrate from which glucose is cleaved, and the term "alpha-glucosidase" emphasizes the bond, whether the substrate is a disaccharide or polysaccharide. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200467 [Multi-domain]  Cd Length: 470  Bit Score: 91.91  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 111 WWHKGALYRI-------------GDLQafvgpeargiaGLKNHLEYLSTLKVKGLVLGPIHKN-QKD---EVneTDLKQI 173
Cdd:cd11328     4 WWENAVFYQIyprsfkdsdgdgiGDLK-----------GITEKLDYFKDIGIDAIWLSPIFKSpMVDfgyDI--SDFTDI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 174 DPDLGSQEDFKDLLQSAKKKSIHIILDLTPN------------------YK--------------------------GQN 209
Cdd:cd11328    71 DPIFGTMEDFEELIAEAKKLGLKVILDFVPNhssdehewfqksvkrdepYKdyyvwhdgknndngtrvppnnwlsvfGGS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 210 AW-------------FLPPQADI------VATKMKEALSSWLQDGVDGFQV----------------RDVGKLANASLYL 254
Cdd:cd11328   151 AWtwneerqqyylhqFAVKQPDLnyrnpkVVEEMKNVLRFWLDKGVDGFRIdavphlfededfldepYSDEPGADPDDYD 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 255 AEWQNITKNFSEDRLLIAG--------TASSDLQQIVNILESTSDLLLTSSYLSQPVFTGEHAEL--LVIKYLNATGS-- 322
Cdd:cd11328   231 YLDHIYTKDQPETYDLVYEwrevldeyAKENNGDTRVMMTEAYSSLDNTMKYYGNETTYGAHFPFnfELITNLNKNSNat 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 323 ----------------RWCSWSVS---QAGLLTSFiPAQFLRLYQLLLFTLPGTPVFSYGDELGLQAV------------ 371
Cdd:cd11328   311 dfkdlidkwldnmpegQTANWVLGnhdNPRVASRF-GEERVDGMNMLSMLLPGVAVTYYGEEIGMEDTtiswedtvdppa 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 372 --ALPGQ-------PMEAPFmLWNESSN---SQTSSP--------VSLNmtVKGQNEDPGSLLTQFRRLSDLRgKERSLL 431
Cdd:cd11328   390 cnAGPENyeaysrdPARTPF-QWDDSKNagfSTANKTwlpvnpnyKTLN--LEAQKKDPRSHYNIYKKLAQLR-KSPTFL 465

                  ....*
gi 1958648956 432 HGDFD 436
Cdd:cd11328   466 RGDLE 470
AmyAc_TreS cd11334
Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) ...
111-424 2.56e-18

Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) catalyzes the reversible interconversion of trehalose and maltose. The enzyme catalyzes the reaction in both directions, but the preferred substrate is maltose. Glucose is formed as a by-product of this reaction. It is believed that the catalytic mechanism may involve the cutting of the incoming disaccharide and transfer of a glucose to an enzyme-bound glucose. This enzyme also catalyzes production of a glucosamine disaccharide from maltose and glucosamine. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200473 [Multi-domain]  Cd Length: 447  Bit Score: 87.23  E-value: 2.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 111 WWHKGALYRIgDLQAFVGPEARGI---AGLKNHLEYLSTLKVKGLVLGPIHK--NQKDEVNETDLKQIDPDLGSQEDFKD 185
Cdd:cd11334     1 WYKNAVIYQL-DVRTFMDSNGDGIgdfRGLTEKLDYLQWLGVTAIWLLPFYPspLRDDGYDIADYYGVDPRLGTLGDFVE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 186 LLQSAKKKSIHIILDLTPNYKG-QNAWFL-------------------PP------------------------------ 215
Cdd:cd11334    80 FLREAHERGIRVIIDLVVNHTSdQHPWFQaarrdpdspyrdyyvwsdtPPkykdariifpdveksnwtwdevagayywhr 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 216 ----QADI------VATKMKEALSSWLQDGVDGFQV------------------------RDVGKLANAS----LYLAE- 256
Cdd:cd11334   160 fyshQPDLnfdnpaVREEILRIMDFWLDLGVDGFRLdavpylieregtncenlpethdflKRLRAFVDRRypdaILLAEa 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 257 --WQNITKNF--SEDRL-----------LIAGTASSDLQQIVNILESTSDLLLTSSYLsqpVFTGEHAELLVIKYLNAtg 321
Cdd:cd11334   240 nqWPEEVREYfgDGDELhmafnfplnprLFLALAREDAFPIIDALRQTPPIPEGCQWA---NFLRNHDELTLEMLTDE-- 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 322 srwcswsvSQAGLLTSFIPAQFLRLYQL----------------------LLFTLPGTPVFSYGDELGL-QAVALPG-QP 377
Cdd:cd11334   315 --------ERDYVYAAFAPDPRMRIYNRgirrrlapmlggdrrrielaysLLFSLPGTPVIYYGDEIGMgDNLYLPDrDG 386
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958648956 378 MEAPfMLWNESSNSQTSS--------PV---------SLNmtVKGQNEDPGSLLTQFRRLSDLR 424
Cdd:cd11334   387 VRTP-MQWSADRNGGFSTadpqklylPViddgpygyeRVN--VEAQRRDPSSLLNWVRRLIALR 447
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
121-368 7.74e-16

Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.


Pssm-ID: 395077 [Multi-domain]  Cd Length: 334  Bit Score: 78.55  E-value: 7.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 121 GDLQafvgpeargiaGLKNHLEYLSTLKVKGLVLGPIHKNQKDE--VNETDLKQIDPDLGSQEDFKDLLQSAKKKSIHII 198
Cdd:pfam00128   1 GDLQ-----------GIIEKLDYLKELGVTAIWLSPIFDSPQADhgYDIADYYKIDPHYGTMEDFKELISKAHERGIKVI 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 199 LDLTPN----------------------------------------YKGQNAW-------------FLPPQADI------ 219
Cdd:pfam00128  70 LDLVVNhtsdehawfqesrsskdnpyrdyyfwrpgggpippnnwrsYFGGSAWtydekgqeyylhlFVAGQPDLnwenpe 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 220 VATKMKEALSSWLQDGVDGFQVrDVGKL---------ANASLYLAEW---QNITKNFSEDRLL---IAGTASSDLQQIVN 284
Cdd:pfam00128 150 VRNELYDVVRFWLDKGIDGFRI-DVVKHiskvpglpfENNGPFWHEFtqaMNETVFGYKDVMTvgeVFHGDGEWARVYTT 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 285 ilESTSDLLLTSSYLSQPVFTGEHAELLVIKY----LNATGSRWCSWSVSQAGLLTSFI--------------PAQFLRL 346
Cdd:pfam00128 229 --EARMELEMGFNFPHNDVALKPFIKWDLAPIsarkLKEMITDWLDALPDTNGWNFTFLgnhdqprflsrfgdDRASAKL 306
                         330       340
                  ....*....|....*....|..
gi 1958648956 347 YQLLLFTLPGTPVFSYGDELGL 368
Cdd:pfam00128 307 LAVFLLTLRGTPYIYQGEEIGM 328
AmyAc_OligoGlu cd11330
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
111-445 5.67e-15

Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins; Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200469 [Multi-domain]  Cd Length: 472  Bit Score: 77.30  E-value: 5.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 111 WWHKGALYRI-------------GDLQafvgpeargiaGLKNHLEYLSTLKVKGLVLGPIHKN-QKD---EVneTDLKQI 173
Cdd:cd11330     2 WWRGAVIYQIyprsfldsngdgiGDLP-----------GITEKLDYIASLGVDAIWLSPFFKSpMKDfgyDV--SDYCAV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 174 DPDLGSQEDFKDLLQSAKKKSIHIILDLTPNYK-----------------------------------------GQNAW- 211
Cdd:cd11330    69 DPLFGTLDDFDRLVARAHALGLKVMIDQVLSHTsdqhpwfeesrqsrdnpkadwyvwadpkpdgsppnnwlsvfGGSAWq 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 212 ------------FLPPQADI------VATKMKEALSSWLQDGVDGFQV-----------------RDVGK----LANASL 252
Cdd:cd11330   149 wdprrgqyylhnFLPSQPDLnfhnpeVQDALLDVARFWLDRGVDGFRLdavnfymhdpalrdnppRPPDEredgVAPTNP 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 253 YlaEWQNITKNFS------------------EDRLLIAGTASSDLQQIVNILESTSDLL---LTSSYLSQPvFTGEHAEL 311
Cdd:cd11330   229 Y--GMQLHIHDKSqpenlaflerlralldeyPGRFLVGEVSDDDPLEVMAEYTSGGDRLhmaYSFDLLGRP-FSAAVVRD 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 312 LVIKYLNATGSRWCSWSVS---QAGLLTSFIPAQ----FLRLYQLLLFTLPGTPVFSYGDELGLQAVALPGQPMEAPF-- 382
Cdd:cd11330   306 ALEAFEAEAPDGWPCWAFSnhdVPRAVSRWAGGAddpaLARLLLALLLSLRGSVCLYQGEELGLPEAELPFEELQDPYgi 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 383 ---------------MLWNES------SNSQTSSPVS---LNMTVKGQNEDPGSLLTQFRRLSDLRGKERSLLHGDFDAL 438
Cdd:cd11330   386 tfwpefkgrdgcrtpMPWQADaphagfSTAKPWLPVPpehLALAVDVQEKDPGSVLNFYRRFLAWRKAQPALRTGTITFL 465

                  ....*..
gi 1958648956 439 SSSSGLF 445
Cdd:cd11330   466 DAPEPLL 472
AmyAc_SI_OligoGlu_DGase cd11333
Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called ...
120-424 1.39e-14

Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), dextran glucosidase (also called glucan 1,6-alpha-glucosidase), and related proteins; The sucrose isomerases (SIs) Isomaltulose synthase (EC 5.4.99.11) and Trehalose synthase (EC 5.4.99.16) catalyze the isomerization of sucrose and maltose to produce isomaltulose and trehalulose, respectively. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Dextran glucosidase (DGase, EC 3.2.1.70) hydrolyzes alpha-1,6-glucosidic linkages at the non-reducing end of panose, isomaltooligosaccharides and dextran to produce alpha-glucose.The common reaction chemistry of the alpha-amylase family enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. Both enzymes contain the three catalytic residues (Asp, Glu and Asp) common to the alpha-amylase family as well as two histidine residues which are predicted to be critical to binding the glucose residue adjacent to the scissile bond in the substrates. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200472 [Multi-domain]  Cd Length: 428  Bit Score: 75.57  E-value: 1.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 120 IGDLQafvgpearGIAglkNHLEYLSTLKVKGLVLGPIHKN-QKD---EVneTDLKQIDPDLGSQEDFKDLLQSAKKKSI 195
Cdd:cd11333    21 IGDLP--------GII---SKLDYLKDLGVDAIWLSPIYPSpQVDngyDI--SDYRAIDPEFGTMEDFDELIKEAHKRGI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 196 HIILDL------------------------------------TPN----YKGQNAW-------------FLPPQADI--- 219
Cdd:cd11333    88 KIIMDLvvnhtsdehpwfqesrssrdnpyrdyyiwrdgkdgkPPNnwrsFFGGSAWeydpetgqyylhlFAKEQPDLnwe 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 220 ---VATKMKEALSSWLQDGVDGFQVrDV----------------------GKLANASL-----YLAEWQNITknFSE-DR 268
Cdd:cd11333   168 npeVRQEIYDMMRFWLDKGVDGFRL-DVinliskdpdfpdappgdgdglsGHKYYANGpgvheYLQELNREV--FSKyDI 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 269 LLIAGTASSDLQQIVNILESTSDLLltssylsQPVFTGEHAEllvIKYLNATGSRWCSWSV---------SQAGLLTSFI 339
Cdd:cd11333   245 MTVGEAPGVDPEEALKYVGPDRGEL-------SMVFNFEHLD---LDYGPGGKWKPKPWDLeelkkilskWQKALQGDGW 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 340 PAQFL-----------------------RLYQLLLFTLPGTPVFSYGDELGlqavalpgqpME-------APfMLWNESS 389
Cdd:cd11333   315 NALFLenhdqprsvsrfgndgeyrvesaKMLATLLLTLRGTPFIYQGEEIG----------MTnsrdnarTP-MQWDDSP 383
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1958648956 390 NS--QTSSP---VSLN---MTVKGQNEDPGSLLTQFRRLSDLR 424
Cdd:cd11333   384 NAgfSTGKPwlpVNPNykeINVEAQLADPDSVLNFYKKLIALR 426
AmyAc_CMD cd11338
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ...
101-435 1.45e-13

Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200477 [Multi-domain]  Cd Length: 389  Bit Score: 72.52  E-value: 1.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 101 PRCRELPVQRWWHKGALYRI----GDLQafvgpearGIAglkNHLEYLSTLKVKGLVLGPI------HKnqkdeVNETDL 170
Cdd:cd11338    29 FGWPDLPDYPPPWGGEPTRRdfygGDLQ--------GII---EKLDYLKDLGVNAIYLNPIfeapsnHK-----YDTADY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 171 KQIDPDLGSQEDFKDLLQSAKKKSIHIILDLTPN--------------YKGQNA---WFLPPQADIVATKMKEALSSW-- 231
Cdd:cd11338    93 FKIDPHLGTEEDFKELVEEAHKRGIRVILDGVFNhtgddspyfqdvlkYGESSAyqdWFSIYYFWPYFTDEPPNYESWwg 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 232 -------------LQD-------------GVDGFqvR-DVgklANaSLYLAEWQNI---TKNFSEDRLLIA---GTASSD 278
Cdd:cd11338   173 vpslpklntenpeVREyldsvarywlkegDIDGW--RlDV---AD-EVPHEFWREFrkaVKAVNPDAYIIGevwEDARPW 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 279 LQQivNILEST-----SDLLLtsSYLSQPVFTGEHAELLVIKYLNATGsrwcsWSVSQAG--LLTS-------FIPAQFL 344
Cdd:cd11338   247 LQG--DQFDSVmnypfRDAVL--DFLAGEEIDAEEFANRLNSLRANYP-----KQVLYAMmnLLDShdtprilTLLGGDK 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 345 RLYQL---LLFTLPGTPVFSYGDELGLQAVALPG--QPMEapfmlWNESSnsqtsspvslnmtvkgQNEDpgsLLTQFRR 419
Cdd:cd11338   318 ARLKLalaLQFTLPGAPCIYYGDEIGLEGGKDPDnrRPMP-----WDEEK----------------WDQD---LLEFYKK 373
                         410
                  ....*....|....*.
gi 1958648956 420 LSDLRGKERSLLHGDF 435
Cdd:cd11338   374 LIALRKEHPALRTGGF 389
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
134-424 5.19e-12

Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200478 [Multi-domain]  Cd Length: 344  Bit Score: 67.28  E-value: 5.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 134 IAGLKNHLEYLSTLKVKGLVLGPIHKNQKDEVNE--------TDLKQIDPDLGSQEDFKDLLQSAKKKSIHIILDLTPNY 205
Cdd:cd11339    44 FKGLIDKLDYIKDLGFTAIWITPVVKNRSVQAGSagyhgywgYDFYRIDPHLGTDADLQDLIDAAHARGIKVILDIVVNH 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 206 KGqnawflppqaDI------VATKMKEALSSWLQDGVDGFQV-----------------------------------RDV 244
Cdd:cd11339   124 TG----------DLntenpeVVDYLIDAYKWWIDTGVDGFRIdtvkhvprefwqefapairqaagkpdffmfgevydGDP 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 245 GKLA--------NASLYLAEWQNITKNFSedrlliAGTASSDLQQivniLESTSDLLLTSSYLsqPVFTGEHaELLVIKY 316
Cdd:cd11339   194 SYIApytttaggDSVLDFPLYGAIRDAFA------GGGSGDLLQD----LFLSDDLYNDATEL--VTFLDNH-DMGRFLS 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 317 LNATGSrwcswsvsqAGLLTSFIPAQFlrlyqlLLFTLPGTPVFSYGDELGLQAVALPGQPMEAPFmlwnessnsqtssP 396
Cdd:cd11339   261 SLKDGS---------ADGTARLALALA------LLFTSRGIPCIYYGTEQGFTGGGDPDNGRRNMF-------------A 312
                         330       340
                  ....*....|....*....|....*....
gi 1958648956 397 VSLNMTVKGQNEDPGSLLTQ-FRRLSDLR 424
Cdd:cd11339   313 STGDLTSADDNFDTDHPLYQyIARLNRIR 341
AmyAc_CMD_like cd11337
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ...
111-435 1.18e-11

Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is mainly bacterial. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200476 [Multi-domain]  Cd Length: 328  Bit Score: 66.01  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 111 WWHkgaLYRIGDLQA-----FVGPEARGIAGLKNHLEYLSTLKVKGLVLGPIHKNQKDEVNETDLKQIDPDLGSQEDFKD 185
Cdd:cd11337     2 FYH---IYPLGFCGApirndFDGPPEHRLLKLEDWLPHLKELGCNALYLGPVFESDSHGYDTRDYYRIDRRLGTNEDFKA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 186 LLQSAKKKSIHIILDLTPNYKGQNAWF--------LPPQADIVATKMKEALSSWLQDG-VDGfqVR-DVGKLANASlYLA 255
Cdd:cd11337    79 LVAALHERGIRVVLDGVFNHVGRDFFWeghydlvkLNLDNPAVVDYLFDVVRFWIEEFdIDG--LRlDAAYCLDPD-FWR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 256 EWQNITKNFSEDRLLIAGTASSDLQQIVNilESTSDLL--------LTSSYLSQPVFtgEhaellvIKYLNATGSRwcSW 327
Cdd:cd11337   156 ELRPFCRELKPDFWLMGEVIHGDYNRWVN--DSMLDSVtnyelykgLWSSHNDHNFF--E------IAHSLNRLFR--HN 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 328 SVSQAGLLTSFI-------------PAQFLRLYQLLLFTLPGTPVFSYGDELGLQAVALPGQPMEAPFMLWNESsnsqts 394
Cdd:cd11337   224 GLYRGFHLYTFVdnhdvtriasilgDKAHLPLAYALLFTMPGIPSIYYGSEWGIEGVKEEGSDADLRPLPLRPA------ 297
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1958648956 395 spvslnmtvkgQNEDPGSLLTQF-RRLSDLRGKERSLLHGDF 435
Cdd:cd11337   298 -----------ELSPLGNELTRLiQALIALRRRSPALCYGSY 328
Aamy smart00642
Alpha-amylase domain;
120-211 1.73e-11

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 62.73  E-value: 1.73e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956  120 IGDLQafvgpeargiaGLKNHLEYLSTLKVKGLVLGPIHKN-QKDEVNE----TDLKQIDPDLGSQEDFKDLLQSAKKKS 194
Cdd:smart00642  15 GGDLQ-----------GIIEKLDYLKDLGVTAIWLSPIFESpQGYPSYHgydiSDYKQIDPRFGTMEDFKELVDAAHARG 83
                           90
                   ....*....|....*..
gi 1958648956  195 IHIILDLTPNYKGQNAW 211
Cdd:smart00642  84 IKVILDVVINHTSDGGF 100
PRK10933 PRK10933
trehalose-6-phosphate hydrolase; Provisional
111-212 2.74e-10

trehalose-6-phosphate hydrolase; Provisional


Pssm-ID: 182849 [Multi-domain]  Cd Length: 551  Bit Score: 62.84  E-value: 2.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 111 WWHKGALYRI--GDLQAFVGPEARGIAGLKNHLEYLSTLKVKGLVLGPIH-----KNQKDEVNETdlkQIDPDLGSQEDF 183
Cdd:PRK10933    7 WWQNGVIYQIypKSFQDTTGSGTGDLRGVTQRLDYLQKLGVDAIWLTPFYvspqvDNGYDVANYT---AIDPTYGTLDDF 83
                          90       100       110
                  ....*....|....*....|....*....|
gi 1958648956 184 KDLLQSAKKKSIHIILDLTPNYKG-QNAWF 212
Cdd:PRK10933   84 DELVAQAKSRGIRIILDMVFNHTStQHAWF 113
AmyAc_bac_CMD_like_3 cd11340
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
134-218 3.99e-10

Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200479 [Multi-domain]  Cd Length: 407  Bit Score: 61.84  E-value: 3.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 134 IAGLKNHLEYLSTLKVKGLVLGPIHKNqkDEVNE-------TDLKQIDPDLGSQEDFKDLLQSAKKKSIHIILDLTPNYK 206
Cdd:cd11340    44 IQGIIDHLDYLQDLGVTAIWLTPLLEN--DMPSYsyhgyaaTDFYRIDPRFGSNEDYKELVSKAHARGMKLIMDMVPNHC 121
                          90
                  ....*....|....
gi 1958648956 207 GQNAWFL--PPQAD 218
Cdd:cd11340   122 GSEHWWMkdLPTKD 135
AmyAc_arch_bac_AmyA cd11313
Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1, ...
134-244 3.55e-09

Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase); AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes firmicutes, bacteroidetes, and proteobacteria. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200452 [Multi-domain]  Cd Length: 336  Bit Score: 58.33  E-value: 3.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 134 IAGLKNHLEYLSTLKVKGLVLGPIH----KNQKDEVNE----TDLKQIDPDLGSQEDFKDLLQSAKKKSIHIILDLTPNY 205
Cdd:cd11313    21 FKAVTKDLPRLKDLGVDILWLMPIHpigeKNRKGSLGSpyavKDYRAVNPEYGTLEDFKALVDEAHDRGMKVILDWVANH 100
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958648956 206 KG-QNAWFLPPQ------------------ADIVA---------TKMKEALSSWLQD-GVDGFQVrDV 244
Cdd:cd11313   101 TAwDHPLVEEHPewylrdsdgnitnkvfdwTDVADldysnpelrDYMIDAMKYWVREfDVDGFRC-DV 167
AmyAc_2 cd11348
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
120-420 6.26e-09

Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The catalytic triad (DED) is not present here. The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200486 [Multi-domain]  Cd Length: 429  Bit Score: 58.09  E-value: 6.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 120 IGDLQafvgpeargiaGLKNHLEYLSTLKVKGLVLGPIHKNQ-KD---EVneTDLKQIDPDLGSQEDFKDLLQSAKKKSI 195
Cdd:cd11348    18 IGDLQ-----------GIISKLDYIKSLGCNAIWLNPCFDSPfKDagyDV--RDYYKVAPRYGTNEDLVRLFDEAHKRGI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 196 HIILDLTPNYKG-QNAWFL---------------------------------------------------------PPQ- 216
Cdd:cd11348    85 HVLLDLVPGHTSdEHPWFKeskkaenneysdryiwtdsiwsggpglpfvggeaerngnyivnffscqpalnygfahPPTe 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 217 --------ADIVATK--MKEALSSWLQDGVDGFQV--------RDVGKLANASLY----------------LAEW----Q 258
Cdd:cd11348   165 pwqqpvdaPGPQATReaMKDIMRFWLDKGADGFRVdmadslvkNDPGNKETIKLWqeirawldeeypeavlVSEWgnpeQ 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 259 NITKNFSEDRLL-IAGTASSDLQQIVNILESTSDlllTSSYLSqPVFTGEHAELL--VIKYLNATGsrwcswsvsqAGLL 335
Cdd:cd11348   245 SLKAGFDMDFLLhFGGNGYNSLFRNLNTDGGHRR---DNCYFD-ASGKGDIKPFVdeYLPQYEATK----------GKGY 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 336 TSFI--------------PAQfLRLYQLLLFTLPGTPVFSYGDELGLQAValPGQP-MEAPF--------MLWNESSNS- 391
Cdd:cd11348   311 ISLPtcnhdtprlnarltEEE-LKLAFAFLLTMPGVPFIYYGDEIGMRYI--EGLPsKEGGYnrtgsrtpMQWDSGKNAg 387
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1958648956 392 -QTSSPVSLNM---------TVKGQNEDPGSLLTQFRRL 420
Cdd:cd11348   388 fSTAPAERLYLpvdpapdrpTVAAQEDDPNSLLNFVRDL 426
AmyAc_bac_CMD_like cd11354
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
111-200 8.66e-09

Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200491 [Multi-domain]  Cd Length: 357  Bit Score: 57.34  E-value: 8.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 111 WWHkgaLYRIGdlqaFVG----------PEARGIAGLKNHLEYLSTLKVKGLVLGPIHKNQKDEVNETDLKQIDPDLGSQ 180
Cdd:cd11354     4 WWH---VYPLG----FVGapirprepeaAVEHRLDRLEPWLDYAVELGCNGLLLGPVFESASHGYDTLDHYRIDPRLGDD 76
                          90       100
                  ....*....|....*....|
gi 1958648956 181 EDFKDLLQSAKKKSIHIILD 200
Cdd:cd11354    77 EDFDALIAAAHERGLRVLLD 96
AmyAc_OligoGlu_TS cd11332
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
111-212 2.85e-08

Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), trehalose synthase (also called maltose alpha-D-glucosyltransferase), and related proteins; Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Trehalose synthase (EC 5.4.99.16) catalyzes the isomerization of maltose to produce trehalulose. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200471 [Multi-domain]  Cd Length: 481  Bit Score: 56.13  E-value: 2.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 111 WWHKGALYRI-------------GDLqafvgpeargiAGLKNHLEYLSTLKVKGLVLGPIHKN-QKD---EVneTDLKQI 173
Cdd:cd11332     2 WWRDAVVYQVyprsfadangdgiGDL-----------AGIRARLPYLAALGVDAIWLSPFYPSpMADggyDV--ADYRDV 68
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958648956 174 DPDLGSQEDFKDLLQSAKKKSIHIILDLTPNY-KGQNAWF 212
Cdd:cd11332    69 DPLFGTLADFDALVAAAHELGLRVIVDIVPNHtSDQHPWF 108
PRK10785 PRK10785
maltodextrin glucosidase; Provisional
134-514 1.50e-07

maltodextrin glucosidase; Provisional


Pssm-ID: 236759 [Multi-domain]  Cd Length: 598  Bit Score: 54.24  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 134 IAGLKNHLEYLSTLKVKGLVLGPI---HKNQKdeVNETDLKQIDPDLGSQEDFKDLLQSAKKKSIHIILDLTPNYKG-QN 209
Cdd:PRK10785  178 LDGISEKLPYLKKLGVTALYLNPIftaPSVHK--YDTEDYRHVDPQLGGDAALLRLRHATQQRGMRLVLDGVFNHTGdSH 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 210 AWFLPPQADIVAT--KMKEALSSWLQDGVDGfqvRDVGKLANASL--------------YLAE------WQNITKNFSED 267
Cdd:PRK10785  256 PWFDRHNRGTGGAchHPDSPWRDWYSFSDDG---RALDWLGYASLpkldfqseevvneiYRGEdsivrhWLKAPYNIDGW 332
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 268 RLLI------AGTASSDLQQIVNILESTSDllltssylSQP---VFtGEH-----------AELLVIKY----------- 316
Cdd:PRK10785  333 RLDVvhmlgeGGGARNNLQHVAGITQAAKE--------ENPeayVL-GEHfgdarqwlqadVEDAAMNYrgfafplrafl 403
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 317 -----------LNA-TGSRW---------CSWSVSQAGLLTSFIPAQFLRL-------YQL---LLFTLPGTPVFSYGDE 365
Cdd:PRK10785  404 antdiayhpqqIDAqTCAAWmdeyraglpHQQQLRQFNQLDSHDTARFKTLlggdkarMPLalvWLFTWPGVPCIYYGDE 483
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 366 LGLQAvalPGQPM-EAPFMlWNESSNSQTsspvslnmtvkgqnedpgsLLTQFRRLSDLRGKERSLLHGDFDALSSSSGL 444
Cdd:PRK10785  484 VGLDG---GNDPFcRKPFP-WDEAKQDGA-------------------LLALYQRMIALRKKSQALRRGGCQVLYAEGNV 540
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 445 FSYVRHWDQnERYLVVLNfqdvglsaRVGASNlpagISLPASAnlLLSTDSTRLSREEGTSLSLENLSLN 514
Cdd:PRK10785  541 VVFARVLQQ-QRVLVAIN--------RGEACE----VVLPASP--LLNVAQWQRKEGHGDLTDGGGVILT 595
AmyAc_5 cd11352
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
109-218 2.67e-07

Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200489 [Multi-domain]  Cd Length: 443  Bit Score: 53.09  E-value: 2.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 109 QRWWHKGAlyrigdlQAFVGpearG-IAGLKNHLEYLSTLKVKGLVLGPIHKNQKDEvnET-------DLKQIDPDLGSQ 180
Cdd:cd11352    34 NFGWESQG-------QRFQG----GtLKGVRSKLGYLKRLGVTALWLSPVFKQRPEL--ETyhgygiqNFLDVDPRFGTR 100
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958648956 181 EDFKDLLQSAKKKSIHIILDLTPNYKGQNaWFLPPQAD 218
Cdd:cd11352   101 EDLRDLVDAAHARGIYVILDIILNHSGDV-FSYDDDRP 137
AmyAc_euk_bac_CMD_like cd11353
Alpha amylase catalytic domain found in eukaryotic and bacterial cyclomaltodextrinases and ...
126-211 1.41e-06

Alpha amylase catalytic domain found in eukaryotic and bacterial cyclomaltodextrinases and related proteins; Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is mainly bacterial. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200490 [Multi-domain]  Cd Length: 366  Bit Score: 50.64  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 126 FVGPEARGIAGLKNHLEYLSTLKVKGLVLGPIHKNQKDEVNETDLKQIDPDLGSQEDFKDLLQSAKKKSIHIILDLTPNY 205
Cdd:cd11353    21 FDGETEHRILKLEDWIPHLKKLGINAIYFGPVFESDSHGYDTRDYYKIDRRLGTNEDFKAVCKKLHENGIKVVLDGVFNH 100

                  ....*.
gi 1958648956 206 KGQNAW 211
Cdd:cd11353   101 VGRDFF 106
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
117-241 5.52e-06

Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins; Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200459 [Multi-domain]  Cd Length: 389  Bit Score: 48.82  E-value: 5.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 117 LYRIGDLQafvgpeargiaGLKNHLEYLSTLKVKGLVLGPIHKNQ---KDEVNET--------DLKQIDPDLGSQEDFKD 185
Cdd:cd11320    40 KYWGGDWQ-----------GIIDKLPYLKDLGVTAIWISPPVENInspIEGGGNTgyhgywarDFKRTNEHFGTWEDFDE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 186 LLQSAKKKSIHIILDLTPN-----------------------YKGQNAWF-------------------LPPQAD----- 218
Cdd:cd11320   109 LVDAAHANGIKVIIDFVPNhsspadyaedgalydngtlvgdyPNDDNGWFhhnggiddwsdreqvryknLFDLADlnqsn 188
                         170       180
                  ....*....|....*....|....
gi 1958648956 219 -IVATKMKEALSSWLQDGVDGFQV 241
Cdd:cd11320   189 pWVDQYLKDAIKFWLDHGIDGIRV 212
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
168-273 5.31e-05

Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase); AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes Firmicutes, Proteobacteria, Actinobacteria, and Cyanobacteria. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200454 [Multi-domain]  Cd Length: 352  Bit Score: 45.35  E-value: 5.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 168 TDLKQIDPDLGSQEDFKDLLQSAKKKSIHIILDLTPNY--------------------KGQNAWF--------------- 212
Cdd:cd11315    55 TDYRIGNNQLGTEDDFKALCAAAHKYGIKIIVDVVFNHmanegsaiedlwypsadielFSPEDFHgnggisnwndrwqvt 134
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958648956 213 ---------LPPQADIVATKMKEALSSWLQDGVDGFQVrDVGK-------LANASLYlaeWQNITKNFSEDRLLIAG 273
Cdd:cd11315   135 qgrlgglpdLNTENPAVQQQQKAYLKALVALGVDGFRF-DAAKhielpdePSKASDF---WTNILNNLDKDGLFIYG 207
PRK14507 PRK14507
malto-oligosyltrehalose synthase;
67-213 2.54e-04

malto-oligosyltrehalose synthase;


Pssm-ID: 237737 [Multi-domain]  Cd Length: 1693  Bit Score: 43.94  E-value: 2.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956   67 GSPGWVR------TRWALLLLFWLGWLGM--LAGAVVIIVRAPRCRELPVQRWWHKgALYRIGDLQAFVGPEARGIaglk 138
Cdd:PRK14507   689 GYPNWRRkldrnlEAIAAPPRLQAVGGALakLRPRLSAEERGPRSGAARLAAAPPR-ATYRLQFHKDFTFADAEAI---- 763
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956  139 nhLEYLSTLKVKGLVLGPIHKNQKDEV---NETDLKQIDPDLGSQEDFKDLLQSAKKKSIHIILDLTPNYKG----QNAW 211
Cdd:PRK14507   764 --LPYLAALGISHVYASPILKARPGSThgyDIVDHSQINPEIGGEEGFERFCAALKAHGLGQLLDIVPNHMGvggaDNPW 841

                   ..
gi 1958648956  212 FL 213
Cdd:PRK14507   842 WL 843
AmyAc_GlgE_like cd11344
Alpha amylase catalytic domain found in GlgE-like proteins; GlgE is a (1,4)-a-D-glucan: ...
171-201 2.15e-03

Alpha amylase catalytic domain found in GlgE-like proteins; GlgE is a (1,4)-a-D-glucan:phosphate a-D-maltosyltransferase, involved in a-glucan biosynthesis in bacteria. It is also an anti-tuberculosis drug target. GlgE isoform I from Streptomyces coelicolor has the same catalytic and very similar kinetic properties to GlgE from Mycobacterium tuberculosis. GlgE from Streptomyces coelicolor forms a homodimer with each subunit comprising five domains (A, B, C, N, and S) and 2 inserts. Domain A is a catalytic alpha-amylase-type domain that along with domain N, which has a beta-sandwich fold and forms the core of the dimer interface, binds cyclodextrins. Domain A, B, and the 2 inserts define a well conserved donor pocket that binds maltose. Cyclodextrins competitively inhibit the binding of maltooligosaccharides to the S. coelicolor enzyme, indicating that the hydrophobic patch overlaps with the acceptor binding site. This is not the case in M. tuberculosis GlgE because cyclodextrins do not inhibit this enzyme, despite acceptor length specificity being conserved. Domain C is hypothesized to help stabilize domain A and could be involved in substrate binding. Domain S is a helix bundle that is inserted within the N domain and it plays a role in the dimer interface and interacts directly with domain B. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200482 [Multi-domain]  Cd Length: 355  Bit Score: 40.28  E-value: 2.15e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1958648956 171 KQIDPDLGSQEDFKDLLQSAKKKSIHIILDL 201
Cdd:cd11344    81 DAIHPELGTLEDFDRLVAEARELGIEVALDI 111
PRK14511 PRK14511
malto-oligosyltrehalose synthase;
141-213 2.29e-03

malto-oligosyltrehalose synthase;


Pssm-ID: 237740 [Multi-domain]  Cd Length: 879  Bit Score: 40.73  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648956 141 LEYLSTLKVKGLVLGPIHKNQK------DEVNETdlkQIDPDLGSQEDFKDLLQSAKKKSIHIILDLTPNYKG----QNA 210
Cdd:PRK14511   26 VPYFADLGVSHLYLSPILAARPgsthgyDVVDHT---RINPELGGEEGLRRLAAALRAHGMGLILDIVPNHMAvggpDNP 102

                  ...
gi 1958648956 211 WFL 213
Cdd:PRK14511  103 WWW 105
AmyAc_MTSase cd11336
Alpha amylase catalytic domain found in maltooligosyl trehalose synthase (MTSase); ...
168-213 2.31e-03

Alpha amylase catalytic domain found in maltooligosyl trehalose synthase (MTSase); Maltooligosyl trehalose synthase (MTSase) domain. MTSase and maltooligosyl trehalose trehalohydrolase (MTHase) work together to produce trehalose. MTSase is responsible for converting the alpha-1,4-glucosidic linkage to an alpha,alpha-1,1-glucosidic linkage at the reducing end of the maltooligosaccharide through an intramolecular transglucosylation reaction, while MTHase hydrolyzes the penultimate alpha-1,4 linkage of the reducing end, resulting in the release of trehalose. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200475 [Multi-domain]  Cd Length: 660  Bit Score: 40.55  E-value: 2.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958648956 168 TDLKQIDPDLGSQEDFKDLLQSAKKKSIHIILDLTPNYKG----QNAWFL 213
Cdd:cd11336    50 VDHTRINPELGGEEGLRRLAAALRAHGMGLILDIVPNHMAvsgaENPWWW 99
AmyAc_Amylosucrase cd11324
Alpha amylase catalytic domain found in Amylosucrase; Amylosucrase is a glucosyltransferase ...
136-204 7.61e-03

Alpha amylase catalytic domain found in Amylosucrase; Amylosucrase is a glucosyltransferase that catalyzes the transfer of a D-glucopyranosyl moiety from sucrose onto an acceptor molecule. When the acceptor is another saccharide, only alpha-1,4 linkages are produced. Unlike most amylopolysaccharide synthases, it does not require any alpha-D-glucosyl nucleoside diphosphate substrate. In the presence of glycogen it catalyzes the transfer of a D-glucose moiety onto a glycogen branch, but in its absence, it hydrolyzes sucrose and synthesizes polymers, smaller maltosaccharides, and sucrose isoforms. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200463  Cd Length: 536  Bit Score: 39.09  E-value: 7.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958648956 136 GLKNHLEYLSTLKVKGLVLGPIHKNQKDEvNE-----TDLKQIDPDLGSQEDFKDLLQSAKKKSIHIILDLTPN 204
Cdd:cd11324    87 GLAEKIPYLKELGVTYLHLMPLLKPPEGD-NDggyavSDYREVDPRLGTMEDLRALAAELRERGISLVLDFVLN 159
 
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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