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Conserved domains on  [gi|569006397|ref|XP_006526740|]
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neutral alpha-glucosidase AB isoform X1 [Mus musculus]

Protein Classification

glycoside hydrolase family 31 protein( domain architecture ID 10201152)

glycoside hydrolase family 31 protein which cleaves a terminal carbohydrate moiety from a substrate, similar to human neutral alpha-glucosidase C which hydrolyzes terminal, non-reducing (1->4)-linked alpha-D-glucose residues to release an alpha-D-glucose molecule

CAZY:  GH31
EC:  3.2.1.-
Gene Ontology:  GO:0004553|GO:0005975

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GH31_GANC_GANAB_alpha cd06603
neutral alpha-glucosidase C, neutral alpha-glucosidase AB; This subgroup includes the closely ...
309-776 0e+00

neutral alpha-glucosidase C, neutral alpha-glucosidase AB; This subgroup includes the closely related glycosyl hydrolase family 31 (GH31) isozymes, neutral alpha-glucosidase C (GANC) and the alpha subunit of heterodimeric neutral alpha-glucosidase AB (GANAB). Initially distinguished on the basis of differences in electrophoretic mobility in starch gel, GANC and GANAB have been shown to have other differences, including those of substrate specificity. GANC and GANAB are key enzymes in glycogen metabolism that hydrolyze terminal, non-reducing 1,4-linked alpha-D-glucose residues from glycogen in the endoplasmic reticulum. The GANC/GANAB family includes the alpha-glucosidase II (ModA) from Dictyostelium discoideum as well as the alpha-glucosidase II (GLS2, or ROT2 - Reversal of TOR2 lethality protein 2) from Saccharomyces cerevisiae.


:

Pssm-ID: 269889  Cd Length: 467  Bit Score: 923.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 309 GTQALPPLFSLGYHQSRWNYRDEADVLEVDQGFDDHNMPCDVIWLDIEHADGKRYFTWDPTRFPQPLNMLEHLASKRRKL 388
Cdd:cd06603    1 GTPPLPPLFALGYHQCRWNYNDQEDVLEVDANFDEHDIPYDVIWLDIEHTDGKRYFTWDKKKFPDPKKMQEKLASKGRKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 389 VAIVDPHIKVDSGYRVHEELRNHGLYVKTRDGSDYEGWCWPGSASYPDFTNPRMRAWWSNMFSFDNYEGSAPNLYVWNDM 468
Cdd:cd06603   81 VTIVDPHIKRDDDYFVYKEAKEKDYFVKDSDGKDFEGWCWPGSSSWPDFLNPEVRDWWASLFSYDKYKGSTENLYIWNDM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 469 NEPSVFNGPEVTMLKDAVHYGGWEHRDIHNIYGLYVHMATADGLIQRSGGIERPFVLSRAFFSGSQRFGAVWTGDNTAEW 548
Cdd:cd06603  161 NEPSVFNGPEITMPKDAIHYGGVEHRDVHNIYGLYMHMATFEGLLKRSNGKKRPFVLTRSFFAGSQRYGAVWTGDNMATW 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 549 DHLKISIPMCLSLALVGLSFCGADVGGFFKNPEPELLVRWYQMGAYQPFFRAHAHLDTGRREPWLLASQYQDAIRDALFQ 628
Cdd:cd06603  241 EHLKISIPMLLSLSIAGIPFVGADVGGFFGNPDEELLVRWYQAGAFYPFFRAHAHIDTKRREPWLFGEETTEIIREAIRL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 629 RYSLLPFWYTLFYQAHKEGFPVMRPLWVQYPEDMSTFSIEDQFMLGDALLIHPVSDAGAHGVQVYLPGqEEVWYDIQSYQ 708
Cdd:cd06603  321 RYRLLPYWYTLFYEASRTGLPIMRPLWYEFPEDESTFDIDDQFMLGDSLLVKPVVEEGATSVTVYLPG-GEVWYDYFTGQ 399
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006397 709 KHHGPQTLYLPVTLSSIPVFQRGGTIVPRWMRVRRSSDCMKDDPITLFVALSPQGTAQGELFLDDGHT 776
Cdd:cd06603  400 RVTGGGTKTVPVPLDSIPVFQRGGSIIPRKERVRRSSKLMRNDPYTLVVALDENGEAEGELYLDDGES 467
GH31_N cd14752
N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to ...
167-309 1.79e-29

N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to the glycosyl-hydrolase domain of Glycoside hydrolase family 31 (GH31). GH31 includes the glycoside hydrolases alpha-glucosidase (EC 3.2.1.20), alpha-1,3-glucosidase (EC 3.2.1.84), alpha-xylosidase (EC 3.2.1.177), sucrase-isomaltase (EC 3.2.1.48 and EC 3.2.1.10), as well as alpha-glucan lyase (EC 4.2.2.13). All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. In most cases, the pyranose moiety recognized in subsite-1 of the substrate binding site is an alpha-D-glucose, though some GH31 family members show a preference for alpha-D-xylose. Several GH31 enzymes can accommodate both glucose and xylose and different levels of discrimination between the two have been observed. Most characterized GH31 enzymes are alpha-glucosidases. In mammals, GH31 members with alpha-glucosidase activity are implicated in at least three distinct biological processes. The lysosomal acid alpha-glucosidase (GAA) is essential for glycogen degradation and a deficiency or malfunction of this enzyme causes glycogen storage disease II, also known as Pompe disease. In the endoplasmic reticulum, alpha-glucosidase II catalyzes the second step in the N-linked oligosaccharide processing pathway that constitutes part of the quality control system for glycoprotein folding and maturation. The intestinal enzymes sucrase-isomaltase (SI) and maltase-glucoamylase (MGAM) play key roles in the final stage of carbohydrate digestion, making alpha-glucosidase inhibitors useful in the treatment of type 2 diabetes. GH31 alpha-glycosidases are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues of the catalytic domain have been identified as the catalytic nucleophile and the acid/base, respectively. A loop of the N-terminal beta-sandwich domain is part of the active site pocket.


:

Pssm-ID: 270212 [Multi-domain]  Cd Length: 122  Bit Score: 113.43  E-value: 1.79e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 167 TSVGLDFSLPGMEHVYGIPEHADSLRLKvtegGEPYRLYNLDVFQYElNNPMALYGSVPVLLAHSFHrdlGIFWLNAAET 246
Cdd:cd14752    8 TPLRLSFKLPPDEHFYGLGERFGGLNKR----GKRYRLWNTDQGGYR-GSTDPLYGSIPFYLSSKGY---GVFLDNPSRT 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006397 247 WVDIssntagktlfgkmldylqgsGETPQTDIRWMSESGIIDVFLMLGPSVFDVFRQYASLTG 309
Cdd:cd14752   80 EFDF--------------------GSEDSDELTFSSEGGDLDYYFFAGPTPKEVIEQYTELTG 122
 
Name Accession Description Interval E-value
GH31_GANC_GANAB_alpha cd06603
neutral alpha-glucosidase C, neutral alpha-glucosidase AB; This subgroup includes the closely ...
309-776 0e+00

neutral alpha-glucosidase C, neutral alpha-glucosidase AB; This subgroup includes the closely related glycosyl hydrolase family 31 (GH31) isozymes, neutral alpha-glucosidase C (GANC) and the alpha subunit of heterodimeric neutral alpha-glucosidase AB (GANAB). Initially distinguished on the basis of differences in electrophoretic mobility in starch gel, GANC and GANAB have been shown to have other differences, including those of substrate specificity. GANC and GANAB are key enzymes in glycogen metabolism that hydrolyze terminal, non-reducing 1,4-linked alpha-D-glucose residues from glycogen in the endoplasmic reticulum. The GANC/GANAB family includes the alpha-glucosidase II (ModA) from Dictyostelium discoideum as well as the alpha-glucosidase II (GLS2, or ROT2 - Reversal of TOR2 lethality protein 2) from Saccharomyces cerevisiae.


Pssm-ID: 269889  Cd Length: 467  Bit Score: 923.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 309 GTQALPPLFSLGYHQSRWNYRDEADVLEVDQGFDDHNMPCDVIWLDIEHADGKRYFTWDPTRFPQPLNMLEHLASKRRKL 388
Cdd:cd06603    1 GTPPLPPLFALGYHQCRWNYNDQEDVLEVDANFDEHDIPYDVIWLDIEHTDGKRYFTWDKKKFPDPKKMQEKLASKGRKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 389 VAIVDPHIKVDSGYRVHEELRNHGLYVKTRDGSDYEGWCWPGSASYPDFTNPRMRAWWSNMFSFDNYEGSAPNLYVWNDM 468
Cdd:cd06603   81 VTIVDPHIKRDDDYFVYKEAKEKDYFVKDSDGKDFEGWCWPGSSSWPDFLNPEVRDWWASLFSYDKYKGSTENLYIWNDM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 469 NEPSVFNGPEVTMLKDAVHYGGWEHRDIHNIYGLYVHMATADGLIQRSGGIERPFVLSRAFFSGSQRFGAVWTGDNTAEW 548
Cdd:cd06603  161 NEPSVFNGPEITMPKDAIHYGGVEHRDVHNIYGLYMHMATFEGLLKRSNGKKRPFVLTRSFFAGSQRYGAVWTGDNMATW 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 549 DHLKISIPMCLSLALVGLSFCGADVGGFFKNPEPELLVRWYQMGAYQPFFRAHAHLDTGRREPWLLASQYQDAIRDALFQ 628
Cdd:cd06603  241 EHLKISIPMLLSLSIAGIPFVGADVGGFFGNPDEELLVRWYQAGAFYPFFRAHAHIDTKRREPWLFGEETTEIIREAIRL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 629 RYSLLPFWYTLFYQAHKEGFPVMRPLWVQYPEDMSTFSIEDQFMLGDALLIHPVSDAGAHGVQVYLPGqEEVWYDIQSYQ 708
Cdd:cd06603  321 RYRLLPYWYTLFYEASRTGLPIMRPLWYEFPEDESTFDIDDQFMLGDSLLVKPVVEEGATSVTVYLPG-GEVWYDYFTGQ 399
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006397 709 KHHGPQTLYLPVTLSSIPVFQRGGTIVPRWMRVRRSSDCMKDDPITLFVALSPQGTAQGELFLDDGHT 776
Cdd:cd06603  400 RVTGGGTKTVPVPLDSIPVFQRGGSIIPRKERVRRSSKLMRNDPYTLVVALDENGEAEGELYLDDGES 467
Glyco_hydro_31 pfam01055
Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. ...
290-735 0e+00

Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.


Pssm-ID: 460044 [Multi-domain]  Cd Length: 443  Bit Score: 636.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397  290 FLMLGPSVFDVFRQYASLTGTQALPPLFSLGYHQSRWNYRDEADVLEVDQGFDDHNMPCDVIWLDIEHADGKRYFTWDPT 369
Cdd:pfam01055   1 YFFLGPTPKDVVKQYTELTGRPPLPPYWALGYHQSRWGYKSEEEVLEVVDGFRERDIPLDVIWLDIDYMDGYRDFTWDPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397  370 RFPQPLNMLEHLASKRRKLVAIVDPHI-KVDSGYRVHEELRNHGLYVKTRDGSDYEGWcWPGSASYPDFTNPRMRAWWSN 448
Cdd:pfam01055  81 RFPDPKGMVDELHAKGQKLVVIIDPGIkKVDPGYPPYDEGLEKGYFVKNPDGSLYVGG-WPGMSAFPDFTNPEARDWWAD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397  449 -MFSFDNYEGsapNLYVWNDMNEPSVF--NGPEVTMLKDAVHYGGWEHRDIHNIYGLYVHMATADGLIQRSGGiERPFVL 525
Cdd:pfam01055 160 qLFKFLLDMG---VDGIWNDMNEPSVFcgSGPEDTVAKDNDPGGGVEHYDVHNLYGLLMAKATYEGLREKRPN-KRPFVL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397  526 SRAFFSGSQRFGAVWTGDNTAEWDHLKISIPMCLSLALVGLSFCGADVGGFFKNPEPELLVRWYQMGAYQPFFRAHAHLD 605
Cdd:pfam01055 236 TRSGFAGSQRYAAHWSGDNTSTWEHLRFSIPGGLSLGLSGIPFWGADIGGFFNPTTPELYVRWYQLGAFSPFFRNHSSID 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397  606 TGRREPWLLASQYQDAIRDALFQRYSLLPFWYTLFYQAHKEGFPVMRPLWVQYPEDMSTFSIEDQFMLGDALLIHPVSDA 685
Cdd:pfam01055 316 TRRREPWLFGEEVEEIIRKAIRLRYRLLPYLYTLFYEAHETGLPVMRPLFLEFPDDPNTFDIDDQFMFGPSLLVAPVLEE 395
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 569006397  686 GAHGVQVYLPGqeEVWYDIQSYQKHHGPQTLYLPVTLSSIPVFQRGGTIV 735
Cdd:pfam01055 396 GATSVDVYLPG--GRWYDFWTGERYEGGGTVPVTAPLDRIPLFVRGGSII 443
alpha_gluc_MalA NF040948
alpha-glucosidase MalA;
179-736 1.21e-125

alpha-glucosidase MalA;


Pssm-ID: 468879 [Multi-domain]  Cd Length: 626  Bit Score: 392.08  E-value: 1.21e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 179 EHVYGIPEHADSLRLKVTEggepYRLYNLDVFQYELNN-PmaLYGSVPVLLAHSFHRDLGIFWLNAAETWVDIssntaGK 257
Cdd:NF040948  61 EHVLGLGEKAFELDRRRGR----FIMYNVDAGAYTKYSdP--LYVSIPFFISVKGGKATGYFVNSPSKLIFDI-----GL 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 258 TLFGKmldylqgsgetpqtdIRWMSESGIIDVFLMLGPSVFDVFRQYASLTGTQALPPLFSLGYHQSRWNYRDEADVLEV 337
Cdd:NF040948 130 ERYDK---------------VKITIPENSVELYVIEGPTIEEVLETYSELTGKPFLPPKWALGYQISRYSYYPQDAVVEV 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 338 DQGFDDHNMPCDVIWLDIEHADGKRYFTWDPTRFPQPLNMLEHLASKRRKLVAIVDPHIKVDSGYRVHEELRnhGLYVKT 417
Cdd:NF040948 195 VDELRKEGFPVSAVYLDIDYMDSYKLFTWDKEKFPDPRKFIEELHSRGVKVITIVDPSVKADQNYEVFRSGL--GKYCET 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 418 RDGSDYEGWCWPGSASYPDFTNPRMRAWWSNMFS--FDNY--EGsapnlyVWNDMNEPSVFNGPEVTMLKD--------- 484
Cdd:NF040948 273 ENGELYVGKLWPGNSVFPDFLNEETREWWAELVEewVKQYgvDG------IWLDMNEPTDFTEDIERAALGphqlredrl 346
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 485 -------AVHYGGW----EHRDIHNIYGLYVHMATADGLiqRSGGIERPFVLSRAFFSGSQRFGAVWTGDNTAEWDHLKI 553
Cdd:NF040948 347 lytfppgAVHRLDDgkkvKHEKVRNAYPYFEAMATYEGL--KRAGKDEPFILSRSGYAGIQRYAAIWTGDNTSSWDDLKL 424
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 554 SIPMCLSLALVGLSFCGADVGGFF-----KNPEPELLVRWYQMGAYQPFFRAHAHLDTGRREPWLLASQYQDAIRDALFQ 628
Cdd:NF040948 425 QLQLVLGLSISGVPYVGCDIGGFAgrsfpIDNSPELLVRYYQAALFFPLFRTHKSKDGNDQEPYFLPSKYKEKVKRVIKL 504
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 629 RYSLLPFWYTLFYQAHKEGFPVMRPLWVQYPEDMSTFSIEDQFMLGDALLIHPVSDAGAHGVQVYLPgqEEVWYDIQSYQ 708
Cdd:NF040948 505 RYKFLPYLYSLAWEAHETGHPIIRPLFYEFQDDEDAYRIEDEYMVGKYLLYAPQIYPKEESRDVYLP--RGKWLDFWTGE 582
                        570       580
                 ....*....|....*....|....*...
gi 569006397 709 KHHGPQTLYlpvTLSSIPVFQRGGTIVP 736
Cdd:NF040948 583 EYEGPSWIE---SEAELPIYIREGSAVP 607
PLN02763 PLN02763
hydrolase, hydrolyzing O-glycosyl compounds
295-811 4.46e-121

hydrolase, hydrolyzing O-glycosyl compounds


Pssm-ID: 215408 [Multi-domain]  Cd Length: 978  Bit Score: 390.40  E-value: 4.46e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 295 PSVFDVFRQYASLTGTQALPPLFSLGYHQSRWNYRDEADVLEVDQGFDDHNMPCDVIWLDIEHADGKRYFTWDPTRFPQP 374
Cdd:PLN02763 164 PSPEALLTSLSHAIGTVFMPPKWALGYQQCRWSYESAKRVAEIARTFREKKIPCDVVWMDIDYMDGFRCFTFDKERFPDP 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 375 LNMLEHLASKRRKLVAIVDPHIKVDSGYRVHEELRNHGLYVKTRDGSDYEGWCWPGSASYPDFTNPRMRAWWSNM---FS 451
Cdd:PLN02763 244 KGLADDLHSIGFKAIWMLDPGIKAEEGYFVYDSGCENDVWIQTADGKPFVGEVWPGPCVFPDFTNKKTRSWWANLvkdFV 323
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 452 FDNYEGsapnlyVWNDMNEPSVFNGPEVTMLKDAVHYGGWE------HRDIHNIYGLYVHMATADGLIqRSGGIERPFVL 525
Cdd:PLN02763 324 SNGVDG------IWNDMNEPAVFKTVTKTMPETNIHRGDEElggvqnHSHYHNVYGMLMARSTYEGML-LANKNKRPFVL 396
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 526 SRAFFSGSQRFGAVWTGDNTAEWDHLKISIPMCLSLALVGLSFCGADVGGFFKNPEPELLVRWYQMGAYQPFFRAHAHLD 605
Cdd:PLN02763 397 TRAGFIGSQRYAATWTGDNLSNWEHLHMSIPMVLQLGLSGQPLSGPDIGGFAGDATPKLFGRWMGVGAMFPFARGHSEQG 476
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 606 TGRREPWLLASQYQDAIRDALFQRYSLLPFWYTLFYQAHKEGFPVMRPLWVQYPEDMSTFSIEDQFMLGDALLI-HPVSD 684
Cdd:PLN02763 477 TIDHEPWSFGEECEEVCRLALKRRYRLLPHFYTLFYKAHTTGLPVMTPIFFADPKDPSLRKVENSFLLGPLLISaSTLPD 556
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 685 AGAHGVQVYLPgqEEVWYDIQSYQKHHGPQTLYLpvtlssipvfqRGGTIVPRWMRVRRSSDCMKDDPITLFVALSPQGT 764
Cdd:PLN02763 557 QGSDNLQHVLP--KGIWQRFDFDDSHPDLPLLYL-----------QGGSIIPLGPPIQHVGEASLSDDLTLLIALDENGK 623
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 569006397 765 AQGELFLDDGHTFNYQtRHEFLLRRFSfsgSTLVSSS-----ADPKGHLETP 811
Cdd:PLN02763 624 AEGVLYEDDGDGFGYT-KGDYLLTHYE---AELVSSEvtvrvASTEGSWKRP 671
YicI COG1501
Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];
171-776 1.12e-117

Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];


Pssm-ID: 441110 [Multi-domain]  Cd Length: 609  Bit Score: 370.65  E-value: 1.12e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 171 LDFSLPGMEHVYGIPEHADSLRLKvtegGEPYRLYNLDVFQYELNNPMalYGSVPVLLAHsfhRDLGIFWlNAAEtWVDI 250
Cdd:COG1501   54 VRKQLDLGEQIYGLGERFTTLHKR----GRIVVNWNLDHGGHKDNGNT--YAPIPFYVSS---KGYGVFV-NSAS-YVTF 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 251 SSNTAGktlfgkmldylqgsgetpqTDIRWMSESG-IIDVFLMLGPSVFDVFRQYASLTGTQALPPLFSLGYHQSRWNYR 329
Cdd:COG1501  123 DVGSAY-------------------SDLVEFTVPGdSLEFYVIEGPSPEDVLEKYTELTGKPPLPPRWAFGYWQSRKSYY 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 330 DEADVLEVDQGFDDHNMPCDVIWLDIEHAD--GKRYFTWDPTRFPQPLNMLEHLASKRRKLVAIVDPHIKVDSGyrVHEE 407
Cdd:COG1501  184 DQDQVLAFADEFRDRGFPLDVIHLDIRWMDkyYWGDFEWDPRRFPDPKAMVKELHDRGVKLVLWINPYVAPDSA--IFAE 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 408 LRNHglYVKTRDGSDYEGWCWPGSASYPDFTNPRMRAWWsnmfsFDNYEGSAPNLYV---WNDMNEpsvfNGPEVTmlkd 484
Cdd:COG1501  262 GMAN--FVKIASGTVFVGKMWPGTTGLLDFTRPDAREWF-----WAGLEKELLSIGVdgiKLDMNE----GWPTDV---- 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 485 AVHYGGWEHRdIHNIYGLYVHMATADGLiqRSGGIERPFVLSRAFFSGSQRFGAVWTGDNTAEWDHLKISIPMCLSLALV 564
Cdd:COG1501  327 ATFPSNVPQQ-MRNLYGLLEAKATFEGF--RTSRNNRTFILTRSGFAGGQRYPVIWTGDNTSSWESLEDQLTQGLNLSLS 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 565 GLSFCGADVGGFFKNPEPELLVRWYQMGAYQPFFRAHAhlDTGRREPWLLASQYQDAIRDALFQRYSLLPFWYTLFYQAH 644
Cdd:COG1501  404 GVPFWTPDIGGFFGSPSRELWIRWFQVGAFSPFARIHG--WASSTEPWFFDEEAKQIVKEYAQLRYRLLPYIYSLFAKAS 481
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 645 KEGFPVMRPLWVQYPEDMSTFSIEDQFMLGDALLIHPVSdAGAHGVQVYLPGQEevWYDIQSYQKHHGPQTLYLPVTLSS 724
Cdd:COG1501  482 TDGTPVIRPLFLEFPDDPTTRFIDDQYMFGEYLLVAPIF-AGTESRLVYLPKGK--WYDFWTGELIEGGQWITVTAPLDR 558
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|..
gi 569006397 725 IPVFQRGGTIVPrWMRVRRSSDCMKDDPITLFValSPQGTAQGELFLDDGHT 776
Cdd:COG1501  559 LPLYVRDGSIIP-LGPVSLRPSMQKIDGIELRV--YGSGETAYTLYDDDGET 607
GH31_N cd14752
N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to ...
167-309 1.79e-29

N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to the glycosyl-hydrolase domain of Glycoside hydrolase family 31 (GH31). GH31 includes the glycoside hydrolases alpha-glucosidase (EC 3.2.1.20), alpha-1,3-glucosidase (EC 3.2.1.84), alpha-xylosidase (EC 3.2.1.177), sucrase-isomaltase (EC 3.2.1.48 and EC 3.2.1.10), as well as alpha-glucan lyase (EC 4.2.2.13). All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. In most cases, the pyranose moiety recognized in subsite-1 of the substrate binding site is an alpha-D-glucose, though some GH31 family members show a preference for alpha-D-xylose. Several GH31 enzymes can accommodate both glucose and xylose and different levels of discrimination between the two have been observed. Most characterized GH31 enzymes are alpha-glucosidases. In mammals, GH31 members with alpha-glucosidase activity are implicated in at least three distinct biological processes. The lysosomal acid alpha-glucosidase (GAA) is essential for glycogen degradation and a deficiency or malfunction of this enzyme causes glycogen storage disease II, also known as Pompe disease. In the endoplasmic reticulum, alpha-glucosidase II catalyzes the second step in the N-linked oligosaccharide processing pathway that constitutes part of the quality control system for glycoprotein folding and maturation. The intestinal enzymes sucrase-isomaltase (SI) and maltase-glucoamylase (MGAM) play key roles in the final stage of carbohydrate digestion, making alpha-glucosidase inhibitors useful in the treatment of type 2 diabetes. GH31 alpha-glycosidases are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues of the catalytic domain have been identified as the catalytic nucleophile and the acid/base, respectively. A loop of the N-terminal beta-sandwich domain is part of the active site pocket.


Pssm-ID: 270212 [Multi-domain]  Cd Length: 122  Bit Score: 113.43  E-value: 1.79e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 167 TSVGLDFSLPGMEHVYGIPEHADSLRLKvtegGEPYRLYNLDVFQYElNNPMALYGSVPVLLAHSFHrdlGIFWLNAAET 246
Cdd:cd14752    8 TPLRLSFKLPPDEHFYGLGERFGGLNKR----GKRYRLWNTDQGGYR-GSTDPLYGSIPFYLSSKGY---GVFLDNPSRT 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006397 247 WVDIssntagktlfgkmldylqgsGETPQTDIRWMSESGIIDVFLMLGPSVFDVFRQYASLTG 309
Cdd:cd14752   80 EFDF--------------------GSEDSDELTFSSEGGDLDYYFFAGPTPKEVIEQYTELTG 122
Gal_mutarotas_2 pfam13802
Galactose mutarotase-like; This family is found N-terminal to glycosyl-hydrolase domains, and ...
179-249 5.04e-23

Galactose mutarotase-like; This family is found N-terminal to glycosyl-hydrolase domains, and appears to be similar to the galactose mutarotase superfamily.


Pssm-ID: 463987 [Multi-domain]  Cd Length: 67  Bit Score: 92.91  E-value: 5.04e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006397  179 EHVYGIPEHADSLRLKvtegGEPYRLYNLDVFQYElNNPMALYGSVPVLLAHSFHRDLGIFWLNAAETWVD 249
Cdd:pfam13802   2 EHVYGLGERAGPLNKR----GTRYRLWNTDAFGYE-LDTDPLYKSIPFYISHNGGRGYGVFWDNPAETWFD 67
 
Name Accession Description Interval E-value
GH31_GANC_GANAB_alpha cd06603
neutral alpha-glucosidase C, neutral alpha-glucosidase AB; This subgroup includes the closely ...
309-776 0e+00

neutral alpha-glucosidase C, neutral alpha-glucosidase AB; This subgroup includes the closely related glycosyl hydrolase family 31 (GH31) isozymes, neutral alpha-glucosidase C (GANC) and the alpha subunit of heterodimeric neutral alpha-glucosidase AB (GANAB). Initially distinguished on the basis of differences in electrophoretic mobility in starch gel, GANC and GANAB have been shown to have other differences, including those of substrate specificity. GANC and GANAB are key enzymes in glycogen metabolism that hydrolyze terminal, non-reducing 1,4-linked alpha-D-glucose residues from glycogen in the endoplasmic reticulum. The GANC/GANAB family includes the alpha-glucosidase II (ModA) from Dictyostelium discoideum as well as the alpha-glucosidase II (GLS2, or ROT2 - Reversal of TOR2 lethality protein 2) from Saccharomyces cerevisiae.


Pssm-ID: 269889  Cd Length: 467  Bit Score: 923.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 309 GTQALPPLFSLGYHQSRWNYRDEADVLEVDQGFDDHNMPCDVIWLDIEHADGKRYFTWDPTRFPQPLNMLEHLASKRRKL 388
Cdd:cd06603    1 GTPPLPPLFALGYHQCRWNYNDQEDVLEVDANFDEHDIPYDVIWLDIEHTDGKRYFTWDKKKFPDPKKMQEKLASKGRKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 389 VAIVDPHIKVDSGYRVHEELRNHGLYVKTRDGSDYEGWCWPGSASYPDFTNPRMRAWWSNMFSFDNYEGSAPNLYVWNDM 468
Cdd:cd06603   81 VTIVDPHIKRDDDYFVYKEAKEKDYFVKDSDGKDFEGWCWPGSSSWPDFLNPEVRDWWASLFSYDKYKGSTENLYIWNDM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 469 NEPSVFNGPEVTMLKDAVHYGGWEHRDIHNIYGLYVHMATADGLIQRSGGIERPFVLSRAFFSGSQRFGAVWTGDNTAEW 548
Cdd:cd06603  161 NEPSVFNGPEITMPKDAIHYGGVEHRDVHNIYGLYMHMATFEGLLKRSNGKKRPFVLTRSFFAGSQRYGAVWTGDNMATW 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 549 DHLKISIPMCLSLALVGLSFCGADVGGFFKNPEPELLVRWYQMGAYQPFFRAHAHLDTGRREPWLLASQYQDAIRDALFQ 628
Cdd:cd06603  241 EHLKISIPMLLSLSIAGIPFVGADVGGFFGNPDEELLVRWYQAGAFYPFFRAHAHIDTKRREPWLFGEETTEIIREAIRL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 629 RYSLLPFWYTLFYQAHKEGFPVMRPLWVQYPEDMSTFSIEDQFMLGDALLIHPVSDAGAHGVQVYLPGqEEVWYDIQSYQ 708
Cdd:cd06603  321 RYRLLPYWYTLFYEASRTGLPIMRPLWYEFPEDESTFDIDDQFMLGDSLLVKPVVEEGATSVTVYLPG-GEVWYDYFTGQ 399
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006397 709 KHHGPQTLYLPVTLSSIPVFQRGGTIVPRWMRVRRSSDCMKDDPITLFVALSPQGTAQGELFLDDGHT 776
Cdd:cd06603  400 RVTGGGTKTVPVPLDSIPVFQRGGSIIPRKERVRRSSKLMRNDPYTLVVALDENGEAEGELYLDDGES 467
Glyco_hydro_31 pfam01055
Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. ...
290-735 0e+00

Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.


Pssm-ID: 460044 [Multi-domain]  Cd Length: 443  Bit Score: 636.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397  290 FLMLGPSVFDVFRQYASLTGTQALPPLFSLGYHQSRWNYRDEADVLEVDQGFDDHNMPCDVIWLDIEHADGKRYFTWDPT 369
Cdd:pfam01055   1 YFFLGPTPKDVVKQYTELTGRPPLPPYWALGYHQSRWGYKSEEEVLEVVDGFRERDIPLDVIWLDIDYMDGYRDFTWDPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397  370 RFPQPLNMLEHLASKRRKLVAIVDPHI-KVDSGYRVHEELRNHGLYVKTRDGSDYEGWcWPGSASYPDFTNPRMRAWWSN 448
Cdd:pfam01055  81 RFPDPKGMVDELHAKGQKLVVIIDPGIkKVDPGYPPYDEGLEKGYFVKNPDGSLYVGG-WPGMSAFPDFTNPEARDWWAD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397  449 -MFSFDNYEGsapNLYVWNDMNEPSVF--NGPEVTMLKDAVHYGGWEHRDIHNIYGLYVHMATADGLIQRSGGiERPFVL 525
Cdd:pfam01055 160 qLFKFLLDMG---VDGIWNDMNEPSVFcgSGPEDTVAKDNDPGGGVEHYDVHNLYGLLMAKATYEGLREKRPN-KRPFVL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397  526 SRAFFSGSQRFGAVWTGDNTAEWDHLKISIPMCLSLALVGLSFCGADVGGFFKNPEPELLVRWYQMGAYQPFFRAHAHLD 605
Cdd:pfam01055 236 TRSGFAGSQRYAAHWSGDNTSTWEHLRFSIPGGLSLGLSGIPFWGADIGGFFNPTTPELYVRWYQLGAFSPFFRNHSSID 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397  606 TGRREPWLLASQYQDAIRDALFQRYSLLPFWYTLFYQAHKEGFPVMRPLWVQYPEDMSTFSIEDQFMLGDALLIHPVSDA 685
Cdd:pfam01055 316 TRRREPWLFGEEVEEIIRKAIRLRYRLLPYLYTLFYEAHETGLPVMRPLFLEFPDDPNTFDIDDQFMFGPSLLVAPVLEE 395
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 569006397  686 GAHGVQVYLPGqeEVWYDIQSYQKHHGPQTLYLPVTLSSIPVFQRGGTIV 735
Cdd:pfam01055 396 GATSVDVYLPG--GRWYDFWTGERYEGGGTVPVTAPLDRIPLFVRGGSII 443
GH31_glucosidase_II_MalA cd06604
Alpha-glucosidase II-like; Alpha-glucosidase II (alpha-D-glucoside glucohydrolase) is a ...
309-647 2.67e-159

Alpha-glucosidase II-like; Alpha-glucosidase II (alpha-D-glucoside glucohydrolase) is a glycosyl hydrolase family 31 (GH31) enzyme, found in bacteria and plants, which has exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities. Alpha-glucosidase II has been characterized in Bacillus thermoamyloliquefaciens where it forms a homohexamer. This subgroup also includes the MalA alpha-glucosidase from Sulfolobus solfataricus and the AglA alpha-glucosidase from Picrophilus torridus. MalA is part of the carbohydrate-metabolizing machinery that allows this organism to utilize carbohydrates, such as maltose, as the sole carbon and energy source.


Pssm-ID: 269890 [Multi-domain]  Cd Length: 339  Bit Score: 468.53  E-value: 2.67e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 309 GTQALPPLFSLGYHQSRWNYRDEADVLEVDQGFDDHNMPCDVIWLDIEHADGKRYFTWDPTRFPQPLNMLEHLASKRRKL 388
Cdd:cd06604    1 GRPPLPPKWALGYQQSRWSYYPEEEVREVAKGFRERDIPCDAIYLDIDYMDGYRVFTWDKERFPDPKELIKELHEQGFRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 389 VAIVDPHIKVDSGYRVHEELRNHGLYVKTRDGSDYEGWCWPGSASYPDFTNPRMRAWWSNMFSF---DNYEGsapnlyVW 465
Cdd:cd06604   81 VTIVDPGVKVDPGYEVYEEGLENDYFVKDPDGELYVGKVWPGKSVFPDFTNPEVREWWGDLYKElvdLGVDG------IW 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 466 NDMNEPSVFNGPEV-TMLKDAVHY---GGWEHRDIHNIYGLYVHMATADGLIQRSGGiERPFVLSRAFFSGSQRFGAVWT 541
Cdd:cd06604  155 NDMNEPAVFNAPGGtTMPLDAVHRldgGKITHEEVHNLYGLLMARATYEGLRRLRPN-KRPFVLSRAGYAGIQRYAAIWT 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 542 GDNTAEWDHLKISIPMCLSLALVGLSFCGADVGGFFKNPEPELLVRWYQMGAYQPFFRAHAHLDTGRREPWLLASQYQDA 621
Cdd:cd06604  234 GDNSSSWEHLRLSIPMLLNLGLSGVPFVGADIGGFAGDPSPELLARWYQLGAFFPFFRNHSAKGTRDQEPWAFGEEVEEI 313
                        330       340
                 ....*....|....*....|....*.
gi 569006397 622 IRDALFQRYSLLPFWYTLFYQAHKEG 647
Cdd:cd06604  314 ARKAIELRYRLLPYLYTLFYEAHETG 339
alpha_gluc_MalA NF040948
alpha-glucosidase MalA;
179-736 1.21e-125

alpha-glucosidase MalA;


Pssm-ID: 468879 [Multi-domain]  Cd Length: 626  Bit Score: 392.08  E-value: 1.21e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 179 EHVYGIPEHADSLRLKVTEggepYRLYNLDVFQYELNN-PmaLYGSVPVLLAHSFHRDLGIFWLNAAETWVDIssntaGK 257
Cdd:NF040948  61 EHVLGLGEKAFELDRRRGR----FIMYNVDAGAYTKYSdP--LYVSIPFFISVKGGKATGYFVNSPSKLIFDI-----GL 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 258 TLFGKmldylqgsgetpqtdIRWMSESGIIDVFLMLGPSVFDVFRQYASLTGTQALPPLFSLGYHQSRWNYRDEADVLEV 337
Cdd:NF040948 130 ERYDK---------------VKITIPENSVELYVIEGPTIEEVLETYSELTGKPFLPPKWALGYQISRYSYYPQDAVVEV 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 338 DQGFDDHNMPCDVIWLDIEHADGKRYFTWDPTRFPQPLNMLEHLASKRRKLVAIVDPHIKVDSGYRVHEELRnhGLYVKT 417
Cdd:NF040948 195 VDELRKEGFPVSAVYLDIDYMDSYKLFTWDKEKFPDPRKFIEELHSRGVKVITIVDPSVKADQNYEVFRSGL--GKYCET 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 418 RDGSDYEGWCWPGSASYPDFTNPRMRAWWSNMFS--FDNY--EGsapnlyVWNDMNEPSVFNGPEVTMLKD--------- 484
Cdd:NF040948 273 ENGELYVGKLWPGNSVFPDFLNEETREWWAELVEewVKQYgvDG------IWLDMNEPTDFTEDIERAALGphqlredrl 346
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 485 -------AVHYGGW----EHRDIHNIYGLYVHMATADGLiqRSGGIERPFVLSRAFFSGSQRFGAVWTGDNTAEWDHLKI 553
Cdd:NF040948 347 lytfppgAVHRLDDgkkvKHEKVRNAYPYFEAMATYEGL--KRAGKDEPFILSRSGYAGIQRYAAIWTGDNTSSWDDLKL 424
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 554 SIPMCLSLALVGLSFCGADVGGFF-----KNPEPELLVRWYQMGAYQPFFRAHAHLDTGRREPWLLASQYQDAIRDALFQ 628
Cdd:NF040948 425 QLQLVLGLSISGVPYVGCDIGGFAgrsfpIDNSPELLVRYYQAALFFPLFRTHKSKDGNDQEPYFLPSKYKEKVKRVIKL 504
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 629 RYSLLPFWYTLFYQAHKEGFPVMRPLWVQYPEDMSTFSIEDQFMLGDALLIHPVSDAGAHGVQVYLPgqEEVWYDIQSYQ 708
Cdd:NF040948 505 RYKFLPYLYSLAWEAHETGHPIIRPLFYEFQDDEDAYRIEDEYMVGKYLLYAPQIYPKEESRDVYLP--RGKWLDFWTGE 582
                        570       580
                 ....*....|....*....|....*...
gi 569006397 709 KHHGPQTLYlpvTLSSIPVFQRGGTIVP 736
Cdd:NF040948 583 EYEGPSWIE---SEAELPIYIREGSAVP 607
PLN02763 PLN02763
hydrolase, hydrolyzing O-glycosyl compounds
295-811 4.46e-121

hydrolase, hydrolyzing O-glycosyl compounds


Pssm-ID: 215408 [Multi-domain]  Cd Length: 978  Bit Score: 390.40  E-value: 4.46e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 295 PSVFDVFRQYASLTGTQALPPLFSLGYHQSRWNYRDEADVLEVDQGFDDHNMPCDVIWLDIEHADGKRYFTWDPTRFPQP 374
Cdd:PLN02763 164 PSPEALLTSLSHAIGTVFMPPKWALGYQQCRWSYESAKRVAEIARTFREKKIPCDVVWMDIDYMDGFRCFTFDKERFPDP 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 375 LNMLEHLASKRRKLVAIVDPHIKVDSGYRVHEELRNHGLYVKTRDGSDYEGWCWPGSASYPDFTNPRMRAWWSNM---FS 451
Cdd:PLN02763 244 KGLADDLHSIGFKAIWMLDPGIKAEEGYFVYDSGCENDVWIQTADGKPFVGEVWPGPCVFPDFTNKKTRSWWANLvkdFV 323
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 452 FDNYEGsapnlyVWNDMNEPSVFNGPEVTMLKDAVHYGGWE------HRDIHNIYGLYVHMATADGLIqRSGGIERPFVL 525
Cdd:PLN02763 324 SNGVDG------IWNDMNEPAVFKTVTKTMPETNIHRGDEElggvqnHSHYHNVYGMLMARSTYEGML-LANKNKRPFVL 396
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 526 SRAFFSGSQRFGAVWTGDNTAEWDHLKISIPMCLSLALVGLSFCGADVGGFFKNPEPELLVRWYQMGAYQPFFRAHAHLD 605
Cdd:PLN02763 397 TRAGFIGSQRYAATWTGDNLSNWEHLHMSIPMVLQLGLSGQPLSGPDIGGFAGDATPKLFGRWMGVGAMFPFARGHSEQG 476
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 606 TGRREPWLLASQYQDAIRDALFQRYSLLPFWYTLFYQAHKEGFPVMRPLWVQYPEDMSTFSIEDQFMLGDALLI-HPVSD 684
Cdd:PLN02763 477 TIDHEPWSFGEECEEVCRLALKRRYRLLPHFYTLFYKAHTTGLPVMTPIFFADPKDPSLRKVENSFLLGPLLISaSTLPD 556
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 685 AGAHGVQVYLPgqEEVWYDIQSYQKHHGPQTLYLpvtlssipvfqRGGTIVPRWMRVRRSSDCMKDDPITLFVALSPQGT 764
Cdd:PLN02763 557 QGSDNLQHVLP--KGIWQRFDFDDSHPDLPLLYL-----------QGGSIIPLGPPIQHVGEASLSDDLTLLIALDENGK 623
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 569006397 765 AQGELFLDDGHTFNYQtRHEFLLRRFSfsgSTLVSSS-----ADPKGHLETP 811
Cdd:PLN02763 624 AEGVLYEDDGDGFGYT-KGDYLLTHYE---AELVSSEvtvrvASTEGSWKRP 671
YicI COG1501
Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];
171-776 1.12e-117

Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];


Pssm-ID: 441110 [Multi-domain]  Cd Length: 609  Bit Score: 370.65  E-value: 1.12e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 171 LDFSLPGMEHVYGIPEHADSLRLKvtegGEPYRLYNLDVFQYELNNPMalYGSVPVLLAHsfhRDLGIFWlNAAEtWVDI 250
Cdd:COG1501   54 VRKQLDLGEQIYGLGERFTTLHKR----GRIVVNWNLDHGGHKDNGNT--YAPIPFYVSS---KGYGVFV-NSAS-YVTF 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 251 SSNTAGktlfgkmldylqgsgetpqTDIRWMSESG-IIDVFLMLGPSVFDVFRQYASLTGTQALPPLFSLGYHQSRWNYR 329
Cdd:COG1501  123 DVGSAY-------------------SDLVEFTVPGdSLEFYVIEGPSPEDVLEKYTELTGKPPLPPRWAFGYWQSRKSYY 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 330 DEADVLEVDQGFDDHNMPCDVIWLDIEHAD--GKRYFTWDPTRFPQPLNMLEHLASKRRKLVAIVDPHIKVDSGyrVHEE 407
Cdd:COG1501  184 DQDQVLAFADEFRDRGFPLDVIHLDIRWMDkyYWGDFEWDPRRFPDPKAMVKELHDRGVKLVLWINPYVAPDSA--IFAE 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 408 LRNHglYVKTRDGSDYEGWCWPGSASYPDFTNPRMRAWWsnmfsFDNYEGSAPNLYV---WNDMNEpsvfNGPEVTmlkd 484
Cdd:COG1501  262 GMAN--FVKIASGTVFVGKMWPGTTGLLDFTRPDAREWF-----WAGLEKELLSIGVdgiKLDMNE----GWPTDV---- 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 485 AVHYGGWEHRdIHNIYGLYVHMATADGLiqRSGGIERPFVLSRAFFSGSQRFGAVWTGDNTAEWDHLKISIPMCLSLALV 564
Cdd:COG1501  327 ATFPSNVPQQ-MRNLYGLLEAKATFEGF--RTSRNNRTFILTRSGFAGGQRYPVIWTGDNTSSWESLEDQLTQGLNLSLS 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 565 GLSFCGADVGGFFKNPEPELLVRWYQMGAYQPFFRAHAhlDTGRREPWLLASQYQDAIRDALFQRYSLLPFWYTLFYQAH 644
Cdd:COG1501  404 GVPFWTPDIGGFFGSPSRELWIRWFQVGAFSPFARIHG--WASSTEPWFFDEEAKQIVKEYAQLRYRLLPYIYSLFAKAS 481
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 645 KEGFPVMRPLWVQYPEDMSTFSIEDQFMLGDALLIHPVSdAGAHGVQVYLPGQEevWYDIQSYQKHHGPQTLYLPVTLSS 724
Cdd:COG1501  482 TDGTPVIRPLFLEFPDDPTTRFIDDQYMFGEYLLVAPIF-AGTESRLVYLPKGK--WYDFWTGELIEGGQWITVTAPLDR 558
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|..
gi 569006397 725 IPVFQRGGTIVPrWMRVRRSSDCMKDDPITLFValSPQGTAQGELFLDDGHT 776
Cdd:COG1501  559 LPLYVRDGSIIP-LGPVSLRPSMQKIDGIELRV--YGSGETAYTLYDDDGET 607
GH31_MGAM_SI_GAA cd06602
maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase; This subgroup ...
309-644 4.32e-111

maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase; This subgroup includes the following three closely related glycosyl hydrolase family 31 (GH31) enzymes: maltase-glucoamylase (MGAM), sucrase-isomaltase (SI), and lysosomal acid alpha-glucosidase (GAA), also known as acid-maltase. MGAM is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion. SI is implicated in the digestion of dietary starch and major disaccharides such as sucrose and isomaltose, while GAA degrades glycogen in the lysosome, cleaving both alpha-1,4 and alpha-1,6 glucosidic linkages. MGAM and SI are anchored to small-intestinal brush-border epithelial cells. The absence of SI from the brush border membrane or its malfunction is associated with malabsorption disorders such as congenital sucrase-isomaltase deficiency (CSID). The domain architectures of MGAM and SI include two tandem GH31 catalytic domains, an N-terminal domain found near the membrane-bound end, and a C-terminal luminal domain. Both of the tandem GH31 domains of MGAM and SI are included in this family. The domain architecture of GAA includes an N-terminal TFF (trefoil factor family) domain in addition to the GH31 catalytic domain. Deficient GAA expression causes Pompe disease, an autosomal recessive genetic disorder also known as glycogen storage disease type II (GSDII).


Pssm-ID: 269888  Cd Length: 367  Bit Score: 344.88  E-value: 4.32e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 309 GTQALPPLFSLGYHQSRWNYRDEADVLEVDQGFDDHNMPCDVIWLDIEHADGKRYFTWDPTRFPQPLNMLEHLASKRRKL 388
Cdd:cd06602    1 GRPAMPPYWSLGFHLCRWGYKNLDELKEVVERYRAAGIPLDVQWNDIDYMDRYRDFTLDPVNFPGLPAFVDDLHANGQHY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 389 VAIVDPHIKV--DSGYRVHEELRNHGLYVKTRDGSDYEGWCWPGSASYPDFTNPRMRAWWSNMFS--FD--NYEGsapnl 462
Cdd:cd06602   81 VPILDPGISAneSGGYPPYDRGLEMDVFIKNDDGSPYVGKVWPGYTVFPDFTNPNTQEWWTEEIKdfHDqvPFDG----- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 463 yVWNDMNEPSVF-NGPEV-------------------------------TMLKDAVHYGGWEHRDIHNIYGLYVHMATAD 510
Cdd:cd06602  156 -LWIDMNEPSNFcTGSCGnspnapgcpdnklnnppyvpnnlgggslsdkTICMDAVHYDGGLHYDVHNLYGLSEAIATYK 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 511 GLIQRSGGiERPFVLSRAFFSGSQRFGAVWTGDNTAEWDHLKISIPMCLSLALVGLSFCGADVGGFFKNPEPELLVRWYQ 590
Cdd:cd06602  235 ALKEIFPG-KRPFIISRSTFPGSGKYAGHWLGDNYSTWEDMRYSIPGMLEFNLFGIPMVGADICGFNGNTTEELCARWMQ 313
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 569006397 591 MGAYQPFFRAHAHLDTGRREPWLLASQYQDAIRDALFQRYSLLPFWYTLFYQAH 644
Cdd:cd06602  314 LGAFYPFSRNHNDIGAIDQEPYVWGPSVADASRKALLIRYSLLPYLYTLFYRAH 367
GH31_MGAM-like cd06600
maltase-glucoamylase (MGAM)-like; This family includes the following closely related glycosyl ...
309-632 2.61e-107

maltase-glucoamylase (MGAM)-like; This family includes the following closely related glycosyl hydrolase family 31 (GH31) enzymes: maltase-glucoamylase (MGAM), sucrase-isomaltase (SI), lysosomal acid alpha-glucosidase (GAA), neutral alpha-glucosidase C (GANC), the alpha subunit of neutral alpha-glucosidase AB (GANAB), and alpha-glucosidase II. MGAM is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion. SI is implicated in the digestion of dietary starch and major disaccharides such as sucrose and isomaltose, while GAA degrades glycogen in the lysosome, cleaving both alpha-1,4 and alpha-1,6 glucosidic linkages. MGAM and SI are anchored to small-intestinal brush-border epithelial cells. The absence of SI from the brush border membrane or its malfunction is associated with malabsorption disorders such as congenital sucrase-isomaltase deficiency (CSID). The domain architectures of MGAM and SI include two tandem GH31 catalytic domains, an N-terminal domain found near the membrane-bound end and a C-terminal luminal domain. Both of the tandem GH31 domains of MGAM and SI are included in this family. The domain architecture of GAA includes an N-terminal TFF (trefoil factor family) domain in addition to the GH31 catalytic domain. Deficient GAA expression causes Pompe disease, an autosomal recessive genetic disorder also known as glycogen storage disease type II (GSDII). GANC and GANAB are key enzymes in glycogen metabolism that hydrolyze terminal, non-reducing 1,4-linked alpha-D-glucose residues from glycogen in the endoplasmic reticulum. Alpha-glucosidase II is a GH31 enzyme, found in bacteria and plants, which has exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities. Alpha-glucosidase II has been characterized in Bacillus thermoamyloliquefaciens where it forms a homohexamer. This family also includes the MalA alpha-glucosidase from Sulfolobus solfataricus and the AglA alpha-glucosidase from Picrophilus torridus. MalA is part of the carbohydrate-metabolizing machinery that allows this organism to utilize carbohydrates, such as maltose, as the sole carbon and energy source. The MGAM-like family corresponds to subgroup 1 in the Ernst et al classification of GH31 enzymes.


Pssm-ID: 269886 [Multi-domain]  Cd Length: 256  Bit Score: 330.61  E-value: 2.61e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 309 GTQALPPLFSLGYHQSRWNYRDEADVLEVDQGFDDHNMPCDVIWLDIEHADGKRYFTWDPTRFPQPLNMLEHLASKRRKL 388
Cdd:cd06600    1 GRPALPPYWAFGYHQSRYSYYDQDKVVEVVDIMQEAGIPYDVMWLDIDYMDSYKDFTWDPVRFPEPKKFVDELHKNGQKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 389 VAIVDPHIkvdsgyrvheelrnhglyvktrdgsdyegwcwpgsasypdftnprMRAWWSNMFSFDNYegSAPNLYVWNDM 468
Cdd:cd06600   81 VTIVDPGI---------------------------------------------TREWWAGLISEFLY--SQGIDGIWIDM 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 469 NEPSVFngpevtmlkdavhyggwehRDIHNIYGLYVHMATADGLIQRSGgiERPFVLSRAFFSGSQRFGAVWTGDNTAEW 548
Cdd:cd06600  114 NEPSNF-------------------YKVHNLYGFYEAMATAEGLRTSHN--ERPFILSRSTFAGSQKYAAHWTGDNTASW 172
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 549 DHLKISIPMCLSLALVGLSFCGADVGGFFKNPEPELLVRWYQMGAYQPFFRAHAHLDTGRREPWLLASQYQDAIRDALFQ 628
Cdd:cd06600  173 DDLKLSIPLVLGLSLSGIPFVGADIGGFAGDTSEELLVRWYQLGAFYPFSRSHKATDTKDQEPVLFPEYYKESVREILEL 252

                 ....
gi 569006397 629 RYSL 632
Cdd:cd06600  253 RYKL 256
GH31_transferase_CtsZ cd06598
CtsZ (cyclic tetrasaccharide-synthesizing enzyme Z)-like; CtsZ is a bacterial ...
309-642 2.43e-71

CtsZ (cyclic tetrasaccharide-synthesizing enzyme Z)-like; CtsZ is a bacterial 6-alpha-glucosyltransferase, first identified in Arthrobacter globiformis, that produces cyclic tetrasaccharides together with a closely related enzyme CtsY. CtsZ and CtsY both have a glycosyl hydrolase family 31 (GH31) catalytic domain; CtsY belongs to a different subfamily. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.


Pssm-ID: 269884  Cd Length: 332  Bit Score: 238.35  E-value: 2.43e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 309 GTQALPPLFSLGYHQSRWNYRDEADVLEVDQGFDDHNMPCDVIWLDI-----EHADGKRY---FTWDPTRFPQPLNMLEH 380
Cdd:cd06598    1 GRPPLPPKWAFGLWQSEFGYDNWAEVDELVDTLRQKDFPLDGVVLDLywfggIIASPDGPmgdLDWDRKAFPDPAKMIAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 381 LASKRRKLVAIVDPHIKVDSGyrVHEELRNHGLYVKTRDGSD--YEGWCWPGSASYPDFTNPRMRAWWSNMFSFDNYEGS 458
Cdd:cd06598   81 LKQQGVGTILIEEPYVLKNSD--EYDELVKKGLLAKDKAGKPepTLFNFWFGEGGMIDWSDPEARAWWHDRYKDLIDMGV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 459 APNlyvWNDMNEPSVFNGpevtmlkDAVHYGGwEHRDIHNIYGLYVHMATADGLiQRSGGIERPFVLSRAFFSGSQRFGA 538
Cdd:cd06598  159 AGW---WTDLGEPEMHPP-------DMVHADG-DAADVHNIYNLLWAKSIYDGY-QRNFPEQRPFIMSRSGTAGSQRYGV 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 539 V-WTGDNTAEWDHLKISIPMCLSLALVGLSFCGADVGGFFKN--PEPELLVRWYQMGAYQPFFRAHAHlDTGRREPWLLA 615
Cdd:cd06598  227 IpWSGDIGRTWGGLASQINLQLHMSLSGIDYYGSDIGGFARGetLDPELYTRWFQYGAFDPPVRPHGQ-NLCNPETAPDR 305
                        330       340
                 ....*....|....*....|....*..
gi 569006397 616 SQYQDAIRDALFQRYSLLPFWYTLFYQ 642
Cdd:cd06598  306 EGTKAINRENIKLRYQLLPYYYSLAYR 332
GH31_glycosidase_Aec37 cd06599
E.coli Aec37-like; Glycosyl hydrolase family 31 (GH31) domain of a bacterial protein family ...
309-626 8.44e-60

E.coli Aec37-like; Glycosyl hydrolase family 31 (GH31) domain of a bacterial protein family represented by Escherichia coli protein Aec37. The gene encoding Aec37 (aec-37) is located within a genomic island (AGI-3) isolated from the extraintestinal avian pathogenic Escherichia coli strain BEN2908. The function of Aec37 and its orthologs is unknown; however, deletion of a region of the genome that includes aec-37 affects the assimilation of seven carbohydrates, decreases growth rate of the strain in minimal medium containing galacturonate or trehalose, and attenuates the virulence of E. coli BEN2908 in chickens. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.


Pssm-ID: 269885 [Multi-domain]  Cd Length: 319  Bit Score: 206.30  E-value: 8.44e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 309 GTQALPPLFSLGYHQSRWNYRDEADVLEVDQGFDD----HNMPCDVIWLD---IEHADGKRY-FTWDPTRFPQPLNMLEH 380
Cdd:cd06599    1 GRPALPPRWSLGYLGSTMYYTEAPDAQEQILDFIDtcreHDIPCDGFHLSsgyTSIEDGKRYvFNWNKDKFPDPKAFFRK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 381 LASKRRKLVAIVDPHIKVDSGYRvhEELRNHGLYVKTRD-GSDYEGWCWPGSASYPDFTNPRMRAWWSNM-------FSF 452
Cdd:cd06599   81 FHERGIRLVANIKPGLLTDHPHY--DELAEKGAFIKDDDgGEPAVGRFWGGGGSYLDFTNPEGREWWKEGlkeqlldYGI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 453 DNyegsapnlyVWNDMNEPSVFNGpevtmlkDAVHYGGWEHRDIHN---IYGLYVHMATADGLIQRSGGiERPFVLSRAF 529
Cdd:cd06599  159 DS---------VWNDNNEYEIWDD-------DAACCGFGKGGPISElrpIQPLLMARASREAQLEHAPN-KRPFVISRSG 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 530 FSGSQRFGAVWTGDNTAEWDHLKISIPMCLSLALVGLSFCGADVGGFFKN-PEPELLVRWYQMGAYQPFFRAH-AHLDTG 607
Cdd:cd06599  222 CAGIQRYAQTWSGDNRTSWKTLKYNIAMGLGMSLSGVANYGHDIGGFAGPaPEPELFVRWVQNGIFQPRFSIHsWNTDNT 301
                        330
                 ....*....|....*....
gi 569006397 608 RREPWLLASqYQDAIRDAL 626
Cdd:cd06599  302 VTEPWMYPE-ATPAIREAI 319
GH31 cd06589
glycosyl hydrolase family 31 (GH31); GH31 enzymes occur in prokaryotes, eukaryotes, and ...
309-626 2.10e-57

glycosyl hydrolase family 31 (GH31); GH31 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. In most cases, the pyranose moiety recognized in subsite -1 of the substrate binding site is an alpha-D-glucose, though some GH31 family members show a preference for alpha-D-xylose. Several GH31 enzymes can accommodate both glucose and xylose and different levels of discrimination between the two have been observed. Most characterized GH31 enzymes are alpha-glucosidases. In mammals, GH31 members with alpha-glucosidase activity are implicated in at least three distinct biological processes. The lysosomal acid alpha-glucosidase (GAA) is essential for glycogen degradation and a deficiency or malfunction of this enzyme causes glycogen storage disease II, also known as Pompe disease. In the endoplasmic reticulum, alpha-glucosidase II catalyzes the second step in the N-linked oligosaccharide processing pathway that constitutes part of the quality control system for glycoprotein folding and maturation. The intestinal enzymes sucrase-isomaltase (SI) and maltase-glucoamylase (MGAM) play key roles in the final stage of carbohydrate digestion, making alpha-glucosidase inhibitors useful in the treatment of type 2 diabetes. GH31 alpha-glycosidases are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.


Pssm-ID: 269876 [Multi-domain]  Cd Length: 265  Bit Score: 197.96  E-value: 2.10e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 309 GTQALPPLFSLGYHQSRWNYRDEADVLEVDQGFDDHNMPCDVIWLDI---EHADGKRYFTWDPTRFPQPLNMLEHLASKR 385
Cdd:cd06589    1 GRPPLLPKWALGFWNSRYGYYSEDEVEELVDRYREEGIPLDGFVLDSdwmDWGGNWGGFTWNREKFPDPKGMIDELHDKG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 386 RKLVAIVdphikvdsgyrvheelrnhglyvktrdgsdyegwcwpgsasypdftNPRMRAWWsnmfsFDNYEGSAPNL--- 462
Cdd:cd06589   81 VKLGLIV----------------------------------------------KPRLRDWW-----WENIKKLLLEQgvd 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 463 YVWNDMNEPSVFngpevtmlKDAVHYGGWEHRDIHNIYGLYVHMATADGLIQrSGGIERPFVLSRAFFSGSQRFGAVWTG 542
Cdd:cd06589  110 GWWTDMGEPLPF--------DDATFHNGGKAQKIHNAYPLNMAEATYEGQKK-TFPNKRPFILSRSGYAGAQRYPAIWSG 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 543 DNTAEWDHLKISIPMCLSLALVGLSFCGADVGGFFKN-PEPELLVRWYQMGAYQPFFRAHAHLDTGRREPWLLASQYQDA 621
Cdd:cd06589  181 DNTTTWDSLAFQIRAGLSASLSGVGYWGHDIGGFTGGdPDKELYTRWVQFGAFSPIFRLHGDNSPRDKEPWVYGEEALAI 260

                 ....*
gi 569006397 622 IRDAL 626
Cdd:cd06589  261 FRKYL 265
GH31_lyase_GLase cd06601
alpha-1,4-glucan lyase; GLases (alpha-1,4-glucan lyases) are glycosyl hydrolase family 31 ...
309-647 1.01e-53

alpha-1,4-glucan lyase; GLases (alpha-1,4-glucan lyases) are glycosyl hydrolase family 31 (GH31) enzymes that degrade alpha-1,4-glucans and maltooligosaccharides via a nonhydrolytic pathway to yield 1,5-D-anhydrofructose from the nonreducing end. GLases cleave the bond between C1 and O1 of the nonreducing sugar residue of alpha-glucans to generate a monosaccharide product with a double bond between C1 and C2. This family corresponds to subgroup 2 in the Ernst et al classification of GH31 enzymes.


Pssm-ID: 269887 [Multi-domain]  Cd Length: 347  Bit Score: 190.31  E-value: 1.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 309 GTQALPPLFSLGYHQSRWNYRDEADVLEVDQGFDDHNMPCDVIWLDIEHADGKRYFTWDPTRFPQPLNMLEHLASKRRKL 388
Cdd:cd06601    1 GRSRMKPRYVFGYHQGCYGYSSRESLEVVVQSYRDANIPLDGLHIDVDFQDNYRTFTTSKDKFPNPKEMFSNLHAQGFKC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 389 VAIVDPHIKvdSGYRVHEelrNHGLYVKTrdgsdyegwcwpgSASYPDFTNPRMRAWWSNmfsfdNYEG--SAPNLYVWN 466
Cdd:cd06601   81 STNITPIIT--DPYIGGV---NYGGGLGS-------------PGFYPDLGRPEVREWWGQ-----QYKYlfDMGLEMVWQ 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 467 DMNEPSVFNG-----------PEVTMLKDAVHYGGWE---HRDIHNIYGLYVHMATADGLIQRSGGIE-RPFVLSRAFFS 531
Cdd:cd06601  138 DMTTPAIAPHkingygdmktfPLRLLVTDDSVKNEHTykpAATLWNLYAYNLHKATYHGLNRLNARPNrRNFIIGRGGYA 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 532 GSQRFGAVWTGDNTAEWDHLKISIPMCLSLALVGLSFCGADVGGFFKNPE--------PELLVRWYQMGAYQPFFRAH-- 601
Cdd:cd06601  218 GAQRFAGLWTGDNASTWDFLQINIPQVLNLGLSGVPISGSDIGGFASGSDenegkwcdPELLIRWVQAGAFLPWFRNHyd 297
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 569006397 602 ----AHLDTGRREPWLLASQYQDAIRDALFQRYSLLPFWYTLFYQAHKEG 647
Cdd:cd06601  298 ryikKKQQEKLYEPYYYYEPVLPICRKYVELRYRLMQVFYDAMYENTQNG 347
GH31_xylosidase_YicI cd06593
alpha-xylosidase YicI-like; YicI alpha-xylosidase is a glycosyl hydrolase family 31 (GH31) ...
312-632 3.06e-53

alpha-xylosidase YicI-like; YicI alpha-xylosidase is a glycosyl hydrolase family 31 (GH31) enzyme that catalyzes the release of an alpha-xylosyl residue from the non-reducing end of alpha-xyloside substrates such as alpha-xylosyl fluoride and isoprimeverose. YicI forms a homohexamer (a trimer of dimers). All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. The YicI family corresponds to subgroup 4 in the Ernst et al classification of GH31 enzymes.


Pssm-ID: 269879 [Multi-domain]  Cd Length: 308  Bit Score: 187.78  E-value: 3.06e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 312 ALPPLFSLGYHQSRWNYRDEADVLEVDQGFDDHNMPCDVI-----WLDIEHADGkryFTWDPTRFPQPLNMLEHLASKRR 386
Cdd:cd06593    4 PLPPAWSFGLWLSRSFYYSEEEVLEVADGMRERGIPCDVIhldcfWMKEDWWCD---FEWDEERFPDPEGMIARLKEKGF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 387 KLVAIVDPHIKVDSgyRVHEELRNHGLYVKTRDGSDYEGWC-WPGSASYPDFTNPRMRAWWSNMFSfdnyegsapNLYvw 465
Cdd:cd06593   81 KVCLWINPYISQDS--PLFKEAAEKGYLVKNPDGSPWHQWDgWQPGMGIIDFTNPEAVAWYKEKLK---------RLL-- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 466 nDMNepsvfngpeVTMLK---------DAVHYGGWEHRDIHNIYGLYVHMATADGLIQRSGgiERPFVLSRAFFSGSQRF 536
Cdd:cd06593  148 -DMG---------VDVIKtdfgeripeDAVYYDGSDGRKMHNLYPLLYNKAVYEATKEVKG--EEAVLWARSAWAGSQRY 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 537 GAVWTGDNTAEWDHLKISIPMCLSLALVGLSFCGADVGGFFKNPEPELLVRWYQMGAYQPFFRAHAhldTGRREPWLLAS 616
Cdd:cd06593  216 PVHWGGDSESTFEGMAASLRGGLSLGLSGFGFWSHDIGGFEGTPSPELYKRWTQFGLLSSHSRLHG---STPREPWEYGE 292
                        330
                 ....*....|....*.
gi 569006397 617 QYQDAIRDALFQRYSL 632
Cdd:cd06593  293 EALDVVRKFAKLRYRL 308
GH31_xylosidase_XylS cd06591
xylosidase XylS-like; XylS is a glycosyl hydrolase family 31 (GH31) alpha-xylosidase found in ...
309-626 6.84e-51

xylosidase XylS-like; XylS is a glycosyl hydrolase family 31 (GH31) alpha-xylosidase found in prokaryotes, eukaryotes, and archaea, that catalyzes the release of alpha-xylose from the non-reducing terminal side of the alpha-xyloside substrate. XylS has been characterized in Sulfolobus solfataricus where it hydrolyzes isoprimeverose, the p-nitrophenyl-beta derivative of isoprimeverose, and xyloglucan oligosaccharides, and has transxylosidic activity. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. The XylS family corresponds to subgroup 3 in the Ernst et al classification of GH31 enzymes.


Pssm-ID: 269877 [Multi-domain]  Cd Length: 322  Bit Score: 181.60  E-value: 6.84e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 309 GTQALPPLFSLGYHQSRWNYRDEADVLEVDQGFDDHNMPCDVIWLDIEH--ADGKRYFTWDPTRFPQPLNMLEHLASKRR 386
Cdd:cd06591    1 GKAPMLPKWALGFWQSKERYKTQEELLEVAREYRERGIPLDVIVQDWFYwtEQGWGDMKFDPERFPDPKGMVDELHKMNV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 387 KLVAIVDPhiKVDSGYRVHEELRNHGLYVKTRDGSDYEGwcwpGSASYPDFTNPRMRAW-WS----NMFS--FDNYegsa 459
Cdd:cd06591   81 KLMISVWP--TFGPGSENYKELDEKGLLLRTNRGNGGFG----GGTAFYDATNPEAREIyWKqlkdNYFDkgIDAW---- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 460 pnlyvWNDMNEPsvFNGPEVTMLKDAVHYGGWEHRdIHNIYGLYVHMATADGLIqRSGGIERPFVLSRAFFSGSQRFGA- 538
Cdd:cd06591  151 -----WLDATEP--ELDPYDFDNYDGRTALGPGAE-VGNAYPLMHAKGIYEGQR-ATGPDKRVVILTRSAFAGQQRYGAa 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 539 VWTGDNTAEWDHLKISIPMCLSLALVGLSFCGADVGGFF--------KNPE-PELLVRWYQMGAYQPFFRAHAhlDTGRR 609
Cdd:cd06591  222 VWSGDISSSWETLRRQIPAGLNFGASGIPYWTTDIGGFFggdpepgeDDPAyRELYVRWFQFGAFCPIFRSHG--TRPPR 299
                        330
                 ....*....|....*..
gi 569006397 610 EPWLLASqYQDAIRDAL 626
Cdd:cd06591  300 EPNEIWS-YGEEAYDIL 315
GH31_NET37 cd06592
glucosidase NET37; NET37 (also known as KIAA1161) is a human lamina-associated nuclear ...
313-696 9.88e-46

glucosidase NET37; NET37 (also known as KIAA1161) is a human lamina-associated nuclear envelope transmembrane protein. A member of the glycosyl hydrolase family 31 (GH31) , it has been shown to be required for myogenic differentiation of C2C12 cells. Related proteins are found in eukaryotes and prokaryotes. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.


Pssm-ID: 269878 [Multi-domain]  Cd Length: 364  Bit Score: 168.17  E-value: 9.88e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 313 LPPLFSLG--YHqsrwNYRDEADVLEVDQGFDDHNMPCDVIWLDiehaDG--KRY--FTWDPTRFPQPLNMLEHLASKRR 386
Cdd:cd06592    1 RPPIWSTWaeYK----YNINQEKVLEYAEEIRANGFPPSVIEID----DGwqTYYgdFEFDPEKFPDPKGMIDKLHEMGF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 387 KLVAIVDPHIKVDSgyRVHEELRNHGLYVK-TRDGSDYEGWCWPGSASYPDFTNPRMRAWWSNM------------FSFD 453
Cdd:cd06592   73 RVTLWVHPFINPDS--PNFRELRDKGYLVKeDSGGPPLIVKWWNGYGAVLDFTNPEARDWFKERlrelqedygidgFKFD 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 454 NYEGSapnlYVWNDmnepsvfngpevtmlkDAVHYGGWEHRDIHNIYGLYvhMATADGLIQ-RSGGI-ERPFVLSRAFFS 531
Cdd:cd06592  151 AGEAS----YLPAD----------------PATFPSGLNPNEYTTLYAEL--AAEFGLLNEvRSGWKsQGLPLFVRMSDK 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 532 GSqrfgaVWTgdntaEWDHLKISIPMCLSLALVGLSFCGAD-VGGFF---KNPEPELLVRWYQMGAYQPFFRAHAHldtg 607
Cdd:cd06592  209 DS-----HWG-----YWNGLRSLIPTALTQGLLGYPFVLPDmIGGNAygnFPPDKELYIRWLQLSAFMPAMQFSVA---- 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 608 rrePWL-LASQYQDAIRDALFQRYSLLPFWYTLFYQAHKEGFPVMRPLWVQYPEDMSTFSIEDQFMLGDALLIHPVSDAG 686
Cdd:cd06592  275 ---PWRnYDEEVVDIARKLAKLREKLLPYIYELAAEAVDTGEPIIRPLWWIAPEDEEALTIDDQFLLGDDILVAPVLEKG 351
                        410
                 ....*....|
gi 569006397 687 AHGVQVYLPG 696
Cdd:cd06592  352 ARSRDVYLPK 361
PRK10658 PRK10658
putative alpha-glucosidase; Provisional
287-732 1.02e-42

putative alpha-glucosidase; Provisional


Pssm-ID: 236731 [Multi-domain]  Cd Length: 665  Bit Score: 165.84  E-value: 1.02e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 287 IDVFLMLGPSVFDVFRQYASLTGTQALPPLFSLGYhqsrW-------NYrDEADVLEVDQGFDDHNMPCDVI-------- 351
Cdd:PRK10658 236 LEYFVIDGPTPKEVLDRYTALTGRPALPPAWSFGL----WlttsfttNY-DEATVNSFIDGMAERDLPLHVFhfdcfwmk 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 352 ---WLDiehadgkryFTWDPTRFPQPLNMLEHLASKRRKLVAIVDPHIKVDSgyRVHEELRNHGLYVKTRDGSDyegWCW 428
Cdd:PRK10658 311 efqWCD---------FEWDPRTFPDPEGMLKRLKAKGLKICVWINPYIAQKS--PLFKEGKEKGYLLKRPDGSV---WQW 376
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 429 ----PGSASYpDFTNPRMRAWWSNMfsfdnyegsapnLYVWNDMNepsvfngpeVTMLK---------DAVHYGGWEHRD 495
Cdd:PRK10658 377 dkwqPGMAIV-DFTNPDACKWYADK------------LKGLLDMG---------VDCFKtdfgeriptDVVWFDGSDPQK 434
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 496 IHNIYGlYVHMATADGLIQRSGGIERPFVLSRAFFSGSQRFGAVWTGDNTAEWDHLKISIPMCLSLALVGLSFCGADVGG 575
Cdd:PRK10658 435 MHNYYT-YLYNKTVFDVLKETRGEGEAVLFARSATVGGQQFPVHWGGDCYSNYESMAESLRGGLSLGLSGFGFWSHDIGG 513
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 576 FFKNPEPELLVRWYQMGayqpFFRAHA--HLDTGRREPWLLASQYQDAIRDALFQRYSLLPFWYTLFYQAHKEGFPVMRP 653
Cdd:PRK10658 514 FENTATADVYKRWCAFG----LLSSHSrlHGSKSYRVPWAYDEEAVDVVRFFTKLKCRLMPYLYREAAEAHERGTPMMRA 589
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 654 LWVQYPEDMSTFSIEDQFMLGDALLIHPV-SDAGAhgVQVYLPgqEEVWYDIQS---------YQKHHGpqtlYLpvtls 723
Cdd:PRK10658 590 MVLEFPDDPACDYLDRQYMLGDSLLVAPVfSEAGD--VEYYLP--EGRWTHLLTgeeveggrwHKEQHD----FL----- 656

                 ....*....
gi 569006397 724 SIPVFQRGG 732
Cdd:PRK10658 657 SLPLLVRPN 665
PRK10426 PRK10426
alpha-glucosidase; Provisional
360-734 5.81e-38

alpha-glucosidase; Provisional


Pssm-ID: 236691 [Multi-domain]  Cd Length: 635  Bit Score: 151.30  E-value: 5.81e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 360 GKRYF---TWDPTRFPQPLNMLEHLASKRRKLVAIVDPHIKVDSGyrVHEELRNHGLYVKTRDGSDYEGWCWPGSASYPD 436
Cdd:PRK10426 254 GKRLMwnwKWDSERYPQLDSRIKQLNEEGIQFLGYINPYLASDGD--LCEEAAEKGYLAKDADGGDYLVEFGEFYAGVVD 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 437 FTNPRMRAWWS-----NMFSFdnyegsapNLYVW-NDMNE--PSvfngpevtmlkDAVHYGGWEHRDIHNIYGLY----V 504
Cdd:PRK10426 332 LTNPEAYEWFKevikkNMIGL--------GCSGWmADFGEylPT-----------DAYLHNGVSAEIMHNAWPALwakcN 392
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 505 HMAtadglIQRSGGIERPFVLSRAFFSGSQRFGAV-WTGDNTAEW---DHLKISIPMCLSLALVGLSFCGADVGGF---F 577
Cdd:PRK10426 393 YEA-----LEETGKLGEILFFMRAGYTGSQKYSTLfWAGDQNVDWsldDGLASVVPAALSLGMSGHGLHHSDIGGYttlF 467
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 578 KNPE-PELLVRWYQMGAYQPFFRAHahlDTGR-REPWLLasqYQDAIRDALFQRYS-----LLPFWYTLFYQAHKEGFPV 650
Cdd:PRK10426 468 GMKRtKELLLRWCEFSAFTPVMRTH---EGNRpGDNWQF---DSDAETIAHFARMTrvfttLKPYLKELVAEAAKTGLPV 541
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 651 MRPLWVQYPEDMSTFSIEDQFMLGDALLIHPVSDAGAHGVQVYLPGQEevWYDIQSyQKHHGPQTLYLPVTLSSIPVFQR 730
Cdd:PRK10426 542 MRPLFLHYEDDAATYTLKYQYLLGRDLLVAPVHEEGRTDWTVYLPEDK--WVHLWT-GEAFAGGEITVEAPIGKPPVFYR 618

                 ....
gi 569006397 731 GGTI 734
Cdd:PRK10426 619 AGSE 622
GH31_transferase_CtsY cd06597
CtsY (cyclic tetrasaccharide-synthesizing enzyme Y)-like; CtsY is a bacterial ...
312-633 4.57e-33

CtsY (cyclic tetrasaccharide-synthesizing enzyme Y)-like; CtsY is a bacterial 3-alpha-isomaltosyltransferase, first identified in Arthrobacter globiformis, that produces cyclic tetrasaccharides together with a closely related enzyme CtsZ. CtsY and CtsZ both have a glycosyl hydrolase family 31 (GH31) catalytic domain; CtsZ belongs to a different subfamily. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.


Pssm-ID: 269883 [Multi-domain]  Cd Length: 326  Bit Score: 130.51  E-value: 4.57e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 312 ALPPLFSLGYHQSRWNYRDEADVLEVDQGFDDHNMPCDVIWLDIEHADGKRY-FTWDPTRFPQPLNMLEHLASKRRKLVA 390
Cdd:cd06597    4 ALPPKWAFGHWVSANEWNSQAEVLELVEEYLAYDIPVGAVVIEAWSDEATFYiFNDATGKWPDPKGMIDSLHEQGIKVIL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 391 IVDPHIKVDSGYRV-----HEELRNHGLYVKTRDGSDY--EGWcWPGSASYPDFTNPRMRAWW----SNMFSFDNYEGsa 459
Cdd:cd06597   84 WQTPVVKTDGTDHAqksndYAEAIAKGYYVKNGDGTPYipEGW-WFGGGSLIDFTNPEAVAWWhdqrDYLLDELGIDG-- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 460 pnlyvWNDmnepsvfNGPEVTMLKDAVHYGGWEHRDIHNIYGL--------YVHMATADGLIqrsggierpfvLSRAFFS 531
Cdd:cd06597  161 -----FKT-------DGGEPYWGEDLIFSDGKKGREMRNEYPNlyykayfdYIREIGNDGVL-----------FSRAGDS 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 532 GSQRFGAVWTGDNTAEWDHLKISIPMCLSLALVGLSFCGADVGGFFKN-PEPELLVRWYQMGAYQPFFRAH---AHLDTG 607
Cdd:cd06597  218 GAQRYPIGWVGDQDSTFEGLQSALKAGLSAAWSGYPFWGWDIGGFSGPlPTAELYLRWTQLAAFSPIMQNHsekNHRPWS 297
                        330       340
                 ....*....|....*....|....*.
gi 569006397 608 RREPWLLASQYQDAIRDALFQRYSLL 633
Cdd:cd06597  298 EERRWNVAERTGDPEVLDIYRKYVKL 323
GH31_CPE1046 cd06596
Clostridium CPE1046-like; CPE1046 is an uncharacterized Clostridium perfringens protein with a ...
509-703 7.04e-31

Clostridium CPE1046-like; CPE1046 is an uncharacterized Clostridium perfringens protein with a glycosyl hydrolase family 31 (GH31) domain. The domain architecture of CPE1046 and its orthologs includes a C-terminal fibronectin type 3 (FN3) domain and a coagulation factor 5/8 type C domain in addition to the GH31 domain. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.


Pssm-ID: 269882  Cd Length: 334  Bit Score: 124.38  E-value: 7.04e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 509 ADGLIQRSGgiERPFVLSRAFFSGSQRFGAVWTGDNTAEWDHLKISIPMCLSLALVGLSFCGADVGGFFKNpEPELLVRW 588
Cdd:cd06596  135 ADGIENNSN--ARPFIWTVDGWAGTQRYAVIWTGDQSGSWEYIRFHIPTYIGSGLSGQAYATSDVDGIFGG-SPETYTRD 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 589 YQMGAYQPFFRAHAHLDTGRREPWLLASQYQDAIRDALFQRYSLLPFWYTLFYQAHKEGFPVMRPLWVQYPEDMSTFSIE 668
Cdd:cd06596  212 LQWKAFTPVLMNMSGWAANDKQPWVFGEPYTSINRKYLKLKMRLMPYIYTYAREASVTGLPMVRAMFLEYPNDPTAYGTA 291
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 569006397 669 D--QFMLGDALLIHPV--SDAGAHGVQ--VYLPgqEEVWYD 703
Cdd:cd06596  292 TqyQFMWGPDFLVAPVyqNTAAGNDVRngIYLP--AGTWID 330
GH31_u1 cd06595
glycosyl hydrolase family 31 (GH31); uncharacterized subgroup; This family represents an ...
308-635 6.34e-30

glycosyl hydrolase family 31 (GH31); uncharacterized subgroup; This family represents an uncharacterized GH31 enzyme subgroup found in bacteria and eukaryotes. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.


Pssm-ID: 269881 [Multi-domain]  Cd Length: 304  Bit Score: 120.77  E-value: 6.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 308 TGTQALPPLFSLGYHQSR-WNYRDEaDVLEVDQGFDDHNMPCDVIWLD-------IEHADGKRYFTWDPTRFPQPLNMLE 379
Cdd:cd06595    1 TGKPPLIPRYALGNWWSRyWAYSDD-DILDLVDNFKRNEIPLSVLVLDmdwhitdKKYKNGWTGYTWNKELFPDPKGFLD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 380 HLASKRRKLVAIVDPHIkvdsGYRVHEELRNHglyVKTRDGSDyegwcWPGSASYP-DFTNPRMRAwwsNMFSF--DNYE 456
Cdd:cd06595   80 WLHERGLRVGLNLHPAE----GIRPHEEAYAE---FAKYLGID-----PAKIIPIPfDVTDPKFLD---AYFKLliHPLE 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 457 GSAPNLYvWNDmnepsvfngpevtmlkdavhYGGWEHRDIHNIYGLYV--HMATADGliQRSGGiERPFVLSRAFFSGSQ 534
Cdd:cd06595  145 KQGVDFW-WLD--------------------WQQGKDSPLAGLDPLWWlnHYHYLDS--GRNGK-RRPLILSRWGGLGSH 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 535 RFGAVWTGDNTAEWDHLKISIPMCLSLALVGLSFCGADVGGFFKNPE-PELLVRWYQMGAYQPFFRAHA-HLDTGRREPW 612
Cdd:cd06595  201 RYPIGFSGDTEVSWETLAFQPYFTATAANVGYSWWSHDIGGHKGGIEdPELYLRWVQFGVFSPILRLHSdKGPYYKREPW 280
                        330       340
                 ....*....|....*....|...
gi 569006397 613 LLASQYQDAIRDALFQRYSLLPF 635
Cdd:cd06595  281 LWDAKTFEIAKDYLRLRHRLIPY 303
GH31_N cd14752
N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to ...
167-309 1.79e-29

N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to the glycosyl-hydrolase domain of Glycoside hydrolase family 31 (GH31). GH31 includes the glycoside hydrolases alpha-glucosidase (EC 3.2.1.20), alpha-1,3-glucosidase (EC 3.2.1.84), alpha-xylosidase (EC 3.2.1.177), sucrase-isomaltase (EC 3.2.1.48 and EC 3.2.1.10), as well as alpha-glucan lyase (EC 4.2.2.13). All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. In most cases, the pyranose moiety recognized in subsite-1 of the substrate binding site is an alpha-D-glucose, though some GH31 family members show a preference for alpha-D-xylose. Several GH31 enzymes can accommodate both glucose and xylose and different levels of discrimination between the two have been observed. Most characterized GH31 enzymes are alpha-glucosidases. In mammals, GH31 members with alpha-glucosidase activity are implicated in at least three distinct biological processes. The lysosomal acid alpha-glucosidase (GAA) is essential for glycogen degradation and a deficiency or malfunction of this enzyme causes glycogen storage disease II, also known as Pompe disease. In the endoplasmic reticulum, alpha-glucosidase II catalyzes the second step in the N-linked oligosaccharide processing pathway that constitutes part of the quality control system for glycoprotein folding and maturation. The intestinal enzymes sucrase-isomaltase (SI) and maltase-glucoamylase (MGAM) play key roles in the final stage of carbohydrate digestion, making alpha-glucosidase inhibitors useful in the treatment of type 2 diabetes. GH31 alpha-glycosidases are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues of the catalytic domain have been identified as the catalytic nucleophile and the acid/base, respectively. A loop of the N-terminal beta-sandwich domain is part of the active site pocket.


Pssm-ID: 270212 [Multi-domain]  Cd Length: 122  Bit Score: 113.43  E-value: 1.79e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 167 TSVGLDFSLPGMEHVYGIPEHADSLRLKvtegGEPYRLYNLDVFQYElNNPMALYGSVPVLLAHSFHrdlGIFWLNAAET 246
Cdd:cd14752    8 TPLRLSFKLPPDEHFYGLGERFGGLNKR----GKRYRLWNTDQGGYR-GSTDPLYGSIPFYLSSKGY---GVFLDNPSRT 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006397 247 WVDIssntagktlfgkmldylqgsGETPQTDIRWMSESGIIDVFLMLGPSVFDVFRQYASLTG 309
Cdd:cd14752   80 EFDF--------------------GSEDSDELTFSSEGGDLDYYFFAGPTPKEVIEQYTELTG 122
Gal_mutarotas_2 pfam13802
Galactose mutarotase-like; This family is found N-terminal to glycosyl-hydrolase domains, and ...
179-249 5.04e-23

Galactose mutarotase-like; This family is found N-terminal to glycosyl-hydrolase domains, and appears to be similar to the galactose mutarotase superfamily.


Pssm-ID: 463987 [Multi-domain]  Cd Length: 67  Bit Score: 92.91  E-value: 5.04e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006397  179 EHVYGIPEHADSLRLKvtegGEPYRLYNLDVFQYElNNPMALYGSVPVLLAHSFHRDLGIFWLNAAETWVD 249
Cdd:pfam13802   2 EHVYGLGERAGPLNKR----GTRYRLWNTDAFGYE-LDTDPLYKSIPFYISHNGGRGYGVFWDNPAETWFD 67
GH31_glucosidase_YihQ cd06594
alpha-glucosidase YihQ-like; YihQ is a bacterial alpha-glucosidase with a conserved glycosyl ...
334-601 7.08e-18

alpha-glucosidase YihQ-like; YihQ is a bacterial alpha-glucosidase with a conserved glycosyl hydrolase family 31 (GH31) domain that catalyzes the release of an alpha-glucosyl residue from the non-reducing end of alpha-glucoside substrates such as alpha-glucosyl fluoride. Orthologs of YihQ that have not yet been functionally characterized are present in plants and fungi. YihQ has sequence similarity to other GH31 enzymes such as CtsZ, a 6-alpha-glucosyltransferase from Bacillus globisporus, and YicI, an alpha-xylosidase from Echerichia coli. These latter two belong to different GH31 subfamilies than YihQ. In bacteria, YihQ (along with YihO) is important for bacterial O-antigen capsule assembly and translocation.


Pssm-ID: 269880 [Multi-domain]  Cd Length: 325  Bit Score: 85.71  E-value: 7.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 334 VLEVDQGFDDHNMPCDVIWLD-----IEHADGKRYF---TWDPTRFPQPLNMLEHLASKRRKLVAIVDPHIKVDSGYRVH 405
Cdd:cd06594   25 VLEVLEQLLAAGVPVAAVWLQdwvgtRKTSFGKRLWwnwEWDEELYPGWDELVKELKEQGIRVLGYINPFLANVGPLYSY 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 406 EELRNHGLYVKTRDGSDYEGWCWPGSASYPDFTNPRMRAWWSNMFSFDNYEGsapNLYVW-NDMNEPSVFngpevtmlkD 484
Cdd:cd06594  105 KEAEEKGYLVKNKTGEPYLVDFGEFDAGLVDLTNPEARRWFKEVIKENMIDF---GLSGWmADFGEYLPF---------D 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006397 485 AVHYGGWEHRDIHNIYGLY---VHMAtadgLIQRSGGIERPFVLSRAFFSGSQRFGAV-WTGDNTAEW---DHLKISIPM 557
Cdd:cd06594  173 AVLHSGEDAALYHNRYPELwarLNRE----AVEEAGKEGEIVFFMRSGYTGSPRYSTLfWAGDQNVDWsrdDGLKSVIPG 248
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 569006397 558 CLSLALVGLSFCGADVGGF--FKNPE------PELLVRWYQMGAYQPFFRAH 601
Cdd:cd06594  249 ALSSGLSGFSLTHSDIGGYttLFNPLvgykrsKELLMRWAEMAAFTPVMRTH 300
DUF5110 pfam17137
Domain of unknown function (DUF5110); This domain is likely to be a carbohydrate-binding ...
752-795 1.33e-03

Domain of unknown function (DUF5110); This domain is likely to be a carbohydrate-binding domain of some description as it is found immediately C-terminal to the glycosyl-hydrolase family Glyco_hydro_31, pfam01055.


Pssm-ID: 465360 [Multi-domain]  Cd Length: 72  Bit Score: 38.00  E-value: 1.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 569006397  752 PITLFVAlsPQGTAQGELFLDDGHTFNYQtRHEFLLRRFSFSGS 795
Cdd:pfam17137   1 PLTLRVY--PGADGSFTLYEDDGDTYAYE-KGAYATTTFTVDDD 41
 
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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