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Conserved domains on  [gi|2017363538|ref|NP_001380857|]
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neutral alpha-glucosidase C isoform 1 [Homo sapiens]

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
PubMed:  12123797

Graphical summary

 Zoom to residue level

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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 ...
353-820 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: 895.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 353 GTQAMPPLFSLGYHQCRWNYEDEQDVKAVDAGFDEHDIPYDAMWLDIEHTEGKRYFTWDKNRFPNPKRMQELLRSKKRKL 432
Cdd:cd06603     1 GTPPLPPLFALGYHQCRWNYNDQEDVLEVDANFDEHDIPYDVIWLDIEHTDGKRYFTWDKKKFPDPKKMQEKLASKGRKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 433 VVISDPHIKIDPDYSVYVKAKDQGFFVKNQEGEDFEGVCWPGLSSYLDFTNPKVREWYSSLFAFPVYQGSTDILFLWNDM 512
Cdd:cd06603    81 VTIVDPHIKRDDDYFVYKEAKEKDYFVKDSDGKDFEGWCWPGSSSWPDFLNPEVRDWWASLFSYDKYKGSTENLYIWNDM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 513 NEPSVFRGPEQTMQKNAIHHGNWEHRELHNIYGFYHQMATAEGLIKRSKGKERPFVLTRSFFAGSQKYGAVWTGDNTAEW 592
Cdd:cd06603   161 NEPSVFNGPEITMPKDAIHYGGVEHRDVHNIYGLYMHMATFEGLLKRSNGKKRPFVLTRSFFAGSQRYGAVWTGDNMATW 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 593 SNLKISIPMLLTLSITGISFCGADIGGFIGNPETELLVRWYQAGAYQPFFRGHATMNTKRREPWLFGEEHTRLIREAIRE 672
Cdd:cd06603   241 EHLKISIPMLLSLSIAGIPFVGADVGGFFGNPDEELLVRWYQAGAFYPFFRAHAHIDTKRREPWLFGEETTEIIREAIRL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 673 RYGLLPYWYSLFYHAHVASQPVMRPLWVEFPDELKTFDMEDEYMLGSALLVHPVTEPKATTVDVFLPGsNEVWYDYKTFA 752
Cdd:cd06603   321 RYRLLPYWYTLFYEASRTGLPIMRPLWYEFPEDESTFDIDDQFMLGDSLLVKPVVEEGATSVTVYLPG-GEVWYDYFTGQ 399
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363538 753 HWEGGCTVKIPVALDTIPVFQRGGSVIPIKTTVGKSTGWMTESSYGLRVALSTKGSSVGELYLDDGHS 820
Cdd:cd06603   400 RVTGGGTKTVPVPLDSIPVFQRGGSIIPRKERVRRSSKLMRNDPYTLVVALDENGEAEGELYLDDGES 467
GH31_N cd14752
N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to ...
213-353 2.90e-25

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: 101.49  E-value: 2.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 213 IGLDFSLHGFEHLYGIPQHAESHQLKntgdGDAYRLYNLDVYGYQiYDKMGIYGSVPYLLAHklgRTIGIFWLNASETLV 292
Cdd:cd14752    10 LRLSFKLPPDEHFYGLGERFGGLNKR----GKRYRLWNTDQGGYR-GSTDPLYGSIPFYLSS---KGYGVFLDNPSRTEF 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363538 293 EINTEpaveytltqmgpvaakqkvrSRTHVHWMSESGIIDVFLLTGPTPSDVFKQYSHLTG 353
Cdd:cd14752    82 DFGSE--------------------DSDELTFSSEGGDLDYYFFAGPTPKEVIEQYTELTG 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 ...
353-820 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: 895.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 353 GTQAMPPLFSLGYHQCRWNYEDEQDVKAVDAGFDEHDIPYDAMWLDIEHTEGKRYFTWDKNRFPNPKRMQELLRSKKRKL 432
Cdd:cd06603     1 GTPPLPPLFALGYHQCRWNYNDQEDVLEVDANFDEHDIPYDVIWLDIEHTDGKRYFTWDKKKFPDPKKMQEKLASKGRKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 433 VVISDPHIKIDPDYSVYVKAKDQGFFVKNQEGEDFEGVCWPGLSSYLDFTNPKVREWYSSLFAFPVYQGSTDILFLWNDM 512
Cdd:cd06603    81 VTIVDPHIKRDDDYFVYKEAKEKDYFVKDSDGKDFEGWCWPGSSSWPDFLNPEVRDWWASLFSYDKYKGSTENLYIWNDM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 513 NEPSVFRGPEQTMQKNAIHHGNWEHRELHNIYGFYHQMATAEGLIKRSKGKERPFVLTRSFFAGSQKYGAVWTGDNTAEW 592
Cdd:cd06603   161 NEPSVFNGPEITMPKDAIHYGGVEHRDVHNIYGLYMHMATFEGLLKRSNGKKRPFVLTRSFFAGSQRYGAVWTGDNMATW 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 593 SNLKISIPMLLTLSITGISFCGADIGGFIGNPETELLVRWYQAGAYQPFFRGHATMNTKRREPWLFGEEHTRLIREAIRE 672
Cdd:cd06603   241 EHLKISIPMLLSLSIAGIPFVGADVGGFFGNPDEELLVRWYQAGAFYPFFRAHAHIDTKRREPWLFGEETTEIIREAIRL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 673 RYGLLPYWYSLFYHAHVASQPVMRPLWVEFPDELKTFDMEDEYMLGSALLVHPVTEPKATTVDVFLPGsNEVWYDYKTFA 752
Cdd:cd06603   321 RYRLLPYWYTLFYEASRTGLPIMRPLWYEFPEDESTFDIDDQFMLGDSLLVKPVVEEGATSVTVYLPG-GEVWYDYFTGQ 399
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363538 753 HWEGGCTVKIPVALDTIPVFQRGGSVIPIKTTVGKSTGWMTESSYGLRVALSTKGSSVGELYLDDGHS 820
Cdd:cd06603   400 RVTGGGTKTVPVPLDSIPVFQRGGSIIPRKERVRRSSKLMRNDPYTLVVALDENGEAEGELYLDDGES 467
Glyco_hydro_31 pfam01055
Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. ...
334-779 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: 666.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 334 FLLTGPTPSDVFKQYSHLTGTQAMPPLFSLGYHQCRWNYEDEQDVKAVDAGFDEHDIPYDAMWLDIEHTEGKRYFTWDKN 413
Cdd:pfam01055   1 YFFLGPTPKDVVKQYTELTGRPPLPPYWALGYHQSRWGYKSEEEVLEVVDGFRERDIPLDVIWLDIDYMDGYRDFTWDPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 414 RFPNPKRMQELLRSKKRKLVVISDPHI-KIDPDYSVYVKAKDQGFFVKNQEGEDFEGVcWPGLSSYLDFTNPKVREWYSS 492
Cdd:pfam01055  81 RFPDPKGMVDELHAKGQKLVVIIDPGIkKVDPGYPPYDEGLEKGYFVKNPDGSLYVGG-WPGMSAFPDFTNPEARDWWAD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 493 -LFAFPVYQGstdILFLWNDMNEPSVFRG--PEQTMQKNAIHHGNWEHRELHNIYGFYHQMATAEGLIKRsKGKERPFVL 569
Cdd:pfam01055 160 qLFKFLLDMG---VDGIWNDMNEPSVFCGsgPEDTVAKDNDPGGGVEHYDVHNLYGLLMAKATYEGLREK-RPNKRPFVL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 570 TRSFFAGSQKYGAVWTGDNTAEWSNLKISIPMLLTLSITGISFCGADIGGFIGNPETELLVRWYQAGAYQPFFRGHATMN 649
Cdd:pfam01055 236 TRSGFAGSQRYAAHWSGDNTSTWEHLRFSIPGGLSLGLSGIPFWGADIGGFFNPTTPELYVRWYQLGAFSPFFRNHSSID 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 650 TKRREPWLFGEEHTRLIREAIRERYGLLPYWYSLFYHAHVASQPVMRPLWVEFPDELKTFDMEDEYMLGSALLVHPVTEP 729
Cdd:pfam01055 316 TRRREPWLFGEEVEEIIRKAIRLRYRLLPYLYTLFYEAHETGLPVMRPLFLEFPDDPNTFDIDDQFMFGPSLLVAPVLEE 395
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 2017363538 730 KATTVDVFLPGsnEVWYDYKTFAHWEGGCTVKIPVALDTIPVFQRGGSVI 779
Cdd:pfam01055 396 GATSVDVYLPG--GRWYDFWTGERYEGGGTVPVTAPLDRIPLFVRGGSII 443
YicI COG1501
Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];
215-818 5.16e-123

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


Pssm-ID: 441110 [Multi-domain]  Cd Length: 609  Bit Score: 385.67  E-value: 5.16e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 215 LDFSLHGFEHLYGIPQHAESHQLKntgdGDAYRLYNLDVYGYQIYDKMgiYGSVPYLLAHKlgrTIGIFWLNASETLVEI 294
Cdd:COG1501    54 VRKQLDLGEQIYGLGERFTTLHKR----GRIVVNWNLDHGGHKDNGNT--YAPIPFYVSSK---GYGVFVNSASYVTFDV 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 295 NTEpavEYTLTQMGPVAAKqkvrsrthvhwmsesgiIDVFLLTGPTPSDVFKQYSHLTGTQAMPPLFSLGYHQCRWNYED 374
Cdd:COG1501   125 GSA---YSDLVEFTVPGDS-----------------LEFYVIEGPSPEDVLEKYTELTGKPPLPPRWAFGYWQSRKSYYD 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 375 EQDVKAVDAGFDEHDIPYDAMWLDIeHTEGKRY---FTWDKNRFPNPKRMQELLRSKKRKLVVISDPHIkiDPDYSVYVK 451
Cdd:COG1501   185 QDQVLAFADEFRDRGFPLDVIHLDI-RWMDKYYwgdFEWDPRRFPDPKAMVKELHDRGVKLVLWINPYV--APDSAIFAE 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 452 AkdQGFFVKNQEGEDFEGVCWPGLSSYLDFTNPKVREW-YSSLFAFPVYQGSTDIlflWNDMNEpsvfRGPEQTmqknAI 530
Cdd:COG1501   262 G--MANFVKIASGTVFVGKMWPGTTGLLDFTRPDAREWfWAGLEKELLSIGVDGI---KLDMNE----GWPTDV----AT 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 531 HHGNWEHReLHNIYGFYHQMATAEGLikRSKGKERPFVLTRSFFAGSQKYGAVWTGDNTAEWSNLKISIPMLLTLSITGI 610
Cdd:COG1501   329 FPSNVPQQ-MRNLYGLLEAKATFEGF--RTSRNNRTFILTRSGFAGGQRYPVIWTGDNTSSWESLEDQLTQGLNLSLSGV 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 611 SFCGADIGGFIGNPETELLVRWYQAGAYQPFFRGHAtmNTKRREPWLFGEEHTRLIREAIRERYGLLPYWYSLFYHAHVA 690
Cdd:COG1501   406 PFWTPDIGGFFGSPSRELWIRWFQVGAFSPFARIHG--WASSTEPWFFDEEAKQIVKEYAQLRYRLLPYIYSLFAKASTD 483
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 691 SQPVMRPLWVEFPDELKTFDMEDEYMLGSALLVHPVTePKATTVDVFLPGSNevWYDYKTFAHWEGGCTVKIPVALDTIP 770
Cdd:COG1501   484 GTPVIRPLFLEFPDDPTTRFIDDQYMFGEYLLVAPIF-AGTESRLVYLPKGK--WYDFWTGELIEGGQWITVTAPLDRLP 560
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*...
gi 2017363538 771 VFQRGGSVIPIKTTvgkSTGWMTESSYGLRVALSTKGSSVGELYLDDG 818
Cdd:COG1501   561 LYVRDGSIIPLGPV---SLRPSMQKIDGIELRVYGSGETAYTLYDDDG 605
PLN02763 PLN02763
hydrolase, hydrolyzing O-glycosyl compounds
339-830 4.32e-119

hydrolase, hydrolyzing O-glycosyl compounds


Pssm-ID: 215408 [Multi-domain]  Cd Length: 978  Bit Score: 386.17  E-value: 4.32e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 339 PTPSDVFKQYSHLTGTQAMPPLFSLGYHQCRWNYEDEQDVKAVDAGFDEHDIPYDAMWLDIEHTEGKRYFTWDKNRFPNP 418
Cdd:PLN02763  164 PSPEALLTSLSHAIGTVFMPPKWALGYQQCRWSYESAKRVAEIARTFREKKIPCDVVWMDIDYMDGFRCFTFDKERFPDP 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 419 KRMQELLRSKKRKLVVISDPHIKIDPDYSVYVKAKDQGFFVKNQEGEDFEGVCWPGLSSYLDFTNPKVREWYSSLFAFPV 498
Cdd:PLN02763  244 KGLADDLHSIGFKAIWMLDPGIKAEEGYFVYDSGCENDVWIQTADGKPFVGEVWPGPCVFPDFTNKKTRSWWANLVKDFV 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 499 YQGSTDIlflWNDMNEPSVFRGPEQTMQKNAIHHGNWE------HRELHNIYGFYHQMATAEGLIKRSKGKeRPFVLTRS 572
Cdd:PLN02763  324 SNGVDGI---WNDMNEPAVFKTVTKTMPETNIHRGDEElggvqnHSHYHNVYGMLMARSTYEGMLLANKNK-RPFVLTRA 399
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 573 FFAGSQKYGAVWTGDNTAEWSNLKISIPMLLTLSITGISFCGADIGGFIGNPETELLVRWYQAGAYQPFFRGHATMNTKR 652
Cdd:PLN02763  400 GFIGSQRYAATWTGDNLSNWEHLHMSIPMVLQLGLSGQPLSGPDIGGFAGDATPKLFGRWMGVGAMFPFARGHSEQGTID 479
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 653 REPWLFGEEHTRLIREAIRERYGLLPYWYSLFYHAHVASQPVMRPLWVEFPDELKTFDMEDEYMLGSaLLVHPVTEPKAT 732
Cdd:PLN02763  480 HEPWSFGEECEEVCRLALKRRYRLLPHFYTLFYKAHTTGLPVMTPIFFADPKDPSLRKVENSFLLGP-LLISASTLPDQG 558
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 733 TVDVFLPGSNEVWYDYktfaHWEggctvkipvalDTIP----VFQRGGSVIPIKTTVGKSTGWMTESSYGLRVALSTKGS 808
Cdd:PLN02763  559 SDNLQHVLPKGIWQRF----DFD-----------DSHPdlplLYLQGGSIIPLGPPIQHVGEASLSDDLTLLIALDENGK 623
                         490       500
                  ....*....|....*....|..
gi 2017363538 809 SVGELYLDDGHSFQYLhQKQFL 830
Cdd:PLN02763  624 AEGVLYEDDGDGFGYT-KGDYL 644
GH31_N cd14752
N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to ...
213-353 2.90e-25

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: 101.49  E-value: 2.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 213 IGLDFSLHGFEHLYGIPQHAESHQLKntgdGDAYRLYNLDVYGYQiYDKMGIYGSVPYLLAHklgRTIGIFWLNASETLV 292
Cdd:cd14752    10 LRLSFKLPPDEHFYGLGERFGGLNKR----GKRYRLWNTDQGGYR-GSTDPLYGSIPFYLSS---KGYGVFLDNPSRTEF 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363538 293 EINTEpaveytltqmgpvaakqkvrSRTHVHWMSESGIIDVFLLTGPTPSDVFKQYSHLTG 353
Cdd:cd14752    82 DFGSE--------------------DSDELTFSSEGGDLDYYFFAGPTPKEVIEQYTELTG 122
Gal_mutarotas_2 pfam13802
Galactose mutarotase-like; This family is found N-terminal to glycosyl-hydrolase domains, and ...
222-293 4.18e-17

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: 76.35  E-value: 4.18e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363538 222 FEHLYGIPQHAESHQLKNTgdgdAYRLYNLDVYGYQIyDKMGIYGSVPYLLAHKLGRTIGIFWLNASETLVE 293
Cdd:pfam13802   1 DEHVYGLGERAGPLNKRGT----RYRLWNTDAFGYEL-DTDPLYKSIPFYISHNGGRGYGVFWDNPAETWFD 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 ...
353-820 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: 895.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 353 GTQAMPPLFSLGYHQCRWNYEDEQDVKAVDAGFDEHDIPYDAMWLDIEHTEGKRYFTWDKNRFPNPKRMQELLRSKKRKL 432
Cdd:cd06603     1 GTPPLPPLFALGYHQCRWNYNDQEDVLEVDANFDEHDIPYDVIWLDIEHTDGKRYFTWDKKKFPDPKKMQEKLASKGRKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 433 VVISDPHIKIDPDYSVYVKAKDQGFFVKNQEGEDFEGVCWPGLSSYLDFTNPKVREWYSSLFAFPVYQGSTDILFLWNDM 512
Cdd:cd06603    81 VTIVDPHIKRDDDYFVYKEAKEKDYFVKDSDGKDFEGWCWPGSSSWPDFLNPEVRDWWASLFSYDKYKGSTENLYIWNDM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 513 NEPSVFRGPEQTMQKNAIHHGNWEHRELHNIYGFYHQMATAEGLIKRSKGKERPFVLTRSFFAGSQKYGAVWTGDNTAEW 592
Cdd:cd06603   161 NEPSVFNGPEITMPKDAIHYGGVEHRDVHNIYGLYMHMATFEGLLKRSNGKKRPFVLTRSFFAGSQRYGAVWTGDNMATW 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 593 SNLKISIPMLLTLSITGISFCGADIGGFIGNPETELLVRWYQAGAYQPFFRGHATMNTKRREPWLFGEEHTRLIREAIRE 672
Cdd:cd06603   241 EHLKISIPMLLSLSIAGIPFVGADVGGFFGNPDEELLVRWYQAGAFYPFFRAHAHIDTKRREPWLFGEETTEIIREAIRL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 673 RYGLLPYWYSLFYHAHVASQPVMRPLWVEFPDELKTFDMEDEYMLGSALLVHPVTEPKATTVDVFLPGsNEVWYDYKTFA 752
Cdd:cd06603   321 RYRLLPYWYTLFYEASRTGLPIMRPLWYEFPEDESTFDIDDQFMLGDSLLVKPVVEEGATSVTVYLPG-GEVWYDYFTGQ 399
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363538 753 HWEGGCTVKIPVALDTIPVFQRGGSVIPIKTTVGKSTGWMTESSYGLRVALSTKGSSVGELYLDDGHS 820
Cdd:cd06603   400 RVTGGGTKTVPVPLDSIPVFQRGGSIIPRKERVRRSSKLMRNDPYTLVVALDENGEAEGELYLDDGES 467
Glyco_hydro_31 pfam01055
Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. ...
334-779 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: 666.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 334 FLLTGPTPSDVFKQYSHLTGTQAMPPLFSLGYHQCRWNYEDEQDVKAVDAGFDEHDIPYDAMWLDIEHTEGKRYFTWDKN 413
Cdd:pfam01055   1 YFFLGPTPKDVVKQYTELTGRPPLPPYWALGYHQSRWGYKSEEEVLEVVDGFRERDIPLDVIWLDIDYMDGYRDFTWDPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 414 RFPNPKRMQELLRSKKRKLVVISDPHI-KIDPDYSVYVKAKDQGFFVKNQEGEDFEGVcWPGLSSYLDFTNPKVREWYSS 492
Cdd:pfam01055  81 RFPDPKGMVDELHAKGQKLVVIIDPGIkKVDPGYPPYDEGLEKGYFVKNPDGSLYVGG-WPGMSAFPDFTNPEARDWWAD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 493 -LFAFPVYQGstdILFLWNDMNEPSVFRG--PEQTMQKNAIHHGNWEHRELHNIYGFYHQMATAEGLIKRsKGKERPFVL 569
Cdd:pfam01055 160 qLFKFLLDMG---VDGIWNDMNEPSVFCGsgPEDTVAKDNDPGGGVEHYDVHNLYGLLMAKATYEGLREK-RPNKRPFVL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 570 TRSFFAGSQKYGAVWTGDNTAEWSNLKISIPMLLTLSITGISFCGADIGGFIGNPETELLVRWYQAGAYQPFFRGHATMN 649
Cdd:pfam01055 236 TRSGFAGSQRYAAHWSGDNTSTWEHLRFSIPGGLSLGLSGIPFWGADIGGFFNPTTPELYVRWYQLGAFSPFFRNHSSID 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 650 TKRREPWLFGEEHTRLIREAIRERYGLLPYWYSLFYHAHVASQPVMRPLWVEFPDELKTFDMEDEYMLGSALLVHPVTEP 729
Cdd:pfam01055 316 TRRREPWLFGEEVEEIIRKAIRLRYRLLPYLYTLFYEAHETGLPVMRPLFLEFPDDPNTFDIDDQFMFGPSLLVAPVLEE 395
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 2017363538 730 KATTVDVFLPGsnEVWYDYKTFAHWEGGCTVKIPVALDTIPVFQRGGSVI 779
Cdd:pfam01055 396 GATSVDVYLPG--GRWYDFWTGERYEGGGTVPVTAPLDRIPLFVRGGSII 443
GH31_glucosidase_II_MalA cd06604
Alpha-glucosidase II-like; Alpha-glucosidase II (alpha-D-glucoside glucohydrolase) is a ...
353-688 8.26e-167

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: 489.33  E-value: 8.26e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 353 GTQAMPPLFSLGYHQCRWNYEDEQDVKAVDAGFDEHDIPYDAMWLDIEHTEGKRYFTWDKNRFPNPKRMQELLRSKKRKL 432
Cdd:cd06604     1 GRPPLPPKWALGYQQSRWSYYPEEEVREVAKGFRERDIPCDAIYLDIDYMDGYRVFTWDKERFPDPKELIKELHEQGFRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 433 VVISDPHIKIDPDYSVYVKAKDQGFFVKNQEGEDFEGVCWPGLSSYLDFTNPKVREWYSSLFAFPVYQGSTDIlflWNDM 512
Cdd:cd06604    81 VTIVDPGVKVDPGYEVYEEGLENDYFVKDPDGELYVGKVWPGKSVFPDFTNPEVREWWGDLYKELVDLGVDGI---WNDM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 513 NEPSVFRGP-EQTMQKNAIHHGNWE---HRELHNIYGFYHQMATAEGLiKRSKGKERPFVLTRSFFAGSQKYGAVWTGDN 588
Cdd:cd06604   158 NEPAVFNAPgGTTMPLDAVHRLDGGkitHEEVHNLYGLLMARATYEGL-RRLRPNKRPFVLSRAGYAGIQRYAAIWTGDN 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 589 TAEWSNLKISIPMLLTLSITGISFCGADIGGFIGNPETELLVRWYQAGAYQPFFRGHATMNTKRREPWLFGEEHTRLIRE 668
Cdd:cd06604   237 SSSWEHLRLSIPMLLNLGLSGVPFVGADIGGFAGDPSPELLARWYQLGAFFPFFRNHSAKGTRDQEPWAFGEEVEEIARK 316
                         330       340
                  ....*....|....*....|
gi 2017363538 669 AIRERYGLLPYWYSLFYHAH 688
Cdd:cd06604   317 AIELRYRLLPYLYTLFYEAH 336
GH31_MGAM-like cd06600
maltase-glucoamylase (MGAM)-like; This family includes the following closely related glycosyl ...
353-676 7.44e-139

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: 413.81  E-value: 7.44e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 353 GTQAMPPLFSLGYHQCRWNYEDEQDVKAVDAGFDEHDIPYDAMWLDIEHTEGKRYFTWDKNRFPNPKRMQELLRSKKRKL 432
Cdd:cd06600     1 GRPALPPYWAFGYHQSRYSYYDQDKVVEVVDIMQEAGIPYDVMWLDIDYMDSYKDFTWDPVRFPEPKKFVDELHKNGQKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 433 VVISDPHIkidpdysvyvkakdqgffvknqegedfegvcwpglssyldftnpkVREWYSSLFAFPVYqgSTDILFLWNDM 512
Cdd:cd06600    81 VTIVDPGI---------------------------------------------TREWWAGLISEFLY--SQGIDGIWIDM 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 513 NEPSVFRgpeqtmqknaihhgnwehrELHNIYGFYHQMATAEGLIKRskGKERPFVLTRSFFAGSQKYGAVWTGDNTAEW 592
Cdd:cd06600   114 NEPSNFY-------------------KVHNLYGFYEAMATAEGLRTS--HNERPFILSRSTFAGSQKYAAHWTGDNTASW 172
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 593 SNLKISIPMLLTLSITGISFCGADIGGFIGNPETELLVRWYQAGAYQPFFRGHATMNTKRREPWLFGEEHTRLIREAIRE 672
Cdd:cd06600   173 DDLKLSIPLVLGLSLSGIPFVGADIGGFAGDTSEELLVRWYQLGAFYPFSRSHKATDTKDQEPVLFPEYYKESVREILEL 252

                  ....
gi 2017363538 673 RYGL 676
Cdd:cd06600   253 RYKL 256
YicI COG1501
Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];
215-818 5.16e-123

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


Pssm-ID: 441110 [Multi-domain]  Cd Length: 609  Bit Score: 385.67  E-value: 5.16e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 215 LDFSLHGFEHLYGIPQHAESHQLKntgdGDAYRLYNLDVYGYQIYDKMgiYGSVPYLLAHKlgrTIGIFWLNASETLVEI 294
Cdd:COG1501    54 VRKQLDLGEQIYGLGERFTTLHKR----GRIVVNWNLDHGGHKDNGNT--YAPIPFYVSSK---GYGVFVNSASYVTFDV 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 295 NTEpavEYTLTQMGPVAAKqkvrsrthvhwmsesgiIDVFLLTGPTPSDVFKQYSHLTGTQAMPPLFSLGYHQCRWNYED 374
Cdd:COG1501   125 GSA---YSDLVEFTVPGDS-----------------LEFYVIEGPSPEDVLEKYTELTGKPPLPPRWAFGYWQSRKSYYD 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 375 EQDVKAVDAGFDEHDIPYDAMWLDIeHTEGKRY---FTWDKNRFPNPKRMQELLRSKKRKLVVISDPHIkiDPDYSVYVK 451
Cdd:COG1501   185 QDQVLAFADEFRDRGFPLDVIHLDI-RWMDKYYwgdFEWDPRRFPDPKAMVKELHDRGVKLVLWINPYV--APDSAIFAE 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 452 AkdQGFFVKNQEGEDFEGVCWPGLSSYLDFTNPKVREW-YSSLFAFPVYQGSTDIlflWNDMNEpsvfRGPEQTmqknAI 530
Cdd:COG1501   262 G--MANFVKIASGTVFVGKMWPGTTGLLDFTRPDAREWfWAGLEKELLSIGVDGI---KLDMNE----GWPTDV----AT 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 531 HHGNWEHReLHNIYGFYHQMATAEGLikRSKGKERPFVLTRSFFAGSQKYGAVWTGDNTAEWSNLKISIPMLLTLSITGI 610
Cdd:COG1501   329 FPSNVPQQ-MRNLYGLLEAKATFEGF--RTSRNNRTFILTRSGFAGGQRYPVIWTGDNTSSWESLEDQLTQGLNLSLSGV 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 611 SFCGADIGGFIGNPETELLVRWYQAGAYQPFFRGHAtmNTKRREPWLFGEEHTRLIREAIRERYGLLPYWYSLFYHAHVA 690
Cdd:COG1501   406 PFWTPDIGGFFGSPSRELWIRWFQVGAFSPFARIHG--WASSTEPWFFDEEAKQIVKEYAQLRYRLLPYIYSLFAKASTD 483
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 691 SQPVMRPLWVEFPDELKTFDMEDEYMLGSALLVHPVTePKATTVDVFLPGSNevWYDYKTFAHWEGGCTVKIPVALDTIP 770
Cdd:COG1501   484 GTPVIRPLFLEFPDDPTTRFIDDQYMFGEYLLVAPIF-AGTESRLVYLPKGK--WYDFWTGELIEGGQWITVTAPLDRLP 560
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*...
gi 2017363538 771 VFQRGGSVIPIKTTvgkSTGWMTESSYGLRVALSTKGSSVGELYLDDG 818
Cdd:COG1501   561 LYVRDGSIIPLGPV---SLRPSMQKIDGIELRVYGSGETAYTLYDDDG 605
PLN02763 PLN02763
hydrolase, hydrolyzing O-glycosyl compounds
339-830 4.32e-119

hydrolase, hydrolyzing O-glycosyl compounds


Pssm-ID: 215408 [Multi-domain]  Cd Length: 978  Bit Score: 386.17  E-value: 4.32e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 339 PTPSDVFKQYSHLTGTQAMPPLFSLGYHQCRWNYEDEQDVKAVDAGFDEHDIPYDAMWLDIEHTEGKRYFTWDKNRFPNP 418
Cdd:PLN02763  164 PSPEALLTSLSHAIGTVFMPPKWALGYQQCRWSYESAKRVAEIARTFREKKIPCDVVWMDIDYMDGFRCFTFDKERFPDP 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 419 KRMQELLRSKKRKLVVISDPHIKIDPDYSVYVKAKDQGFFVKNQEGEDFEGVCWPGLSSYLDFTNPKVREWYSSLFAFPV 498
Cdd:PLN02763  244 KGLADDLHSIGFKAIWMLDPGIKAEEGYFVYDSGCENDVWIQTADGKPFVGEVWPGPCVFPDFTNKKTRSWWANLVKDFV 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 499 YQGSTDIlflWNDMNEPSVFRGPEQTMQKNAIHHGNWE------HRELHNIYGFYHQMATAEGLIKRSKGKeRPFVLTRS 572
Cdd:PLN02763  324 SNGVDGI---WNDMNEPAVFKTVTKTMPETNIHRGDEElggvqnHSHYHNVYGMLMARSTYEGMLLANKNK-RPFVLTRA 399
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 573 FFAGSQKYGAVWTGDNTAEWSNLKISIPMLLTLSITGISFCGADIGGFIGNPETELLVRWYQAGAYQPFFRGHATMNTKR 652
Cdd:PLN02763  400 GFIGSQRYAATWTGDNLSNWEHLHMSIPMVLQLGLSGQPLSGPDIGGFAGDATPKLFGRWMGVGAMFPFARGHSEQGTID 479
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 653 REPWLFGEEHTRLIREAIRERYGLLPYWYSLFYHAHVASQPVMRPLWVEFPDELKTFDMEDEYMLGSaLLVHPVTEPKAT 732
Cdd:PLN02763  480 HEPWSFGEECEEVCRLALKRRYRLLPHFYTLFYKAHTTGLPVMTPIFFADPKDPSLRKVENSFLLGP-LLISASTLPDQG 558
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 733 TVDVFLPGSNEVWYDYktfaHWEggctvkipvalDTIP----VFQRGGSVIPIKTTVGKSTGWMTESSYGLRVALSTKGS 808
Cdd:PLN02763  559 SDNLQHVLPKGIWQRF----DFD-----------DSHPdlplLYLQGGSIIPLGPPIQHVGEASLSDDLTLLIALDENGK 623
                         490       500
                  ....*....|....*....|..
gi 2017363538 809 SVGELYLDDGHSFQYLhQKQFL 830
Cdd:PLN02763  624 AEGVLYEDDGDGFGYT-KGDYL 644
GH31_MGAM_SI_GAA cd06602
maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase; This subgroup ...
353-688 1.30e-115

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: 357.98  E-value: 1.30e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 353 GTQAMPPLFSLGYHQCRWNYEDEQDVKAVDAGFDEHDIPYDAMWLDIEHTEGKRYFTWDKNRFPNPKRMQELLRSKKRKL 432
Cdd:cd06602     1 GRPAMPPYWSLGFHLCRWGYKNLDELKEVVERYRAAGIPLDVQWNDIDYMDRYRDFTLDPVNFPGLPAFVDDLHANGQHY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 433 VVISDPHIKIDP--DYSVYVKAKDQGFFVKNQEGEDFEGVCWPGLSSYLDFTNPKVREWYSSLFA-FpvyqgSTDILF-- 507
Cdd:cd06602    81 VPILDPGISANEsgGYPPYDRGLEMDVFIKNDDGSPYVGKVWPGYTVFPDFTNPNTQEWWTEEIKdF-----HDQVPFdg 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 508 LWNDMNEPSVF-----------RGPEQ---------------------TMQKNAIHHGNWEHRELHNIYGFYHQMATAEG 555
Cdd:cd06602   156 LWIDMNEPSNFctgscgnspnaPGCPDnklnnppyvpnnlgggslsdkTICMDAVHYDGGLHYDVHNLYGLSEAIATYKA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 556 LIKRSKGKeRPFVLTRSFFAGSQKYGAVWTGDNTAEWSNLKISIPMLLTLSITGISFCGADIGGFIGNPETELLVRWYQA 635
Cdd:cd06602   236 LKEIFPGK-RPFIISRSTFPGSGKYAGHWLGDNYSTWEDMRYSIPGMLEFNLFGIPMVGADICGFNGNTTEELCARWMQL 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2017363538 636 GAYQPFFRGHATMNTKRREPWLFGEEHTRLIREAIRERYGLLPYWYSLFYHAH 688
Cdd:cd06602   315 GAFYPFSRNHNDIGAIDQEPYVWGPSVADASRKALLIRYSLLPYLYTLFYRAH 367
GH31_transferase_CtsZ cd06598
CtsZ (cyclic tetrasaccharide-synthesizing enzyme Z)-like; CtsZ is a bacterial ...
353-685 3.58e-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: 3.58e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 353 GTQAMPPLFSLGYHQCRWNYEDEQDVKAVDAGFDEHDIPYDAMWLD------IEHTEGKRY--FTWDKNRFPNPKRMQEL 424
Cdd:cd06598     1 GRPPLPPKWAFGLWQSEFGYDNWAEVDELVDTLRQKDFPLDGVVLDlywfggIIASPDGPMgdLDWDRKAFPDPAKMIAD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 425 LRSKKRKLVVISDPHIKIDPDysVYVKAKDQGFFVKNQEGED----FEGvcWPGLSSYLDFTNPKVREWYSSLFAFPVYQ 500
Cdd:cd06598    81 LKQQGVGTILIEEPYVLKNSD--EYDELVKKGLLAKDKAGKPeptlFNF--WFGEGGMIDWSDPEARAWWHDRYKDLIDM 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 501 GstdILFLWNDMNEPSVFRGpeqtmqkNAIHHGNwEHRELHNIYGFYHQMATAEGLiKRSKGKERPFVLTRSFFAGSQKY 580
Cdd:cd06598   157 G---VAGWWTDLGEPEMHPP-------DMVHADG-DAADVHNIYNLLWAKSIYDGY-QRNFPEQRPFIMSRSGTAGSQRY 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 581 GAV-WTGDNTAEWSNLKISIPMLLTLSITGISFCGADIGGFIGN--PETELLVRWYQAGAYQPFFRGHaTMNTKRREPWL 657
Cdd:cd06598   225 GVIpWSGDIGRTWGGLASQINLQLHMSLSGIDYYGSDIGGFARGetLDPELYTRWFQYGAFDPPVRPH-GQNLCNPETAP 303
                         330       340
                  ....*....|....*....|....*...
gi 2017363538 658 FGEEHTRLIREAIRERYGLLPYWYSLFY 685
Cdd:cd06598   304 DREGTKAINRENIKLRYQLLPYYYSLAY 331
GH31 cd06589
glycosyl hydrolase family 31 (GH31); GH31 enzymes occur in prokaryotes, eukaryotes, and ...
353-670 1.03e-64

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: 218.38  E-value: 1.03e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 353 GTQAMPPLFSLGYHQCRWNYEDEQDVKAVDAGFDEHDIPYDAMWLDIEHTE---GKRYFTWDKNRFPNPKRMQELLRSKK 429
Cdd:cd06589     1 GRPPLLPKWALGFWNSRYGYYSEDEVEELVDRYREEGIPLDGFVLDSDWMDwggNWGGFTWNREKFPDPKGMIDELHDKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 430 RKLVVIsdphikidpdysvyvkakdqgffvknqegedfegvcwpglssyldfTNPKVREWYSSLFAFPVYQGSTDilFLW 509
Cdd:cd06589    81 VKLGLI----------------------------------------------VKPRLRDWWWENIKKLLLEQGVD--GWW 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 510 NDMNEPSVFRgpeqtmqkNAIHHGNWEHRELHNIYGFYHQMATAEGLIKrSKGKERPFVLTRSFFAGSQKYGAVWTGDNT 589
Cdd:cd06589   113 TDMGEPLPFD--------DATFHNGGKAQKIHNAYPLNMAEATYEGQKK-TFPNKRPFILSRSGYAGAQRYPAIWSGDNT 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 590 AEWSNLKISIPMLLTLSITGISFCGADIGGFIGNPET-ELLVRWYQAGAYQPFFRGHATMNTKRREPWLFGEEHTRLIRE 668
Cdd:cd06589   184 TTWDSLAFQIRAGLSASLSGVGYWGHDIGGFTGGDPDkELYTRWVQFGAFSPIFRLHGDNSPRDKEPWVYGEEALAIFRK 263

                  ..
gi 2017363538 669 AI 670
Cdd:cd06589   264 YL 265
GH31_glycosidase_Aec37 cd06599
E.coli Aec37-like; Glycosyl hydrolase family 31 (GH31) domain of a bacterial protein family ...
353-670 7.43e-64

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: 217.85  E-value: 7.43e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 353 GTQAMPPLFSLGYHQCRWNYEDEQDVKAVDAGF----DEHDIPYDAMWLDIEHT---EGKRY-FTWDKNRFPNPKRMQEL 424
Cdd:cd06599     1 GRPALPPRWSLGYLGSTMYYTEAPDAQEQILDFidtcREHDIPCDGFHLSSGYTsieDGKRYvFNWNKDKFPDPKAFFRK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 425 LRSKKRKLVvisdPHIK-----IDPDYSVYvkAKDQGFFVKNQEGEDFEGVCWPGLSSYLDFTNPKVREWYSSLFAFPVY 499
Cdd:cd06599    81 FHERGIRLV----ANIKpglltDHPHYDEL--AEKGAFIKDDDGGEPAVGRFWGGGGSYLDFTNPEGREWWKEGLKEQLL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 500 QGSTDILflWNDMNEPSVFRGpeqtmqkNAIHHGNWEHR---ELHNIYGFYHQMATAEGLIKRSKGKeRPFVLTRSFFAG 576
Cdd:cd06599   155 DYGIDSV--WNDNNEYEIWDD-------DAACCGFGKGGpisELRPIQPLLMARASREAQLEHAPNK-RPFVISRSGCAG 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 577 SQKYGAVWTGDNTAEWSNLKISIPMLLTLSITGISFCGADIGGFIGN-PETELLVRWYQAGAYQPFFRGHATmNTKR--R 653
Cdd:cd06599   225 IQRYAQTWSGDNRTSWKTLKYNIAMGLGMSLSGVANYGHDIGGFAGPaPEPELFVRWVQNGIFQPRFSIHSW-NTDNtvT 303
                         330
                  ....*....|....*..
gi 2017363538 654 EPWLFgEEHTRLIREAI 670
Cdd:cd06599   304 EPWMY-PEATPAIREAI 319
GH31_xylosidase_XylS cd06591
xylosidase XylS-like; XylS is a glycosyl hydrolase family 31 (GH31) alpha-xylosidase found in ...
353-673 2.08e-52

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: 186.22  E-value: 2.08e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 353 GTQAMPPLFSLGYHQCRWNYEDEQDVKAVDAGFDEHDIPYDAMWLDIEH-TEGKR-YFTWDKNRFPNPKRMQELLRSKKR 430
Cdd:cd06591     1 GKAPMLPKWALGFWQSKERYKTQEELLEVAREYRERGIPLDVIVQDWFYwTEQGWgDMKFDPERFPDPKGMVDELHKMNV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 431 KLVVISDPhiKIDPDYSVYVKAKDQGFFVKNQEGEDFEGvcwpGLSSYLDFTNPKVREWYsslfafpvYQGSTDILF--- 507
Cdd:cd06591    81 KLMISVWP--TFGPGSENYKELDEKGLLLRTNRGNGGFG----GGTAFYDATNPEAREIY--------WKQLKDNYFdkg 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 508 ---LWNDMNEPSVFRGPEQTMQKnAIHHGNWEhrELHNIYGFYHQMATAEGLIKRSKGKeRPFVLTRSFFAGSQKYGA-V 583
Cdd:cd06591   147 idaWWLDATEPELDPYDFDNYDG-RTALGPGA--EVGNAYPLMHAKGIYEGQRATGPDK-RVVILTRSAFAGQQRYGAaV 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 584 WTGDNTAEWSNLKISIPMLLTLSITGISFCGADIGGFIGNPET---------ELLVRWYQAGAYQPFFRGHATM-NTKRR 653
Cdd:cd06591   223 WSGDISSSWETLRRQIPAGLNFGASGIPYWTTDIGGFFGGDPEpgeddpayrELYVRWFQFGAFCPIFRSHGTRpPREPN 302
                         330       340
                  ....*....|....*....|
gi 2017363538 654 EPWLFGEEHTRLIREAIRER 673
Cdd:cd06591   303 EIWSYGEEAYDILVKYIKLR 322
GH31_xylosidase_YicI cd06593
alpha-xylosidase YicI-like; YicI alpha-xylosidase is a glycosyl hydrolase family 31 (GH31) ...
356-676 1.77e-51

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: 183.15  E-value: 1.77e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 356 AMPPLFSLGYHQCRWNYEDEQDVKAVDAGFDEHDIP-----YDAMWLDIEHTEGkryFTWDKNRFPNPKRMQELLRSKKR 430
Cdd:cd06593     4 PLPPAWSFGLWLSRSFYYSEEEVLEVADGMRERGIPcdvihLDCFWMKEDWWCD---FEWDEERFPDPEGMIARLKEKGF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 431 KLVVISDPHIKIDPDYsvYVKAKDQGFFVKNQEGEDFEGVC-WPGLSSYLDFTNPKVREWYSSLFAFPVYQGstdILFLW 509
Cdd:cd06593    81 KVCLWINPYISQDSPL--FKEAAEKGYLVKNPDGSPWHQWDgWQPGMGIIDFTNPEAVAWYKEKLKRLLDMG---VDVIK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 510 NDMNEpsvfRGPEqtmqkNAIHHGNWEHRELHNIYGFYHQMATAEGLikRSKGKERPFVLTRSFFAGSQKYGAVWTGDNT 589
Cdd:cd06593   156 TDFGE----RIPE-----DAVYYDGSDGRKMHNLYPLLYNKAVYEAT--KEVKGEEAVLWARSAWAGSQRYPVHWGGDSE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 590 AEWSNLKISIPMLLTLSITGISFCGADIGGFIGNPETELLVRWYQAGAYQPFFRGHATMntkRREPWLFGEEHTRLIREA 669
Cdd:cd06593   225 STFEGMAASLRGGLSLGLSGFGFWSHDIGGFEGTPSPELYKRWTQFGLLSSHSRLHGST---PREPWEYGEEALDVVRKF 301

                  ....*..
gi 2017363538 670 IRERYGL 676
Cdd:cd06593   302 AKLRYRL 308
GH31_lyase_GLase cd06601
alpha-1,4-glucan lyase; GLases (alpha-1,4-glucan lyases) are glycosyl hydrolase family 31 ...
353-685 2.31e-50

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: 181.07  E-value: 2.31e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 353 GTQAMPPLFSLGYHQCRWNYEDEQDVKAVDAGFDEHDIPYDAMWLDIEHTEGKRYFTWDKNRFPNPKRMQELLRSKKRKL 432
Cdd:cd06601     1 GRSRMKPRYVFGYHQGCYGYSSRESLEVVVQSYRDANIPLDGLHIDVDFQDNYRTFTTSKDKFPNPKEMFSNLHAQGFKC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 433 V-----VISDPHIKidpdysvyvkakdqgffvknqeGEDF-EGVCWPGLssYLDFTNPKVREW----YSSLFafpvyqgS 502
Cdd:cd06601    81 StnitpIITDPYIG----------------------GVNYgGGLGSPGF--YPDLGRPEVREWwgqqYKYLF-------D 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 503 TDILFLWNDMNEPSVFRG-----------PEQTMQKNAIHHGNWE---HRELHNIYGFYHQMATAEGLIK-RSKGKERPF 567
Cdd:cd06601   130 MGLEMVWQDMTTPAIAPHkingygdmktfPLRLLVTDDSVKNEHTykpAATLWNLYAYNLHKATYHGLNRlNARPNRRNF 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 568 VLTRSFFAGSQKYGAVWTGDNTAEWSNLKISIPMLLTLSITGISFCGADIGGFI----GNPET----ELLVRWYQAGAYQ 639
Cdd:cd06601   210 IIGRGGYAGAQRFAGLWTGDNASTWDFLQINIPQVLNLGLSGVPISGSDIGGFAsgsdENEGKwcdpELLIRWVQAGAFL 289
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2017363538 640 PFFRGH------ATMNTKRREPWLFGEEHTRLIREAIRERYGLLPYWYSLFY 685
Cdd:cd06601   290 PWFRNHydryikKKQQEKLYEPYYYYEPVLPICRKYVELRYRLMQVFYDAMY 341
PRK10658 PRK10658
putative alpha-glucosidase; Provisional
331-776 2.16e-49

putative alpha-glucosidase; Provisional


Pssm-ID: 236731 [Multi-domain]  Cd Length: 665  Bit Score: 186.26  E-value: 2.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 331 IDVFLLTGPTPSDVFKQYSHLTGTQAMPPLFSLGYhqcrW-------NYeDEQDV-KAVDaGFDEHDIP-----YDAMWL 397
Cdd:PRK10658  236 LEYFVIDGPTPKEVLDRYTALTGRPALPPAWSFGL----WlttsfttNY-DEATVnSFID-GMAERDLPlhvfhFDCFWM 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 398 diehtegKRY----FTWDKNRFPNPKRMQELLRSKKRKLVVISDPHIKidPDYSVYVKAKDQGFFVKNQEGEDFEGVCW- 472
Cdd:PRK10658  310 -------KEFqwcdFEWDPRTFPDPEGMLKRLKAKGLKICVWINPYIA--QKSPLFKEGKEKGYLLKRPDGSVWQWDKWq 380
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 473 PGLSSYlDFTNPKVREWYSSLFAFPVYQG------------STDILflWNDMNEPsvfrgpeQTMqknaihhgnwehrel 540
Cdd:PRK10658  381 PGMAIV-DFTNPDACKWYADKLKGLLDMGvdcfktdfgeriPTDVV--WFDGSDP-------QKM--------------- 435
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 541 HNIYGFYHQMATAEgLIKRSKGKERPFVLTRSFFAGSQKYGAVWTGDNTAEWSNLKISIPMLLTLSITGISFCGADIGGF 620
Cdd:PRK10658  436 HNYYTYLYNKTVFD-VLKETRGEGEAVLFARSATVGGQQFPVHWGGDCYSNYESMAESLRGGLSLGLSGFGFWSHDIGGF 514
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 621 IGNPETELLVRWYQAGAYQPFFRGHAtmNTKRREPWLFGEEHTRLIREAIRERYGLLPYWYSLFYHAHVASQPVMRPLWV 700
Cdd:PRK10658  515 ENTATADVYKRWCAFGLLSSHSRLHG--SKSYRVPWAYDEEAVDVVRFFTKLKCRLMPYLYREAAEAHERGTPMMRAMVL 592
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017363538 701 EFPDELKTFDMEDEYMLGSALLVHPVTEPkATTVDVFLPGSneVWYDYKTFAHWEGGCTVKIPVALDTIPVFQRGG 776
Cdd:PRK10658  593 EFPDDPACDYLDRQYMLGDSLLVAPVFSE-AGDVEYYLPEG--RWTHLLTGEEVEGGRWHKEQHDFLSLPLLVRPN 665
GH31_NET37 cd06592
glucosidase NET37; NET37 (also known as KIAA1161) is a human lamina-associated nuclear ...
357-740 4.44e-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: 169.32  E-value: 4.44e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 357 MPPLFSLG----YHQcrwnyeDEQDVKAVDAGFDEHDIPYDAMWLDiehtEG--KRY--FTWDKNRFPNPKRMQELLRSK 428
Cdd:cd06592     1 RPPIWSTWaeykYNI------NQEKVLEYAEEIRANGFPPSVIEID----DGwqTYYgdFEFDPEKFPDPKGMIDKLHEM 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 429 KRKLVVISDPHIkiDPDYSVYVKAKDQGFFVKNQEGEDFE-GVCWPGLSSYLDFTNPKVREWYSS-LFAFPVYQGST--- 503
Cdd:cd06592    71 GFRVTLWVHPFI--NPDSPNFRELRDKGYLVKEDSGGPPLiVKWWNGYGAVLDFTNPEARDWFKErLRELQEDYGIDgfk 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 504 ----DILFLWNDMNEPSVFRGPEQTMQKnaihhgnwehrelhniygfYHQMATAEGLIKrskgkErpfvlTRSFFAGSQK 579
Cdd:cd06592   149 fdagEASYLPADPATFPSGLNPNEYTTL-------------------YAELAAEFGLLN-----E-----VRSGWKSQGL 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 580 YGAVWTGDNTAEWSN---LKISIPMLLTLSITGISFCGAD-IGGF---IGNPETELLVRWYQAGAYQPFFRGHATmntkr 652
Cdd:cd06592   200 PLFVRMSDKDSHWGYwngLRSLIPTALTQGLLGYPFVLPDmIGGNaygNFPPDKELYIRWLQLSAFMPAMQFSVA----- 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 653 rePWL-FGEEHTRLIREAIRERYGLLPYWYSLFYHAHVASQPVMRPLWVEFPDELKTFDMEDEYMLGSALLVHPVTEPKA 731
Cdd:cd06592   275 --PWRnYDEEVVDIARKLAKLREKLLPYIYELAAEAVDTGEPIIRPLWWIAPEDEEALTIDDQFLLGDDILVAPVLEKGA 352

                  ....*....
gi 2017363538 732 TTVDVFLPG 740
Cdd:cd06592   353 RSRDVYLPK 361
GH31_u1 cd06595
glycosyl hydrolase family 31 (GH31); uncharacterized subgroup; This family represents an ...
352-679 1.67e-37

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: 142.73  E-value: 1.67e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 352 TGTQAMPPLFSLGYHQCR-WNYeDEQDVKAVDAGFDEHDIPYDAMWLDIE-HTEGKRY------FTWDKNRFPNPKRMQE 423
Cdd:cd06595     1 TGKPPLIPRYALGNWWSRyWAY-SDDDILDLVDNFKRNEIPLSVLVLDMDwHITDKKYkngwtgYTWNKELFPDPKGFLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 424 LLRSKKRKLVVISDPHIKIDPDYSVYVK-AKDQGffVKNQEGEDFEgvcwpglssyLDFTNPKVREWYSSLFAFPVYQGS 502
Cdd:cd06595    80 WLHERGLRVGLNLHPAEGIRPHEEAYAEfAKYLG--IDPAKIIPIP----------FDVTDPKFLDAYFKLLIHPLEKQG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 503 TDilFLWNDMNEPSVFRGPEQTMQkNAIHHgnwehrelhniygfYHQMATAEGlikrskGKERPFVLTRSFFAGSQKYGA 582
Cdd:cd06595   148 VD--FWWLDWQQGKDSPLAGLDPL-WWLNH--------------YHYLDSGRN------GKRRPLILSRWGGLGSHRYPI 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 583 VWTGDNTAEWSNLKISIPMLLTLSITGISFCGADIGGFIGNPET-ELLVRWYQAGAYQPFFRGHATMNTK-RREPWLFGE 660
Cdd:cd06595   205 GFSGDTEVSWETLAFQPYFTATAANVGYSWWSHDIGGHKGGIEDpELYLRWVQFGVFSPILRLHSDKGPYyKREPWLWDA 284
                         330
                  ....*....|....*....
gi 2017363538 661 EHTRLIREAIRERYGLLPY 679
Cdd:cd06595   285 KTFEIAKDYLRLRHRLIPY 303
PRK10426 PRK10426
alpha-glucosidase; Provisional
379-777 1.88e-37

alpha-glucosidase; Provisional


Pssm-ID: 236691 [Multi-domain]  Cd Length: 635  Bit Score: 149.76  E-value: 1.88e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 379 KAVDAGfdehdIPYDAMWldIEHTEGKRY----------FTWDKNRFPN-PKRMQELLRSKKRKLVVIsDPHIKIDPDys 447
Cdd:PRK10426  229 TMRNAG-----VKVNGIW--AQDWSGIRMtsfgkrlmwnWKWDSERYPQlDSRIKQLNEEGIQFLGYI-NPYLASDGD-- 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 448 VYVKAKDQGFFVKNQEGEDFE---GVCWPGLssyLDFTNPKVREWYSSLFAfpvyqgstdilflwNDMNEPSVfRG---- 520
Cdd:PRK10426  299 LCEEAAEKGYLAKDADGGDYLvefGEFYAGV---VDLTNPEAYEWFKEVIK--------------KNMIGLGC-SGwmad 360
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 521 -----PEQTMQKNAIhhgnwEHRELHNIYGFYHQMATAEGLikRSKGKE-RPFVLTRSFFAGSQKYGAV-WTGDNTAEWS 593
Cdd:PRK10426  361 fgeylPTDAYLHNGV-----SAEIMHNAWPALWAKCNYEAL--EETGKLgEILFFMRAGYTGSQKYSTLfWAGDQNVDWS 433
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 594 ---NLKISIPMLLTLSITGISFCGADIGGFI---GNPET-ELLVRWYQAGAYQPFFRGHATmNTKRREPWLFGEEHT-RL 665
Cdd:PRK10426  434 lddGLASVVPAALSLGMSGHGLHHSDIGGYTtlfGMKRTkELLLRWCEFSAFTPVMRTHEG-NRPGDNWQFDSDAETiAH 512
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 666 IREAIRERYGLLPYWYSLFYHAHVASQPVMRPLWVEFPDELKTFDMEDEYMLGSALLVHPVTEPKATTVDVFLPGSN--E 743
Cdd:PRK10426  513 FARMTRVFTTLKPYLKELVAEAAKTGLPVMRPLFLHYEDDAATYTLKYQYLLGRDLLVAPVHEEGRTDWTVYLPEDKwvH 592
                         410       420       430
                  ....*....|....*....|....*....|....
gi 2017363538 744 VWYDyKTFAhwegGCTVKIPVALDTIPVFQRGGS 777
Cdd:PRK10426  593 LWTG-EAFA----GGEITVEAPIGKPPVFYRAGS 621
GH31_CPE1046 cd06596
Clostridium CPE1046-like; CPE1046 is an uncharacterized Clostridium perfringens protein with a ...
553-750 9.26e-36

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: 138.63  E-value: 9.26e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 553 AEGLIKRSKgkERPFVLTRSFFAGSQKYGAVWTGDNTAEWSNLKISIPMLLTLSITGISFCGADIGG-FIGNPETEllVR 631
Cdd:cd06596   135 ADGIENNSN--ARPFIWTVDGWAGTQRYAVIWTGDQSGSWEYIRFHIPTYIGSGLSGQAYATSDVDGiFGGSPETY--TR 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 632 WYQAGAYQPFFRGHATMNTKRREPWLFGEEHTRLIREAIRERYGLLPYWYSLFYHAHVASQPVMRPLWVEFPDELKTFDM 711
Cdd:cd06596   211 DLQWKAFTPVLMNMSGWAANDKQPWVFGEPYTSINRKYLKLKMRLMPYIYTYAREASVTGLPMVRAMFLEYPNDPTAYGT 290
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2017363538 712 EDEY--MLGSALLVHPVTEPKATTVDV----FLPGsnEVWYDYKT 750
Cdd:cd06596   291 ATQYqfMWGPDFLVAPVYQNTAAGNDVrngiYLPA--GTWIDYWT 333
GH31_transferase_CtsY cd06597
CtsY (cyclic tetrasaccharide-synthesizing enzyme Y)-like; CtsY is a bacterial ...
369-656 2.12e-30

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: 122.81  E-value: 2.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 369 RWNyeDEQDVKAVDAGFDEHDIPYDAMWLDIEHTEGKRY-FTWDKNRFPNPKRMQELLRSKKRKLVVISDPHIKIDPDYS 447
Cdd:cd06597    19 EWN--SQAEVLELVEEYLAYDIPVGAVVIEAWSDEATFYiFNDATGKWPDPKGMIDSLHEQGIKVILWQTPVVKTDGTDH 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 448 V-----YVKAKDQGFFVKNQEGEDFEGVC-WPGLSSYLDFTNPKVREWYSS----LFAFPVYQGstdilflW-NDMNEPS 516
Cdd:cd06597    97 AqksndYAEAIAKGYYVKNGDGTPYIPEGwWFGGGSLIDFTNPEAVAWWHDqrdyLLDELGIDG-------FkTDGGEPY 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 517 VFRgpeqtmqkNAIHHGNWEHRELHNIYgfYHQMATAEGLIKRSKGKERpFVLTRSFFAGSQKYGAVWTGDNTAEWSNLK 596
Cdd:cd06597   170 WGE--------DLIFSDGKKGREMRNEY--PNLYYKAYFDYIREIGNDG-VLFSRAGDSGAQRYPIGWVGDQDSTFEGLQ 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363538 597 ISIPMLLTLSITGISFCGADIGGFIGN-PETELLVRWYQAGAYQPFFRGHatmNTKRREPW 656
Cdd:cd06597   239 SALKAGLSAAWSGYPFWGWDIGGFSGPlPTAELYLRWTQLAAFSPIMQNH---SEKNHRPW 296
GH31_N cd14752
N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to ...
213-353 2.90e-25

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: 101.49  E-value: 2.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 213 IGLDFSLHGFEHLYGIPQHAESHQLKntgdGDAYRLYNLDVYGYQiYDKMGIYGSVPYLLAHklgRTIGIFWLNASETLV 292
Cdd:cd14752    10 LRLSFKLPPDEHFYGLGERFGGLNKR----GKRYRLWNTDQGGYR-GSTDPLYGSIPFYLSS---KGYGVFLDNPSRTEF 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017363538 293 EINTEpaveytltqmgpvaakqkvrSRTHVHWMSESGIIDVFLLTGPTPSDVFKQYSHLTG 353
Cdd:cd14752    82 DFGSE--------------------DSDELTFSSEGGDLDYYFFAGPTPKEVIEQYTELTG 122
GH31_glucosidase_YihQ cd06594
alpha-glucosidase YihQ-like; YihQ is a bacterial alpha-glucosidase with a conserved glycosyl ...
378-645 2.60e-20

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: 93.03  E-value: 2.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 378 VKAVDAGFDEHDIPYDAMWL-D----IEHTEGKRYF---TWDKNRFPNPKRMQELLRSKKRKLVVISDPHIKIDPDYSVY 449
Cdd:cd06594    25 VLEVLEQLLAAGVPVAAVWLqDwvgtRKTSFGKRLWwnwEWDEELYPGWDELVKELKEQGIRVLGYINPFLANVGPLYSY 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 450 VKAKDQGFFVKNQEGEDFEGVCWPGLSSYLDFTNPKVREWYSSLfafpvyqgstdilflwndmnepsvfrgpeqtMQKNA 529
Cdd:cd06594   105 KEAEEKGYLVKNKTGEPYLVDFGEFDAGLVDLTNPEARRWFKEV-------------------------------IKENM 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363538 530 IHHG--NW-----EH-------------RELHNIYGFYHQMATAEGLIKRSKGKERPFvLTRSFFAGSQKYGAV-WTGDN 588
Cdd:cd06594   154 IDFGlsGWmadfgEYlpfdavlhsgedaALYHNRYPELWARLNREAVEEAGKEGEIVF-FMRSGYTGSPRYSTLfWAGDQ 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363538 589 TAEWSN---LKISIPMLLTLSITGISFCGADIGGF--IGNPET------ELLVRWYQAGAYQPFFRGH 645
Cdd:cd06594   233 NVDWSRddgLKSVIPGALSSGLSGFSLTHSDIGGYttLFNPLVgykrskELLMRWAEMAAFTPVMRTH 300
Gal_mutarotas_2 pfam13802
Galactose mutarotase-like; This family is found N-terminal to glycosyl-hydrolase domains, and ...
222-293 4.18e-17

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: 76.35  E-value: 4.18e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017363538 222 FEHLYGIPQHAESHQLKNTgdgdAYRLYNLDVYGYQIyDKMGIYGSVPYLLAHKLGRTIGIFWLNASETLVE 293
Cdd:pfam13802   1 DEHVYGLGERAGPLNKRGT----RYRLWNTDAFGYEL-DTDPLYKSIPFYISHNGGRGYGVFWDNPAETWFD 67
 
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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