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Basic Information | |
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Species | Thellungiella halophila |
Cazyme ID | Thhalv10019989m |
Family | GH31 |
Protein Properties | Length: 992 Molecular Weight: 111242 Isoelectric Point: 5.7973 |
Chromosome | Chromosome/Scaffold: 13 Start: 88837 End: 96955 |
Description | heteroglycan glucosidase 1 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH31 | 176 | 587 | 0 |
SSPTAVLESLSHAVGTVFMPPKWALGYHQCRWSYMSDKRVAEIAETFRDKKIPSDVIWMDIDYMDGFRCFTFDKERFPDPSALAKHLHNNGFKAIWMLDP GIKKEEGYYVYDGGSKNDVWIRRKDGKPFTGEVWPGPCVFPDYTNSEARSWWANLVKDFISNGVDGIWNDMNEPAIFKVVTKTMPENNIHRGDDELGGVQ NHSHYHNVYGMLMARSTYEGMELADKNKRPFVLTRAGFIGSQRYAATWTGDNLSTWEHLHMSISMVLQLGLSGQPLSGPDIGGFAGNATPRLFGRWMGVG AMFPFCRGHSEAGTDDHEPWSFGEECEEVCRAALKRRYQLLPHFYTLFYIAHTTGAPVAAPIFFADPKDSRLRTVENAFLLGSLLIHASTFSNQGSHELQ HILPRGIWLRFD |
Full Sequence |
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Protein Sequence Length: 992 Download |
MTLRGDDSET IEMAPTGMIF EPILEQGVFR FDCSVEHRRS AFPSVSFKNS KDREVPIISH 60 NVPAYTPTCA CLQEKQVVTF EFSPGTSFYG TGEVGGQLER TGKRVFTWNT DAWGYGSGTT 120 SLYQSHPWVL AVLPSGETLG VLADTTRKCE IDLRKEGIIR IIAPTSYPII TFGPFSSPTA 180 VLESLSHAVG TVFMPPKWAL GYHQCRWSYM SDKRVAEIAE TFRDKKIPSD VIWMDIDYMD 240 GFRCFTFDKE RFPDPSALAK HLHNNGFKAI WMLDPGIKKE EGYYVYDGGS KNDVWIRRKD 300 GKPFTGEVWP GPCVFPDYTN SEARSWWANL VKDFISNGVD GIWNDMNEPA IFKVVTKTMP 360 ENNIHRGDDE LGGVQNHSHY HNVYGMLMAR STYEGMELAD KNKRPFVLTR AGFIGSQRYA 420 ATWTGDNLST WEHLHMSISM VLQLGLSGQP LSGPDIGGFA GNATPRLFGR WMGVGAMFPF 480 CRGHSEAGTD DHEPWSFGEE CEEVCRAALK RRYQLLPHFY TLFYIAHTTG APVAAPIFFA 540 DPKDSRLRTV ENAFLLGSLL IHASTFSNQG SHELQHILPR GIWLRFDFED SHPDLPTLYL 600 QGGSIISVGP PHLHVGESSL SDDLTLLVSL DENGKALGLL FEDDGDGYGY TKGRYLITHY 660 IAERHSSIVT VKVLKTEGEW QRPKRCIHVQ LLLGGGAMLD AWGMDGEIIQ IKVPSESEVS 720 ELISTSNERF KLHMENTKLI PEKEVLHGQK GMELSRVPVE LNSGNWKLNI VPWIGGRILS 780 MTHVPSGVQW LHSRIDINGY EEYSGTEYRS AGCTEEYKVI ERDLEHAGEE ESLILEGDVG 840 GGLVLQRKIA IPKDNPRVFQ IASSIEARSV GAGSGGFSRL VCLRVHPTFC LMHPIESFVS 900 FTSVDGTKHE VWPESGEQLY EGNNLPHGEW MLVDKSLNLR LVNRFEVSQV FKCIVHWDCG 960 TVNLELWSED RPVSKESPLK IEHEYEVTSF P* 1020 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd06603 | GH31_GANC_GANAB_alpha | 1.0e-133 | 190 | 530 | 345 | + This family 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. | ||
COG1501 | COG1501 | 6.0e-138 | 73 | 679 | 629 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] | ||
pfam01055 | Glyco_hydro_31 | 2.0e-167 | 170 | 606 | 455 | + Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases. | ||
PLN02763 | PLN02763 | 0 | 13 | 990 | 978 | + hydrolase, hydrolyzing O-glycosyl compounds | ||
cd06604 | GH31_glucosidase_II_MalA | 0 | 190 | 530 | 342 | + 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 family also includes the MalA alpha-glucosidase from Sulfolobus sulfataricus 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. |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
DDBJ | BAB02784.1 | 0 | 13 | 991 | 1 | 959 | alpha glucosidase-like protein [Arabidopsis thaliana] |
EMBL | CBI37476.1 | 0 | 18 | 991 | 84 | 1057 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_566736.1 | 0 | 1 | 991 | 1 | 991 | HGL1 (heteroglycan glucosidase 1); hydrolase, hydrolyzing O-glycosyl compounds [Arabidopsis thaliana] |
RefSeq | XP_002263148.1 | 0 | 18 | 991 | 1 | 973 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002519886.1 | 0 | 10 | 987 | 10 | 987 | neutral alpha-glucosidase ab precursor, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3w38_A | 0 | 88 | 671 | 207 | 826 | A Chain A, Family Gh5 Endo-Beta-Mannanase From Lycopersicon Esculentum (Tomato) |
PDB | 3w37_A | 0 | 88 | 671 | 207 | 826 | A Chain A, Family Gh5 Endo-Beta-Mannanase From Lycopersicon Esculentum (Tomato) |
PDB | 2g3n_F | 0 | 90 | 621 | 66 | 624 | A Chain A, Family Gh5 Endo-Beta-Mannanase From Lycopersicon Esculentum (Tomato) |
PDB | 2g3n_E | 0 | 90 | 621 | 66 | 624 | A Chain A, Family Gh5 Endo-Beta-Mannanase From Lycopersicon Esculentum (Tomato) |
PDB | 2g3n_D | 0 | 90 | 621 | 66 | 624 | A Chain A, Family Gh5 Endo-Beta-Mannanase From Lycopersicon Esculentum (Tomato) |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO779383 | 649 | 345 | 987 | 0 |
EG431953 | 280 | 324 | 603 | 0 |
ES901722 | 269 | 273 | 541 | 0 |
EG431954 | 283 | 367 | 649 | 0 |
HO783906 | 313 | 227 | 539 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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