| Basic Information | |
|---|---|
| Species | Arabidopsis thaliana |
| Cazyme ID | AT3G52840.1 |
| Family | GH35 |
| Protein Properties | Length: 728 Molecular Weight: 82014.9 Isoelectric Point: 8.5552 |
| Chromosome | Chromosome/Scaffold: 3 Start: 19581113 End: 19586299 |
| Description | beta-galactosidase, putative, expressed |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH35 | 36 | 338 | 0 |
| LIINGQRRILISGSIHYPRSTPEMWPDLIKKAKEGGLDVIQTYVFWNGHEPSPGNYYFQDRYDLVKFTKLVHQAGLYLDLRIGPYVCAEWNFGGFPVWLK YVPGMVFRTDNEPFKIAMQKFTKKIVDMMKEEKLFETQGGPIILSQIENEYGPMQWEMGAAGKAYSKWTAEMALGLSTGVPWIMCKQEDAPYPIIDTCNG FYCEGFKPNSDNKPKLWTENWTGWFTEFGGAIPNRPVEDIAFSVARFIQNGGSFMNYYMYYGGTNFDRTAGVFIATSYDYDAPIDEYGLLREPKYSHLKE LHK | |||
| Full Sequence |
|---|
| Protein Sequence Length: 728 Download |
| MSMHFRNKAW IILAILCFSS LIHSTEAVVT YDHKALIING QRRILISGSI HYPRSTPEMW 60 PDLIKKAKEG GLDVIQTYVF WNGHEPSPGN YYFQDRYDLV KFTKLVHQAG LYLDLRIGPY 120 VCAEWNFGGF PVWLKYVPGM VFRTDNEPFK IAMQKFTKKI VDMMKEEKLF ETQGGPIILS 180 QIENEYGPMQ WEMGAAGKAY SKWTAEMALG LSTGVPWIMC KQEDAPYPII DTCNGFYCEG 240 FKPNSDNKPK LWTENWTGWF TEFGGAIPNR PVEDIAFSVA RFIQNGGSFM NYYMYYGGTN 300 FDRTAGVFIA TSYDYDAPID EYGLLREPKY SHLKELHKVI KLCEPALVSV DPTITSLGDK 360 QEIHVFKSKT SCAAFLSNYD TSSAARVMFR GFPYDLPPWS VSILPDCKTE YYNTAKIRAP 420 TILMKMIPTS TKFSWESYNE GSPSSNEAGT FVKDGLVEQI SMTRDKTDYF WYFTDITIGS 480 DESFLKTGDN PLLTIFSAGH ALHVFVNGLL AGTSYGALSN SKLTFSQNIK LSVGINKLAL 540 LSTAVGLPNA GVHYETWNTG ILGPVTLKGV NSGTWDMSKW KWSYKIGLRG EAMSLHTLAG 600 SSAVKWWIKG FVVKKQPLTW YKSSFDTPRG NEPLALDMNT MGKGQVWVNG HNIGRHWPAY 660 TARGNCGRCN YAGIYNEKKC LSHCGEPSQR WYHVPRSWLK PFGNLLVIFE EWGGDPSGIS 720 LVKRTAK* 780 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam02449 | Glyco_hydro_42 | 0.0003 | 51 | 187 | 152 | + Beta-galactosidase. This group of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. The enzyme catalyzes the hydrolysis of terminal, non-reducing terminal beta-D-galactosidase residues. | ||
| COG1874 | LacA | 1.0e-21 | 29 | 331 | 352 | + Beta-galactosidase [Carbohydrate transport and metabolism] | ||
| pfam01301 | Glyco_hydro_35 | 6.0e-155 | 35 | 340 | 322 | + Glycosyl hydrolases family 35. | ||
| PLN03059 | PLN03059 | 0 | 11 | 725 | 716 | + beta-galactosidase; Provisional | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0003824 | catalytic activity |
| GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| GO:0004565 | beta-galactosidase activity |
| GO:0005975 | carbohydrate metabolic process |
| GO:0005990 | lactose catabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAK96780.1 | 0 | 1 | 725 | 1 | 724 | beta-galactosidase [Arabidopsis thaliana] |
| EMBL | CAB39679.1 | 0 | 1 | 727 | 1 | 729 | putative beta-galactosidase [Arabidopsis thaliana] |
| RefSeq | NP_190852.2 | 0 | 1 | 727 | 1 | 727 | BGAL2 (beta-galactosidase 2); beta-galactosidase/ catalytic/ cation binding [Arabidopsis thaliana] |
| RefSeq | NP_849553.1 | 0 | 1 | 727 | 1 | 728 | BGAL12 (beta-galactosidase 12); beta-galactosidase/ catalytic/ cation binding [Arabidopsis thaliana] |
| Swiss-Prot | Q9LFA6 | 0 | 1 | 727 | 1 | 727 | BGAL2_ARATH RecName: Full=Beta-galactosidase 2; Short=Lactase 2; Flags: Precursor |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3thd_D | 1.99993e-41 | 29 | 344 | 11 | 339 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
| PDB | 3thd_C | 1.99993e-41 | 29 | 344 | 11 | 339 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
| PDB | 3thd_B | 1.99993e-41 | 29 | 344 | 11 | 339 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| lactose degradation III | BETAGALACTOSID-RXN | EC-3.2.1.23 | β-galactosidase |
