Reviewed, UniProtKB/Swiss-Prot Q9LFA6 (BGAL2_ARATH)

Names and origin

Protein names

Recommended name:
    Beta-galactosidase 2
      Short name=Lactase 2
    EC=3.2.1.23

Gene names

Name:	BGAL2
Ordered Locus Names:	At3g52840
ORF Names:	F8J2.10

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	727 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Subcellular location	Secreted › extracellular space › apoplast Potential.
Tissue specificity	Ubiquitous, with higher expression levels in roots and siliques. Ref.5 Ref.6
Induction	By sugar starvation. Ref.7
Sequence similarities	Belongs to the glycosyl hydrolase 35 family.

Ontologies

Keywords
Cellular component	Apoplast Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	apoplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	beta-galactosidase activity Inferred from electronic annotation. Source: EC cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27	Potential
	Chain	28 – 727	700	Beta-galactosidase 2		PRO_5000065878
Sites
	Active site	185	1	Proton donor Potential
	Active site	254	1	Nucleophile Potential
Amino acid modifications
	Glycosylation	255	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	12	1	I → F in AAN60229. Ref.4
	Sequence conflict	220	1	S → C in CAB64738. Ref.1
	Sequence conflict	220	1	S → C in AAK32914. Ref.3
	Sequence conflict	220	1	S → C in AAN18080. Ref.3
	Sequence conflict	220	1	S → C in AAN60229. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9LFA6-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 21FF5473F877F5C5	FASTA	727	81,999
	10 20 30 40 50 60 MSMHFRNKAW IILAILCFSS LIHSTEAVVT YDHKALIING QRRILISGSI HYPRSTPEMW 70 80 90 100 110 120 PDLIKKAKEG GLDVIQTYVF WNGHEPSPGN YYFQDRYDLV KFTKLVHQAG LYLDLRIGPY 130 140 150 160 170 180 VCAEWNFGGF PVWLKYVPGM VFRTDNEPFK IAMQKFTKKI VDMMKEEKLF ETQGGPIILS 190 200 210 220 230 240 QIENEYGPMQ WEMGAAGKAY SKWTAEMALG LSTGVPWIMS KQEDAPYPII DTCNGFYCEG 250 260 270 280 290 300 FKPNSDNKPK LWTENWTGWF TEFGGAIPNR PVEDIAFSVA RFIQNGGSFM NYYMYYGGTN 310 320 330 340 350 360 FDRTAGVFIA TSYDYDAPID EYGLLREPKY SHLKELHKVI KLCEPALVSV DPTITSLGDK 370 380 390 400 410 420 QEIHVFKSKT SCAAFLSNYD TSSAARVMFR GFPYDLPPWS VSILPDCKTE YYNTAKIRAP 430 440 450 460 470 480 TILMKMIPTS TKFSWESYNE GSPSSNEAGT FVKDGLVEQI SMTRDKTDYF WYFTDITIGS 490 500 510 520 530 540 DESFLKTGDN PLLTIFSAGH ALHVFVNGLL AGTSYGALSN SKLTFSQNIK LSVGINKLAL 550 560 570 580 590 600 LSTAVGLPNA GVHYETWNTG ILGPVTLKGV NSGTWDMSKW KWSYKIGLRG EAMSLHTLAG 610 620 630 640 650 660 SSAVKWWIKG FVVKKQPLTW YKSSFDTPRG NEPLALDMNT MGKGQVWVNG HNIGRHWPAY 670 680 690 700 710 720 TARGNCGRCN YAGIYNEKKC LSHCGEPSQR WYHVPRSWLK PFGNLLVIFE EWGGDPSGIS LVKRTAK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The beta-galactosidases are encoding by a multigene family in Arabidopsis thaliana." Gy I., Kreis M., Lecharny A. Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves and guard cells." Stracke R., Palme K. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-569.
[5]	"Apoplastic glycosidases active against xyloglucan oligosaccharides of Arabidopsis thaliana." Iglesias N., Abelenda J.A., Rodino M., Sampedro J., Revilla G., Zarra I. Plant Cell Physiol. 47:55-63(2006) [PubMed: 16267099] [Abstract] Cited for: TISSUE SPECIFICITY.
[6]	"Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase family 35." Ahn Y.O., Zheng M., Bevan D.R., Esen A., Shiu S.-H., Benson J., Peng H.-P., Miller J.T., Cheng C.-L., Poulton J.E., Shih M.-C. Phytochemistry 68:1510-1520(2007) [PubMed: 17466346] [Abstract] Cited for: TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
[7]	"Glycosyl hydrolases of cell wall are induced by sugar starvation in Arabidopsis." Lee E.-J., Matsumura Y., Soga K., Hoson T., Koizumi N. Plant Cell Physiol. 48:405-413(2007) [PubMed: 17234672] [Abstract] Cited for: INDUCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ270298 mRNA. Translation: CAB64738.1. AL132969 Genomic DNA. Translation: CAB86888.1. AF367327 mRNA. Translation: AAK32914.1. BT000511 mRNA. Translation: AAN18080.1. AF083670 mRNA. Translation: AAN60229.1.
IPI	IPI00537018.
PIR	T47541.
RefSeq	NP_190852.2.
UniGene	At.702
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9LFA6.
Protein family/group databases
CAZy	GH35. Glycoside Hydrolase Family 35.
Proteomic databases
PRIDE	Q9LFA6.
Genome annotation databases
GeneID	824450.
GenomeReviews	Gene locus AT3G52840 in contig BA000014_GR.
NMPDR	fig|3702.1.peg.16556.
Organism-specific databases
GeneFarm	490. 90.
TAIR	At3g52840.
Enzyme and pathway databases
BRENDA	3.2.1.23. 302.
Gene expression databases
Genevestigator	Q9LFA6.
Family and domain databases
InterPro	IPR019801. Glyco_hydro_35_CS. IPR013781. Glyco_hydro_sg_catalytic. IPR001944. Glycoside_Hdrlase_35. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHER	PTHR23421. Glyco_hydro_35. 1 hit.
Pfam	PF01301. Glyco_hydro_35. 1 hit. [Graphical view]
PRINTS	PR00742. GLHYDRLASE35.
PROSITE	PS01182. GLYCOSYL_HYDROL_F35. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BGAL2_ARATH

Accession

Primary (citable) accession number: Q9LFA6
Secondary accession number(s): Q8H7H7, Q9SCW0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	October 1, 2000
Last modified:	October 13, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)