[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Limbras 10; TISSUE=Spear; DOI=10.1104/pp.108.1.419; PubMed=7784512 [NCBI, ExPASy, EBI, Israel, Japan] King G.A., Davies K.M.; "Cloning of a harvest-induced beta-galactosidase from tips of harvested asparagus spears."; Plant Physiol. 108:419-420(1995).

Comments

CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast (Potential).
SIMILARITY: Belongs to the glycosyl hydrolase 35 family [view classification].
SIMILARITY: Contains 1 SUEL-type lectin domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X77319; CAA54525.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S41889; S41889.

3D structure databases

ModBase

P45582.

Protein family/group databases

CAZy

GH35; Glycoside Hydrolase Family 35.

Enzyme and pathway databases

BRENDA

3.2.1.23; 129.

Ontologies

GO:0048046;	Cellular component: apoplast (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005615;	Cellular component: extracellular space (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004565;	Molecular function: beta-galactosidase activity (inferred from electronic annotation from EC).
GO:0043169;	Molecular function: cation binding (inferred from electronic annotation from InterPro).
GO:0005529;	Molecular function: sugar binding (inferred from electronic annotation from InterPro).
GO:0005975;	Biological process: carbohydrate metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR019801; Glyco_hydro_35_CS.
IPR013781; Glyco_hydro_sg_catalytic.
IPR001944; Glycoside_Hdrlase_35.
IPR000922; Lectin_gal_bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.80; Glyco_hydro_cat; 1.

PANTHER

PTHR23421; Glyco_hydro_35; 1.

Pfam

PF02140; Gal_Lectin; 1.
PF01301; Glyco_hydro_35; 1.
Pfam graphical view of domain structure.

PRINTS

PR00742; GLHYDRLASE35.

ProDom

PD005612; Gal_lectin; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS01182; GLYCOSYL_HYDROL_F35; 1.
PS50228; SUEL_LECTIN; 1.
PROSITE graphical view of domain structure (profiles).

Other

ProtoNet

P45582.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Apoplast; Glycosidase; Hydrolase; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 25`	`25`	`Potential.`
`CHAIN`	`26 832`	`807`	`Beta-galactosidase.`	`PRO_0000012193`
`DOMAIN`	`741 832`	`92`	`SUEL-type lectin.`
`ACT_SITE`	`183 183`		`Proton donor (Potential).`
`ACT_SITE`	`252 252`		`Nucleophile (Potential).`

Sequence information

Length: 832 AA [This is the length of the unprocessed precursor]

Molecular weight: 92214 Da [This is the MW of the unprocessed precursor]

CRC64: 94ABDC61EC4164AE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALKLVLMLM VALLAAVWSP PAVTASVTYD HKSVIINGQR RILISGSIHY PRSTPEMWPD 

        70         80         90        100        110        120 
LIQKAKDGGL DVIQTYVFWN GHEPSPGQYY FGGRYDLVRF LKLVKQAGLY AHLRIGPYVC 

       130        140        150        160        170        180 
AEWNFGGFPV WLKYVPGIHF RTDNGPFKAA MGKFTEKIVS MMKAEGLYET QGGPIILSQI 

       190        200        210        220        230        240 
ENEYGPVEYY DGAAGKSYTN WAAKMAVGLN TGVPWVMCKQ DDAPDPVINT CNGFYCDYFS 

       250        260        270        280        290        300 
PNKDNKPKMW TEAWTGWFTG FGGAVPQRPA EDMAFAVARF IQKGGSFINY YMYHGGTNFG 

       310        320        330        340        350        360 
RTAGGPFIST SYDYDAPIDE YGLLRQPKWG HLRDLHKAIK LCEPALVSGE PTITSLGQNQ 

       370        380        390        400        410        420 
ESYVYRSKSS CAAFLANFNS RYYATVTFNG MHYNLPPWSV SILPDCKTTV FNTARVGAQT 

       430        440        450        460        470        480 
TTMKMQYLGG FSWKAYTEDT DALNDNTFTK DGLVEQLSTT WDRSDYLWYT TYVDIAKNEE 

       490        500        510        520        530        540 
FLKTGKYPYL TVMSAGHAVH VFINGQLSGT AYGSLDNPKL TYSGSAKLWA GSNKISILSV 

       550        560        570        580        590        600 
SVGLPNVGNH FETWNTGVLG PVTLTGLNEG KRDLSLQKWT YQIGLHGETL SLHSLTGSSN 

       610        620        630        640        650        660 
VEWGEASQKQ PLTWYKTFFN APPGNEPLAL DMNTMGKGQI WINGQSIGRY WPAYKASGSC 

       670        680        690        700        710        720 
GSCDYRGTYN EKKCLSNCGE ASQRWYHVPR SWLIPTGNFL VVLEEWGGDP TGISMVKRSV 

       730        740        750        760        770        780 
ASVCAEVEEL QPTMDNWRTK AYGRPKVHLS CDPGQKMSKI KFASFGTPQG TCGSFSEGSC 

       790        800        810        820        830 
HAHKSYDAFE QEGLMQNCVG QEFCSVNVAP EVFGGDPCPG TMKKLAVEAI CE

P45582 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools