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Beta-galactosidase (EC 3.2.1.23)

 F4JUE3_ARATH            Unreviewed;      1052 AA.
F4JUE3;
28-JUN-2011, integrated into UniProtKB/TrEMBL.
28-JUN-2011, sequence version 1.
23-MAY-2018, entry version 62.
RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
Name=BGAL14 {ECO:0000313|EMBL:AEE86952.1};
Synonyms=beta-galactosidase 14 {ECO:0000313|EMBL:AEE86952.1};
OrderedLocusNames=At4g38590 {ECO:0000313|Araport:AT4G38590,
ECO:0000313|EMBL:AEE86952.1};
ORFNames=F20M13.150 {ECO:0000313|EMBL:AEE86952.1},
F20M13_150 {ECO:0000313|EMBL:AEE86952.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702 {ECO:0000313|EMBL:AEE86952.1, ECO:0000313|Proteomes:UP000006548};
[1] {ECO:0000313|EMBL:AEE86952.1, ECO:0000313|Proteomes:UP000006548}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
PubMed=10617198; DOI=10.1038/47134;
EU;
CSHL and WU Arabidopsis Sequencing Project;
Mayer K., Schuller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
Dusterhoft A., Stiekema W., Entian K.D., Terryn N., Harris B.,
Ansorge W., Brandt P., Grivell L., Rieger M., Weichselgartner M.,
de Simone V., Obermaier B., Mache R., Muller M., Kreis M., Delseny M.,
Puigdomenech P., Watson M., Schmidtheini T., Reichert B.,
Portatelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P.,
Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.A.,
McCullagh B., Bilham L., Robben J., Van der Schueren J.,
Grymonprez B., Chuang Y.J., Vandenbussche F., Braeken M., Weltjens I.,
Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G.,
Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S.,
van Staveren M., Dirske W., Mooijman P., Klein Lankhorst R., Rose M.,
Hauf J., Kotter P., Berneiser S., Hempel S., Feldpausch M.,
Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J.,
Villarroel R., De Clercq R., Van Montagu M., Rogers J., Cronin A.,
Quail M., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M.,
Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M.,
Benes V., Rechmann S., Borkova D., Blocker H., Scharfe M., Grimm M.,
Lohnert T.H., Dose S., de Haan M., Maarse A., Schafer M.,
Muller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K.,
Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R.,
Piravandi E., Massenet O., Quigley F., Clabauld G., Mundlein A.,
Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Montfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.W., Stocker S., Zaccaria P.,
Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L.,
Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sehkon M.,
Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T.,
Kalicki J., Graves T., Harmon G., Edwards J., Latreille P.,
Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P.,
Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J.,
Fulton L., Mardis E., Dante M., Pepin K., Hillier L., Nelson J.,
Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J.,
Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
O'Shaughnessy A., Rodriguez M., Hoffmann J., Till S., Granat S.,
Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E.,
Marra M., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[2] {ECO:0000313|Proteomes:UP000006548}
GENOME REANNOTATION.
STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
galactose residues in beta-D-galactosides.
{ECO:0000256|RuleBase:RU000675, ECO:0000256|SAAS:SAAS00108875}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
{ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
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EMBL; CP002687; AEE86952.1; -; Genomic_DNA.
RefSeq; NP_001154292.1; NM_001160820.1.
UniGene; At.70242; -.
ProteinModelPortal; F4JUE3; -.
SMR; F4JUE3; -.
PRIDE; F4JUE3; -.
EnsemblPlants; AT4G38590.2; AT4G38590.2; AT4G38590.
GeneID; 830016; -.
Gramene; AT4G38590.2; AT4G38590.2; AT4G38590.
Araport; AT4G38590; -.
TAIR; locus:2121214; AT4G38590.
eggNOG; KOG0495; Eukaryota.
eggNOG; KOG0496; Eukaryota.
eggNOG; COG1874; LUCA.
OMA; ICSAFAT; -.
OrthoDB; EOG093601FL; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; F4JUE3; differential.
GO; GO:0005634; C:nucleus; IEA:InterPro.
GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
Gene3D; 2.60.120.260; -; 1.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR031330; Gly_Hdrlase_35_cat.
InterPro; IPR019801; Glyco_hydro_35_CS.
InterPro; IPR001944; Glycoside_Hdrlase_35.
InterPro; IPR017853; Glycoside_hydrolase_SF.
InterPro; IPR000922; Lectin_gal-bd_dom.
InterPro; IPR010491; PRP1_N.
PANTHER; PTHR23421; PTHR23421; 1.
Pfam; PF02140; Gal_Lectin; 1.
Pfam; PF01301; Glyco_hydro_35; 1.
Pfam; PF06424; PRP1_N; 1.
PRINTS; PR00742; GLHYDRLASE35.
SUPFAM; SSF49785; SSF49785; 2.
SUPFAM; SSF51445; SSF51445; 1.
PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PROSITE; PS50228; SUEL_LECTIN; 1.
3: Inferred from homology;
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000006548};
Glycosidase {ECO:0000256|RuleBase:RU000675,
ECO:0000256|SAAS:SAAS00108888};
Hydrolase {ECO:0000256|RuleBase:RU000675,
ECO:0000256|SAAS:SAAS00108888};
Reference proteome {ECO:0000313|Proteomes:UP000006548};
Signal {ECO:0000256|SAM:SignalP}.
SIGNAL 1 23 {ECO:0000256|SAM:SignalP}.
CHAIN 24 1052 Beta-galactosidase.
{ECO:0000256|SAM:SignalP}.
/FTId=PRO_5003315527.
DOMAIN 746 832 SUEL-type lectin.
{ECO:0000259|PROSITE:PS50228}.
COILED 833 854 {ECO:0000256|SAM:Coils}.
SEQUENCE 1052 AA; 119544 MW; 5A97922E99FAE447 CRC64;
MKSRTRYLIA ILLVISLCSK ASSHDDEKKK KGVTYDGSER NFIDHKWKKR ASFLWFCSLP
SKHTSRKHMW PSIIDKARIG GLNTIQTYVF WNVHEPEQGK YDFKGRFDLV KFIKLIHEKG
LYVTLRLGPF IQAEWNHGGL PYWLREVPDV YFRTNNEPFK EHTERYVRKI LGMMKEEKLF
ASQGGPIILG QIENEYNAVQ LAYKENGEKY IKWAANLVES MNLGIPWVMC KQNDAPGNLI
NACNGRHCGD TFPGPNRHDK PSLWTENWTT QFRVFGDPPT QRTVEDIAFS VARYFSKNGS
HVNYYMYHGG TNFGRTSAHF VTTRYYDDAP LDEFGLEKAP KYGHLKHVHR ALRLCKKALF
WGQLRAQTLG PDTEVRYYEQ PGTKVCAAFL SNNNTRDTNT IKFKGQDYVL PSRSISILPD
CKTVVYNTAQ IVAQHSWRDF VKSEKTSKGL KFEMFSENIP SLLDGDSLIP GELYYLTKDK
TDYACVKIDE DDFPDQKGLK TILRVASLGH ALIVYVNGEY AGKAHGRHEM KSFEFAKPVN
FKTGDNRISI LGVLTGLPDS GSYMEHRFAG PRAISIIGLK SGTRDLTENN EWGHLAGLEG
EKKEVYTEEG SKKVKWEKDG KRKPLTWYKT YFETPEGVNA VAIRMKAMGK GLIWVNGIGV
GRYWMSFLSP LGEPTQTEYH IPRSFMKGEK KKNMLVILEE EPGVKLESID FVLVNRDTIC
SNVGEDYPVS VKSWKREGPK IVSRSKDMRL KAVMRCPPEK QMVEVQFASF GDPTGTCGNF
TMGKCSASKS KEVVEKECLG RNYCSIVVAR ETFGDKGCPE IVKTLAVQVK CEKKEGKQDE
KKKKEDKDEE EEDDEDDDEE EEEEDKENKD TKDMENKNQD ILDSDSALVS DLGFGPFSTV
VVNVPLIGGA APPQPRFNLM PPSNYVAGLG RGAAGFTTRS DIGPARANGD GNADVNHKFD
DFEGHDAGLF ANAESDDQDK EADAIWDAID RRMDSRRKDR REAKLKQEIE NYRASNPKVS
GQFVDLTRKL HTLSEDEWDS IPEIGNYSHR LY


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