ID A0A0K9P906_ZOSMR Unreviewed; 843 AA.
AC A0A0K9P906;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
GN ORFNames=ZOSMA_31G01490 {ECO:0000313|EMBL:KMZ65558.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ65558.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001412,
CC ECO:0000256|RuleBase:RU000675};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMZ65558.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFYR01001032; KMZ65558.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9P906; -.
DR STRING; 29655.A0A0K9P906; -.
DR OMA; RKEPNIT; -.
DR OrthoDB; 1204541at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd22842; Gal_Rha_Lectin_BGal; 1.
DR Gene3D; 2.60.120.740; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR048913; BetaGal_gal-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR041392; GHD.
DR InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR InterPro; IPR019801; Glyco_hydro_35_CS.
DR InterPro; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR PANTHER; PTHR23421:SF52; BETA-GALACTOSIDASE 14; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF21467; BetaGal_gal-bd; 1.
DR Pfam; PF02140; Gal_Lectin; 1.
DR Pfam; PF17834; GHD; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
DR PROSITE; PS50228; SUEL_LECTIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..843
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005527358"
FT DOMAIN 746..832
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
SQ SEQUENCE 843 AA; 95472 MW; FA4B4CADF26EA460 CRC64;
MMAGLHFSWI SMLPVLVLLA TVGLSSAAGN GTSNIGVKYD SRSLIVNGKR ELFFSGSLHY
PRITTKMWPE IIGKAKRGGL NTIQTYVFWN VHEPRQGQYD FTGNYDLVKF IREIEKQGLW
VILRIGPYIQ AEWNFGGLPY WLREVPKILF RTNNKPFKHH MKNWTNVVIK LMKNEKLFAS
QGGPIILAQI ENEYNNIAKA YKKDGIKYVQ WAGKMAEETN IGVPWIMCKE KYAPDDVISV
CNGRNCGDTF EGPNSPDKPT LWTENWTAQY RVFGDPPSQR SAEDLAYSIA RFFSKNGTLA
NYYMYHGGTN VGRGASAFVK TAYYDEAPID SFGLTKEPKY GHLKDCHSAL KLARKGLLWG
KLSVQSLGNF LEAHIFEKND MNICVAFLSN NNTRVDTDVV FRGVKYFLPH RSISILPDCK
TVVFNTQRVN SQRNARIYYH AQESNKDISW KMWQETLPTF EEAPMESMRP QEQIGLTKDT
SDYLWYTTNF VLEEDDLSMH NEIRPVIQIT SLGHAMNVFV NGKFVGNGHG TKIEKAFAFQ
KQVELKVGMN HITLLGVVIG LPDSGVYLEH RMAGVRYVTC QGLNTGTLDL TRNRWRHQVG
ISGELNMIYK EEESKKVQWS DPQPDIPLTW YQRYFDAPHG DEPVAIDISS MGKGMVWVNG
QSIGRYWVSY LSPIGKPTQT MYHIPRCYLK AAENLMVVFE EIGGKPDGIV VMTVARNVIC
TKVSEFHPAN VRSWKRKKNV IFETVEDVKP KAVLRCPDGN RIRKISFASF GNPTGKCGNM
TVGNCHKDAT AIAEQACLGK SSCVMSIKAN DYDADVNCPE TTLTLAVEAI CRRRRQISPS
KRI
//
