ID B7FYH5_PHATC Unreviewed; 951 AA.
AC B7FYH5;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=PHATRDRAFT_45673 {ECO:0000313|EMBL:EEC48727.1};
OS Phaeodactylum tricornutum (strain CCAP 1055/1).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC Phaeodactylum.
OX NCBI_TaxID=556484 {ECO:0000313|EMBL:EEC48727.1, ECO:0000313|Proteomes:UP000000759};
RN [1] {ECO:0000313|EMBL:EEC48727.1, ECO:0000313|Proteomes:UP000000759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1055/1 {ECO:0000313|EMBL:EEC48727.1,
RC ECO:0000313|Proteomes:UP000000759};
RX PubMed=18923393; DOI=10.1038/nature07410;
RA Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA Grigoriev I.V.;
RT "The Phaeodactylum genome reveals the evolutionary history of diatom
RT genomes.";
RL Nature 456:239-244(2008).
RN [2] {ECO:0000313|Proteomes:UP000000759}
RP GENOME REANNOTATION.
RC STRAIN=CCAP 1055/1 {ECO:0000313|Proteomes:UP000000759};
RG Diatom Consortium;
RA Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., Detter J.C.,
RA Lindquist E., Shapiro H., Lucas S., Glavina del Rio T., Pitluck S.,
RA Rokhsar D., Bowler C.;
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR EMBL; CM000610; EEC48727.1; -; Genomic_DNA.
DR RefSeq; XP_002179741.1; XM_002179705.1.
DR AlphaFoldDB; B7FYH5; -.
DR STRING; 556484.B7FYH5; -.
DR PaxDb; 2850-Phatr45673; -.
DR GeneID; 7200457; -.
DR KEGG; pti:PHATRDRAFT_45673; -.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_248596_0_0_1; -.
DR InParanoid; B7FYH5; -.
DR OrthoDB; 5489808at2759; -.
DR Proteomes; UP000000759; Chromosome 7.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR025300; BetaGal_jelly_roll_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR InterPro; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR23421:SF124; BETA-GALACTOSIDASE 2-RELATED; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF13364; BetaGal_ABD2; 1.
DR Pfam; PF21467; BetaGal_gal-bd; 1.
DR Pfam; PF01301; Glyco_hydro_35; 2.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:EEC48727.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EEC48727.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000759};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 65..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 158..351
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 364..528
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 671..763
FT /note="Beta-galactosidase jelly roll"
FT /evidence="ECO:0000259|Pfam:PF13364"
FT DOMAIN 839..904
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
SQ SEQUENCE 951 AA; 106202 MW; 5A4E195ABA76054D CRC64;
MKTMPSLEFR QSLKGGRPIP ADELRQSLSH QEVEYGSFLP KSSTFHETEL RPCSELQKRR
YQRDLILLAC AALIILYVSG FPPRIKNAGI FKKTSSIIPE GTTYAATTAE LKNEIPACGD
EPCFHPDRVQ VRRDRPYFPS FWNYNGNLSV SYDERAIRIN DKRVLLLSGS MHPVRATRGT
WEHALDEAVY NGLNMITVYI FWGAHQSFRD EPLNWSLDGS SIGPKESQWE LADALRSAAN
RGLFIHVRIG PYACGEYTYG GIPEWLPLQS STMRMRRLNR PWLDAMEGFV AATITYLSSF
NLWAHQGGPI LIAQIENELG SGVDGSAAAN YVVLERDEFN DDKHEDSHLL QLDRYGHILE
NASSRGMDSE LRNATVQDYA DWCGNLVARL APNVIWTMCN GLSAENTIST FNGNNGIDWL
EKYGDSGRIQ VDQPAIWTED EGGFQLWGDQ PSKPSDYFWG RTSRAMATDA LQWFARGGTH
LNYYMWWGGY NRGRSSAAGI MNAYATDAFL CSSGQRRHPK YDHFLALHLV IADIAAILLH
APTSLLKNAS VEIMDGDDWI VGDNQRQFLY QVLDTHDSKQ VIFLENDANT TEMARLTGAK
ADDSLVFVMK PYSSQIVIDG IVAFDSSTIS TKAMSFRRTL HYEPAVLLHL TSWSEPIAGA
DTDQNAHVST EPLEQTNLNS KASISSDYAW YGTDVKIDVV LSQVKLYIGT EKATALAVFI
DGAFIGEANN HQHAEGPTVL SIEIESLAAG THRLAILCES LGYHNLIGRW GAITTAKPKG
ITGNVLIGSP LLSENISLVD GRQMWWSLPG LSVERKAARH GLRRESFEDA AQAEAGLHPL
WSSVLFTSPQ FDSTVHSLFL DLTSGRGHLW LNGKDLGRYW NITRGNSWND YSQRYYFLPA
DFLHLDGQLN ELILFDMLGG DHSAARLLLS SIEESETSKF SDEVDFALAC I
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