ID A0A1Y1ZNX9_9FUNG Unreviewed; 1604 AA.
AC A0A1Y1ZNX9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN ORFNames=LY90DRAFT_677813 {ECO:0000313|EMBL:ORY11963.1};
OS Neocallimastix californiae.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Neocallimastix.
OX NCBI_TaxID=1754190 {ECO:0000313|EMBL:ORY11963.1, ECO:0000313|Proteomes:UP000193920};
RN [1] {ECO:0000313|EMBL:ORY11963.1, ECO:0000313|Proteomes:UP000193920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G1 {ECO:0000313|EMBL:ORY11963.1,
RC ECO:0000313|Proteomes:UP000193920};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL Submitted (AUG-2016) 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 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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:ORY11963.1}.
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DR EMBL; MCOG01000376; ORY11963.1; -; Genomic_DNA.
DR STRING; 1754190.A0A1Y1ZNX9; -.
DR OrthoDB; 276651at2759; -.
DR Proteomes; UP000193920; Unassembled WGS sequence.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.80.10.50; -; 2.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032312; LacZ_4.
DR InterPro; IPR006558; LamG-like.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF02929; Bgal_small_N; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF16353; LacZ_4; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR Pfam; PF14200; RicinB_lectin_2; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SMART; SM00560; LamGL; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000193920};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1604
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012395290"
FT DOMAIN 829..1103
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
FT DOMAIN 1175..1310
FT /note="LamG-like jellyroll fold"
FT /evidence="ECO:0000259|SMART:SM00560"
FT DOMAIN 1371..1505
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 1604 AA; 178675 MW; 01A822D5EA022103 CRC64;
MKFIKAFSIT ATFVGSLLQF QVNAVSFTGN EWTGKYGAED IFAINREPAS CNPVPYQDIE
SAVNAVWDYN AREQSSFLQM LTGKNENWDL VVVQNSNQAQ SHINSGCFKS DFRPSADRGW
KTVQLPKSWT CQGFDFSIYT NVGEPWQSRY DGYVPVPEAP VNYNPVGLYR KKFTLDSSMR
KSGRRIYIEF DGVESAYYVY VNGQAVGYSE DTFSPHRFDI TNVLSSGENT LAVEVHKFCD
GTWFEDQDMI YDGGIFRDVF LVSAPDVQIR DYTVRTDLDS SFTNANLEIS MDIRNLSGGE
KSGWSVIAEA YDEAGNNILK GASVKLDRLN TGRDNTFVLK TSVNSPKLWS AEIPNLYALV
LKLIDNSGNV QEILSTQLGF RKIGFTRAEV NWAYQLTTNN WQPITINGKR LLLKGVNRHD
SDPFNGKAVP QQTLREDITL MKKNNINAIR TSHYSNDSYL YWLCNKYGMY VMGETNMESH
ALMDNNDAKA KFYEVGMDRT ETAYKRLKNN PSIVAWSIGN EMAYTGNPSD AGGLFRDMIW
YFKKNDNSRP VHSEGQGSGM GVDMSSNMYP GSDGLGFHAG RGKMPYVMCE YDHAMGNSVG
ALKEYWDVIR SADNMLGGFI WDWVDQSRAV TLKNGGWDYY SQSYAKTNLY SEEIKGKFYG
YGGDWGDWPN DNSFCVNGLI NPDRTPQPEL AEVKFQYQSF WFSADASQLD NQQVSVYNEN
NFLNINDFDV TWTLLKNGIA IKTGNVKNAN VAPLTKGTLK VPFEIPQDSL AGDEFYLDMS
VKVKNGSDLL PEGTEISYGQ IHLTSTGKPV KYDKGSDNIT IDNNSSSYSI SGKNFNFIID
KSTGTLKTYK YKGETLINEG PTPNFWRGYV ENDNNGGGWA KAFDSKWRNA MDGARVDSID
VKNGVGSEKI IVSHLTLPKV GNTRVDITYT IQSNGSVDVE FNVDGTRAGL GNYLRVGSIM
ILPKGAEKLS WYGNGPVETF NDRKTNGRKG VWESTVSDMF YPYMKADDCG NLTDIKWIAV
QNNGKGASLL IAADGTVEAS ALHFTPEDLM RADHPFKLKP RKETILSVDY GSMGTGSATC
GQATLDKYRL PSGKQYRWKF TIFPISSSNT GEEITTIYAK LRSDGNLIQD KSNNGLIIPI
SSGAKLQKDN NGNYISGALT IPHNSKIDSA LEGRNSFTIE VNVVPTGVQQ FNMLAGKGDR
SIGFRTSTNS IDFFIYAGNE WRTINYNMGV DSASGWVGRK HQVAGIYDAE NNMLRVYADG
RILGERSVGT NSGVAHSNYN LMLGACPDTG RNSQGNFYEM RVYSKALTAS ELASQNTSSP
KYPPNNQNVL LWLDFDNLSE GDTIEVGENI NPSINPSEDN EEDTHLLKDG WYYIKNTGSN
KYLTVKDGRG ASSQNVEVNS KKQKWLLTNV GDDEITLTTE LGNYMLDVNS GSENNGANIQ
IYNSHGGDSQ RFIIEETYQS DVYVIGTKVT NGYKVIDVER EGKDDGSNVC QWDNGEKPNQ
TWVFEFDSYP NGEKEKEPKQ NPPQQEDKCW STSLGYSCCK TCTDVVFVDS VVNGVLKEMT
GVVFQLVVKN NPVVFKVIPV VNLAVMFMKK ILMVNGVLKM TNGA
//
