ID A0A162GEV8_9MICO Unreviewed; 918 AA.
AC A0A162GEV8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, 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 Name=lacZ {ECO:0000313|EMBL:KZX20029.1};
GN ORFNames=ACH61_02862 {ECO:0000313|EMBL:KZX20029.1};
OS Rathayibacter tanaceti.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=1671680 {ECO:0000313|EMBL:KZX20029.1, ECO:0000313|Proteomes:UP000076717};
RN [1] {ECO:0000313|EMBL:KZX20029.1, ECO:0000313|Proteomes:UP000076717}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-2596 {ECO:0000313|EMBL:KZX20029.1,
RC ECO:0000313|Proteomes:UP000076717};
RA Vasilenko O.V., Starodumova I.P., Tarlachkov S.V., Dorofeeva L.V.,
RA Evtushenko L.I.;
RT "Draft Genome Sequence of Rathayibacter sp. Strain VKM Ac-2596 Isolated
RT from Leaf Gall Induced by Plant-Parasitic Nematodes.";
RL Submitted (AUG-2015) 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:KZX20029.1}.
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DR EMBL; LIIN01000149; KZX20029.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162GEV8; -.
DR PATRIC; fig|1671680.3.peg.3083; -.
DR Proteomes; UP000076717; 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 Gene3D; 2.70.98.10; -; 1.
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; 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; IPR023232; Glyco_hydro_2_AS.
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 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 PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:KZX20029.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KZX20029.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076717}.
FT DOMAIN 725..914
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 918 AA; 100821 MW; 335ED9B3B06542D6 CRC64;
MTTTPTSAHY LTDTGPGSGR RRAARSWLHT DAPALSLDGE WRFRLLPAAP GTPGGADALP
DGEEVDAVGA ESFDDSDWDL LRVPSHWVLE GDGRYGRPAY TNVQYPFATE PPFVPDENPT
GDYRRTIEVP ESWDRAEAVV LRFDGVESRY RLWVNGVEVG IGSGSRLAQE FDVTGVVRPG
RNLVVVRVHQ WSAASYVEDQ DQWWLPGIFR SVHLLARPVG GIEDVWLRTS FADGAGRIET
EVTAAAAAYP LTLRVPELGV ETVWSSAEEV APIELPAVEP WSAEAPRLYD AQLSSASETV
SLRLGFRTIE IRGDRFLVNG ERVVFHGVNR HETHPDRGRA FDEDFAREDL AMMKRFNVTA
IRTSHYPPHP RLLDLADELG FWVILECDLE THGFERYGWA GNPSDDPAWR EAYLDRIERT
VERDKNHPSI VLWSLGNESG TGANLAAMSA WVHGRDPERP VHYEGDYSGA YTDVYSRMYS
SVPETEQIGR DDSRTPLLGC SPGESARQRA KPFLLCEYVH AMGNGPGAID QYEDLVERYP
RLHGGFVWEW RDHGLRARTS EGIEYYAYGG DFGEVLHDGN FVMDGMVLSD GTPSPGLFEW
KQIVAPVRLT VRADGVVIEN RRHDASTADL RFTWRVELDG RITDEGVLEA PTVPAGEAVH
VALPGFVPPT GGEGWLTVDA VLASATPWAE EGHVLSTGQH LLSAPAAAPA WTRAVRSAPP
AEDGALGLAR FRHGRLTSIA GLAVDGPRAE LWRAPTDNDE GDGFPGYVSG DPFDGNGTGT
PAPSSSARWR EAGLDRLVAR VEEVDSTAGV RRRTRVSAAD LDAALLMEEH WSVDGSSTVL
RVDLAPTRGW DLVWPRLGIR FDLPASIDGA EWFGTGPRES YPDSSVPHGS AGSRRGSTSS
PRRTRDRRRA VTAAPCAN
//
