ID A0A1Y1RP85_9MICC Unreviewed; 1021 AA.
AC A0A1Y1RP85;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230, ECO:0000256|RuleBase:RU361154};
GN ORFNames=A7979_05220 {ECO:0000313|EMBL:ORC16016.1};
OS Rothia nasimurium.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=85336 {ECO:0000313|EMBL:ORC16016.1, ECO:0000313|Proteomes:UP000192359};
RN [1] {ECO:0000313|EMBL:ORC16016.1, ECO:0000313|Proteomes:UP000192359}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PT-32 {ECO:0000313|EMBL:ORC16016.1,
RC ECO:0000313|Proteomes:UP000192359};
RA Gaiser R.A., Van Baarlen P., Wells J.M.;
RT "Draft genome sequence of a porcine commensal Rothia nasimurium.";
RL Submitted (MAY-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 ECO:0000256|RuleBase:RU361154};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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:ORC16016.1}.
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DR EMBL; LXWF01000041; ORC16016.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1RP85; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000192359; 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; IPR023230; Glyco_hydro_2_CS.
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; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW Reference proteome {ECO:0000313|Proteomes:UP000192359}.
FT DOMAIN 750..1018
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1021 AA; 116527 MW; 940790E84AE73341 CRC64;
MYPTKHHESL NVLHENVLAP RAYYVPASHD MGPLVNNRES SDRFLNLNGT WQFTYFNDDS
ELPQDFHTAT YAHTDASPII VPGAWQTQSF DTHQYTNFKY PFPLDPPFVP HENPCGLYTL
DFQYAQDQQA PLAHLTFEGV DSCFYLWVNG SYIGYSQVSH ASSEFDITEY LTNGSNRLTV
LVYKWCDGSY LEDQDKFRMS GIFRDVYILS RPRHALYDYF ITTDLNEKTS DATLNIAARF
LSQETHTTLT LTKAEGEEVA SSTLTPNAAN PNFTHSATLH IPNAHTWNPE NPYLYTLHLK
TQDEVITERV GVRTIRIEHN VILLNGKPIT FRGVNRHDSD PVTGPTVDYN HIKRDLGLIK
QHNFNAIRSS HYPNSPYFYQ MCDEYGFLVM SEADNESHGT QVQYLEDGSF DNQVNHWNER
ISDNPEWTEA TLDRVQLCVL REKNRPSIVS WSAGNECGYG VTLEESLAWV KSYDTTRITQ
YESAYYDDKK RRYGYSNIDL YSRMYPPFED IEQYLNSNPN KPFLLVEYAH AMGNGPGNLE
DYFQVIDQNQ AMCGGFVWEW CDHAIYAGTT KNGTPKYLYG GDHGEEVHDG NFCMDGLVYP
DRTPHVGLLE YRNVYRPLRV VSFDTVSGSL TLKNYLDFTD AQEAIELKYT FSQDGVEVAS
GTYHFEQAFL PHQETTINLE APSLTSGRCY LHIEYILKKD LPLLPTGLFL GRDEVPVHTI
NPTHAKALDI LGTTNNAQNL AVTKTGKHYT VQGDGFTYTF NRRTGVFDQL STKDHNLLTQ
PMNINIWRAP TDNDMYIKLK WAEAHYHQAY SRVYTSGYTH TENGVTISCT LNMVAPTVQP
IFTGTVLWNI TNDGKITARF NIERAPEFPD LPRFGVRLFL DKSFADVEYF GMGPHESYSD
KHEASYHGTF QSSVEDLHED YIMPQENGSR FDCDYVHLSS PHHQLSVASE HPFSFSASHY
TQEELTNKNH NFELVEADST VLCLDYAHNG IGSNSCGPEV LDEYKLNAQN INFGFTLAPT
L
//
