ID A0A1T4X011_9CLOT Unreviewed; 1016 AA.
AC A0A1T4X011;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00013303, 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=SAMN05443428_10518 {ECO:0000313|EMBL:SKA82983.1};
OS Caloramator quimbayensis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Caloramator.
OX NCBI_TaxID=1147123 {ECO:0000313|EMBL:SKA82983.1, ECO:0000313|Proteomes:UP000190105};
RN [1] {ECO:0000313|EMBL:SKA82983.1, ECO:0000313|Proteomes:UP000190105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USBA 833 {ECO:0000313|EMBL:SKA82983.1,
RC ECO:0000313|Proteomes:UP000190105};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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}.
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DR EMBL; FUYH01000005; SKA82983.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4X011; -.
DR STRING; 1147123.SAMN05443428_10518; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000190105; 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}.
FT DOMAIN 725..996
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1016 AA; 119175 MW; B9B35001AB91E625 CRC64;
MKVWENINID SINRLSPRAY FYSYLDKEAA LTFEKKLSMG YKLLNGIWDF YYTDAPEYSP
EGFYDEDFDS SNWCKIRVPG HWQLQGFKSP HYTDLYYPFT LNPPYVPTMN PTGIYRRNFY
IDESFLGKKI ILRFNGVDSA FHVWINGKEI GYSKGSRLTS EFDISDYIRI GENTIVVRVY
QWSDGSYLED QDMWWLSGIF RDVEIICEPI NGIEDVFVIA DTDSDYKDGI IKVSTKLIQN
LKGYSLDYEI YDFDDNLIYK ENQIAQCNDI YFEGKIKGIK KWSAEEPNLY KILIILKKDE
SDTQIISLRI GFRKIELKDN VFLINGAAIK LKGVNRHDFN SETGRYVSKD DIEKDIILMK
QHNINAIRTS HYPNSPEFYD LCDEYGMYVI GENDFECHGF ELNDMFESFI NDSKWEKAAV
SRMERTVQRD KNHPCIIMWS LGNESSFGSN ITAMADKVRE LDKTRLLHYE GDRECKVADV
YSCMYTWIET KERMALEEAI KKFNKPFILC EYAHAMGNGP GNLKEYQEYI YENENFQGAF
VWEWKDHGIK AVDSSENVYY KYGGDFNDEP NNKNFCMDGF VMANGEVSPG LLEYKKIVQP
VKIEQIDVKK GLFKIKNLYD FITLDDFDLV YTIYKDNDIW YSSQIDIKGI NPNEQREIKI
DKILDITERN SSYSIIFSLV LNKNKKWANI GLELGKDEFF IYNGMKSLNK LNLGIIKKDT
NMLAYFNSND KVICFDKVLG KIKYIKKDGE VLLEDGPDLN LWRAPIDNDM YLLEDYYNKY
FLNDIKFRVD SIECDDDLKF IVNKTYGTTN SPWYYKCRYE YKFLPDGSIK IKVKGVPSGK
KECAPVMIPR IGFKMKINRN LNKVRWEGRG PHPNYPDSKD SALYGIYEKT VDELFVDYPY
PQENASRGGC RWVNLSDYWG NSLMINTKKE FSFSAMYYDD KDLEKAKHCN ELIKRDYIVL
NIDYKQNGLG SNSCGQNQLK KYRCEFEEFE FEFVISAFNK NEISEINLLR LQNNNF
//
