ID H4GKC1_9LACO Unreviewed; 1009 AA.
AC H4GKC1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=PS3_12859 {ECO:0000313|EMBL:EHS85573.1};
OS Limosilactobacillus gastricus PS3.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=1144300 {ECO:0000313|EMBL:EHS85573.1, ECO:0000313|Proteomes:UP000004567};
RN [1] {ECO:0000313|EMBL:EHS85573.1, ECO:0000313|Proteomes:UP000004567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PS3 {ECO:0000313|EMBL:EHS85573.1,
RC ECO:0000313|Proteomes:UP000004567};
RX PubMed=23846278;
RA Martin V., Cardenas N., Jimenez E., Maldonado A., Rodriguez J.M.,
RA Fernandez L.;
RT "Genome Sequence of Lactobacillus gastricus PS3, a Strain Isolated from
RT Human Milk.";
RL Genome Announc. 1:E00489-E00413(2013).
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:EHS85573.1}.
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DR EMBL; AICN01000062; EHS85573.1; -; Genomic_DNA.
DR RefSeq; WP_007122504.1; NZ_AICN01000062.1.
DR AlphaFoldDB; H4GKC1; -.
DR STRING; 1144300.PS3_12859; -.
DR PATRIC; fig|1144300.3.peg.1392; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000004567; 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:UP000004567}.
FT DOMAIN 736..1006
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1009 AA; 115608 MW; 8E94DE7991DE0457 CRC64;
MIKQNITTAD LNWLADPQVD AVNTVPAHSD HHYYASLSEL SQGKSTFVQS LDGQWKVNYV
RDADLRPRDF YQTDFDDTDF TTITVPGHLE LQGYGKPQYV NTQYPWDGGE FLRPPMIPQH
HNAVASYIRY FRVNDHLIHD SERVRLVFEG ASTAIYVWLN GHFIGYHEDS FTPAEFDITS
ALVEGENKLA VALYRFSTAN WVEDQDFWRL TGLFRSVVLK GQPKVHLEDI KTNATLDDSY
QRGILDAQVS LTGPIDANLT VEALLLDRQN KVLASQSQPA KAELNFHFED LAIEAWSDEQ
PQLYRLRLAV RKDRFVYEVV PVEVGFRRFE LIDRVMYLNG KRLVFRGVNR HEFDARLGRA
VTDDDMRWDI QYLKQHNINA VRTSHYPNQS RWYELCDQYG IYVIDEANLE SHGTWQKLGE
CEPSWNIPAS EPEWLDTCLY RANNMYQRDK NHPSILIWSC GNESYAGDDI AAMSKFFHEQ
DPSRLVHYEG VTWNREYDQI TDIESRMYAK PAEIETYLKD NPQKPYISCE YMHAMGNSLG
GLQLYTALEK YSQYQGGFIW DFIDQGIYQQ QANGVERLTY GGDWDDRPAD YEFCGDGLVL
ANRQDTPKGS AVKQLYSPIQ IEPDQAGVKI INRRLFTMTD DLYFVATVMQ DGHQVWQSEP
MNWLVKARTS AHFAIEYPKD LSGEIVYTVT AYLASSKQWA AKGYPIVSGQ TVIQESLPKF
VASGQPQLIE GDFNYGVKGK NFQALFSRAQ GTLVSLKYGG QELIQKLPRL TFFRALTDND
RGAGYGYDFH KWMDLGHYAK MTEVKAELKA QVAQITYQYL LPSQMGKASV CYQVDQTGKI
NVVAEYDGHL VGEYLPEFGL EFGVPAQLDQ FDYYGLGPDD NYWDRQAGVQ LGRYQVKVAD
NNIPYLRPQE SGNRMQVREL AVHDGQQHGF KVVADQQVFE ANVQSHQTLE YELADHQEEL
APSQITWVKL LAVQMGVGGD DSWGATVHAE FMLPADQKYR LSFTIEPLQ
//
