ID H6NLM3_9BACL Unreviewed; 1058 AA.
AC H6NLM3;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=PM3016_4179 {ECO:0000313|EMBL:AFC30957.1};
OS Paenibacillus mucilaginosus 3016.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1116391 {ECO:0000313|EMBL:AFC30957.1, ECO:0000313|Proteomes:UP000007523};
RN [1] {ECO:0000313|EMBL:AFC30957.1, ECO:0000313|Proteomes:UP000007523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3016 {ECO:0000313|EMBL:AFC30957.1,
RC ECO:0000313|Proteomes:UP000007523};
RX PubMed=22535950; DOI=10.1128/JB.00323-12;
RA Ma M., Wang Z., Li L., Jiang X., Guan D., Cao F., Chen H., Wang X.,
RA Shen D., Du B., Li J.;
RT "Complete Genome Sequence of Paenibacillus mucilaginosus 3016, a Bacterium
RT Functional as Microbial Fertilizer.";
RL J. Bacteriol. 194:2777-2778(2012).
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; CP003235; AFC30957.1; -; Genomic_DNA.
DR RefSeq; WP_014370784.1; NC_016935.1.
DR AlphaFoldDB; H6NLM3; -.
DR STRING; 1116391.PM3016_4179; -.
DR KEGG; pmq:PM3016_4179; -.
DR HOGENOM; CLU_002346_0_2_9; -.
DR Proteomes; UP000007523; Chromosome.
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:UP000007523}.
FT DOMAIN 761..1035
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1058 AA; 117722 MW; ECD68EE8C023953E CRC64;
MYPTGTTGVH ETKTADGPAD DRIKDWSDPQ MLGRGGERPH ALSVPYADEE SALRGERENS
SYVLPLNGVW RFYYAESPQE APAACELAEY DDTQWADLPV PSNWQLHGYG TPLYSSCPYP
FPVDPPHVPK RNPTGIYRRR FRQPEDWSGR RTLLVFEGVD AAFHLYVNGE QAGYGQGSHY
PHEFDITPYL RAGENTIAVR VYQWCAGSYL EDQDKWRLSG IFRDVYLVSA PAAGLRDAAV
QAVPTGSGGG QLTVDVTAAR RSAGPESGFT VQLKLMDEAG EPIHESQLSD APLNPQPGEE
DELRTVISLS GVRSWTAETP VLYTLLLTTR DAAGTVQEVR SVPVGFRDIA VREGKLLVNG
APVILKGVNR NEFDPDRGFA VTYESMVRDI ELMKQHNINT VRTSHYPNDP RWLDLCDRYG
LYVIDEADLE THGFVLAGGN ESRLSEDPEW RAPYLDRIIR LVERDKNHPS VIVWSLGNES
GYGCNHDAMA EWVRGRDSSR PIHYERAYEA PVVDIVSSMY PSVEMLEEEG KKEDARPYLM
VEFGHAMGNA LGNQKEYWDT VHRYPRLLGG LIWEWCDMGL RRKEDGGQPS YTYGGDYGDE
PHSGHFCIDG LVFPDRTVKP ALIEYKKAIE PVSVTGLELE SGLVQVANRY SFLDLSHLRA
EWTLYCDGDA VESGELTELA VPPGEERTVR IPYRNGPQNS GGEYWLRVRF VLRAGTRWAP
AGHEVAWTDL PLQRKITAGM DAAVSDQLPA LKTTLEGTSL TVIGSSFHAT FGIDTGQLTG
WVSQGTRLLQ EGPVIRLWRA PVDNDVHLAK EWRKAKYDKL TAEVRSVDYR TAARNHAVQV
RVREVIGAKG EAVAFTAERI YTLYGSGDLT LDIKLSPARE ELPPLPRYGV LLTVPEEFDR
MAWFGRGPHE CYPDRKESGK LGMYAGSIAE QFVPYIKPQE NGNKADVRWA AVTDSTGAGL
LIAGMPLVDV TVHGVAPQVL TAAKHREDLV RADRTFVYID SGQSGLGNHS CGYAPTLDAY
LLPAGEERRL RFRLKPLAAG QSPMLASKGE PEAIVWED
//
