ID A0A1G1STZ0_9BACT Unreviewed; 1080 AA.
AC A0A1G1STZ0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ORFNames=BEN49_02795 {ECO:0000313|EMBL:OGX82097.1};
OS Hymenobacter coccineus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1908235 {ECO:0000313|EMBL:OGX82097.1, ECO:0000313|Proteomes:UP000177506};
RN [1] {ECO:0000313|EMBL:OGX82097.1, ECO:0000313|Proteomes:UP000177506}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 8649 {ECO:0000313|EMBL:OGX82097.1,
RC ECO:0000313|Proteomes:UP000177506};
RA Sedlacek I., Kralova S., Kyrova K., Maslanova I., Stankova E., Vrbovska V.,
RA Nemec M., Bartak M., Svec P., Busse H.-J., Pantucek R.;
RT "Hymenobacter coccineus sp. nov., Hymenobacter lapidarius sp. nov. and
RT Hymenobacter glacialis sp. nov., isolated from Antarctic soil.";
RL Submitted (AUG-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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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:OGX82097.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MDZA01000437; OGX82097.1; -; Genomic_DNA.
DR RefSeq; WP_070746858.1; NZ_MDZA01000437.1.
DR AlphaFoldDB; A0A1G1STZ0; -.
DR Proteomes; UP000177506; 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OGX82097.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1080
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009578423"
FT DOMAIN 788..1061
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1080 AA; 120380 MW; A6DDEC1083DD7DF3 CRC64;
MKYTLFKKHT FKLSLAAAFM FGAQLGWGQQ APDAQFLAKT DTAAVPKEIE NPECIGINKE
ASHATLMPYG SLPEALAANR HASSFSRSLN GKWKFHWVDW PQKRPVDFYK PAFDVSDWKD
IKVPSNFQVE GYGTPNYSNF TLIFKKDFPR VMSTPSEKYT TFKERNPVGS YRRDFTVPTA
WKGRRTFITF DGVDAGFFVW VNGRKVGYSV NSRNAAEFDL TKYLKPGPNT LAVEVYRFTS
GSYLENQDMW RLSGIFRNVT LWSAPMEHIR DYFIKTDLDP QFRDADVLVT AKVKNYGPTP
VKARALKATL YNGTTAVAGA LGEKTVPALR PGQETTVTLR FHVRNPQKWT AETPKLYTTV
LALQEGSAAV ETVSSRTGFR ELEIKGRLFT VNGVPIKLKG VNRHENWPDD GHAVTEAQMI
RDLELIKQAN CNHVRTCHYS DDPRWYELCD EFGIYLVAEA NVECHEQQNQ FNEEPTFKAA
IVDRNVANAE NFKNHPSVVI WSLGNENGEG GTNFRAALAA VRAIDPSRPT HYEGFGIGSK
NPADIDSRMY TGVVELEKNA NDNALTKPFY LQEYAHAMFN SMGSVDIYNE LFDKYPALLG
GAIWEWQDQG IYNNRNPQHP ITAFGGGFGE YPNDHFFIHK GVVFSDRSLK PHYPELKHAY
QWITIRPKDA KNGVVIIKNR YQFSNLTGLT AKWEVSEDGT TIATGPLTVG AISPGQEKSL
TIPYQVKAKP GALYFARVSF ALAADQRWAK KGYEVAEQQF ELPVAVPAAP APAPAGSVTL
TDSKDNIKVS GPDFACDFNK AKGTFTQLEK GGESLLQANG GPMLHLWRAP HQKDDIWAYE
NWEKNGLKNL TWTTDNVSSR QVSPTAVEIK ASLTGTGQQG FVVHHQVVYT INGAGLINVA
NNVTFSDPKL ILARIGVRMQ LAKDLNRFDY LGRGPMENYG DRKSGYDVGH YASSVSQQMT
PYEKPMECGN HEDVRWANLT SAKGVELTVR ADTALMQVSA LPYTDEEMDP VEYKIDLPAS
KGTVLCLSHK TLGVGSNGCG PRPLEPYMVY AKPTTFSYQL QLSKKAPATS RGSVGALLKN
//
