ID Q9F4D5_BIFBI Unreviewed; 1752 AA.
AC Q9F4D5;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 2.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:CAC14566.2};
DE EC=3.2.1.23 {ECO:0000313|EMBL:CAC14566.2};
OS Bifidobacterium bifidum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1681 {ECO:0000313|EMBL:CAC14566.2};
RN [1] {ECO:0000313|EMBL:CAC14566.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 20215 {ECO:0000313|EMBL:CAC14566.2};
RA Madsen S., Poulsen U., Stougaard P.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007829|PDB:6QUB, ECO:0007829|PDB:6QUC}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 33-917 AND 56-912 IN COMPLEX WITH
RP CA(2+) AND BETA-D-GALACTOSE.
RA Nielsen J.A., Andersen J.L., Alsarraf H., Blaise M., Thirup S.S.,
RA Larsen M.K., Cramer J.F.;
RT "Truncated beta-galactosidase III from Bifidobacterium bifidum.";
RL Submitted (FEB-2019) to the PDB data bank.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; AJ224435; CAC14566.2; -; Genomic_DNA.
DR PDB; 6QUB; X-ray; 1.95 A; A=33-917, B=56-912.
DR PDB; 6QUC; X-ray; 2.30 A; A/B=33-917.
DR PDB; 6QUD; X-ray; 2.10 A; A=33-917.
DR PDBsum; 6QUB; -.
DR PDBsum; 6QUC; -.
DR PDBsum; 6QUD; -.
DR SMR; Q9F4D5; -.
DR CAZy; CBM32; Carbohydrate-Binding Module Family 32.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR SABIO-RK; Q9F4D5; -.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.3630; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011081; Big_4.
DR InterPro; IPR032311; DUF4982.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR040605; Glyco_hydro2_dom5.
DR InterPro; IPR006101; Glyco_hydro_2.
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; IPR008964; Invasin/intimin_cell_adhesion.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF07532; Big_4; 2.
DR Pfam; PF16355; DUF4982; 1.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR Pfam; PF18565; Glyco_hydro2_C5; 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 PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 3.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR PROSITE; PS50022; FA58C_3; 2.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:6QUB, ECO:0007829|PDB:6QUC};
KW Calcium {ECO:0007829|PDB:6QUB, ECO:0007829|PDB:6QUC};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:CAC14566.2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAC14566.2};
KW Metal-binding {ECO:0007829|PDB:6QUB, ECO:0007829|PDB:6QUC};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1752
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004325941"
FT DOMAIN 1080..1242
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1317..1476
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:6QUB, ECO:0007829|PDB:6QUC"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:6QUB, ECO:0007829|PDB:6QUC"
FT BINDING 197
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0007829|PDB:6QUB"
FT BINDING 424
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:6QUC"
FT BINDING 426
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:6QUB, ECO:0007829|PDB:6QUC"
FT BINDING 478
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0007829|PDB:6QUB"
FT BINDING 479
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0007829|PDB:6QUB"
FT BINDING 565
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0007829|PDB:6QUB"
FT BINDING 600
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0007829|PDB:6QUB"
FT BINDING 631
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0007829|PDB:6QUB"
FT BINDING 638
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:6QUB, ECO:0007829|PDB:6QUC"
FT BINDING 675
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:6QUB, ECO:0007829|PDB:6QUC"
FT BINDING 678
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:6QUB, ECO:0007829|PDB:6QUC"
FT BINDING 707
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:6QUB, ECO:0007829|PDB:6QUC"
SQ SEQUENCE 1752 AA; 188246 MW; 8FF5858F7413F2E1 CRC64;
MAVRRLGGRI VAFAATVALS IPLGLLTNSA WAVEDATRSD STTQMSSTPE VVYSSAVDSK
QNRTSDFDAN WKFMLSDSVQ AQDPAFDDSA WQQVDLPHDY SITQKYSQSN EAESAYLPGG
TGWYRKSFTI DRDLAGKRIA INFDGVYMNA TVWFNGVKLG THPYGYSPFS FDLTGNAKFG
GENTIVVKVE NRLPSSRWYS GSGIYRDVTL TVTDGVHVGN NGVAIKTPSL ATQNGGDVTM
NLTTKVANDT EAAANITLKQ TVFPKGGKTD AAIGTVTTAS KSIAAGASAD VTSTITAASP
KLWSIKNPNL YTVRTEVLNG GKVLDTYDTE YGFRWTGFDA TSGFSLNGEK VKLKGVSMHH
DQGSLGAVAN RRAIERQVEI LQKMGVNSIR TTHNPAAKAL IDVCNEKGVL VVEEVFDMWN
RSKNGNTEDY GKWFGQAIAG DNAVLGGDKD ETWAKFDLTS TINRDRNAPS VIMWSLGNEM
MEGISGSVSG FPATSAKLVA WTKAADSTRP MTYGDNKIKA NWNESNTMGD NLTANGGVVG
TNYSDGANYD KIRTTHPSWA IYGSETASAI NSRGIYNRTT GGAQSSDKQL TSYDNSAVGW
GAVASSAWYD VVQRDFVAGT YVWTGFDYLG EPTPWNGTGS GAVGSWPSPK NSYFGIVDTA
GFPKDTYYFY QSQWNDDVHT LHILPAWNEN VVAKGSGNNV PVVVYTDAAK VKLYFTPKGS
TEKRLIGEKS FTKKTTAAGY TYQVYEGSDK DSTAHKNMYL TWNVPWAEGT ISAEAYDENN
RLIPEGSTEG NASVTTTGKA AKLKADADRK TITADGKDLS YIEVDVTDAN GHIVPDAANR
VTFDVKGAGK LVGVDNGSSP DHDSYQADNR KAFSGKVLAI VQSTKEAGEI TVTAKADGLQ
SSTVKIATTA VPGTSTEKTV RSFYYSRNYY VKTGNKPILP SDVEVRYSDG TSDRQNVTWD
AVSDDQIAKA GSFSVAGTVA GQKISVRVTM IDEIGALLNY SASTPVGTPA VLPGSRPAVL
PDGTVTSANF AVHWTKPADT VYNTAGTVKV PGTATVFGKE FKVTATIRVQ RSQVTIGSSV
SGNALRLTQN IPADKQSDTL DAIKDGSTTV DANTGGGANP SAWTNWAYSK AGHNTAEITF
EYATEQQLGQ IVMYFFRDSN AVRFPDAGKT KIQISADGKN WTDLAATETI AAQESSDRVK
PYTYDFAPVG ATFVKVTVTN ADTTTPSGVV CAGLTEIELK TATSKFVTNT SAALSSLTVN
GTKVSDSVLA AGSYNTPAII ADVKAEGEGN ASVTVLPAHD NVIRVITESE DHVTRKTFTI
NLGTEQEFPA DSDERDYPAA DMTVTVGSEQ TSGTATEGPK KFAVDGNTST YWHSNWTPTT
VNDLWIAFEL QKPTKLDALR YLPRPAGSKN GSVTEYKVQV SDDGTNWTDA GSGTWTTDYG
WKLAEFNQPV TTKHVRLKAV HTYADSGNDK FMSASEIRLR KAVDTTDISG ATVTVPAKLT
VDRVDADHPA TFATKDVTVT LGDATLRYGV DYLLDYAGNT AVGKATVTVR GIDKYSGTVA
KTFTIELKNA PAPEPTLTSV SVKTKPSKLT YVVGDAFDPA GLVLQHDRQA DRPPQPLVGE
QADERGLTCG TRCDRVEQLR KHENREAHRT GLDHLEFVGA ADGAVGEQAT FKVHVHADQG
DGRHDDADER DIDPHVPVDH AVGELARAAC HHVIGLRVDT HRLKASGFQI PADDMAEIDR
ITGFHRFERH VG
//
