ID A0A0M2Y080_9SPHI Unreviewed; 909 AA.
AC A0A0M2Y080;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Beta-galactosidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AAW12_11945 {ECO:0000313|EMBL:KKO91244.1};
OS Sphingobacterium sp. Ag1.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1643451 {ECO:0000313|EMBL:KKO91244.1, ECO:0000313|Proteomes:UP000034524};
RN [1] {ECO:0000313|EMBL:KKO91244.1, ECO:0000313|Proteomes:UP000034524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKO91244.1,
RC ECO:0000313|Proteomes:UP000034524};
RA Pei D., Yu W., Kukutla P., Xu J.;
RT "Draft Genome Sequences of Sphingobacterium sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKO91244.1}.
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DR EMBL; LBGU01000037; KKO91244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2Y080; -.
DR PATRIC; fig|1643451.3.peg.2530; -.
DR Proteomes; UP000034524; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR032311; DUF4982.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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; IPR021720; Malectin_dom.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF16355; DUF4982; 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; PF11721; Malectin; 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; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..909
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005647467"
FT DOMAIN 39..181
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 198..304
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 312..612
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 647..697
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 724..892
FT /note="Malectin"
FT /evidence="ECO:0000259|Pfam:PF11721"
SQ SEQUENCE 909 AA; 104294 MW; 4DF6C218C4885F67 CRC64;
MNIIFKQLIN LCAIGCLFFS WSLHAQTVLD GRVSVDFSSN WKFRKDDDSL DRIAKQKQQT
VNLPHSWNIA DVMDDTPGYY RGATQYQNTL DWKTSWQNKR IVLHVGAANQ EALLLVNGKE
VKAHRGGYTA FNVDITDYLH RKENARNTIA IQVNNRFNQD IAPLSGDFTF FGGIYRKVSL
LLLDQIHFAD PQYGSSGLRL TAKLDARQNA TINLDGAIQN ASTLQQAVLI ETTLVDADGV
TVKKVQQKEK LKPHSHSNFQ LNMVQIEQPK LWSPELPYLY RLITRIYDSK GRQLDRLDNS
VGFRWFSFDP QKGFFLNGKP LKLIGASRHQ DFKGMGNAVP DSLQVQDLVK LKAMGGNFLR
VAHYPQDPAV LKACDSLGLL ASVEIPLVNE ISESPAFADH SFQMQKEMIR QYFNHPSIII
WGYMNEIFLR PHFPKDKDRQ EKYFKSVVSL AQQLETLTRN EDSTRYTMIA NHGNFELYHR
TGLTKIPMLV GWNLYPGWYG GKIADFGRQL EHIHQQLPGK PLLVTEYGAD ADYRIHADKP
IRFDKSVEYA VRYHQGYLNE LIKKPFVAGG VAWNLSDFNS ETREESMPHI NTKGLLTWDR
KEKNTYFLYQ AYLRPEPFIK IGVTHGKKWG VRTDADSALL GSGWLQLPIF SNADSVELLL
DAVSLGARKP VDRMVIWPVS LSRGSHTVKA RAFHNGKLSG MDESMLDCEV LPYDLKRDKE
WQELRINVGD NREYIDSLGN RWYPDQPYER GSWGYVKGEK YRLKNTGREN LGTDVNIRGT
GDDPLFQTQL QRLESYRFDL PNGDYEIELF FAELDGPNDK ENLLYDLEQR EKKQDQKGID
RVFDIRIGDR ALATDVNVRR EVGAFRVLRR KFPLKVNDEG NLAISFIRKK GEPMLNAIRL
KKINQSVNP
//
