ID A0A0A2MAH5_9FLAO Unreviewed; 879 AA.
AC A0A0A2MAH5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Beta-galactosidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=Q765_16820 {ECO:0000313|EMBL:KGO85285.1};
OS Flavobacterium rivuli WB 3.3-2 = DSM 21788.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1121895 {ECO:0000313|EMBL:KGO85285.1, ECO:0000313|Proteomes:UP000030152};
RN [1] {ECO:0000313|EMBL:KGO85285.1, ECO:0000313|Proteomes:UP000030152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WB 3.3-2 {ECO:0000313|EMBL:KGO85285.1,
RC ECO:0000313|Proteomes:UP000030152};
RA Zeng Z., Chen C.;
RL Submitted (SEP-2013) 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:KGO85285.1}.
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DR EMBL; JRLX01000024; KGO85285.1; -; Genomic_DNA.
DR RefSeq; WP_020214289.1; NZ_KB899973.1.
DR AlphaFoldDB; A0A0A2MAH5; -.
DR STRING; 1121895.GCA_000378485_03126; -.
DR eggNOG; COG3250; Bacteria.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000030152; 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 Reference proteome {ECO:0000313|Proteomes:UP000030152};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..879
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001992068"
FT DOMAIN 26..168
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 189..284
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 291..596
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 623..674
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 705..855
FT /note="Malectin"
FT /evidence="ECO:0000259|Pfam:PF11721"
SQ SEQUENCE 879 AA; 99891 MW; 3EBA507FE2DF353D CRC64;
MKIKNIVAFI AILLTPVIAN AQRIKQSINT SWQFHKGSDE NETAPDYWQT INIPHTWNAD
DVMDDTPGYF RGIGWYQKEI FLPKGWTGKT IYVYFEGASQ LAEVFINGKS VGTHAGSYLA
FSFDITKQVH EGKNILRVKL DNSHDPDIAP LGGDFSVYGG LYRDVYLLVA DANHFDMDNY
ATNGVFISTP QVSEDNATVN VKGKVNAFQK VKIITTVYDR KGIQVAKTDS RPNKDGSFVA
NIKGIKSPQL WSPEHPNLYK VVNTLTDAKT GKVLDEVTNP LGFRWFSFNA DKGFSLNGEP
YKIMGASRHQ DYKEIGSALP DALHINDVQW LKDMGGSFLR VSHYPQDPAI MEACDRLGIL
TAVETPGNNQ VTESEGYTRT MLNMQCEMIR QNYNHPSVII WSYMNEVLIQ PLHKEKTLER
EQYWKNLHNL AQKLENLCRE EDPARFTMVA FHGDFDLYKR IGLIDIPMIA GWNLYQGWYS
GKFEDFETFV LRHHNEFPEK PLIISEYGAD ADYRLHNFKP TRFDKTQEYT NMYHDAYLKT
IMKYTFISGA IMWNLVEFVN EGRQEAVPHV NNKGLLTTER KPKDIYYIYK ALLSKVPFIK
IGGSNWNSRA QVADAGKEAT ATQPVTVYSN QAEVTLFANY MKVGTQKVVN GKAVFDVIFG
NGDNHLKAVA SNNEEDFATI NFHVIANNLK VKNNPFTTLN VSLGDYRMFM DDITHEAWVP
EQEYTPGSWG YIGGKVYKED EKGDRYGSSR NILGTPYDAM YETQRTGLNS FKADVPDGVY
EVTLHFAELL TKEQQEKLVY NLDKSAVAQK NSFTGRSFDV IINGFTILEN LSNENYLVPI
QAYNTKITVT VKDVKGITID FKTNRGEAIL NGLQLRKIY
//
