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Database: UniProt
Entry: A0A1H9IWC5_9FLAO
LinkDB: A0A1H9IWC5_9FLAO
Original site: A0A1H9IWC5_9FLAO 
ID   A0A1H9IWC5_9FLAO        Unreviewed;      1009 AA.
AC   A0A1H9IWC5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:SEQ78913.1};
GN   ORFNames=SAMN05421824_2308 {ECO:0000313|EMBL:SEQ78913.1};
OS   Hyunsoonleella jejuensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=419940 {ECO:0000313|EMBL:SEQ78913.1, ECO:0000313|Proteomes:UP000198999};
RN   [1] {ECO:0000313|EMBL:SEQ78913.1, ECO:0000313|Proteomes:UP000198999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21035 {ECO:0000313|EMBL:SEQ78913.1,
RC   ECO:0000313|Proteomes:UP000198999};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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DR   EMBL; FOFN01000003; SEQ78913.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9IWC5; -.
DR   STRING; 419940.SAMN05421824_2308; -.
DR   OrthoDB; 9801077at2; -.
DR   Proteomes; UP000198999; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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; 2.
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; IPR005084; CMB_fam6.
DR   InterPro; IPR032311; DUF4982.
DR   InterPro; IPR026876; Fn3_assoc_repeat.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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   PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR   Pfam; PF16355; DUF4982; 1.
DR   Pfam; PF13287; Fn3_assoc; 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; 2.
DR   PROSITE; PS51175; CBM6; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198999};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1009
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011497668"
FT   DOMAIN          884..1009
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
SQ   SEQUENCE   1009 AA;  115191 MW;  7BC447A911951D54 CRC64;
     MKNIFFALLL SFCACYSYAQ RTETNFNNNW RFILEDNAEY SKENIDDSSW KTLNIPHDWS
     FEKGVRKGGD QGQGGGYHDG GIGWYRKQFN IKKESLSKIT YINFDGVYMN SEVWINGNYL
     GKRPYGYISF RYNISKFLKE GKNTIAVRVD NSLEPSARWY HPCGIYAAVK LIEVNPIHFK
     PNTVFVTTPL IENPKAIVNI DAEVTSTQKG LEYEVILFSP DGKELDKNCE KLKTVHSKIQ
     LEVNKPQLWS PEKPILYKAV TRILNGNKVI DEIETTFGFK TVEWKTETGF WLNGENVKLK
     GVCEHWEGGP VGGAWTKPML RWKLELLKGM GTNAIRPSHN PAPPMFYDIC DEIGLLVMDE
     IFDGWHKKAP EDYGKQAFDE WWQADVKEWI TRDRNHPSIF VWSLGNETHS DVAPELVSFG
     KSLDPTRLFT SGAGNPEDMD IQGVNGGSET KVFIENNKLT KPFISTEAPH TWQTRGYYRT
     QTWWRDNELP GTYELPNLTE KEIFFYEGLN PKDWRNRKQR FNSSYDNATV RVSARKYWEV
     MRDTPWHSGH FRWTGFDYYG EAGLVHGGLP FNLFMGGAID VAGFEKDLYY FYQSQWTQEP
     MIHMLPHWSH PRMEKGTKIP VWVYSNTDEV ELFLNGKPLG KDKPGAVWNE MQCEWLVPYE
     EGTIEAVGYI DGKEVNRTSF STAQQPSTLQ NTVTKLEAEG DFRASYILTS EGMDADYNLN
     PYAENRVYYN IVGDVAKVSM ENGNPIDPTS RTKADYRSMF FGKTRLFLEE GQNAKEASVI
     VGSILGDKAL YVSDDITIDV QSVSLFGNDA SNDFEVLYTI DGKNPETDGI AYAEPFKVED
     GTTVKAIVKQ NGVLVLTMEE TFGKNEGLFW GDEHSADMWI GRGVNISAED GILTGSAKPS
     RNAHRFKGSG FVDFKGGEGS ITWYQENDGE RGDYSIRFRY MHNNEGKLYP MKLYVNDEYV
     RDMEFPATGG WEKEWKFVPA IIVLKSGANN IKLVTKGESG PYIDELFID
//
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