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Database: UniProt
Entry: A3XK70_LEEBM
LinkDB: A3XK70_LEEBM
Original site: A3XK70_LEEBM 
ID   A3XK70_LEEBM            Unreviewed;       620 AA.
AC   A3XK70;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Putative exported beta-galactosidase {ECO:0000313|EMBL:EAQ50052.1};
GN   ORFNames=MED217_02840 {ECO:0000313|EMBL:EAQ50052.1};
OS   Leeuwenhoekiella blandensis (strain CECT 7118 / CCUG 51940 / KCTC 22103 /
OS   MED217) (Flavobacterium sp. (strain MED217)).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Leeuwenhoekiella.
OX   NCBI_TaxID=398720 {ECO:0000313|EMBL:EAQ50052.1, ECO:0000313|Proteomes:UP000001601};
RN   [1] {ECO:0000313|EMBL:EAQ50052.1, ECO:0000313|Proteomes:UP000001601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED217 {ECO:0000313|EMBL:EAQ50052.1,
RC   ECO:0000313|Proteomes:UP000001601};
RX   PubMed=17215843; DOI=10.1038/nature05381;
RA   Gomez-Consarnau L., Gonzalez J.M., Coll-Llado M., Gourdon P., Pascher T.,
RA   Neutze R., Pedros-Alio C., Pinhassi J.;
RT   "Light stimulates growth of proteorhodopsin-containing marine
RT   Flavobacteria.";
RL   Nature 445:210-213(2007).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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:EAQ50052.1}.
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DR   EMBL; AANC01000003; EAQ50052.1; -; Genomic_DNA.
DR   RefSeq; WP_009778961.1; NZ_CH672395.1.
DR   AlphaFoldDB; A3XK70; -.
DR   STRING; 398720.MED217_02840; -.
DR   eggNOG; COG1874; Bacteria.
DR   HOGENOM; CLU_007853_7_1_10; -.
DR   OrthoDB; 703126at2; -.
DR   Proteomes; UP000001601; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; 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   InterPro; IPR026283; B-gal_1-like.
DR   InterPro; IPR048912; BetaGal1-like_ABD1.
DR   InterPro; IPR048913; BetaGal_gal-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF21317; BetaGal_ABD_1; 1.
DR   Pfam; PF21467; BetaGal_gal-bd; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PIRSF; PIRSF006336; B-gal; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001601};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..620
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002662464"
FT   DOMAIN          35..360
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          404..513
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          533..591
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   ACT_SITE        184
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   ACT_SITE        268
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ   SEQUENCE   620 AA;  69919 MW;  802B1C4FF90D0DC0 CRC64;
     MQVVRTNFFA LVLIVLSFGF AQAQDDASFK IENGSFVYNG KPTPIYSGEM HYERIPKEYW
     RHRIQMMKAM GLNTIATYVF WNYHNPAPGV WDFESGNRNV AEFIKIAKEE EMFVILRPGP
     YACGEWEFGG YPWFLQNIPG LKVRENNAQF LAACKEYINE LAKQVAPLQV NNGGNIIMTQ
     VENEFGSYVA QREDIAPEDH KAYKEAIFKM LKDAGFQAPF FTSDGAWLFE GGSLEGVLPT
     ANGEGNIDNL KKVVNKFNNN EGPYMVAEFY PGWLDHWAEP FVKISASDIA KQTEVYLKNG
     VNFNFYMAHG GTNFGFTSGA NYNDEHDIQP DITSYDYDAP ISEAGWVTPK YDSIRALMQK
     YAPYEIPAVP EQIPVIEIPQ IQLAKTTDAL TFIKKQKPVT SDSPLTFEQL EQGFGYVLYK
     KRFTQPITGT LKVPGLRDFA TVYVNGKKVG ELNRVFNSYE MPIKIPFNGS LEILVENMGR
     INYGAEIVNN LKGITAPVSI NDYEITGGWE MYKAPFAEVP EVINSTEVKT GRPVVYSGSF
     DLKKQGDTFL NMSEMGKGIV FVNGHNLGRY WKVGPQQTLY VPGCWLKKKG NTITIFEQLN
     EVAATSIFAQ KTPILEDLKN
//
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