ID B7GTV5_BIFLS Unreviewed; 606 AA.
AC B7GTV5; E8MP42;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE SubName: Full=Glycoside hydrolase family 2, sugar binding {ECO:0000313|EMBL:ACJ51396.1};
GN OrderedLocusNames=Blon_0268 {ECO:0000313|EMBL:ACJ51396.1};
OS Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM
OS 1222 / NCTC 11817 / S12).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=391904 {ECO:0000313|EMBL:ACJ51396.1, ECO:0000313|Proteomes:UP000001360};
RN [1] {ECO:0000313|EMBL:ACJ51396.1, ECO:0000313|Proteomes:UP000001360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12 [JGI]
RC {ECO:0000313|Proteomes:UP000001360};
RX PubMed=19033196; DOI=10.1073/pnas.0809584105;
RA Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R.,
RA Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P.,
RA Richardson P.M., Mills D.A.;
RT "The genome sequence of Bifidobacterium longum subsp. infantis reveals
RT adaptations for milk utilization within the infant microbiome.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; CP001095; ACJ51396.1; -; Genomic_DNA.
DR RefSeq; WP_012576707.1; NZ_JDTT01000027.1.
DR AlphaFoldDB; B7GTV5; -.
DR SMR; B7GTV5; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR KEGG; bln:Blon_0268; -.
DR PATRIC; fig|391904.8.peg.271; -.
DR OMA; IHDHVGW; -.
DR Proteomes; UP000001360; Chromosome.
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; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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 Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
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, ECO:0000313|EMBL:ACJ51396.1}.
FT DOMAIN 18..188
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 194..296
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 305..527
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 606 AA; 69008 MW; 0AA9768D8C2A0C60 CRC64;
MERIQYPDPQ CVRRNWVDLN GTWDFAIPGA PAGTKNGNQG NNAMESTPET LQAAASMAFP
EFDRTIEVPY SYTFPKSGVD EPQYHPVVWY RRSFDLDMRP GKRYLLNFEA VDYACDVWLN
GRHVGSHQGG HTPFRFDVTP YAAKENELVV KVVDFNRTDQ PLGKQAWKDG NFACWYTRTI
GIWQSVWLEE TGDVHLTDFT MTPHANQARL DVDASLNVNV DAELDYNVTF EGKPVTHGTV
SFTNARARFS VEIRNYDPSP EPHPWTPSTP DLYDIDFTVR SGGETTDEVS SYFGLRDVTS
DGKMIFLNDQ KYYMKLLLNQ GYYPGGGLTG TADEFRADIE KMKAMGFNGN RIHQKLESNR
MLYLCDKLGF IVWAEMPSAY EFGPELIANV ERELPAYLRK HVNHPSVFAY VLMNESWGVF
DIAHSEQERT FVNSLYYQAK AFDPSRLVIG NDGYEQTRTD IATIHDYNAD ADELLETYQG
RRDEVLAGAP SPMGGRRVFC QGYEQQRVPV MVTEYGGVAY EPGGHTEDSW GYGERITDPD
KVVDQIAALT RAVMDIDYCV GFCYTQTSDV EQEVNGLLDH DHEYKFDPKR IREVLLSKHT
YGYVQV
//