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Database: UniProt
Entry: B6XW55_9BIFI
LinkDB: B6XW55_9BIFI
Original site: B6XW55_9BIFI 
ID   B6XW55_9BIFI            Unreviewed;       701 AA.
AC   B6XW55;
DT   20-JAN-2009, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2009, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Glycosyl hydrolase family 2, sugar binding domain protein {ECO:0000313|EMBL:EEB21080.1};
GN   ORFNames=BIFCAT_01444 {ECO:0000313|EMBL:EEB21080.1};
OS   Bifidobacterium catenulatum DSM 16992 = JCM 1194 = LMG 11043.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=566552 {ECO:0000313|EMBL:EEB21080.1, ECO:0000313|Proteomes:UP000003882};
RN   [1] {ECO:0000313|EMBL:EEB21080.1, ECO:0000313|Proteomes:UP000003882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16992 {ECO:0000313|EMBL:EEB21080.1,
RC   ECO:0000313|Proteomes:UP000003882};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Bifidobacterium catenulatum (DSM 16992).";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEB21080.1, ECO:0000313|Proteomes:UP000003882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16992 {ECO:0000313|EMBL:EEB21080.1,
RC   ECO:0000313|Proteomes:UP000003882};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (OCT-2008) 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:EEB21080.1}.
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DR   EMBL; ABXY01000021; EEB21080.1; -; Genomic_DNA.
DR   RefSeq; WP_003835858.1; NZ_JGYT01000011.1.
DR   AlphaFoldDB; B6XW55; -.
DR   GeneID; 45583458; -.
DR   KEGG; bcat:BBCT_1583; -.
DR   PATRIC; fig|566552.18.peg.1666; -.
DR   eggNOG; COG3250; Bacteria.
DR   Proteomes; UP000003882; 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; 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   PANTHER; PTHR42732:SF2; BETA-MANNOSIDASE; 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:EEB21080.1}.
FT   DOMAIN          176..263
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          318..359
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          384..600
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
SQ   SEQUENCE   701 AA;  79137 MW;  00546D7119DEB7EF CRC64;
     MLDVKRVLKA APTKMRSQEP LQQLWTPWGE QIASEWLSSN AAHKAFCPTK DGERKLENGR
     TPILDEHPRP TMMRSNHTML NGFWDYAIVS IPESDNGSKW RKSTTVLTRD EAVQAVKEAA
     IPETFDGKIL VPFSPESALS GVHQTIYPDN MIWYRTIVHP VTLGGEEAVR QIGDANRLIL
     HFEAVDYVCA CFINGQFAGV HVGGYLPFDV DISAFVDPDD DFEIALCVYD PNDSGTQMRG
     KQKIEREGIW YTAQSGIWQS VWMEIVPEAY MQTLTLKGAA DGRLFIRAEI GGDKPNAKLR
     IVVTDPADGA IVADERFAAG MRKVRTEIAT RAEHLWSPED PYLYDVTATL EFGAAKSQEK
     QDIVRSYCAF RTVEIKPDLK GVARFHLNGK PLFLKGVLDQ GYWPDGLMTA PSDKALIHDI
     IAMKESGFNM LRKHIKIETA RWYYHCDRLG MLVWQDAVSG GGEYNAWTTN RKPTLVRATW
     NKYRDDTAKH FAALGADDST YRRDWSRTCD AMVHMLAGHP SIVAWVLFNE GWGQFNACDA
     AERIHALDPT RPIDATSGWY DQRCGDFHSV HNYFRPLEIY PDKGPLRGYV AEYEKKHKRR
     CRAAHYAVLP VMQHGVRAFM ISEFGGLAQL VADHAAVSRA YGYGEYDSIE DWRAAVRSVL
     ASAESLESRG LAGYVYTQVS DVEEELNGLL TYDRRLNKFV Q
//
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