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Database: UniProt
Entry: Q8A4C3_BACTN
LinkDB: Q8A4C3_BACTN
Original site: Q8A4C3_BACTN 
ID   Q8A4C3_BACTN            Unreviewed;      1001 AA.
AC   Q8A4C3;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:AAO77786.1};
GN   OrderedLocusNames=BT_2680 {ECO:0000313|EMBL:AAO77786.1};
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186 {ECO:0000313|EMBL:AAO77786.1, ECO:0000313|Proteomes:UP000001414};
RN   [1] {ECO:0000313|EMBL:AAO77786.1, ECO:0000313|Proteomes:UP000001414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414};
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
RN   [2] {ECO:0000313|EMBL:AAO77786.1, ECO:0000313|Proteomes:UP000001414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414};
RX   PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA   Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA   Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA   Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA   Hettich R.L., Gordon J.I.;
RT   "Characterizing a model human gut microbiota composed of members of its two
RT   dominant bacterial phyla.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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DR   EMBL; AE015928; AAO77786.1; -; Genomic_DNA.
DR   RefSeq; NP_811592.1; NC_004663.1.
DR   RefSeq; WP_011108444.1; NC_004663.1.
DR   AlphaFoldDB; Q8A4C3; -.
DR   STRING; 226186.BT_2680; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   PaxDb; 226186-BT_2680; -.
DR   EnsemblBacteria; AAO77786; AAO77786; BT_2680.
DR   GeneID; 60923851; -.
DR   KEGG; bth:BT_2680; -.
DR   PATRIC; fig|226186.12.peg.2721; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_006501_3_0_10; -.
DR   InParanoid; Q8A4C3; -.
DR   OrthoDB; 9801077at2; -.
DR   Proteomes; UP000001414; 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; 3.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR032311; DUF4982.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR040605; Glyco_hydro2_dom5.
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; PF18565; Glyco_hydro2_C5; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001414}.
FT   DOMAIN          34..183
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          209..311
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          317..447
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
FT   DOMAIN          633..690
FT                   /note="DUF4982"
FT                   /evidence="ECO:0000259|Pfam:PF16355"
FT   DOMAIN          712..804
FT                   /note="Glycoside hydrolase family 2"
FT                   /evidence="ECO:0000259|Pfam:PF18565"
SQ   SEQUENCE   1001 AA;  114536 MW;  8632EB9D2C89583A CRC64;
     MRHRILFFFL AFIGISQFVT SSDVRNKYNF NSDWLLYVGD VPEAKQPRFS DSEWKKVTLP
     HAFNEDEAFR LSIDELTDTI MWYRKHFRLP ANSKNKKVFV EFEGVRQGAD FYINGQNVGL
     HENGVMAVGF DLTPYIKYGQ ENVIAVRIDN DWNYKERATG TKYQWSNKNF NANYGGIPKN
     VWLHVTDRLY QTLPLYSNLK TTGVYIYAED IRVKSRKAII HAESEIRNEY NRDKQVSYQV
     ELIDRDGTSI QTFEGTKAVV KPGETITLKA ASEVDNLHFW SWGYGYLYTV KTSLWVDGRK
     VDEVATRTGF RKTRFGKGMI WLNDRVIQMK GFAQRTSNEW PGVGMSVPAW LSDYSNHLMV
     EGNANLVRWM HVTPWKQDIE SCDRVGLIQA MQAGDAEKDC EGRQWEQRTE LMRDAIIYNR
     NNPSILFYEC GNESISREHM IEMKAIRDLY DPHGGRAIGS REMLDIREAE YGGEMLYINK
     SAHHPMWAME YCRDEGLRKY WDDYSYPYHK DGDGSNSYKS TVTNKVQKKV DARVYNRNQD
     SFTIENIIRW FDYWRERPGT GDRVSSGGVK IIFSDTNTHY RGVENYRRSG VTDAMRIPKD
     PFFAHQVMWD GWVDTECPRI YIVGHWNYND TVVKPVYVVS SADKVELFLN GKSLGYGEQD
     YHFLYTFKDI AFVPGRLEAV GYDENGKECC RTQLQTAGKP EQIQLSFIQS PEGWKADGAD
     MVLLQVEVMD KDGNRCPLAN DLIHFEVEGP AEWRGGIAQG ENNYILSKDL PVECGINRAL
     IRSLTTAGNV RITAKADGLK PAEISLTSSP VEVKNGLSNY IPGDELEGRL TRGETPQTPS
     YKVSKVDVGI VSAIAGANNE STVNSFDDNE LSEWRNDGKA ATAWITYKLE RAARVDEVCM
     KLTGWRMRSY PLEIYAGKEL IWSGDTDKSL GYVHLDVKPV LTNEITIRLK GTSKEGDAFG
     QIVEVAAPVA NELDLFKAKD GDKTGHELRI VEIEFKENLL K
//
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