BGH2A_BACO1
ID BGH2A_BACO1 Reviewed; 851 AA.
AC A7LXS9;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Beta-galactosidase BoGH2A;
DE Short=Beta-gal;
DE EC=3.2.1.23;
DE AltName: Full=Glycosyl hydrolase family protein 2A;
DE Short=BoGH2A;
DE Flags: Precursor;
GN ORFNames=BACOVA_02645;
OS Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 /
OS CCUG 4943 / NCTC 11153).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=411476;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC
RC 11153;
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bacteroides ovatus (ATCC 8483).";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=24463512; DOI=10.1038/nature12907;
RA Larsbrink J., Rogers T.E., Hemsworth G.R., McKee L.S., Tauzin A.S.,
RA Spadiut O., Klinter S., Pudlo N.A., Urs K., Koropatkin N.M., Creagh A.L.,
RA Haynes C.A., Kelly A.G., Cederholm S.N., Davies G.J., Martens E.C.,
RA Brumer H.;
RT "A discrete genetic locus confers xyloglucan metabolism in select human gut
RT Bacteroidetes.";
RL Nature 506:498-502(2014).
CC -!- FUNCTION: Catalyzes the hydrolysis of terminal non-reducing beta-D-
CC galactose residues in beta-D-galactosides in xyloglucan degradation,
CC converting 'L' units to 'X' units. {ECO:0000269|PubMed:24463512}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC Evidence={ECO:0000269|PubMed:24463512};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.087 mM for Gal-beta-PNP {ECO:0000269|PubMed:24463512};
CC Note=kcat is 4.0 sec(-1) for Gal-beta-PNP.;
CC pH dependence:
CC Optimum pH is 6.0-7.0. {ECO:0000269|PubMed:24463512};
CC -!- PATHWAY: Glucan metabolism; xyloglucan degradation.
CC {ECO:0000269|PubMed:24463512}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}. Note=Cell inner membrane localization is predicted by
CC analogy with the archetypal sus locus. {ECO:0000269|PubMed:24463512}.
CC -!- MISCELLANEOUS: Gut bacteria supply the human body with energy from
CC dietary polysaccharides through glycosidases that are absent in the
CC human genome. Xyloglucans are a ubiquitous family of highly branched
CC plant cell wall polysaccharides present in the vegetables we consume.
CC Enzymes involved in xyloglucan degradation mediate the conversion of
CC otherwise indigestible plant polysaccharides to short-chain fatty acids
CC (PubMed:24463512). {ECO:0000305|PubMed:24463512}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
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DR EMBL; AAXF02000049; EDO11436.1; -; Genomic_DNA.
DR AlphaFoldDB; A7LXS9; -.
DR SMR; A7LXS9; -.
DR STRING; 411476.BACOVA_02645; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR PRIDE; A7LXS9; -.
DR EnsemblBacteria; EDO11436; EDO11436; BACOVA_02645.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_006501_0_1_10; -.
DR SABIO-RK; A7LXS9; -.
DR UniPathway; UPA01045; -.
DR Proteomes; UP000005475; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004565; F:beta-galactosidase activity; IDA:UniProtKB.
DR GO; GO:0085030; P:symbiotic process benefiting host; IDA:UniProtKB.
DR GO; GO:2000899; P:xyloglucan catabolic process; IDA:UniProtKB.
DR Gene3D; 2.60.40.10; -; 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; 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 InterPro; IPR008964; Invasin/intimin_cell_adhesion.
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 PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF49303; SSF49303; 1.
DR SUPFAM; SSF49373; SSF49373; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell inner membrane; Cell membrane; Glycosidase;
KW Hydrolase; Lipoprotein; Membrane; Palmitate; Polysaccharide degradation;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..851
FT /note="Beta-galactosidase BoGH2A"
FT /id="PRO_0000425891"
FT ACT_SITE 437
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P00722"
FT ACT_SITE 544
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00722"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 851 AA; 95475 MW; 8D45DE63D7DAD6D4 CRC64;
MMIGKLKYLM LGGCLILGSC LALGGCLMLL GACSSSSLVS PRERSDFNAD WRFHLGDGLQ
AAQPGFADND WRVLDLPHDW AIEGDFSQEN PSGTGGGALP GGVGWYRKTF SVDKADAGKI
FRIEFDGVYM NSEVFINGVS LGVRPYGYIS FSYDLTPYLK WDEPNVLAVR VDNAEQPNSR
WYSGCGIYRN VWLSKTGPIH VGGWGTYVTT SSVDEKQAVL NLATTLVNES DTNENVTVCS
SLQDAEGREV AETRSSGEAE AGKEVVFTQQ LTVKQPQLWD IDTPYLYTLV TKVMRNEECM
DRYTTPVGIR TFSLDARKGF TLNGRQTKIN GVCMHHDLGC LGAAVNTRAI ERHLQILKEM
GCNGIRCSHN PPAPELLDLC DRMGFIVMDE AFDMWRKKKT AHDYARYFNE WHERDLNDFI
LRDRNHPSVF MWSIGNEVLE QWSDAKADTL SLEEANLILN FGHSSEMLAK EGEESVNSLL
TKKLVSFVKG LDPTRPVTAG CNEPNSGNHL FRSGVLDVIG YNYHNKDIPN VPANFPDKPF
IITESNSALM TRGYYRMPSD RMFIWPKRWD KSFADSTFAC SSYENCHVPW GNTHEESLKL
VRDNDFISGQ YVWTGFDYIG EPTPYGWPAR SSYFGIVDLA GFPKDVYYLY QSEWTDKQVL
HLFPHWNWTP GQEIDMWCYY NQADEVELFV NGKSQGVKRK DLDNLHVAWR VKFEPGTVKV
IARESGKVVA EKEICTAGKP AEIRLTPDRS ILTADGKDLC FVTVEVLDEK GNLCPDADNL
VNFTVQGNGF IAGVDNGNPV SMERFKDEKR KAFYGKCLVV IQNDGKPGKA KLTATSEGLR
QAVLKISAEE L
