BGH5A_BACO1
ID BGH5A_BACO1 Reviewed; 502 AA.
AC A7LXT7;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Xyloglucan-specific endo-beta-1,4-glucanase BoGH5A;
DE EC=3.2.1.151;
DE AltName: Full=Glycosyl hydrolase family protein 5A;
DE Short=BoGH5A;
DE Flags: Precursor;
GN ORFNames=BACOVA_02653;
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 X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 37-502 IN COMPLEX WITH
RP HEPTASACCHARIDE XXXG, ACTIVE SITE, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, DISRUPTION PHENOTYPE,
RP PALMITOYLATION AT CYS-33, AND MUTAGENESIS OF CYS-33 AND GLU-430.
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 endohydrolysis of 1,4-beta-D-glucosidic linkages in
CC xyloglucan with retention of the beta-configuration of the glycosyl
CC residues in xyloglucan degradation. Cleaves the backbone of the 3 major
CC types of natural xyloglucans (seed galactoxyloglucan from tamarind
CC kernel, dicot fucogalactoxyloglucan from lettuce leaves, and
CC solanaceous arabinogalactoxyloglucan from tomato fruit), to produce
CC xyloglucan oligosaccharides. {ECO:0000269|PubMed:24463512}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=xyloglucan + H2O = xyloglucan oligosaccharides.; EC=3.2.1.151;
CC Evidence={ECO:0000269|PubMed:24463512};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.036 mM for XXXG-beta-CNP {ECO:0000269|PubMed:24463512};
CC KM=0.145 mM for XLLG-beta-CNP {ECO:0000269|PubMed:24463512};
CC KM=3.59 mM for GGGG-beta-CNP {ECO:0000269|PubMed:24463512};
CC Note=kcat is 10.5 sec(-1) for XXXG-beta-CNP. kcat is 11.1 sec(-1) for
CC XLLG-beta-CNP. kcat is 0.12 sec(-1) for GGGG-beta-CNP.;
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 outer membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}. Note=Cell outer membrane localization is predicted by
CC analogy with the archetypal sus locus. {ECO:0000269|PubMed:24463512}.
CC -!- DOMAIN: The BACON domain was initially thought to act as a
CC carbohydrate-binding domain. However, it does not bind carbohydrates
CC and may rather be required to distance the catalytic module from the
CC cell surface and confer additional mobility to the catalytic domain for
CC attack of the polysaccharide (PubMed:24463512).
CC {ECO:0000269|PubMed:24463512}.
CC -!- DISRUPTION PHENOTYPE: Cells are not able to growth on xyloglucan
CC polysaccharide, This phenotype can be directly rescued by the addition
CC of xyloglucan oligosaccharides. {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 5 (cellulase A) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAXF02000049; EDO11444.1; -; Genomic_DNA.
DR RefSeq; WP_004298445.1; NZ_DS264579.1.
DR PDB; 3ZMR; X-ray; 1.43 A; A/B=37-502.
DR PDBsum; 3ZMR; -.
DR AlphaFoldDB; A7LXT7; -.
DR SMR; A7LXT7; -.
DR STRING; 411476.BACOVA_02653; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR PRIDE; A7LXT7; -.
DR EnsemblBacteria; EDO11444; EDO11444; BACOVA_02653.
DR GeneID; 29452215; -.
DR eggNOG; COG2730; Bacteria.
DR HOGENOM; CLU_018668_3_0_10; -.
DR SABIO-RK; A7LXT7; -.
DR UniPathway; UPA01045; -.
DR Proteomes; UP000005475; Unassembled WGS sequence.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033946; F:xyloglucan-specific endo-beta-1,4-glucanase 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 CDD; cd14948; BACON; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR024361; BACON.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF13004; BACON; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell outer membrane; Glycosidase;
KW Hydrolase; Lipoprotein; Membrane; Palmitate; Polysaccharide degradation;
KW Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 33..502
FT /note="Xyloglucan-specific endo-beta-1,4-glucanase BoGH5A"
FT /id="PRO_0000425894"
FT DOMAIN 67..127
FT /note="BACON"
FT ACT_SITE 297
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 430
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:24463512"
FT BINDING 165
FT /ligand="substrate"
FT BINDING 172
FT /ligand="substrate"
FT BINDING 251
FT /ligand="substrate"
FT BINDING 296
FT /ligand="substrate"
FT BINDING 472
FT /ligand="substrate"
FT LIPID 33
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:24463512"
FT LIPID 33
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT MUTAGEN 33
FT /note="C->A: Abolishes surface localization and hampers
FT growth on xyloglucans."
FT /evidence="ECO:0000269|PubMed:24463512"
FT MUTAGEN 430
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24463512"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:3ZMR"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:3ZMR"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:3ZMR"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:3ZMR"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:3ZMR"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:3ZMR"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:3ZMR"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:3ZMR"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:3ZMR"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:3ZMR"
FT HELIX 150..157
FT /evidence="ECO:0007829|PDB:3ZMR"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:3ZMR"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:3ZMR"
FT HELIX 192..200
FT /evidence="ECO:0007829|PDB:3ZMR"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:3ZMR"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:3ZMR"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:3ZMR"
FT HELIX 226..241
FT /evidence="ECO:0007829|PDB:3ZMR"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:3ZMR"
FT HELIX 262..283
FT /evidence="ECO:0007829|PDB:3ZMR"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:3ZMR"
FT HELIX 310..328
FT /evidence="ECO:0007829|PDB:3ZMR"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:3ZMR"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:3ZMR"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:3ZMR"
FT HELIX 348..354
FT /evidence="ECO:0007829|PDB:3ZMR"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:3ZMR"
FT STRAND 366..372
FT /evidence="ECO:0007829|PDB:3ZMR"
FT HELIX 376..379
FT /evidence="ECO:0007829|PDB:3ZMR"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:3ZMR"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:3ZMR"
FT HELIX 406..414
FT /evidence="ECO:0007829|PDB:3ZMR"
FT HELIX 417..421
FT /evidence="ECO:0007829|PDB:3ZMR"
FT STRAND 426..431
FT /evidence="ECO:0007829|PDB:3ZMR"
FT HELIX 441..464
FT /evidence="ECO:0007829|PDB:3ZMR"
FT STRAND 468..471
FT /evidence="ECO:0007829|PDB:3ZMR"
FT TURN 483..485
FT /evidence="ECO:0007829|PDB:3ZMR"
FT HELIX 491..502
FT /evidence="ECO:0007829|PDB:3ZMR"
SQ SEQUENCE 502 AA; 55653 MW; 59990DE33869CCC2 CRC64;
MEKQSFSDGL FSPLGIKRVI FMLVLLTTSF ISCSNSDEKG GSLEVAQEYR NLEFDARGSR
QTIQIDGPAE WHISTSESWC KSSHTIGEGK QYVNITVEAN DTQKERTATV TVSASGAPDI
IINVKQSLYS VPAYDEYIAP DNTGMRDLTS MQLSALMKAG VNVGNTFEAV IVGNDGSLSG
DETCWGNPTP NKVLFEGIKA AGFDVVRIPV AYSHQFEDAA TYKIKSAWMD KVEAAVKAAL
DAGLYVIINI HWEGGWLNHP VDANKEALDE RLEAMWKQIA LRFRDYDDRL LFAGTNEVNN
DDANGAQPTE ENYRVQNGFN QVFVNTVRAT GGRNHYRHLI VQAYNTDVAK AVAHFTMPLD
IVQNRIFLEC HYYDPYDFTI MPNDENFKSQ WGAAFAGGDV SATGQEGDIE ATLSSLNVFI
NNNVPVIIGE YGPTLRDQLT GEALENHLKS RNDYIEYVVK TCVKNKLVPL YWDAGYTEKL
FDRTTGQPHN AASIAAIMKG LN
