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Xyloglucan-specific endo-beta-1,4-glucanase BoGH5A (EC 3.2.1.151) (Glycosyl hydrolase family protein 5A) (BoGH5A)

 BGH5A_BACO1             Reviewed;         502 AA.
A7LXT7;
19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
02-OCT-2007, sequence version 1.
25-OCT-2017, entry version 49.
RecName: Full=Xyloglucan-specific endo-beta-1,4-glucanase BoGH5A;
EC=3.2.1.151;
AltName: Full=Glycosyl hydrolase family protein 5A;
Short=BoGH5A;
Flags: Precursor;
ORFNames=BACOVA_02653;
Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / NCTC
11153).
Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
Bacteroides.
NCBI_TaxID=411476;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 8483 / DSM 1896 / JCM 5824 / NCTC 11153;
Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M.,
Liep D., Gordon J.;
"Draft genome sequence of Bacteroides ovatus (ATCC 8483).";
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
[2]
X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 37-502 IN COMPLEX WITH
HEPTASACCHARIDE XXXG, ACTIVE SITE, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, DISRUPTION PHENOTYPE,
PALMITOYLATION AT CYS-33, AND MUTAGENESIS OF CYS-33 AND GLU-430.
PubMed=24463512; DOI=10.1038/nature12907;
Larsbrink J., Rogers T.E., Hemsworth G.R., McKee L.S., Tauzin A.S.,
Spadiut O., Klinter S., Pudlo N.A., Urs K., Koropatkin N.M.,
Creagh A.L., Haynes C.A., Kelly A.G., Cederholm S.N., Davies G.J.,
Martens E.C., Brumer H.;
"A discrete genetic locus confers xyloglucan metabolism in select
human gut Bacteroidetes.";
Nature 506:498-502(2014).
-!- FUNCTION: Catalyzes endohydrolysis of 1,4-beta-D-glucosidic
linkages in xyloglucan with retention of the beta-configuration of
the glycosyl residues in xyloglucan degradation. Cleaves the
backbone of the 3 major types of natural xyloglucans (seed
galactoxyloglucan from tamarind kernel, dicot
fucogalactoxyloglucan from lettuce leaves, and solanaceous
arabinogalactoxyloglucan from tomato fruit), to produce xyloglucan
oligosaccharides. {ECO:0000269|PubMed:24463512}.
-!- CATALYTIC ACTIVITY: Xyloglucan + H(2)O = xyloglucan
oligosaccharides. {ECO:0000269|PubMed:24463512}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.036 mM for XXXG-beta-CNP {ECO:0000269|PubMed:24463512};
KM=0.145 mM for XLLG-beta-CNP {ECO:0000269|PubMed:24463512};
KM=3.59 mM for GGGG-beta-CNP {ECO:0000269|PubMed:24463512};
Note=kcat is 10.5 sec(-1) for XXXG-beta-CNP. kcat is 11.1 sec(-
1) for XLLG-beta-CNP. kcat is 0.12 sec(-1) for GGGG-beta-CNP.;
pH dependence:
Optimum pH is 6.0-7.0. {ECO:0000269|PubMed:24463512};
-!- PATHWAY: Glucan metabolism; xyloglucan degradation.
{ECO:0000269|PubMed:24463512}.
-!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-
anchor {ECO:0000305}. Note=Cell outer membrane localization is
predicted by analogy with the archetypal sus locus.
{ECO:0000269|PubMed:24463512}.
-!- DOMAIN: The BACON domain was initially thought to act as a
carbohydrate-binding domain. However, it does not bind
carbohydrates and may rather be required to distance the catalytic
module from the cell surface and confer additional mobility to the
catalytic domain for attack of the polysaccharide
(PubMed:24463512). {ECO:0000269|PubMed:24463512}.
-!- DISRUPTION PHENOTYPE: Cells are not able to growth on xyloglucan
polysaccharide, This phenotype can be directly rescued by the
addition of xyloglucan oligosaccharides.
{ECO:0000269|PubMed:24463512}.
-!- MISCELLANEOUS: Gut bacteria supply the human body with energy from
dietary polysaccharides through glycosidases that are absent in
the human genome. Xyloglucans are a ubiquitous family of highly
branched plant cell wall polysaccharides present in the vegetables
we consume. Enzymes involved in xyloglucan degradation mediate the
conversion of otherwise indigestible plant polysaccharides to
short-chain fatty acids (PubMed:24463512).
{ECO:0000305|PubMed:24463512}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A)
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AAXF02000049; EDO11444.1; -; Genomic_DNA.
RefSeq; WP_004298445.1; NZ_DS264579.1.
PDB; 3ZMR; X-ray; 1.43 A; A/B=37-502.
PDBsum; 3ZMR; -.
ProteinModelPortal; A7LXT7; -.
SMR; A7LXT7; -.
STRING; 411476.BACOVA_02653; -.
CAZy; GH5; Glycoside Hydrolase Family 5.
EnsemblBacteria; EDO11444; EDO11444; BACOVA_02653.
GeneID; 29452215; -.
eggNOG; ENOG4108K2F; Bacteria.
eggNOG; COG2730; LUCA.
UniPathway; UPA01045; -.
Proteomes; UP000005475; Unassembled WGS sequence.
GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0033946; F:xyloglucan-specific endo-beta-1,4-glucanase activity; IDA:UniProtKB.
GO; GO:0085030; P:mutualism; IDA:UniProtKB.
GO; GO:2000899; P:xyloglucan catabolic process; IDA:UniProtKB.
CDD; cd14948; BACON; 1.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR024361; BACON.
InterPro; IPR001547; Glyco_hydro_5.
InterPro; IPR017853; Glycoside_hydrolase_SF.
InterPro; IPR013783; Ig-like_fold.
Pfam; PF13004; BACON; 1.
Pfam; PF00150; Cellulase; 1.
SUPFAM; SSF51445; SSF51445; 1.
PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
1: Evidence at protein level;
3D-structure; Carbohydrate metabolism; Cell outer membrane;
Complete proteome; Glycosidase; Hydrolase; Lipoprotein; Membrane;
Palmitate; Polysaccharide degradation; Signal.
SIGNAL 1 32 {ECO:0000255|PROSITE-ProRule:PRU00303}.
CHAIN 33 502 Xyloglucan-specific endo-beta-1,4-
glucanase BoGH5A.
/FTId=PRO_0000425894.
DOMAIN 67 127 BACON.
ACT_SITE 297 297 Proton donor. {ECO:0000250}.
ACT_SITE 430 430 Nucleophile.
{ECO:0000305|PubMed:24463512}.
BINDING 165 165 Substrate.
BINDING 172 172 Substrate; via amide nitrogen.
BINDING 251 251 Substrate.
BINDING 296 296 Substrate.
BINDING 472 472 Substrate.
LIPID 33 33 N-palmitoyl cysteine.
{ECO:0000305|PubMed:24463512}.
LIPID 33 33 S-diacylglycerol cysteine. {ECO:0000305}.
MUTAGEN 33 33 C->A: Abolishes surface localization and
hampers growth on xyloglucans.
{ECO:0000269|PubMed:24463512}.
MUTAGEN 430 430 E->A: Loss of activity.
{ECO:0000269|PubMed:24463512}.
HELIX 47 49 {ECO:0000244|PDB:3ZMR}.
STRAND 50 54 {ECO:0000244|PDB:3ZMR}.
STRAND 59 66 {ECO:0000244|PDB:3ZMR}.
STRAND 71 77 {ECO:0000244|PDB:3ZMR}.
STRAND 80 83 {ECO:0000244|PDB:3ZMR}.
STRAND 85 87 {ECO:0000244|PDB:3ZMR}.
STRAND 89 97 {ECO:0000244|PDB:3ZMR}.
STRAND 102 104 {ECO:0000244|PDB:3ZMR}.
STRAND 106 113 {ECO:0000244|PDB:3ZMR}.
STRAND 120 126 {ECO:0000244|PDB:3ZMR}.
HELIX 150 157 {ECO:0000244|PDB:3ZMR}.
STRAND 160 162 {ECO:0000244|PDB:3ZMR}.
TURN 182 185 {ECO:0000244|PDB:3ZMR}.
HELIX 192 200 {ECO:0000244|PDB:3ZMR}.
STRAND 205 208 {ECO:0000244|PDB:3ZMR}.
STRAND 215 218 {ECO:0000244|PDB:3ZMR}.
TURN 219 222 {ECO:0000244|PDB:3ZMR}.
HELIX 226 241 {ECO:0000244|PDB:3ZMR}.
STRAND 245 249 {ECO:0000244|PDB:3ZMR}.
HELIX 262 283 {ECO:0000244|PDB:3ZMR}.
STRAND 290 293 {ECO:0000244|PDB:3ZMR}.
HELIX 310 328 {ECO:0000244|PDB:3ZMR}.
HELIX 332 335 {ECO:0000244|PDB:3ZMR}.
STRAND 339 342 {ECO:0000244|PDB:3ZMR}.
HELIX 344 346 {ECO:0000244|PDB:3ZMR}.
HELIX 348 354 {ECO:0000244|PDB:3ZMR}.
STRAND 361 364 {ECO:0000244|PDB:3ZMR}.
STRAND 366 372 {ECO:0000244|PDB:3ZMR}.
HELIX 376 379 {ECO:0000244|PDB:3ZMR}.
HELIX 393 395 {ECO:0000244|PDB:3ZMR}.
STRAND 398 400 {ECO:0000244|PDB:3ZMR}.
HELIX 406 414 {ECO:0000244|PDB:3ZMR}.
HELIX 417 421 {ECO:0000244|PDB:3ZMR}.
STRAND 426 431 {ECO:0000244|PDB:3ZMR}.
HELIX 441 464 {ECO:0000244|PDB:3ZMR}.
STRAND 468 471 {ECO:0000244|PDB:3ZMR}.
TURN 483 485 {ECO:0000244|PDB:3ZMR}.
HELIX 491 502 {ECO:0000244|PDB:3ZMR}.
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


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