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Protein

Xyloglucan-specific endo-beta-1,4-glucanase BoGH5A

Gene

BACOVA_02653

Organism
Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / NCTC 11153)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Xyloglucan + H2O = xyloglucan oligosaccharides.1 Publication

Kineticsi

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.

  1. KM=0.036 mM for XXXG-beta-CNP1 Publication
  2. KM=0.145 mM for XLLG-beta-CNP1 Publication
  3. KM=3.59 mM for GGGG-beta-CNP1 Publication

    pH dependencei

    Optimum pH is 6.0-7.0.1 Publication

    Pathwayi: xyloglucan degradation

    This protein is involved in the pathway xyloglucan degradation, which is part of Glucan metabolism.1 Publication
    View all proteins of this organism that are known to be involved in the pathway xyloglucan degradation and in Glucan metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei165 – 1651Substrate
    Binding sitei172 – 1721Substrate; via amide nitrogen
    Binding sitei251 – 2511Substrate
    Binding sitei296 – 2961Substrate
    Active sitei297 – 2971Proton donorBy similarity
    Active sitei430 – 4301Nucleophile1 Publication
    Binding sitei472 – 4721Substrate

    GO - Molecular functioni

    • xyloglucan-specific endo-beta-1,4-glucanase activity Source: UniProtKB

    GO - Biological processi

    • mutualism Source: UniProtKB
    • xyloglucan catabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation

    Enzyme and pathway databases

    UniPathwayiUPA01045.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Xyloglucan-specific endo-beta-1,4-glucanase BoGH5A (EC:3.2.1.151)
    Alternative name(s):
    Glycosyl hydrolase family protein 5A
    Short name:
    BoGH5A
    Gene namesi
    ORF Names:BACOVA_02653
    OrganismiBacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / NCTC 11153)
    Taxonomic identifieri411476 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
    Proteomesi
    • UP000005475 Componenti: Unassembled WGS sequence

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cell outer membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Cells are not able to growth on xyloglucan polysaccharide, This phenotype can be directly rescued by the addition of xyloglucan oligosaccharides.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi33 – 331C → A: Abolishes surface localization and hampers growth on xyloglucans. 1 Publication
    Mutagenesisi430 – 4301E → A: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3232PROSITE-ProRule annotationAdd
    BLAST
    Chaini33 – 502470Xyloglucan-specific endo-beta-1,4-glucanase BoGH5APRO_0000425894Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi33 – 331N-palmitoyl cysteineCurated
    Lipidationi33 – 331S-diacylglycerol cysteineCurated

    Keywords - PTMi

    Lipoprotein, Palmitate

    Interactioni

    Protein-protein interaction databases

    STRINGi411476.BACOVA_02653.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi47 – 493Combined sources
    Beta strandi50 – 545Combined sources
    Beta strandi59 – 668Combined sources
    Beta strandi71 – 777Combined sources
    Beta strandi80 – 834Combined sources
    Beta strandi85 – 873Combined sources
    Beta strandi89 – 979Combined sources
    Beta strandi102 – 1043Combined sources
    Beta strandi106 – 1138Combined sources
    Beta strandi120 – 1267Combined sources
    Helixi150 – 1578Combined sources
    Beta strandi160 – 1623Combined sources
    Turni182 – 1854Combined sources
    Helixi192 – 2009Combined sources
    Beta strandi205 – 2084Combined sources
    Beta strandi215 – 2184Combined sources
    Turni219 – 2224Combined sources
    Helixi226 – 24116Combined sources
    Beta strandi245 – 2495Combined sources
    Helixi262 – 28322Combined sources
    Beta strandi290 – 2934Combined sources
    Helixi310 – 32819Combined sources
    Helixi332 – 3354Combined sources
    Beta strandi339 – 3424Combined sources
    Helixi344 – 3463Combined sources
    Helixi348 – 3547Combined sources
    Beta strandi361 – 3644Combined sources
    Beta strandi366 – 3727Combined sources
    Helixi376 – 3794Combined sources
    Helixi393 – 3953Combined sources
    Beta strandi398 – 4003Combined sources
    Helixi406 – 4149Combined sources
    Helixi417 – 4215Combined sources
    Beta strandi426 – 4316Combined sources
    Helixi441 – 46424Combined sources
    Beta strandi468 – 4714Combined sources
    Turni483 – 4853Combined sources
    Helixi491 – 50212Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ZMRX-ray1.43A/B37-502[»]
    ProteinModelPortaliA7LXT7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini67 – 12761BACONAdd
    BLAST

    Domaini

    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).1 Publication

    Sequence similaritiesi

    Contains 1 BACON domain.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG4108K2F. Bacteria.
    COG2730. LUCA.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR024361. BACON.
    IPR001547. Glyco_hydro_5.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF13004. BACON. 1 hit.
    PF00150. Cellulase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    A7LXT7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MEKQSFSDGL FSPLGIKRVI FMLVLLTTSF ISCSNSDEKG GSLEVAQEYR
    60 70 80 90 100
    NLEFDARGSR QTIQIDGPAE WHISTSESWC KSSHTIGEGK QYVNITVEAN
    110 120 130 140 150
    DTQKERTATV TVSASGAPDI IINVKQSLYS VPAYDEYIAP DNTGMRDLTS
    160 170 180 190 200
    MQLSALMKAG VNVGNTFEAV IVGNDGSLSG DETCWGNPTP NKVLFEGIKA
    210 220 230 240 250
    AGFDVVRIPV AYSHQFEDAA TYKIKSAWMD KVEAAVKAAL DAGLYVIINI
    260 270 280 290 300
    HWEGGWLNHP VDANKEALDE RLEAMWKQIA LRFRDYDDRL LFAGTNEVNN
    310 320 330 340 350
    DDANGAQPTE ENYRVQNGFN QVFVNTVRAT GGRNHYRHLI VQAYNTDVAK
    360 370 380 390 400
    AVAHFTMPLD IVQNRIFLEC HYYDPYDFTI MPNDENFKSQ WGAAFAGGDV
    410 420 430 440 450
    SATGQEGDIE ATLSSLNVFI NNNVPVIIGE YGPTLRDQLT GEALENHLKS
    460 470 480 490 500
    RNDYIEYVVK TCVKNKLVPL YWDAGYTEKL FDRTTGQPHN AASIAAIMKG

    LN
    Length:502
    Mass (Da):55,653
    Last modified:October 2, 2007 - v1
    Checksum:i59990DE33869CCC2
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AAXF02000049 Genomic DNA. Translation: EDO11444.1.
    RefSeqiWP_004298445.1. NZ_DS264579.1.

    Genome annotation databases

    EnsemblBacteriaiEDO11444; EDO11444; BACOVA_02653.
    PATRICi27042300. VBIBacOva42630_2232.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AAXF02000049 Genomic DNA. Translation: EDO11444.1.
    RefSeqiWP_004298445.1. NZ_DS264579.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ZMRX-ray1.43A/B37-502[»]
    ProteinModelPortaliA7LXT7.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi411476.BACOVA_02653.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiEDO11444; EDO11444; BACOVA_02653.
    PATRICi27042300. VBIBacOva42630_2232.

    Phylogenomic databases

    eggNOGiENOG4108K2F. Bacteria.
    COG2730. LUCA.

    Enzyme and pathway databases

    UniPathwayiUPA01045.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR024361. BACON.
    IPR001547. Glyco_hydro_5.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF13004. BACON. 1 hit.
    PF00150. Cellulase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Draft genome sequence of Bacteroides ovatus (ATCC 8483)."
      Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D., Gordon J.
      Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 8483 / DSM 1896 / JCM 5824 / NCTC 11153.
    2. Cited for: X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 37-502 IN COMPLEX WITH HEPTASACCHARIDE XXXG, ACTIVE SITE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, DISRUPTION PHENOTYPE, PROBABLE PALMITOYLATION AT CYS-33, MUTAGENESIS OF CYS-33 AND GLU-430.

    Entry informationi

    Entry nameiBGH5A_BACO1
    AccessioniPrimary (citable) accession number: A7LXT7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 19, 2014
    Last sequence update: October 2, 2007
    Last modified: December 9, 2015
    This is version 41 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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).1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.