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Protein

Extracellular xylan exo-alpha-(1->2)-glucuronosidase

Gene

gla67A

Organism
Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Alpha-glucuronidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. It catalyzes the cleavage of the alpha-1,2-glycosidic bond at the non-reducing end of 4-O-methyl-D-glucuronic acid (4-O-MeGlcA) side chain of short xylooligosaccharides and releases 4-O-methylglucuronic acid. It can also hydrolyze small soluble oligosaccharides such as dobiouronic acid, aldotriouronic acid, aldotetraouronic acid, and aldopentaouronic acid.3 Publications

Catalytic activityi

Hydrolysis of (1->2)-alpha-D-(4-O-methyl)glucuronosyl links in the main chain of hardwood xylans.1 Publication

Enzyme regulationi

Inhibited by 4-O-MeGlcA.1 Publication

Kineticsi

  1. KM=0.28 mM for aldotriouronic acid (at 37 degrees Celsius)2 Publications
  2. KM=0.36 mM for aldotetraouronic acid (at 37 degrees Celsius)2 Publications
  3. KM=0.42 mM for aldopentaouronic acid (at 37 degrees Celsius)2 Publications
  4. KM=0.53 mM for aldobiouronic acid (at 37 degrees Celsius)2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei180 – 1801Participates in a stacking interactions with the sugar rings of 4-O-MeGlcA
    Binding sitei231 – 2311beta-D-glucuronic acid
    Binding sitei308 – 3081Substrate
    Active sitei312 – 3121Proton donor1 Publication
    Binding sitei345 – 3451Substrate
    Binding sitei356 – 3561Substrate
    Binding sitei380 – 3801Substrate
    Active sitei385 – 3851Proton acceptor1 Publication
    Binding sitei407 – 4071SubstrateBy similarity
    Active sitei413 – 4131Proton acceptor1 Publication
    Binding sitei541 – 5411Substrate
    Binding sitei563 – 5631Substrate
    Sitei563 – 5631Participates in a stacking interactions with the sugar rings of 4-O-MeGlcA

    GO - Molecular functioni

    • alpha-glucuronidase activity Source: InterPro
    • xylan alpha-1,2-glucuronosidase activity Source: UniProtKB

    GO - Biological processi

    • glucuronoxylan catabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

    Enzyme and pathway databases

    BioCyciCJAP498211:GHIT-2878-MONOMER.
    BRENDAi3.2.1.139. 5103.

    Protein family/group databases

    CAZyiGH67. Glycoside Hydrolase Family 67.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Extracellular xylan exo-alpha-(1->2)-glucuronosidase (EC:3.2.1.131)
    Alternative name(s):
    Alpha-glucuronidase
    Gene namesi
    Name:gla67A
    Synonyms:glcA67A
    Ordered Locus Names:CJA_2887
    OrganismiCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
    Taxonomic identifieri498211 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaCellvibrionalesCellvibrionaceaeCellvibrio
    Proteomesi
    • UP000001036 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cell outer membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi180 – 1801W → A: Greatly reduced the glucuronosidase activity. 1 Publication
    Mutagenesisi230 – 2301V → A: No influence on the glucuronosidase activity. 1 Publication
    Mutagenesisi230 – 2301V → G: Little influence on the glucuronosidase activity. 1 Publication
    Mutagenesisi230 – 2301V → N: Considerabely less active than wild-type. 1 Publication
    Mutagenesisi230 – 2301V → S: Considerabely less active than wild-type. 1 Publication
    Mutagenesisi308 – 3081K → A: Greatly reduced the glucuronosidase activity.
    Mutagenesisi312 – 3121E → A: Loss of glucuronosidase activity. 1 Publication
    Mutagenesisi312 – 3121E → C: Loss of glucuronosidase activity. 1 Publication
    Mutagenesisi345 – 3451R → A: Loss of glucuronosidase activity. 1 Publication
    Mutagenesisi380 – 3801K → A: Greatly reduced the glucuronosidase activity. 1 Publication
    Mutagenesisi385 – 3851D → A: Loss of glucuronosidase activity. 1 Publication
    Mutagenesisi385 – 3851D → C: Loss of glucuronosidase activity. 1 Publication
    Mutagenesisi413 – 4131E → A: Loss of glucuronosidase activity. 1 Publication
    Mutagenesisi413 – 4131E → C: Retains 20% of the of glucuronosidase activity. 1 Publication
    Mutagenesisi563 – 5631W → A: Greatly reduced the glucuronosidase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence analysisAdd
    BLAST
    Chaini21 – 732712Extracellular xylan exo-alpha-(1->2)-glucuronosidasePRO_0000422176Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Protein-protein interaction databases

    STRINGi498211.CJA_2887.

    Structurei

    Secondary structure

    1
    732
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni28 – 314Combined sources
    Helixi40 – 4910Combined sources
    Beta strandi51 – 555Combined sources
    Helixi60 – 7718Combined sources
    Beta strandi90 – 967Combined sources
    Turni98 – 1003Combined sources
    Helixi102 – 1065Combined sources
    Helixi111 – 1144Combined sources
    Turni115 – 1195Combined sources
    Beta strandi121 – 1288Combined sources
    Beta strandi131 – 14010Combined sources
    Helixi141 – 15616Combined sources
    Beta strandi165 – 1684Combined sources
    Beta strandi173 – 1786Combined sources
    Helixi199 – 2013Combined sources
    Turni202 – 2043Combined sources
    Helixi208 – 21811Combined sources
    Turni219 – 2213Combined sources
    Beta strandi224 – 2263Combined sources
    Helixi234 – 2374Combined sources
    Helixi239 – 25214Combined sources
    Helixi253 – 2553Combined sources
    Beta strandi258 – 2636Combined sources
    Helixi267 – 2704Combined sources
    Helixi282 – 29817Combined sources
    Beta strandi304 – 3074Combined sources
    Helixi317 – 3204Combined sources
    Helixi324 – 33512Combined sources
    Helixi336 – 3383Combined sources
    Beta strandi341 – 3455Combined sources
    Helixi356 – 3583Combined sources
    Helixi359 – 3646Combined sources
    Helixi365 – 3673Combined sources
    Beta strandi375 – 38612Combined sources
    Helixi395 – 3984Combined sources
    Beta strandi400 – 40910Combined sources
    Turni413 – 4197Combined sources
    Helixi425 – 4328Combined sources
    Helixi445 – 4506Combined sources
    Beta strandi452 – 4543Combined sources
    Beta strandi460 – 4645Combined sources
    Beta strandi473 – 4764Combined sources
    Helixi479 – 49113Combined sources
    Helixi497 – 50812Combined sources
    Helixi513 – 53220Combined sources
    Turni545 – 5473Combined sources
    Beta strandi549 – 5513Combined sources
    Helixi561 – 5633Combined sources
    Helixi566 – 5694Combined sources
    Beta strandi573 – 5764Combined sources
    Turni582 – 5854Combined sources
    Helixi587 – 5904Combined sources
    Helixi593 – 6008Combined sources
    Turni602 – 6043Combined sources
    Helixi607 – 6126Combined sources
    Helixi628 – 65124Combined sources
    Helixi652 – 6565Combined sources
    Helixi659 – 69133Combined sources
    Helixi706 – 71510Combined sources
    Beta strandi721 – 7233Combined sources
    Helixi724 – 7274Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GQIX-ray1.48A/B25-732[»]
    1GQJX-ray1.90A/B25-732[»]
    1GQKX-ray1.90A/B25-732[»]
    1GQLX-ray1.67A/B25-732[»]
    1H41X-ray1.50A/B25-732[»]
    ProteinModelPortaliB3PC73.
    SMRiB3PC73. Positions 25-732.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni188 – 1892Substrate binding

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 67 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG4105D0H. Bacteria.
    COG3661. LUCA.
    HOGENOMiHOG000177796.
    KOiK01235.
    OMAiMVNPGHH.
    OrthoDBiEOG6J48K3.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    3.30.379.10. 1 hit.
    3.90.1330.10. 1 hit.
    InterProiIPR029018. Chitobiase/Hex_dom_2-like.
    IPR011395. Glyco_hydro_67_aGlcAse.
    IPR005154. Glyco_hydro_67_aGlcAse_N.
    IPR011099. Glyco_hydro_67_C.
    IPR011100. Glyco_hydro_67_cat.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF07477. Glyco_hydro_67C. 1 hit.
    PF07488. Glyco_hydro_67M. 1 hit.
    PF03648. Glyco_hydro_67N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF029900. Alpha-glucuronds. 1 hit.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF55545. SSF55545. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    B3PC73-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSTFARLFLC LVFFASLQPA MAQTEDGYDM WLRYQPIADQ TLLKTYQKQI
    60 70 80 90 100
    RHLHVAGDSP TINAAAAELQ RGLSGLLNKP IVARDEKLKD YSLVIGTPDN
    110 120 130 140 150
    SPLIASLNLG ERLQALGAEG YLLEQTRINK RHVVIVAANS DVGVLYGSFH
    160 170 180 190 200
    LLRLIQTQHA LEKLSLSSAP RLQHRVVNHW DNLNRVVERG YAGLSLWDWG
    210 220 230 240 250
    SLPNYLAPRY TDYARINASL GINGTVINNV NADPRVLSDQ FLQKIAALAD
    260 270 280 290 300
    AFRPYGIKMY LSINFNSPRA FGDVDTADPL DPRVQQWWKT RAQKIYSYIP
    310 320 330 340 350
    DFGGFLVKAD SEGQPGPQGY GRDHAEGANM LAAALKPFGG VVFWRAFVYH
    360 370 380 390 400
    PDIEDRFRGA YDEFMPLDGK FADNVILQIK NGPIDFQPRE PFSALFAGMS
    410 420 430 440 450
    RTNMMMEFQI TQEYFGFATH LAYQGPLFEE SLKTETHARG EGSTIGNILE
    460 470 480 490 500
    GKVFKTRHTG MAGVINPGTD RNWTGHPFVQ SSWYAFGRMA WDHQISAATA
    510 520 530 540 550
    ADEWLRMTFS NQPAFIEPVK QMMLVSREAG VNYRSPLGLT HLYSQGDHYG
    560 570 580 590 600
    PAPWTDDLPR ADWTAVYYHR ASKTGIGFNR TKTGSNALAQ YPEPIAKAWG
    610 620 630 640 650
    DLNSVPEDLI LWFHHLSWDH RMQSGRNLWQ ELVHKYYQGV EQVRAMQRTW
    660 670 680 690 700
    DQQEAYVDAA RFAQVKALLQ VQEREAVRWR NSCVLYFQSV AGRPIPANYE
    710 720 730
    QPEHDLEYYK MLARTTYVPE PWHPASSSRV LK
    Length:732
    Mass (Da):83,021
    Last modified:September 2, 2008 - v1
    Checksum:iE3219C0AB50E7685
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY065638 Genomic DNA. Translation: AAL57752.1.
    CP000934 Genomic DNA. Translation: ACE83468.1.
    RefSeqiWP_012488471.1. NC_010995.1.

    Genome annotation databases

    EnsemblBacteriaiACE83468; ACE83468; CJA_2887.
    KEGGicja:CJA_2887.
    PATRICi21329159. VBICelJap122165_2845.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY065638 Genomic DNA. Translation: AAL57752.1.
    CP000934 Genomic DNA. Translation: ACE83468.1.
    RefSeqiWP_012488471.1. NC_010995.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GQIX-ray1.48A/B25-732[»]
    1GQJX-ray1.90A/B25-732[»]
    1GQKX-ray1.90A/B25-732[»]
    1GQLX-ray1.67A/B25-732[»]
    1H41X-ray1.50A/B25-732[»]
    ProteinModelPortaliB3PC73.
    SMRiB3PC73. Positions 25-732.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi498211.CJA_2887.

    Protein family/group databases

    CAZyiGH67. Glycoside Hydrolase Family 67.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiACE83468; ACE83468; CJA_2887.
    KEGGicja:CJA_2887.
    PATRICi21329159. VBICelJap122165_2845.

    Phylogenomic databases

    eggNOGiENOG4105D0H. Bacteria.
    COG3661. LUCA.
    HOGENOMiHOG000177796.
    KOiK01235.
    OMAiMVNPGHH.
    OrthoDBiEOG6J48K3.

    Enzyme and pathway databases

    BioCyciCJAP498211:GHIT-2878-MONOMER.
    BRENDAi3.2.1.139. 5103.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    3.30.379.10. 1 hit.
    3.90.1330.10. 1 hit.
    InterProiIPR029018. Chitobiase/Hex_dom_2-like.
    IPR011395. Glyco_hydro_67_aGlcAse.
    IPR005154. Glyco_hydro_67_aGlcAse_N.
    IPR011099. Glyco_hydro_67_C.
    IPR011100. Glyco_hydro_67_cat.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF07477. Glyco_hydro_67C. 1 hit.
    PF07488. Glyco_hydro_67M. 1 hit.
    PF03648. Glyco_hydro_67N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF029900. Alpha-glucuronds. 1 hit.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF55545. SSF55545. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The membrane-bound alpha-glucuronidase from Pseudomonas cellulosa hydrolyzes 4-O-methyl-D-glucuronoxylooligosaccharides but not 4-O-methyl-D-glucuronoxylan."
      Nagy T., Emami K., Fontes C.M., Ferreira L.M., Humphry D.R., Gilbert H.J.
      J. Bacteriol. 184:4925-4929(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, SUBUNIT.
    2. "Insights into plant cell wall degradation from the genome sequence of the soil bacterium Cellvibrio japonicus."
      DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H., Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J., Nelson K.E.
      J. Bacteriol. 190:5455-5463(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Ueda107.
    3. "The structural basis for catalysis and specificity of the Pseudomonas cellulosa alpha-glucuronidase, GlcA67A."
      Nurizzo D., Nagy T., Gilbert H.J., Davies G.J.
      Structure 10:547-556(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 25-732 IN COMPLEX WITH SUBSTRATE ANALOGS, FUNCTION, MUTAGENESIS OF GLU-312; ASP-385 AND GLU-413, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, REACTION MECHANISM, SUBUNIT.
    4. "The alpha-glucuronidase, GlcA67A, of Cellvibrio japonicus utilizes the carboxylate and methyl groups of aldobiouronic acid as important substrate recognition determinants."
      Nagy T., Nurizzo D., Davies G.J., Biely P., Lakey J.H., Bolam D.N., Gilbert H.J.
      J. Biol. Chem. 278:20286-20292(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 25-732 OF MUTANT ALA-312 IN COMPLEX WITH SUBSTRATE ANALOGS, FUNCTION, MUTAGENESIS OF TRP-180; VAL-230; ARG-345; LYS-380 AND TRP-563, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.

    Entry informationi

    Entry nameiAGUA_CELJU
    AccessioniPrimary (citable) accession number: B3PC73
    Secondary accession number(s): Q8VP74
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 2013
    Last sequence update: September 2, 2008
    Last modified: November 11, 2015
    This is version 48 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.