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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)DescriptionActionsGraphical viewLength
    Sitei180Participates in a stacking interactions with the sugar rings of 4-O-MeGlcA1
    Binding sitei231beta-D-glucuronic acid1
    Binding sitei308Substrate1
    Active sitei312Proton donor1 Publication1
    Binding sitei345Substrate1
    Binding sitei356Substrate1
    Binding sitei380Substrate1
    Active sitei385Proton acceptor1 Publication1
    Binding sitei407SubstrateBy similarity1
    Active sitei413Proton acceptor1 Publication1
    Binding sitei541Substrate1
    Binding sitei563Substrate1
    Sitei563Participates in a stacking interactions with the sugar rings of 4-O-MeGlcA1

    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

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi180W → A: Greatly reduced the glucuronosidase activity. 1 Publication1
    Mutagenesisi230V → A: No influence on the glucuronosidase activity. 1 Publication1
    Mutagenesisi230V → G: Little influence on the glucuronosidase activity. 1 Publication1
    Mutagenesisi230V → N: Considerabely less active than wild-type. 1 Publication1
    Mutagenesisi230V → S: Considerabely less active than wild-type. 1 Publication1
    Mutagenesisi308K → A: Greatly reduced the glucuronosidase activity. 1
    Mutagenesisi312E → A: Loss of glucuronosidase activity. 1 Publication1
    Mutagenesisi312E → C: Loss of glucuronosidase activity. 1 Publication1
    Mutagenesisi345R → A: Loss of glucuronosidase activity. 1 Publication1
    Mutagenesisi380K → A: Greatly reduced the glucuronosidase activity. 1 Publication1
    Mutagenesisi385D → A: Loss of glucuronosidase activity. 1 Publication1
    Mutagenesisi385D → C: Loss of glucuronosidase activity. 1 Publication1
    Mutagenesisi413E → A: Loss of glucuronosidase activity. 1 Publication1
    Mutagenesisi413E → C: Retains 20% of the of glucuronosidase activity. 1 Publication1
    Mutagenesisi563W → A: Greatly reduced the glucuronosidase activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 20Sequence analysisAdd BLAST20
    ChainiPRO_000042217621 – 732Extracellular xylan exo-alpha-(1->2)-glucuronosidaseAdd BLAST712

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Protein-protein interaction databases

    STRINGi498211.CJA_2887.

    Structurei

    Secondary structure

    1732
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni28 – 31Combined sources4
    Helixi40 – 49Combined sources10
    Beta strandi51 – 55Combined sources5
    Helixi60 – 77Combined sources18
    Beta strandi90 – 96Combined sources7
    Turni98 – 100Combined sources3
    Helixi102 – 106Combined sources5
    Helixi111 – 114Combined sources4
    Turni115 – 119Combined sources5
    Beta strandi121 – 128Combined sources8
    Beta strandi131 – 140Combined sources10
    Helixi141 – 156Combined sources16
    Beta strandi165 – 168Combined sources4
    Beta strandi173 – 178Combined sources6
    Helixi199 – 201Combined sources3
    Turni202 – 204Combined sources3
    Helixi208 – 218Combined sources11
    Turni219 – 221Combined sources3
    Beta strandi224 – 226Combined sources3
    Helixi234 – 237Combined sources4
    Helixi239 – 252Combined sources14
    Helixi253 – 255Combined sources3
    Beta strandi258 – 263Combined sources6
    Helixi267 – 270Combined sources4
    Helixi282 – 298Combined sources17
    Beta strandi304 – 307Combined sources4
    Helixi317 – 320Combined sources4
    Helixi324 – 335Combined sources12
    Helixi336 – 338Combined sources3
    Beta strandi341 – 345Combined sources5
    Helixi356 – 358Combined sources3
    Helixi359 – 364Combined sources6
    Helixi365 – 367Combined sources3
    Beta strandi375 – 386Combined sources12
    Helixi395 – 398Combined sources4
    Beta strandi400 – 409Combined sources10
    Turni413 – 419Combined sources7
    Helixi425 – 432Combined sources8
    Helixi445 – 450Combined sources6
    Beta strandi452 – 454Combined sources3
    Beta strandi460 – 464Combined sources5
    Beta strandi473 – 476Combined sources4
    Helixi479 – 491Combined sources13
    Helixi497 – 508Combined sources12
    Helixi513 – 532Combined sources20
    Turni545 – 547Combined sources3
    Beta strandi549 – 551Combined sources3
    Helixi561 – 563Combined sources3
    Helixi566 – 569Combined sources4
    Beta strandi573 – 576Combined sources4
    Turni582 – 585Combined sources4
    Helixi587 – 590Combined sources4
    Helixi593 – 600Combined sources8
    Turni602 – 604Combined sources3
    Helixi607 – 612Combined sources6
    Helixi628 – 651Combined sources24
    Helixi652 – 656Combined sources5
    Helixi659 – 691Combined sources33
    Helixi706 – 715Combined sources10
    Beta strandi721 – 723Combined sources3
    Helixi724 – 727Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni188 – 189Substrate binding2

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 67 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG4105D0H. Bacteria.
    COG3661. LUCA.
    HOGENOMiHOG000177796.
    KOiK01235.
    OMAiMVNPGHH.
    OrthoDBiPOG091H2EIW.

    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
    PDB 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.
    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.
    OrthoDBiPOG091H2EIW.

    Enzyme and pathway databases

    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...

    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 2, 2016
    This is version 51 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.