Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9AQS0

- XANLY_BACGL

UniProt

Q9AQS0 - XANLY_BACGL

Protein

Xanthan lyase

Gene

xly

Organism
Bacillus sp. (strain GL1)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Plays a role in xanthan depolymerization pathway by cleaving the linkage between the terminal mannosyl and glucuronyl residues of the side chain of xanthan to liberate pyruvylated mannose.3 Publications

    Catalytic activityi

    Eliminative cleavage of the terminal beta-D-mannosyl-(1->4)-beta-D-glucuronosyl linkage of the side-chain of the polysaccharide xanthan, leaving a 4-deoxy-alpha-L-threo-hex-4-enuronosyl group at the terminus of the side-chain.3 Publications

    Enzyme regulationi

    Highly specific for pyruvylated xanthan but not effective with hyaluronate, chondroitin A, gellan, heparin or pectin. Affinity for pyruvylated mannose is 400-fold stronger in comparison with mannose. Activated by Co2+ at 1 mM. Completely inhibited by Hg2+ but not affected by other divalent cations. Intensely inhibited by NaCl and KCl at 150 mM, in particular by the Na+ and K+ ions but not the Cl- ions. Partially inhibited by iodoacetamide and N-ethylmaleimide at 1 mM but not by dithiothreitol, reduced glutathione or 2-mercaptoethanol.3 Publications

    Kineticsi

    1. KM=0.25 mM for xanthan2 Publications

    pH dependencei

    Optimum pH is 5.5 (in the presence of sodium acetate). Active between pH 6.5 and 9.2 Publications

    Temperature dependencei

    Optimum temperature is 50 degrees Celsius. Stable at 4 degrees Celsius at pH 6.5 - 9. 60% loss of activity when incubated at 45 degrees Celsius and pH 7.0 for 10 minutes.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei148 – 1481Carbohydrate1 Publication
    Binding sitei148 – 1481Substrate 12 Publications
    Binding sitei246 – 2461Substrate 21 Publication
    Binding sitei255 – 2551Carbohydrate1 Publication
    Binding sitei255 – 2551Substrate 12 Publications
    Binding sitei309 – 3091Carbohydrate1 Publication
    Binding sitei309 – 3091Substrate 1 and 22 Publications
    Binding sitei313 – 3131Carbohydrate1 Publication
    Binding sitei424 – 4241Substrate 21 Publication
    Metal bindingi515 – 5151Calcium2 Publications
    Metal bindingi516 – 5161Calcium2 Publications
    Metal bindingi517 – 5171Calcium2 Publications
    Binding sitei612 – 6121Substrate 1 and 22 Publications
    Metal bindingi676 – 6761Calcium2 Publications

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. mannose binding Source: UniProtKB
    3. xanthan lyase activity Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Calcium, Metal-binding

    Protein family/group databases

    CAZyiPL8. Polysaccharide Lyase Family 8.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Xanthan lyaseImported (EC:4.2.2.121 Publication)
    Gene namesi
    Name:xlyImported
    OrganismiBacillus sp. (strain GL1)
    Taxonomic identifieri84635 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

    Subcellular locationi

    Secretedextracellular space 1 Publication

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi194 – 1941N → A: Loss of activity by 60%. 1 Publication
    Mutagenesisi246 – 2461H → A: Loss of activity by 60%. 1 Publication
    Mutagenesisi255 – 2551Y → F: Loss of activity by 50%. 1 Publication
    Mutagenesisi313 – 3131R → A: Reduced catalytic activity. 1 Publication
    Mutagenesisi315 – 3151Y → F: Negligible change in catalytic activity. 1 Publication
    Mutagenesisi612 – 6121R → A: Increased catalysis rate but decreased affinity with substrate. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 25251 PublicationAdd
    BLAST
    Chaini26 – 930905Xanthan lyaseSequence AnalysisPRO_0000417933Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.4 Publications

    Structurei

    Secondary structure

    1
    930
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi28 – 4114
    Turni43 – 453
    Helixi51 – 7020
    Helixi82 – 843
    Helixi90 – 10819
    Turni113 – 1164
    Helixi118 – 13417
    Beta strandi144 – 1463
    Helixi147 – 1515
    Helixi153 – 16412
    Helixi166 – 1683
    Helixi171 – 18414
    Helixi192 – 20918
    Helixi212 – 22110
    Beta strandi227 – 2293
    Beta strandi232 – 2376
    Beta strandi243 – 2453
    Turni246 – 2483
    Turni252 – 2543
    Helixi255 – 27016
    Helixi280 – 2834
    Helixi284 – 2918
    Helixi294 – 2963
    Helixi304 – 3063
    Helixi308 – 3125
    Helixi314 – 3163
    Helixi318 – 33215
    Turni333 – 3353
    Helixi340 – 35415
    Helixi360 – 3634
    Helixi366 – 37611
    Beta strandi389 – 3935
    Helixi394 – 3963
    Beta strandi398 – 4036
    Beta strandi406 – 4116
    Beta strandi415 – 4173
    Turni431 – 4344
    Beta strandi435 – 4417
    Turni445 – 4484
    Beta strandi449 – 4513
    Helixi452 – 4554
    Beta strandi465 – 4673
    Beta strandi474 – 4763
    Beta strandi482 – 4876
    Turni488 – 4903
    Beta strandi491 – 4999
    Beta strandi501 – 5033
    Beta strandi506 – 5138
    Beta strandi518 – 5269
    Beta strandi529 – 54113
    Beta strandi550 – 5523
    Beta strandi555 – 5573
    Beta strandi563 – 57513
    Beta strandi578 – 5825
    Beta strandi585 – 60420
    Helixi606 – 6083
    Beta strandi620 – 63415
    Beta strandi636 – 64611
    Helixi650 – 6589
    Beta strandi661 – 67616
    Turni677 – 6804
    Beta strandi681 – 6866
    Beta strandi688 – 6903
    Beta strandi692 – 6943
    Beta strandi697 – 71014
    Turni711 – 7133
    Beta strandi714 – 7207
    Beta strandi727 – 73610
    Beta strandi738 – 7436
    Beta strandi747 – 7515
    Beta strandi753 – 7619
    Beta strandi769 – 7768

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1J0MX-ray2.30A26-777[»]
    1J0NX-ray2.40A26-777[»]
    1X1HX-ray2.30A26-777[»]
    1X1IX-ray1.80A26-777[»]
    1X1JX-ray2.10A26-777[»]
    2E22X-ray2.40A26-777[»]
    2E24X-ray2.15A26-777[»]
    ProteinModelPortaliQ9AQS0.
    SMRiQ9AQS0. Positions 26-777.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9AQS0.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni146 – 1483Substrate binding1 Publication
    Regioni313 – 3153Substrate binding2 Publications

    Sequence similaritiesi

    Belongs to the polysaccharide lyase 8 family.Sequence Analysis

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di1.50.10.100. 1 hit.
    2.60.220.10. 1 hit.
    2.70.98.10. 1 hit.
    InterProiIPR008929. Chondroitin_lyas.
    IPR011013. Gal_mutarotase_SF_dom.
    IPR014718. Glyco_hydro-type_carb-bd_sub.
    IPR011071. Lyase_8-like_C.
    IPR012970. Lyase_8_alpha_N.
    IPR004103. Lyase_8_C.
    IPR003159. Lyase_8_central_dom.
    IPR012329. Lyase_8_N.
    [Graphical view]
    PfamiPF02278. Lyase_8. 1 hit.
    PF02884. Lyase_8_C. 1 hit.
    PF08124. Lyase_8_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF48230. SSF48230. 1 hit.
    SSF49863. SSF49863. 1 hit.
    SSF74650. SSF74650. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q9AQS0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSGILIAAL LMTLWGGWQP DIAHASDEFD ALRIKWATLL TGGPALDPAD    50
    SDIAARTDKL AQDANDYWED MDLSSSRTYI WYALRGNGTS DNVNAVYERL 100
    RTMALAATTV GSSLYGNADL KEDILDALDW LYVNSYNSTR SRSAYNWWHW 150
    QLGIPMSLND IAVLLYDDIS AARMATYMDT IDYFTPSIGL TGANRAWQAI 200
    VVGVRAVIVK DAVKLAAARN GLSGTGIFPY ATGGDGFYAD GSFVQHTTFA 250
    YTGGYGSSVL ETTANLMYLL SGSTWSVSDP NQSNVWQWIY EAYRPLLYKG 300
    AMMDMVRGRE ISRSYAQDHA VGHGIVASIV RLAQFAPAPH AAAFKQIAKR 350
    VIQEDTFSSF YGDVSTDTIR LAKAIVDDPS IAPAAAPNLY KQYAAMDRAV 400
    LQRPGFALGL ALYSTRISSY ESINSENGRG WYTGAGATYL YNQDLAQYSE 450
    DYWPTVDAYR IPGTTVASGT PIASGTGTSS WTGGVSLAGQ YGASGMDLSY 500
    GAYNLSARKS WFMFDDEIVA LGSGISSTAG IPIETVVDNR KLNGAGDNAW 550
    TANGAALSTG LGVAQTLTGV NWVHLAGNTA DGSDIGYYFP GGATLQTKRE 600
    ARTGTWKQIN NRPATPSTAV TRNYETMWID HGTNPSGASY GYVLLPNKTS 650
    AQVGAYAADP AIEIVVNTSG VQSVKEKTLG LVGANFWTDT TQTADLITSN 700
    KKASVMTREI ADERLEASVS DPTQANNGTI AIELARSAEG YSADPGITVT 750
    QLAPTIKFTV NVNGAKGKSF HASFQLGEDT SGPVDPGEPE LPSVIVDNAD 800
    SAGVTRTGTW KTASTQTDRY GANYLHDDNA GKGTKSVTFT PNLPIAGSYE 850
    VYLMWPAHFN REDAVQVDVG HASGTTRTAV DQRSGGGVWH SIGTYEFLAG 900
    SGGSVTIRND ALGSPDGYVV ADAVKFVAVG 930
    Length:930
    Mass (Da):99,313
    Last modified:June 1, 2001 - v1
    Checksum:i5E8B69D3E94019C4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB037178 Genomic DNA. Translation: BAB21059.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB037178 Genomic DNA. Translation: BAB21059.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1J0M X-ray 2.30 A 26-777 [» ]
    1J0N X-ray 2.40 A 26-777 [» ]
    1X1H X-ray 2.30 A 26-777 [» ]
    1X1I X-ray 1.80 A 26-777 [» ]
    1X1J X-ray 2.10 A 26-777 [» ]
    2E22 X-ray 2.40 A 26-777 [» ]
    2E24 X-ray 2.15 A 26-777 [» ]
    ProteinModelPortali Q9AQS0.
    SMRi Q9AQS0. Positions 26-777.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi PL8. Polysaccharide Lyase Family 8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q9AQS0.

    Family and domain databases

    Gene3Di 1.50.10.100. 1 hit.
    2.60.220.10. 1 hit.
    2.70.98.10. 1 hit.
    InterProi IPR008929. Chondroitin_lyas.
    IPR011013. Gal_mutarotase_SF_dom.
    IPR014718. Glyco_hydro-type_carb-bd_sub.
    IPR011071. Lyase_8-like_C.
    IPR012970. Lyase_8_alpha_N.
    IPR004103. Lyase_8_C.
    IPR003159. Lyase_8_central_dom.
    IPR012329. Lyase_8_N.
    [Graphical view ]
    Pfami PF02278. Lyase_8. 1 hit.
    PF02884. Lyase_8_C. 1 hit.
    PF08124. Lyase_8_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48230. SSF48230. 1 hit.
    SSF49863. SSF49863. 1 hit.
    SSF74650. SSF74650. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Polysaccharide lyase: molecular cloning, sequencing, and overexpression of the xanthan lyase gene of Bacillus sp. strain GL1."
      Hashimoto W., Miki H., Tsuchiya N., Nankai H., Murata K.
      Appl. Environ. Microbiol. 67:713-720(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-35; 315-323; 332-341 AND 374-383, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT.
    2. "Xanthan lyase of Bacillus sp. strain GL1 liberates pyruvylated mannose from xanthan side chains."
      Hashimoto W., Miki H., Tsuchiya N., Nankai H., Murata K.
      Appl. Environ. Microbiol. 64:3765-3768(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION.
    3. "Microbial system for polysaccharide depolymerization: enzymatic route for xanthan depolymerization by Bacillus sp. strain GL1."
      Nankai H., Hashimoto W., Miki H., Kawai S., Murata K.
      Appl. Environ. Microbiol. 65:2520-2526(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    4. "Crystal structure of Bacillus sp. GL1 xanthan lyase, which acts on the side chains of xanthan."
      Hashimoto W., Nankai H., Mikami B., Murata K.
      J. Biol. Chem. 278:7663-7673(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 26-777 IN COMPLEX WITH PYRUVYLATED MANNOSE AND CALCIUM.
    5. "Crystal structure of Bacillus sp. GL1 xanthan lyase complexed with a substrate: insights into the enzyme reaction mechanism."
      Maruyama Y., Hashimoto W., Mikami B., Murata K.
      J. Mol. Biol. 350:974-986(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF MUTANT ASN-194 IN COMPLEXES WITH PYRUVYLATED MANNOSE; PENTASACCHARIDE COMPLEX AND CALCIUM, MUTAGENESIS OF ASN-194; HIS-246 AND TYR-255, BIOPHYSICOCHEMICAL PROPERTIES.
    6. "A structural factor responsible for substrate recognition by Bacillus sp. GL1 xanthan lyase that acts specifically on pyruvated side chains of xanthan."
      Maruyama Y., Mikami B., Hashimoto W., Murata K.
      Biochemistry 46:781-791(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 26-777 IN COMPLEX WITH MANNOSE AND MUTANT ARG-612, MUTAGENESIS OF ARG-313; TYR-315 AND ARG-612, ENZYME REGULATION.

    Entry informationi

    Entry nameiXANLY_BACGL
    AccessioniPrimary (citable) accession number: Q9AQS0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 13, 2012
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 57 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The 99 kDa precursor is converted to a mature form (77 kDa) through the removal of a C-terminal (22 kDa) fragment without any loss in activity.Curated

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3