Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Xanthan lyase

Gene

xly

Organism
Bacillus sp. (strain GL1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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)DescriptionActionsGraphical viewLength
    Binding sitei148Carbohydrate1 Publication1
    Binding sitei148Substrate 12 Publications1
    Binding sitei246Substrate 21 Publication1
    Binding sitei255Carbohydrate1 Publication1
    Binding sitei255Substrate 12 Publications1
    Binding sitei309Carbohydrate1 Publication1
    Binding sitei309Substrate 1 and 22 Publications1
    Binding sitei313Carbohydrate1 Publication1
    Binding sitei424Substrate 21 Publication1
    Metal bindingi515Calcium2 Publications1
    Metal bindingi516Calcium2 Publications1
    Metal bindingi517Calcium2 Publications1
    Binding sitei612Substrate 1 and 22 Publications1
    Metal bindingi676Calcium2 Publications1

    GO - Molecular functioni

    • calcium ion binding Source: UniProtKB
    • mannose binding Source: UniProtKB
    • xanthan lyase activity Source: UniProtKB

    GO - Biological processi

    • polysaccharide metabolic process Source: UniProtKB
    Complete GO annotation...

    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

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi194N → A: Loss of activity by 60%. 1 Publication1
    Mutagenesisi246H → A: Loss of activity by 60%. 1 Publication1
    Mutagenesisi255Y → F: Loss of activity by 50%. 1 Publication1
    Mutagenesisi313R → A: Reduced catalytic activity. 1 Publication1
    Mutagenesisi315Y → F: Negligible change in catalytic activity. 1 Publication1
    Mutagenesisi612R → A: Increased catalysis rate but decreased affinity with substrate. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 251 PublicationAdd BLAST25
    ChainiPRO_000041793326 – 930Xanthan lyaseSequence analysisAdd BLAST905

    Interactioni

    Subunit structurei

    Monomer.4 Publications

    Structurei

    Secondary structure

    1930
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi28 – 41Combined sources14
    Turni43 – 45Combined sources3
    Helixi51 – 70Combined sources20
    Helixi82 – 84Combined sources3
    Helixi90 – 108Combined sources19
    Turni113 – 116Combined sources4
    Helixi118 – 134Combined sources17
    Beta strandi144 – 146Combined sources3
    Helixi147 – 151Combined sources5
    Helixi153 – 164Combined sources12
    Helixi166 – 168Combined sources3
    Helixi171 – 184Combined sources14
    Helixi192 – 209Combined sources18
    Helixi212 – 221Combined sources10
    Beta strandi227 – 229Combined sources3
    Beta strandi232 – 237Combined sources6
    Beta strandi243 – 245Combined sources3
    Turni246 – 248Combined sources3
    Turni252 – 254Combined sources3
    Helixi255 – 270Combined sources16
    Helixi280 – 283Combined sources4
    Helixi284 – 291Combined sources8
    Helixi294 – 296Combined sources3
    Helixi304 – 306Combined sources3
    Helixi308 – 312Combined sources5
    Helixi314 – 316Combined sources3
    Helixi318 – 332Combined sources15
    Turni333 – 335Combined sources3
    Helixi340 – 354Combined sources15
    Helixi360 – 363Combined sources4
    Helixi366 – 376Combined sources11
    Beta strandi389 – 393Combined sources5
    Helixi394 – 396Combined sources3
    Beta strandi398 – 403Combined sources6
    Beta strandi406 – 411Combined sources6
    Beta strandi415 – 417Combined sources3
    Turni431 – 434Combined sources4
    Beta strandi435 – 441Combined sources7
    Turni445 – 448Combined sources4
    Beta strandi449 – 451Combined sources3
    Helixi452 – 455Combined sources4
    Beta strandi465 – 467Combined sources3
    Beta strandi474 – 476Combined sources3
    Beta strandi482 – 487Combined sources6
    Turni488 – 490Combined sources3
    Beta strandi491 – 499Combined sources9
    Beta strandi501 – 503Combined sources3
    Beta strandi506 – 513Combined sources8
    Beta strandi518 – 526Combined sources9
    Beta strandi529 – 541Combined sources13
    Beta strandi550 – 552Combined sources3
    Beta strandi555 – 557Combined sources3
    Beta strandi563 – 575Combined sources13
    Beta strandi578 – 582Combined sources5
    Beta strandi585 – 604Combined sources20
    Helixi606 – 608Combined sources3
    Beta strandi620 – 634Combined sources15
    Beta strandi636 – 646Combined sources11
    Helixi650 – 658Combined sources9
    Beta strandi661 – 676Combined sources16
    Turni677 – 680Combined sources4
    Beta strandi681 – 686Combined sources6
    Beta strandi688 – 690Combined sources3
    Beta strandi692 – 694Combined sources3
    Beta strandi697 – 710Combined sources14
    Turni711 – 713Combined sources3
    Beta strandi714 – 720Combined sources7
    Beta strandi727 – 736Combined sources10
    Beta strandi738 – 743Combined sources6
    Beta strandi747 – 751Combined sources5
    Beta strandi753 – 761Combined sources9
    Beta strandi769 – 776Combined sources8

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ9AQS0.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni146 – 148Substrate binding1 Publication3
    Regioni313 – 315Substrate binding2 Publications3

    Sequence similaritiesi

    Belongs to the polysaccharide lyase 8 family.Sequence analysis

    Keywords - Domaini

    Signal

    Family and domain databases

    CDDicd14488. CBM6-CBM35-CBM36_like_2. 1 hit.
    Gene3Di1.50.10.100. 1 hit.
    2.60.220.10. 1 hit.
    2.70.98.10. 1 hit.
    InterProiIPR033803. CBM6/CBM35/CBM36-like_2.
    IPR008929. Chondroitin_lyas.
    IPR011013. Gal_mutarotase_SF_dom.
    IPR014718. GH-type_carb-bd.
    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

            10         20         30         40         50
    MLSGILIAAL LMTLWGGWQP DIAHASDEFD ALRIKWATLL TGGPALDPAD
    60 70 80 90 100
    SDIAARTDKL AQDANDYWED MDLSSSRTYI WYALRGNGTS DNVNAVYERL
    110 120 130 140 150
    RTMALAATTV GSSLYGNADL KEDILDALDW LYVNSYNSTR SRSAYNWWHW
    160 170 180 190 200
    QLGIPMSLND IAVLLYDDIS AARMATYMDT IDYFTPSIGL TGANRAWQAI
    210 220 230 240 250
    VVGVRAVIVK DAVKLAAARN GLSGTGIFPY ATGGDGFYAD GSFVQHTTFA
    260 270 280 290 300
    YTGGYGSSVL ETTANLMYLL SGSTWSVSDP NQSNVWQWIY EAYRPLLYKG
    310 320 330 340 350
    AMMDMVRGRE ISRSYAQDHA VGHGIVASIV RLAQFAPAPH AAAFKQIAKR
    360 370 380 390 400
    VIQEDTFSSF YGDVSTDTIR LAKAIVDDPS IAPAAAPNLY KQYAAMDRAV
    410 420 430 440 450
    LQRPGFALGL ALYSTRISSY ESINSENGRG WYTGAGATYL YNQDLAQYSE
    460 470 480 490 500
    DYWPTVDAYR IPGTTVASGT PIASGTGTSS WTGGVSLAGQ YGASGMDLSY
    510 520 530 540 550
    GAYNLSARKS WFMFDDEIVA LGSGISSTAG IPIETVVDNR KLNGAGDNAW
    560 570 580 590 600
    TANGAALSTG LGVAQTLTGV NWVHLAGNTA DGSDIGYYFP GGATLQTKRE
    610 620 630 640 650
    ARTGTWKQIN NRPATPSTAV TRNYETMWID HGTNPSGASY GYVLLPNKTS
    660 670 680 690 700
    AQVGAYAADP AIEIVVNTSG VQSVKEKTLG LVGANFWTDT TQTADLITSN
    710 720 730 740 750
    KKASVMTREI ADERLEASVS DPTQANNGTI AIELARSAEG YSADPGITVT
    760 770 780 790 800
    QLAPTIKFTV NVNGAKGKSF HASFQLGEDT SGPVDPGEPE LPSVIVDNAD
    810 820 830 840 850
    SAGVTRTGTW KTASTQTDRY GANYLHDDNA GKGTKSVTFT PNLPIAGSYE
    860 870 880 890 900
    VYLMWPAHFN REDAVQVDVG HASGTTRTAV DQRSGGGVWH SIGTYEFLAG
    910 920 930
    SGGSVTIRND ALGSPDGYVV ADAVKFVAVG
    Length:930
    Mass (Da):99,313
    Last modified:June 1, 2001 - v1
    Checksum:i5E8B69D3E94019C4
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB037178 Genomic DNA. Translation: BAB21059.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB037178 Genomic DNA. Translation: BAB21059.1.

    3D structure databases

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

    Protein family/group databases

    CAZyiPL8. Polysaccharide Lyase Family 8.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9AQS0.

    Family and domain databases

    CDDicd14488. CBM6-CBM35-CBM36_like_2. 1 hit.
    Gene3Di1.50.10.100. 1 hit.
    2.60.220.10. 1 hit.
    2.70.98.10. 1 hit.
    InterProiIPR033803. CBM6/CBM35/CBM36-like_2.
    IPR008929. Chondroitin_lyas.
    IPR011013. Gal_mutarotase_SF_dom.
    IPR014718. GH-type_carb-bd.
    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.
    ProtoNetiSearch...

    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: November 30, 2016
    This is version 70 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

    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.