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Protein

Glucan 1,4-alpha-glucosidase SusB

Gene

susB

Organism
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Glucoamylase that hydrolyzes alpha-1,4-glucosidic linkages, alpha-1,6-, alpha-1,3- and alpha-1,2-glucosidic linkages during starch degradation.2 Publications

Catalytic activityi

Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.1 Publication

Cofactori

Ca2+1 PublicationNote: Binds 1 Ca2+ ion per subunit.1 Publication

Kineticsi

  1. KM=1.05 mM for maltose1 Publication
  2. KM=0.29 mM for maltotriose1 Publication
  3. KM=0.64 mM for maltotetraose1 Publication
  4. KM=1.29 mM for maltopentaose1 Publication
  5. KM=2.71 mM for maltohexaose1 Publication
  6. KM=4.58 mM for maltoheptaose1 Publication
  7. KM=6.89 mM for amylose DP171 Publication
  8. KM=0.67 mM for soluble starch1 Publication
  9. KM=2.39 mM for kojibiose1 Publication
  10. KM=3.14 mM for nigerose1 Publication
  11. KM=6.34 mM for isomaltose1 Publication
  12. KM=0.31 mM for panose1 Publication
  13. KM=0.16 mM for p-nitrophenyl alpha-glucoside. Note=kcat is 182 sec(-1) for maltose. kcat is 270 sec(-1) for maltotriose. kcat is 321 sec(-1) for maltotetraose. kcat is 434 sec(-1) for maltopentaose. kcat is 346 sec(-1) for maltohexaose. kcat is 381 sec(-1) for maltoheptaose. kcat is 321 sec(-1) for amylose DP17. kcat is 115 sec(-1) for soluble starch. kcat is 141 sec(-1) for kojibiose. kcat is 207 sec(-1) for nigerose. kcat is 105 sec(-1) for isomaltose. kcat is 160 sec(-1) for panose. kcat is 161 sec(-1) for p-nitrophenyl alpha-glucoside.1 Publication

    pH dependencei

    Optimum pH is 6.5.1 Publication

    Pathway: starch degradation

    This protein is involved in the pathway starch degradation, which is part of Glycan degradation.
    View all proteins of this organism that are known to be involved in the pathway starch degradation and in Glycan degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi194 – 1941Calcium1 Publication
    Sitei194 – 1941Substrate
    Sitei331 – 3311Substrate
    Sitei467 – 4671Substrate
    Metal bindingi508 – 5081Calcium1 Publication
    Metal bindingi526 – 5261Calcium1 Publication
    Active sitei532 – 5321Proton donor/proton acceptor1 Publication
    Metal bindingi532 – 5321Calcium1 Publication

    GO - Molecular functioni

    • alpha-1,4-glucosidase activity Source: MENGO
    • calcium ion binding Source: UniProtKB
    • glucan 1,4-alpha-glucosidase activity Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BioCyciBTHE226186:GJXV-3769-MONOMER.
    UniPathwayiUPA00153.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucan 1,4-alpha-glucosidase SusB (EC:3.2.1.3)
    Alternative name(s):
    Alpha-glucosidase SusB
    Glucoamylase SusB
    Starch-utilization system protein B
    Gene namesi
    Name:susB
    Ordered Locus Names:BT_3703
    OrganismiBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
    Taxonomic identifieri226186 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
    ProteomesiUP000001414 Componenti: Chromosome

    Subcellular locationi

    • Periplasm 1 Publication

    GO - Cellular componenti

    • periplasmic space Source: UniProtKB-SubCell
    • plasma membrane Source: MENGO
    Complete GO annotation...

    Keywords - Cellular componenti

    Periplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi439 – 4391E → Q: Abolishes enzyme activity. 1 Publication
    Mutagenesisi508 – 5081E → Q: Abolishes enzyme activity. 1 Publication
    Mutagenesisi532 – 5321E → Q: Abolishes enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 738717Glucan 1,4-alpha-glucosidase SusBPRO_0000425886Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi226186.BT_3703.

    Structurei

    Secondary structure

    1
    738
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi23 – 264Combined sources
    Beta strandi32 – 387Combined sources
    Beta strandi44 – 507Combined sources
    Beta strandi53 – 608Combined sources
    Beta strandi63 – 653Combined sources
    Helixi88 – 903Combined sources
    Beta strandi91 – 955Combined sources
    Beta strandi97 – 11014Combined sources
    Beta strandi113 – 1186Combined sources
    Beta strandi120 – 13314Combined sources
    Helixi134 – 1363Combined sources
    Beta strandi138 – 14710Combined sources
    Beta strandi150 – 1578Combined sources
    Beta strandi163 – 1719Combined sources
    Beta strandi174 – 1763Combined sources
    Beta strandi182 – 1854Combined sources
    Beta strandi189 – 1913Combined sources
    Beta strandi198 – 2014Combined sources
    Helixi202 – 2043Combined sources
    Helixi205 – 2128Combined sources
    Beta strandi229 – 2346Combined sources
    Beta strandi240 – 2467Combined sources
    Beta strandi254 – 2596Combined sources
    Turni260 – 2634Combined sources
    Beta strandi264 – 2696Combined sources
    Beta strandi279 – 2857Combined sources
    Beta strandi288 – 2969Combined sources
    Helixi297 – 3026Combined sources
    Helixi305 – 3084Combined sources
    Helixi318 – 3214Combined sources
    Beta strandi325 – 3306Combined sources
    Helixi332 – 3354Combined sources
    Beta strandi338 – 3414Combined sources
    Beta strandi343 – 3464Combined sources
    Turni352 – 3543Combined sources
    Helixi357 – 3593Combined sources
    Helixi370 – 38213Combined sources
    Beta strandi386 – 3905Combined sources
    Helixi397 – 3993Combined sources
    Beta strandi401 – 4033Combined sources
    Helixi420 – 42910Combined sources
    Beta strandi433 – 4397Combined sources
    Helixi444 – 46017Combined sources
    Beta strandi465 – 4695Combined sources
    Helixi484 – 49916Combined sources
    Beta strandi503 – 5064Combined sources
    Helixi515 – 5173Combined sources
    Beta strandi522 – 5254Combined sources
    Helixi531 – 5355Combined sources
    Helixi543 – 5453Combined sources
    Helixi547 – 5493Combined sources
    Turni550 – 5545Combined sources
    Helixi568 – 5703Combined sources
    Helixi583 – 59210Combined sources
    Beta strandi596 – 5994Combined sources
    Helixi604 – 6074Combined sources
    Helixi611 – 6199Combined sources
    Beta strandi622 – 63312Combined sources
    Turni634 – 6363Combined sources
    Beta strandi637 – 6448Combined sources
    Beta strandi650 – 6567Combined sources
    Beta strandi661 – 6666Combined sources
    Beta strandi676 – 6838Combined sources
    Turni689 – 6913Combined sources
    Beta strandi696 – 7038Combined sources
    Beta strandi708 – 7136Combined sources
    Beta strandi718 – 7258Combined sources
    Helixi729 – 7313Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2D73X-ray1.60A/B22-738[»]
    2JKAX-ray1.90A/B22-738[»]
    2JKEX-ray1.70A/B22-738[»]
    2JKPX-ray1.99A/B22-738[»]
    2ZQ0X-ray1.60A/B22-738[»]
    3WFAX-ray2.00A/B22-738[»]
    ProteinModelPortaliG8JZS4.
    SMRiG8JZS4. Positions 22-738.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni215 – 2173Substrate binding
    Regioni437 – 4393Substrate binding
    Regioni507 – 5082Substrate binding

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 97 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000291494.
    OMAiKMIMHHE.
    OrthoDBiEOG6Z3KGW.

    Family and domain databases

    InterProiIPR029483. GH97_C.
    IPR019563. GH97_catalytic.
    IPR029486. GH97_N.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF14509. GH97_C. 1 hit.
    PF14508. GH97_N. 1 hit.
    PF10566. Glyco_hydro_97. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    G8JZS4-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKKRKILSLI AFLCISFIAN AQQKLTSPDN NLVMTFQVDS KGAPTYELTY
    60 70 80 90 100
    KNKVVIKPST LGLELKKEDN TRTDFDWVDR RDLTKLDSKT NLYDGFEVKD
    110 120 130 140 150
    TQTATFDETW QPVWGEEKEI RNHYNELAVT LYQPMNDRSI VIRFRLFNDG
    160 170 180 190 200
    LGFRYEFPQQ KSLNYFVIKE EHSQFGMNGD HIAFWIPGDY DTQEYDYTIS
    210 220 230 240 250
    RLSEIRGLMK EAITPNSSQT PFSQTGVQTA LMMKTDDGLY INLHEAALVD
    260 270 280 290 300
    YSCMHLNLDD KNMVFESWLT PDAKGDKGYM QTPCNTPWRT IIVSDDARNI
    310 320 330 340 350
    LASRITLNLN EPCKIADAAS WVKPVKYIGV WWDMITGKGS WAYTDELTSV
    360 370 380 390 400
    KLGETDYSKT KPNGKHSANT ANVKRYIDFA AAHGFDAVLV EGWNEGWEDW
    410 420 430 440 450
    FGNSKDYVFD FVTPYPDFDV KEIHRYAARK GIKMMMHHET SASVRNYERH
    460 470 480 490 500
    MDKAYQFMAD NGYNSVKSGY VGNIIPRGEH HYGQWMNNHY LYAVKKAADY
    510 520 530 540 550
    KIMVNAHEAT RPTGICRTYP NLIGNESARG TEYESFGGNK VYHTTILPFT
    560 570 580 590 600
    RLVGGPMDYT PGIFETHCNK MNPANNSQVR STIARQLALY VTMYSPLQMA
    610 620 630 640 650
    ADIPENYERF MDAFQFIKDV ALDWDETNYL EAEPGEYITI ARKAKDTDDW
    660 670 680 690 700
    YVGCTAGENG HTSKLVFDFL TPGKQYIATV YADAKDADWK ENPQAYTIKK
    710 720 730
    GILTNKSKLN LHAANGGGYA ISIKEVKDKS EAKGLKRL
    Length:738
    Mass (Da):84,378
    Last modified:January 25, 2012 - v1
    Checksum:i2BFE87C3552C9A12
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U66897 Genomic DNA. Translation: AAC44671.1.
    AE015928 Genomic DNA. Translation: AAO78808.1.
    RefSeqiNP_812614.1. NC_004663.1.
    WP_008767003.1. NC_004663.1.

    Genome annotation databases

    EnsemblBacteriaiAAO78808; AAO78808; BT_3703.
    GeneIDi1072064.
    KEGGibth:BT_3703.
    PATRICi21062407. VBIBacThe70966_3763.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U66897 Genomic DNA. Translation: AAC44671.1.
    AE015928 Genomic DNA. Translation: AAO78808.1.
    RefSeqiNP_812614.1. NC_004663.1.
    WP_008767003.1. NC_004663.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2D73X-ray1.60A/B22-738[»]
    2JKAX-ray1.90A/B22-738[»]
    2JKEX-ray1.70A/B22-738[»]
    2JKPX-ray1.99A/B22-738[»]
    2ZQ0X-ray1.60A/B22-738[»]
    3WFAX-ray2.00A/B22-738[»]
    ProteinModelPortaliG8JZS4.
    SMRiG8JZS4. Positions 22-738.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi226186.BT_3703.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAO78808; AAO78808; BT_3703.
    GeneIDi1072064.
    KEGGibth:BT_3703.
    PATRICi21062407. VBIBacThe70966_3763.

    Phylogenomic databases

    HOGENOMiHOG000291494.
    OMAiKMIMHHE.
    OrthoDBiEOG6Z3KGW.

    Enzyme and pathway databases

    UniPathwayiUPA00153.
    BioCyciBTHE226186:GJXV-3769-MONOMER.

    Miscellaneous databases

    PROiG8JZS4.

    Family and domain databases

    InterProiIPR029483. GH97_C.
    IPR019563. GH97_catalytic.
    IPR029486. GH97_N.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF14509. GH97_C. 1 hit.
    PF14508. GH97_N. 1 hit.
    PF10566. Glyco_hydro_97. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Contribution of a neopullulanase, a pullulanase, and an alpha-glucosidase to growth of Bacteroides thetaiotaomicron on starch."
      D'Elia J.N., Salyers A.A.
      J. Bacteriol. 178:7173-7179(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
      Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.
    2. "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
      Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
      Science 299:2074-2076(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.
    3. "Structural and functional analysis of a glycoside hydrolase family 97 enzyme from Bacteroides thetaiotaomicron."
      Kitamura M., Okuyama M., Tanzawa F., Mori H., Kitago Y., Watanabe N., Kimura A., Tanaka I., Yao M.
      J. Biol. Chem. 283:36328-36337(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 22-738 IN COMPLEX WITH CALCIUM AND ACARBOSE, FUNCTION, ACTIVE SITE, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF GLU-439; GLU-508 AND GLU-532.

    Entry informationi

    Entry nameiSUSB_BACTN
    AccessioniPrimary (citable) accession number: G8JZS4
    Secondary accession number(s): P71094, Q7C3Z2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 19, 2014
    Last sequence update: January 25, 2012
    Last modified: May 27, 2015
    This is version 24 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    Although initially defined as an alpha-glucosidase, it produces beta-glucose by an inverting mechanism, suggesting it rather acts as a glucan 1,4-alpha-glucosidase.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference 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

    External Data

    Dasty 3

    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 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.