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G8JZS4

- SUSB_BACTN

UniProt

G8JZS4 - SUSB_BACTN

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: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 17 (01 Oct 2014)
      Sequence version 1 (25 Jan 2012)
      Previous versions | rss
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    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

    Binds 1 calcium 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-glucoside1 Publication

    pH dependencei

    Optimum pH is 6.5.1 Publication

    Pathwayi

    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

    1. alpha-1,4-glucosidase activity Source: MENGO
    2. calcium ion binding Source: UniProtKB
    3. glucan 1,4-alpha-glucosidase activity Source: UniProtKB

    GO - Biological processi

    1. starch catabolic process Source: UniProtKB

    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: Chromosome

    Subcellular locationi

    Periplasm 1 Publication

    GO - Cellular componenti

    1. periplasmic space Source: UniProtKB-SubCell
    2. plasma membrane Source: MENGO

    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

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    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

    OMAiPNGKHSA.
    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

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    MKKRKILSLI AFLCISFIAN AQQKLTSPDN NLVMTFQVDS KGAPTYELTY    50
    KNKVVIKPST LGLELKKEDN TRTDFDWVDR RDLTKLDSKT NLYDGFEVKD 100
    TQTATFDETW QPVWGEEKEI RNHYNELAVT LYQPMNDRSI VIRFRLFNDG 150
    LGFRYEFPQQ KSLNYFVIKE EHSQFGMNGD HIAFWIPGDY DTQEYDYTIS 200
    RLSEIRGLMK EAITPNSSQT PFSQTGVQTA LMMKTDDGLY INLHEAALVD 250
    YSCMHLNLDD KNMVFESWLT PDAKGDKGYM QTPCNTPWRT IIVSDDARNI 300
    LASRITLNLN EPCKIADAAS WVKPVKYIGV WWDMITGKGS WAYTDELTSV 350
    KLGETDYSKT KPNGKHSANT ANVKRYIDFA AAHGFDAVLV EGWNEGWEDW 400
    FGNSKDYVFD FVTPYPDFDV KEIHRYAARK GIKMMMHHET SASVRNYERH 450
    MDKAYQFMAD NGYNSVKSGY VGNIIPRGEH HYGQWMNNHY LYAVKKAADY 500
    KIMVNAHEAT RPTGICRTYP NLIGNESARG TEYESFGGNK VYHTTILPFT 550
    RLVGGPMDYT PGIFETHCNK MNPANNSQVR STIARQLALY VTMYSPLQMA 600
    ADIPENYERF MDAFQFIKDV ALDWDETNYL EAEPGEYITI ARKAKDTDDW 650
    YVGCTAGENG HTSKLVFDFL TPGKQYIATV YADAKDADWK ENPQAYTIKK 700
    GILTNKSKLN LHAANGGGYA ISIKEVKDKS EAKGLKRL 738
    Length:738
    Mass (Da):84,378
    Last modified:January 25, 2012 - v1
    Checksum:i2BFE87C3552C9A12
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U66897 Genomic DNA. Translation: AAC44671.1.
    AE015928 Genomic DNA. Translation: AAO78808.1.
    RefSeqiNP_812614.1. NC_004663.1.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U66897 Genomic DNA. Translation: AAC44671.1 .
    AE015928 Genomic DNA. Translation: AAO78808.1 .
    RefSeqi NP_812614.1. NC_004663.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2D73 X-ray 1.60 A/B 22-738 [» ]
    2JKA X-ray 1.90 A/B 22-738 [» ]
    2JKE X-ray 1.70 A/B 22-738 [» ]
    2JKP X-ray 1.99 A/B 22-738 [» ]
    2ZQ0 X-ray 1.60 A/B 22-738 [» ]
    ProteinModelPortali G8JZS4.
    SMRi G8JZS4. Positions 22-738.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAO78808 ; AAO78808 ; BT_3703 .
    GeneIDi 1072064.
    KEGGi bth:BT_3703.

    Phylogenomic databases

    OMAi PNGKHSA.
    OrthoDBi EOG6Z3KGW.

    Enzyme and pathway databases

    UniPathwayi UPA00153 .
    BioCyci BTHE226186:GJXV-3769-MONOMER.

    Family and domain databases

    InterProi IPR029483. GH97_C.
    IPR019563. GH97_catalytic.
    IPR029486. GH97_N.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF14509. GH97_C. 1 hit.
    PF14508. GH97_N. 1 hit.
    PF10566. Glyco_hydro_97. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 17 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