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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

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

Manual assertion based on experiment ini

  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-glucoside1 Publication

    pH dependencei

    Optimum pH is 6.5.1 Publication

    Pathwayi: 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)DescriptionActionsGraphical viewLength
    Metal bindingi194Calcium1 Publication1
    Sitei194Substrate1
    Sitei331Substrate1
    Sitei467Substrate1
    Metal bindingi508Calcium1 Publication1
    Metal bindingi526Calcium1 Publication1
    Active sitei532Proton donor/proton acceptor1 Publication1
    Metal bindingi532Calcium1 Publication1

    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

    SABIO-RKG8JZS4.
    UniPathwayiUPA00153.

    Protein family/group databases

    CAZyiGH97. Glycoside Hydrolase Family 97.

    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
    Proteomesi
    • UP000001414 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)DescriptionActionsGraphical viewLength
    Mutagenesisi439E → Q: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi508E → Q: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi532E → Q: Abolishes enzyme activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 21Sequence analysisAdd BLAST21
    ChainiPRO_000042588622 – 738Glucan 1,4-alpha-glucosidase SusBAdd BLAST717

    Proteomic databases

    PaxDbiG8JZS4.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi226186.BT_3703.

    Structurei

    Secondary structure

    1738
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi23 – 26Combined sources4
    Beta strandi32 – 38Combined sources7
    Beta strandi44 – 50Combined sources7
    Beta strandi53 – 60Combined sources8
    Beta strandi63 – 65Combined sources3
    Helixi88 – 90Combined sources3
    Beta strandi91 – 95Combined sources5
    Beta strandi97 – 110Combined sources14
    Beta strandi113 – 118Combined sources6
    Beta strandi120 – 133Combined sources14
    Helixi134 – 136Combined sources3
    Beta strandi138 – 147Combined sources10
    Beta strandi150 – 157Combined sources8
    Beta strandi163 – 171Combined sources9
    Beta strandi174 – 176Combined sources3
    Beta strandi182 – 185Combined sources4
    Beta strandi189 – 191Combined sources3
    Beta strandi198 – 201Combined sources4
    Helixi202 – 204Combined sources3
    Helixi205 – 212Combined sources8
    Beta strandi229 – 234Combined sources6
    Beta strandi240 – 246Combined sources7
    Beta strandi254 – 259Combined sources6
    Turni260 – 263Combined sources4
    Beta strandi264 – 269Combined sources6
    Beta strandi279 – 285Combined sources7
    Beta strandi288 – 296Combined sources9
    Helixi297 – 302Combined sources6
    Helixi305 – 308Combined sources4
    Helixi318 – 321Combined sources4
    Beta strandi325 – 330Combined sources6
    Helixi332 – 335Combined sources4
    Beta strandi338 – 341Combined sources4
    Beta strandi343 – 346Combined sources4
    Turni352 – 354Combined sources3
    Helixi357 – 359Combined sources3
    Helixi370 – 382Combined sources13
    Beta strandi386 – 390Combined sources5
    Helixi397 – 399Combined sources3
    Beta strandi401 – 403Combined sources3
    Helixi420 – 429Combined sources10
    Beta strandi433 – 439Combined sources7
    Helixi444 – 460Combined sources17
    Beta strandi465 – 469Combined sources5
    Helixi484 – 499Combined sources16
    Beta strandi503 – 506Combined sources4
    Helixi515 – 517Combined sources3
    Beta strandi522 – 525Combined sources4
    Helixi531 – 535Combined sources5
    Helixi543 – 545Combined sources3
    Helixi547 – 549Combined sources3
    Turni550 – 554Combined sources5
    Helixi568 – 570Combined sources3
    Helixi583 – 592Combined sources10
    Beta strandi596 – 599Combined sources4
    Helixi604 – 607Combined sources4
    Helixi611 – 619Combined sources9
    Beta strandi622 – 633Combined sources12
    Turni634 – 636Combined sources3
    Beta strandi637 – 644Combined sources8
    Beta strandi650 – 656Combined sources7
    Beta strandi661 – 666Combined sources6
    Beta strandi676 – 683Combined sources8
    Turni689 – 691Combined sources3
    Beta strandi696 – 703Combined sources8
    Beta strandi708 – 713Combined sources6
    Beta strandi718 – 725Combined sources8
    Helixi729 – 731Combined sources3

    3D structure databases

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

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni215 – 217Substrate binding3
    Regioni437 – 439Substrate binding3
    Regioni507 – 508Substrate binding2

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 97 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000291494.
    OMAiVWWDMIT.
    OrthoDBiPOG091H0JWM.

    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
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi226186.BT_3703.

    Protein family/group databases

    CAZyiGH97. Glycoside Hydrolase Family 97.

    Proteomic databases

    PaxDbiG8JZS4.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Phylogenomic databases

    HOGENOMiHOG000291494.
    OMAiVWWDMIT.
    OrthoDBiPOG091H0JWM.

    Enzyme and pathway databases

    UniPathwayiUPA00153.
    SABIO-RKG8JZS4.

    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...

    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: November 2, 2016
    This is version 33 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

    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.