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Q8A1G3

- SUSG_BACTN

UniProt

Q8A1G3 - SUSG_BACTN

Protein

Alpha-amylase SusG

Gene

susG

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 83 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    Alpha-amylase that cleaves starch into oligosaccharides before internalization for degradation, the first step in starch degradation.3 Publications

    Catalytic activityi

    Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.1 Publication

    Cofactori

    Binds 1 calcium ion per subunit.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi73 – 731Magnesium
    Metal bindingi75 – 751Magnesium
    Metal bindingi77 – 771Magnesium
    Metal bindingi79 – 791Magnesium; via carbonyl oxygen
    Metal bindingi81 – 811Magnesium
    Metal bindingi153 – 1531Calcium
    Sitei304 – 3041Starch
    Metal bindingi352 – 3521Calcium
    Active sitei388 – 3881NucleophileBy similarity
    Metal bindingi392 – 3921Calcium; via carbonyl oxygen
    Active sitei431 – 4311Proton donorBy similarity
    Sitei472 – 4732Starch
    Sitei498 – 4981Transition state stabilizerCurated
    Sitei545 – 5451Starch
    Sitei549 – 5491Starch

    GO - Molecular functioni

    1. alpha-amylase activity Source: UniProtKB
    2. calcium ion binding Source: UniProtKB
    3. magnesium ion binding Source: UniProtKB
    4. starch binding 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, Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciBTHE226186:GJXV-3764-MONOMER.
    UniPathwayiUPA00153.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-amylase SusG (EC:3.2.1.1)
    Alternative name(s):
    Starch-utilization system protein G
    Gene namesi
    Name:susG
    Ordered Locus Names:BT_3698
    OrganismiBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
    Taxonomic identifieri226186 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
    ProteomesiUP000001414: Chromosome

    Subcellular locationi

    Cell outer membrane 1 Publication; Lipid-anchor 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. cell outer membrane Source: UniProtKB-SubCell
    2. outer membrane Source: MENGO

    Keywords - Cellular componenti

    Cell outer membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi460 – 4601W → A: Slight reduction in catalytic activity, while it does not affect the catalytic turnover rate; when associated with A-469 and V-473. 1 Publication
    Mutagenesisi469 – 4691Y → A: Slight reduction in catalytic activity, while it does not affect the catalytic turnover rate; when associated with A-460 and V-473. 1 Publication
    Mutagenesisi473 – 4731D → V: Slight reduction in catalytic activity, while it does not affect the catalytic turnover rate; when associated with A-460 and A-469. 1 Publication
    Mutagenesisi498 – 4981D → N: Abolishes alpha-amylase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222PROSITE-ProRule annotationAdd
    BLAST
    Chaini23 – 692670Alpha-amylase SusGPRO_0000425887Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi23 – 231N-palmitoyl cysteinePROSITE-ProRule annotation
    Lipidationi23 – 231S-diacylglycerol cysteinePROSITE-ProRule annotation

    Keywords - PTMi

    Lipoprotein, Palmitate

    Expressioni

    Inductioni

    By maltose.1 Publication

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi226186.BT_3698.

    Structurei

    Secondary structure

    1
    692
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi63 – 664
    Turni68 – 703
    Beta strandi74 – 796
    Helixi82 – 865
    Helixi89 – 935
    Turni94 – 963
    Beta strandi98 – 1025
    Beta strandi106 – 1105
    Beta strandi115 – 1173
    Turni124 – 1263
    Helixi129 – 14113
    Beta strandi145 – 1506
    Beta strandi153 – 1564
    Helixi160 – 1678
    Helixi174 – 1763
    Beta strandi179 – 1813
    Helixi183 – 1886
    Helixi193 – 1953
    Helixi199 – 2024
    Helixi205 – 2073
    Beta strandi208 – 2114
    Beta strandi218 – 22710
    Turni229 – 2324
    Beta strandi235 – 2406
    Beta strandi258 – 2614
    Turni262 – 2643
    Beta strandi265 – 2684
    Beta strandi270 – 2734
    Beta strandi276 – 28712
    Beta strandi289 – 2935
    Beta strandi296 – 2983
    Beta strandi304 – 3096
    Beta strandi325 – 3273
    Beta strandi331 – 3333
    Beta strandi340 – 3423
    Beta strandi350 – 3534
    Helixi358 – 3636
    Helixi365 – 37814
    Turni379 – 3813
    Beta strandi384 – 3874
    Helixi390 – 3923
    Beta strandi393 – 3953
    Beta strandi397 – 4004
    Helixi401 – 41919
    Beta strandi427 – 4304
    Helixi436 – 4394
    Helixi440 – 4445
    Beta strandi447 – 4504
    Helixi452 – 46312
    Helixi470 – 48213
    Beta strandi489 – 4913
    Helixi502 – 5054
    Turni506 – 5083
    Helixi510 – 52112
    Beta strandi523 – 5253
    Beta strandi528 – 5303
    Turni531 – 5366
    Helixi545 – 5484
    Helixi570 – 5734
    Helixi577 – 5815
    Helixi587 – 60014
    Helixi602 – 6065
    Beta strandi608 – 6114
    Beta strandi613 – 6164
    Helixi617 – 6193
    Turni620 – 6223
    Beta strandi626 – 6338
    Beta strandi636 – 6438
    Beta strandi645 – 6473
    Beta strandi649 – 6535
    Beta strandi657 – 6659
    Beta strandi667 – 6704
    Helixi672 – 6743
    Beta strandi676 – 6805
    Beta strandi685 – 6906

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3K8KX-ray2.20A/B24-692[»]
    3K8LX-ray2.30A/B24-692[»]
    3K8MX-ray2.50A/B24-692[»]
    ProteinModelPortaliQ8A1G3.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8A1G3.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni154 – 1541Starch binding
    Regioni260 – 2634Starch binding
    Regioni330 – 3334Starch binding
    Regioni386 – 3927Starch binding
    Regioni437 – 4371Starch binding
    Regioni457 – 4571Starch binding

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    OMAiSHISFTH.
    OrthoDBiEOG6RZB0T.

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.80. 2 hits.
    InterProiIPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR006589. Glyco_hydro_13_sub_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10357. PTHR10357. 1 hit.
    PfamiPF00128. Alpha-amylase. 2 hits.
    [Graphical view]
    SMARTiSM00642. Aamy. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 2 hits.
    PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8A1G3-1 [UniParc]FASTAAdd to Basket

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    MNKHLHFLSL LWLSMLMAFM TACSDDKNIT DPAPEPEPPV EGQWTALTAS    50
    PDTWDETKRA DISYQLLLYS FADSDGDGYG DLNGVTQKLD YLNQLGVKAL 100
    WLSPIHPCMS YHGYDVTDYT KVNPQLGTES DFDRLVTEAH NRGIKIYLDY 150
    VMNHTGTAHP WFTEASSSSE SPYRNYYSFS EDPKTDIAAG KIAMITQEGA 200
    AGYNAAEWFQ VSDETAAVKG LLKFTLDWSN APSPILVVST GTKADEDNPD 250
    TGTDNAKYLY YGEDICKKFY DKGNNIYELT VDFESTWGLL IRTSNASFWP 300
    SGTKYGASSS SEKLALNKDF KLTNAGNPAN IMFDSQQITY FHSHFCTDWF 350
    ADLNYGPVDQ AGESPAYQAI ADAAKGWIAR GVDGLRLDAV KHIYHSETSE 400
    ENPRFLKMFY EDMNAYYKQK GHTDDFYMIG EVLSEYDKVA PYYKGLPALF 450
    EFSFWYRLEW GINNSTGCYF AKDILSYQQK YANYRSDYIE ATKLSNHDED 500
    RTSSKLGKSA DKCKLAAAVL LTSAGHPYIY YGEELGLYGT KDNGDEYVRS 550
    PMLWGDSYTT NYTDKTDATV SKNVKTVADQ QADTHSLLNI YFSLTRLRNT 600
    YPALAEGNMT KHSVYNESQE KDYKPIAAWY MTKDNEKLLV IHNFGGTAMQ 650
    LPLTDKIEKV LFVNGETQQN TDSDSYTLKL GGYASVVFKL GN 692
    Length:692
    Mass (Da):77,959
    Last modified:June 1, 2003 - v1
    Checksum:iEB7EC2281844B0F9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti456 – 4561Y → N in AAB42174. (PubMed:9006015)Curated
    Sequence conflicti465 – 4651S → R in AAB42174. (PubMed:9006015)Curated
    Sequence conflicti579 – 5791D → H in AAB42174. (PubMed:9006015)Curated
    Sequence conflicti607 – 6071G → A in AAB42174. (PubMed:9006015)Curated
    Sequence conflicti685 – 6851S → C in AAB42174. (PubMed:9006015)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L77732 Genomic DNA. Translation: AAB42174.1.
    AE015928 Genomic DNA. Translation: AAO78803.1.
    RefSeqiNP_812609.1. NC_004663.1.

    Genome annotation databases

    EnsemblBacteriaiAAO78803; AAO78803; BT_3698.
    GeneIDi1072061.
    KEGGibth:BT_3698.
    PATRICi21062397. VBIBacThe70966_3758.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L77732 Genomic DNA. Translation: AAB42174.1 .
    AE015928 Genomic DNA. Translation: AAO78803.1 .
    RefSeqi NP_812609.1. NC_004663.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3K8K X-ray 2.20 A/B 24-692 [» ]
    3K8L X-ray 2.30 A/B 24-692 [» ]
    3K8M X-ray 2.50 A/B 24-692 [» ]
    ProteinModelPortali Q8A1G3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 226186.BT_3698.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAO78803 ; AAO78803 ; BT_3698 .
    GeneIDi 1072061.
    KEGGi bth:BT_3698.
    PATRICi 21062397. VBIBacThe70966_3758.

    Phylogenomic databases

    OMAi SHISFTH.
    OrthoDBi EOG6RZB0T.

    Enzyme and pathway databases

    UniPathwayi UPA00153 .
    BioCyci BTHE226186:GJXV-3764-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q8A1G3.

    Family and domain databases

    Gene3Di 2.60.40.1180. 1 hit.
    3.20.20.80. 2 hits.
    InterProi IPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR006589. Glyco_hydro_13_sub_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR10357. PTHR10357. 1 hit.
    Pfami PF00128. Alpha-amylase. 2 hits.
    [Graphical view ]
    SMARTi SM00642. Aamy. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 2 hits.
    PROSITEi PS51257. PROKAR_LIPOPROTEIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of four outer membrane proteins that play a role in utilization of starch by Bacteroides thetaiotaomicron."
      Reeves A.R., Wang G.R., Salyers A.A.
      J. Bacteriol. 179:643-649(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
      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. "Physiological characterization of SusG, an outer membrane protein essential for starch utilization by Bacteroides thetaiotaomicron."
      Shipman J.A., Cho K.H., Siegel H.A., Salyers A.A.
      J. Bacteriol. 181:7206-7211(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
      Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.
    4. "Biochemical analysis of interactions between outer membrane proteins that contribute to starch utilization by Bacteroides thetaiotaomicron."
      Cho K.H., Salyers A.A.
      J. Bacteriol. 183:7224-7230(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.
    5. "SusG: a unique cell-membrane-associated alpha-amylase from a prominent human gut symbiont targets complex starch molecules."
      Koropatkin N.M., Smith T.J.
      Structure 18:200-215(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 24-692 IN COMPLEXES WITH MALTOOLIGOSACCHARIDE; CALCIUM AND MAGNESIUM, COFACTOR, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF TRP-460; TYR-469; ASP-473 AND ASP-498.
      Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

    Entry informationi

    Entry nameiSUSG_BACTN
    AccessioniPrimary (citable) accession number: Q8A1G3
    Secondary accession number(s): Q45772
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 19, 2014
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 83 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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