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Q8A1G3 (SUSG_BACTN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-amylase SusG

EC=3.2.1.1
Alternative name(s):
Starch-utilization system protein G
Gene names
Name:susG
Ordered Locus Names:BT_3698
OrganismBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482) [Reference proteome] [HAMAP]
Taxonomic identifier226186 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length692 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Alpha-amylase that cleaves starch into oligosaccharides before internalization for degradation, the first step in starch degradation. Ref.3 Ref.4 Ref.5

Catalytic activity

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Ref.5

Cofactor

Binds 1 calcium ion per subunit. Ref.5

Pathway

Glycan degradation; starch degradation.

Subunit structure

Monomer. Ref.5

Subcellular location

Cell outer membrane; Lipid-anchor Ref.3.

Induction

By maltose. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   Cellular componentCell outer membrane
Membrane
   DomainSignal
   LigandCalcium
Magnesium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   PTMLipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processstarch catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcell outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

outer membrane

Inferred from direct assay Ref.1. Source: MENGO

   Molecular_functionalpha-amylase activity

Inferred from direct assay. Source: MENGO

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 692670Alpha-amylase SusG
PRO_0000425887

Regions

Region1541Starch binding
Region260 – 2634Starch binding
Region330 – 3334Starch binding
Region386 – 3927Starch binding
Region4371Starch binding
Region4571Starch binding

Sites

Active site3881Nucleophile By similarity
Active site4311Proton donor By similarity
Metal binding731Magnesium
Metal binding751Magnesium
Metal binding771Magnesium
Metal binding791Magnesium; via carbonyl oxygen
Metal binding811Magnesium
Metal binding1531Calcium
Metal binding3521Calcium
Metal binding3921Calcium; via carbonyl oxygen
Site3041Starch
Site472 – 4732Starch
Site4981Transition state stabilizer Probable
Site5451Starch
Site5491Starch

Amino acid modifications

Lipidation231N-palmitoyl cysteine Potential
Lipidation231S-diacylglycerol cysteine Potential

Experimental info

Mutagenesis4601W → A: Slight reduction in catalytic activity, while it does not affect the catalytic turnover rate; when associated with A-469 and V-473. Ref.5
Mutagenesis4691Y → A: Slight reduction in catalytic activity, while it does not affect the catalytic turnover rate; when associated with A-460 and V-473. Ref.5
Mutagenesis4731D → V: Slight reduction in catalytic activity, while it does not affect the catalytic turnover rate; when associated with A-460 and A-469. Ref.5
Mutagenesis4981D → N: Abolishes alpha-amylase activity. Ref.5
Sequence conflict4561Y → N in AAB42174. Ref.1
Sequence conflict4651S → R in AAB42174. Ref.1
Sequence conflict5791D → H in AAB42174. Ref.1
Sequence conflict6071G → A in AAB42174. Ref.1
Sequence conflict6851S → C in AAB42174. Ref.1

Secondary structure

........................................................................................................................................... 692
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8A1G3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: EB7EC2281844B0F9

FASTA69277,959
        10         20         30         40         50         60 
MNKHLHFLSL LWLSMLMAFM TACSDDKNIT DPAPEPEPPV EGQWTALTAS PDTWDETKRA 

        70         80         90        100        110        120 
DISYQLLLYS FADSDGDGYG DLNGVTQKLD YLNQLGVKAL WLSPIHPCMS YHGYDVTDYT 

       130        140        150        160        170        180 
KVNPQLGTES DFDRLVTEAH NRGIKIYLDY VMNHTGTAHP WFTEASSSSE SPYRNYYSFS 

       190        200        210        220        230        240 
EDPKTDIAAG KIAMITQEGA AGYNAAEWFQ VSDETAAVKG LLKFTLDWSN APSPILVVST 

       250        260        270        280        290        300 
GTKADEDNPD TGTDNAKYLY YGEDICKKFY DKGNNIYELT VDFESTWGLL IRTSNASFWP 

       310        320        330        340        350        360 
SGTKYGASSS SEKLALNKDF KLTNAGNPAN IMFDSQQITY FHSHFCTDWF ADLNYGPVDQ 

       370        380        390        400        410        420 
AGESPAYQAI ADAAKGWIAR GVDGLRLDAV KHIYHSETSE ENPRFLKMFY EDMNAYYKQK 

       430        440        450        460        470        480 
GHTDDFYMIG EVLSEYDKVA PYYKGLPALF EFSFWYRLEW GINNSTGCYF AKDILSYQQK 

       490        500        510        520        530        540 
YANYRSDYIE ATKLSNHDED RTSSKLGKSA DKCKLAAAVL LTSAGHPYIY YGEELGLYGT 

       550        560        570        580        590        600 
KDNGDEYVRS PMLWGDSYTT NYTDKTDATV SKNVKTVADQ QADTHSLLNI YFSLTRLRNT 

       610        620        630        640        650        660 
YPALAEGNMT KHSVYNESQE KDYKPIAAWY MTKDNEKLLV IHNFGGTAMQ LPLTDKIEKV 

       670        680        690 
LFVNGETQQN TDSDSYTLKL GGYASVVFKL GN 

« Hide

References

« Hide 'large scale' references
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77732 Genomic DNA. Translation: AAB42174.1.
AE015928 Genomic DNA. Translation: AAO78803.1.
RefSeqNP_812609.1. NC_004663.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3K8KX-ray2.20A/B24-692[»]
3K8LX-ray2.30A/B24-692[»]
3K8MX-ray2.50A/B24-692[»]
ProteinModelPortalQ8A1G3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226186.BT_3698.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO78803; AAO78803; BT_3698.
GeneID1072061.
KEGGbth:BT_3698.
PATRIC21062397. VBIBacThe70966_3758.

Phylogenomic databases

OMASHISFTH.
OrthoDBEOG6RZB0T.

Enzyme and pathway databases

BioCycBTHE226186:GJXV-3764-MONOMER.
UniPathwayUPA00153.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProIPR015902. 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]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 2 hits.
[Graphical view]
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 2 hits.
PROSITEPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8A1G3.

Entry information

Entry nameSUSG_BACTN
AccessionPrimary (citable) accession number: Q8A1G3
Secondary accession number(s): Q45772
Entry history
Integrated into UniProtKB/Swiss-Prot: March 19, 2014
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries