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G8JZS4 (SUSB_BACTN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 15. 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:
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 names
Name:susB
Ordered Locus Names:BT_3703
OrganismBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482) [Reference proteome] [HAMAP]
Taxonomic identifier226186 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length738 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose. Ref.3

Cofactor

Binds 1 calcium ion per subunit. Ref.3

Pathway

Glycan degradation; starch degradation.

Subunit structure

Monomer. Ref.3

Subcellular location

Periplasm Probable Ref.1.

Sequence similarities

Belongs to the glycosyl hydrolase 97 family.

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 (Ref.3).

Biophysicochemical properties

Kinetic parameters:

KM=1.05 mM for maltose Ref.3

KM=0.29 mM for maltotriose

KM=0.64 mM for maltotetraose

KM=1.29 mM for maltopentaose

KM=2.71 mM for maltohexaose

KM=4.58 mM for maltoheptaose

KM=6.89 mM for amylose DP17

KM=0.67 mM for soluble starch

KM=2.39 mM for kojibiose

KM=3.14 mM for nigerose

KM=6.34 mM for isomaltose

KM=0.31 mM for panose

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

pH dependence:

Optimum pH is 6.5.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   Cellular componentPeriplasm
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processstarch catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay Ref.1. Source: MENGO

   Molecular_functionalpha-glucosidase activity

Inferred from mutant phenotype Ref.1. Source: MENGO

glucan 1,4-alpha-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

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 – 2121 Potential
Chain22 – 738717Glucan 1,4-alpha-glucosidase SusB
PRO_0000425886

Regions

Region215 – 2173Substrate binding
Region437 – 4393Substrate binding
Region507 – 5082Substrate binding

Sites

Active site5321Proton donor/proton acceptor Probable
Metal binding1941Calcium
Metal binding5081Calcium
Metal binding5261Calcium
Metal binding5321Calcium
Site1941Substrate
Site3311Substrate
Site4671Substrate

Experimental info

Mutagenesis4391E → Q: Abolishes enzyme activity. Ref.3
Mutagenesis5081E → Q: Abolishes enzyme activity. Ref.3
Mutagenesis5321E → Q: Abolishes enzyme activity. Ref.3

Secondary structure

............................................................................................................................... 738
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
G8JZS4 [UniParc].

Last modified January 25, 2012. Version 1.
Checksum: 2BFE87C3552C9A12

FASTA73884,378
        10         20         30         40         50         60 
MKKRKILSLI AFLCISFIAN AQQKLTSPDN NLVMTFQVDS KGAPTYELTY KNKVVIKPST 

        70         80         90        100        110        120 
LGLELKKEDN TRTDFDWVDR RDLTKLDSKT NLYDGFEVKD TQTATFDETW QPVWGEEKEI 

       130        140        150        160        170        180 
RNHYNELAVT LYQPMNDRSI VIRFRLFNDG LGFRYEFPQQ KSLNYFVIKE EHSQFGMNGD 

       190        200        210        220        230        240 
HIAFWIPGDY DTQEYDYTIS RLSEIRGLMK EAITPNSSQT PFSQTGVQTA LMMKTDDGLY 

       250        260        270        280        290        300 
INLHEAALVD YSCMHLNLDD KNMVFESWLT PDAKGDKGYM QTPCNTPWRT IIVSDDARNI 

       310        320        330        340        350        360 
LASRITLNLN EPCKIADAAS WVKPVKYIGV WWDMITGKGS WAYTDELTSV KLGETDYSKT 

       370        380        390        400        410        420 
KPNGKHSANT ANVKRYIDFA AAHGFDAVLV EGWNEGWEDW FGNSKDYVFD FVTPYPDFDV 

       430        440        450        460        470        480 
KEIHRYAARK GIKMMMHHET SASVRNYERH MDKAYQFMAD NGYNSVKSGY VGNIIPRGEH 

       490        500        510        520        530        540 
HYGQWMNNHY LYAVKKAADY KIMVNAHEAT RPTGICRTYP NLIGNESARG TEYESFGGNK 

       550        560        570        580        590        600 
VYHTTILPFT RLVGGPMDYT PGIFETHCNK MNPANNSQVR STIARQLALY VTMYSPLQMA 

       610        620        630        640        650        660 
ADIPENYERF MDAFQFIKDV ALDWDETNYL EAEPGEYITI ARKAKDTDDW YVGCTAGENG 

       670        680        690        700        710        720 
HTSKLVFDFL TPGKQYIATV YADAKDADWK ENPQAYTIKK GILTNKSKLN LHAANGGGYA 

       730 
ISIKEVKDKS EAKGLKRL 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U66897 Genomic DNA. Translation: AAC44671.1.
AE015928 Genomic DNA. Translation: AAO78808.1.
RefSeqNP_812614.1. NC_004663.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalG8JZS4.
SMRG8JZS4. Positions 22-738.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO78808; AAO78808; BT_3703.
GeneID1072064.
KEGGbth:BT_3703.

Phylogenomic databases

OMAPNGKHSA.
OrthoDBEOG6Z3KGW.

Enzyme and pathway databases

BioCycBTHE226186:GJXV-3769-MONOMER.
UniPathwayUPA00153.

Family and domain databases

InterProIPR029483. GH97_C.
IPR019563. GH97_catalytic.
IPR029486. GH97_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF14509. GH97_C. 1 hit.
PF14508. GH97_N. 1 hit.
PF10566. Glyco_hydro_97. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSUSB_BACTN
AccessionPrimary (citable) accession number: G8JZS4
Secondary accession number(s): P71094, Q7C3Z2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 19, 2014
Last sequence update: January 25, 2012
Last modified: June 11, 2014
This is version 15 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