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G8JZS4

- SUSB_BACTN

UniProt

G8JZS4 - SUSB_BACTN

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Protein

Glucan 1,4-alpha-glucosidase SusB

Gene
susB, BT_3703
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

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 maltotriose
  3. KM=0.64 mM for maltotetraose
  4. KM=1.29 mM for maltopentaose
  5. KM=2.71 mM for maltohexaose
  6. KM=4.58 mM for maltoheptaose
  7. KM=6.89 mM for amylose DP17
  8. KM=0.67 mM for soluble starch
  9. KM=2.39 mM for kojibiose
  10. KM=3.14 mM for nigerose
  11. KM=6.34 mM for isomaltose
  12. KM=0.31 mM for panose
  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-glucoside

pH dependencei

Optimum pH is 6.5.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi194 – 1941Calcium
Sitei194 – 1941Substrate
Sitei331 – 3311Substrate
Sitei467 – 4671Substrate
Metal bindingi508 – 5081Calcium
Metal bindingi526 – 5261Calcium
Active sitei532 – 5321Proton donor/proton acceptor Inferred
Metal bindingi532 – 5321Calcium

GO - Molecular functioni

  1. alpha-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
Complete GO annotation...

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 Inferred 1 Publication

GO - Cellular componenti

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

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 – 2121 Reviewed predictionAdd
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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni215 – 2173Substrate binding
Regioni437 – 4393Substrate binding
Regioni507 – 5082Substrate binding

Sequence similaritiesi

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

« Hide

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 16 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

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