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G8JZS4

- SUSB_BACTN

UniProt

G8JZS4 - SUSB_BACTN

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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: 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 Ca(2+) ion per subunit.1 Publication

Kineticsi

  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-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-glucoside1 Publication

pH dependencei

Optimum pH is 6.5.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi194 – 1941Calcium1 Publication
Sitei194 – 1941Substrate
Sitei331 – 3311Substrate
Sitei467 – 4671Substrate
Metal bindingi508 – 5081Calcium1 Publication
Metal bindingi526 – 5261Calcium1 Publication
Active sitei532 – 5321Proton donor/proton acceptor1 Publication
Metal bindingi532 – 5321Calcium1 Publication

GO - Molecular functioni

  1. alpha-1,4-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 1 Publication

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-KW
  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 – 2121Sequence AnalysisAdd
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 – 264Combined sources
Beta strandi32 – 387Combined sources
Beta strandi44 – 507Combined sources
Beta strandi53 – 608Combined sources
Beta strandi63 – 653Combined sources
Helixi88 – 903Combined sources
Beta strandi91 – 955Combined sources
Beta strandi97 – 11014Combined sources
Beta strandi113 – 1186Combined sources
Beta strandi120 – 13314Combined sources
Helixi134 – 1363Combined sources
Beta strandi138 – 14710Combined sources
Beta strandi150 – 1578Combined sources
Beta strandi163 – 1719Combined sources
Beta strandi174 – 1763Combined sources
Beta strandi182 – 1854Combined sources
Beta strandi189 – 1913Combined sources
Beta strandi198 – 2014Combined sources
Helixi202 – 2043Combined sources
Helixi205 – 2128Combined sources
Beta strandi229 – 2346Combined sources
Beta strandi240 – 2467Combined sources
Beta strandi254 – 2596Combined sources
Turni260 – 2634Combined sources
Beta strandi264 – 2696Combined sources
Beta strandi279 – 2857Combined sources
Beta strandi288 – 2969Combined sources
Helixi297 – 3026Combined sources
Helixi305 – 3084Combined sources
Helixi318 – 3214Combined sources
Beta strandi325 – 3306Combined sources
Helixi332 – 3354Combined sources
Beta strandi338 – 3414Combined sources
Beta strandi343 – 3464Combined sources
Turni352 – 3543Combined sources
Helixi357 – 3593Combined sources
Helixi370 – 38213Combined sources
Beta strandi386 – 3905Combined sources
Helixi397 – 3993Combined sources
Beta strandi401 – 4033Combined sources
Helixi420 – 42910Combined sources
Beta strandi433 – 4397Combined sources
Helixi444 – 46017Combined sources
Beta strandi465 – 4695Combined sources
Helixi484 – 49916Combined sources
Beta strandi503 – 5064Combined sources
Helixi515 – 5173Combined sources
Beta strandi522 – 5254Combined sources
Helixi531 – 5355Combined sources
Helixi543 – 5453Combined sources
Helixi547 – 5493Combined sources
Turni550 – 5545Combined sources
Helixi568 – 5703Combined sources
Helixi583 – 59210Combined sources
Beta strandi596 – 5994Combined sources
Helixi604 – 6074Combined sources
Helixi611 – 6199Combined sources
Beta strandi622 – 63312Combined sources
Turni634 – 6363Combined sources
Beta strandi637 – 6448Combined sources
Beta strandi650 – 6567Combined sources
Beta strandi661 – 6666Combined sources
Beta strandi676 – 6838Combined sources
Turni689 – 6913Combined sources
Beta strandi696 – 7038Combined sources
Beta strandi708 – 7136Combined sources
Beta strandi718 – 7258Combined sources
Helixi729 – 7313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
3WFAX-ray2.00A/B22-738[»]
ProteinModelPortaliG8JZS4.
SMRiG8JZS4. Positions 22-738.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the glycosyl hydrolase 97 family.Curated

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

        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.

Genome annotation databases

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

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 .
RefSeqi NP_812614.1. NC_004663.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 [» ]
3WFA X-ray 2.00 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: November 26, 2014
This is version 19 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