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Q8A1G3

- SUSG_BACTN

UniProt

Q8A1G3 - SUSG_BACTN

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Protein
Alpha-amylase SusG
Gene
susG, BT_3698
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

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 – 3881Nucleophile By similarity
Metal bindingi392 – 3921Calcium; via carbonyl oxygen
Active sitei431 – 4311Proton donor By similarity
Sitei472 – 4732Starch
Sitei498 – 4981Transition state stabilizer Inferred
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
Complete GO annotation...

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; Lipid-anchor 1 Publication

GO - Cellular componenti

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

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 – 2222 Reviewed prediction
Add
BLAST
Chaini23 – 692670Alpha-amylase SusG
PRO_0000425887Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi23 – 231N-palmitoyl cysteine Reviewed prediction
Lipidationi23 – 231S-diacylglycerol cysteine Reviewed prediction

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

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.

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

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

« Hide

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti456 – 4561Y → N in AAB42174. 1 Publication
Sequence conflicti465 – 4651S → R in AAB42174. 1 Publication
Sequence conflicti579 – 5791D → H in AAB42174. 1 Publication
Sequence conflicti607 – 6071G → A in AAB42174. 1 Publication
Sequence conflicti685 – 6851S → C in AAB42174. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 82 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

Similar proteinsi