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Q8A1G3

- SUSG_BACTN

UniProt

Q8A1G3 - SUSG_BACTN

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Protein

Alpha-amylase SusG

Gene

susG

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

Ca2+1 PublicationNote: Binds 1 Ca(2+) 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 – 3881NucleophileBy similarity
Metal bindingi392 – 3921Calcium; via carbonyl oxygen
Active sitei431 – 4311Proton donorBy similarity
Sitei472 – 4732Starch
Sitei498 – 4981Transition state stabilizerCurated
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 1 Publication; Lipid-anchor 1 PublicationPROSITE-ProRule annotation

GO - Cellular componenti

  1. cell outer membrane Source: UniProtKB-KW
  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 – 2222PROSITE-ProRule annotationAdd
BLAST
Chaini23 – 692670Alpha-amylase SusGPRO_0000425887Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi23 – 231N-palmitoyl cysteinePROSITE-ProRule annotation
Lipidationi23 – 231S-diacylglycerol cysteinePROSITE-ProRule annotation

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

1
692
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi63 – 664Combined sources
Turni68 – 703Combined sources
Beta strandi74 – 796Combined sources
Helixi82 – 865Combined sources
Helixi89 – 935Combined sources
Turni94 – 963Combined sources
Beta strandi98 – 1025Combined sources
Beta strandi106 – 1105Combined sources
Beta strandi115 – 1173Combined sources
Turni124 – 1263Combined sources
Helixi129 – 14113Combined sources
Beta strandi145 – 1506Combined sources
Beta strandi153 – 1564Combined sources
Helixi160 – 1678Combined sources
Helixi174 – 1763Combined sources
Beta strandi179 – 1813Combined sources
Helixi183 – 1886Combined sources
Helixi193 – 1953Combined sources
Helixi199 – 2024Combined sources
Helixi205 – 2073Combined sources
Beta strandi208 – 2114Combined sources
Beta strandi218 – 22710Combined sources
Turni229 – 2324Combined sources
Beta strandi235 – 2406Combined sources
Beta strandi258 – 2614Combined sources
Turni262 – 2643Combined sources
Beta strandi265 – 2684Combined sources
Beta strandi270 – 2734Combined sources
Beta strandi276 – 28712Combined sources
Beta strandi289 – 2935Combined sources
Beta strandi296 – 2983Combined sources
Beta strandi304 – 3096Combined sources
Beta strandi325 – 3273Combined sources
Beta strandi331 – 3333Combined sources
Beta strandi340 – 3423Combined sources
Beta strandi350 – 3534Combined sources
Helixi358 – 3636Combined sources
Helixi365 – 37814Combined sources
Turni379 – 3813Combined sources
Beta strandi384 – 3874Combined sources
Helixi390 – 3923Combined sources
Beta strandi393 – 3953Combined sources
Beta strandi397 – 4004Combined sources
Helixi401 – 41919Combined sources
Beta strandi427 – 4304Combined sources
Helixi436 – 4394Combined sources
Helixi440 – 4445Combined sources
Beta strandi447 – 4504Combined sources
Helixi452 – 46312Combined sources
Helixi470 – 48213Combined sources
Beta strandi489 – 4913Combined sources
Helixi502 – 5054Combined sources
Turni506 – 5083Combined sources
Helixi510 – 52112Combined sources
Beta strandi523 – 5253Combined sources
Beta strandi528 – 5303Combined sources
Turni531 – 5366Combined sources
Helixi545 – 5484Combined sources
Helixi570 – 5734Combined sources
Helixi577 – 5815Combined sources
Helixi587 – 60014Combined sources
Helixi602 – 6065Combined sources
Beta strandi608 – 6114Combined sources
Beta strandi613 – 6164Combined sources
Helixi617 – 6193Combined sources
Turni620 – 6223Combined sources
Beta strandi626 – 6338Combined sources
Beta strandi636 – 6438Combined sources
Beta strandi645 – 6473Combined sources
Beta strandi649 – 6535Combined sources
Beta strandi657 – 6659Combined sources
Beta strandi667 – 6704Combined sources
Helixi672 – 6743Combined sources
Beta strandi676 – 6805Combined sources
Beta strandi685 – 6906Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3K8KX-ray2.20A/B24-692[»]
3K8LX-ray2.30A/B24-692[»]
3K8MX-ray2.50A/B24-692[»]
ProteinModelPortaliQ8A1G3.
ModBaseiSearch...
MobiDBiSearch...

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

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiQ8A1G3.
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

        10         20         30         40         50
MNKHLHFLSL LWLSMLMAFM TACSDDKNIT DPAPEPEPPV EGQWTALTAS
60 70 80 90 100
PDTWDETKRA DISYQLLLYS FADSDGDGYG DLNGVTQKLD YLNQLGVKAL
110 120 130 140 150
WLSPIHPCMS YHGYDVTDYT KVNPQLGTES DFDRLVTEAH NRGIKIYLDY
160 170 180 190 200
VMNHTGTAHP WFTEASSSSE SPYRNYYSFS EDPKTDIAAG KIAMITQEGA
210 220 230 240 250
AGYNAAEWFQ VSDETAAVKG LLKFTLDWSN APSPILVVST GTKADEDNPD
260 270 280 290 300
TGTDNAKYLY YGEDICKKFY DKGNNIYELT VDFESTWGLL IRTSNASFWP
310 320 330 340 350
SGTKYGASSS SEKLALNKDF KLTNAGNPAN IMFDSQQITY FHSHFCTDWF
360 370 380 390 400
ADLNYGPVDQ AGESPAYQAI ADAAKGWIAR GVDGLRLDAV KHIYHSETSE
410 420 430 440 450
ENPRFLKMFY EDMNAYYKQK GHTDDFYMIG EVLSEYDKVA PYYKGLPALF
460 470 480 490 500
EFSFWYRLEW GINNSTGCYF AKDILSYQQK YANYRSDYIE ATKLSNHDED
510 520 530 540 550
RTSSKLGKSA DKCKLAAAVL LTSAGHPYIY YGEELGLYGT KDNGDEYVRS
560 570 580 590 600
PMLWGDSYTT NYTDKTDATV SKNVKTVADQ QADTHSLLNI YFSLTRLRNT
610 620 630 640 650
YPALAEGNMT KHSVYNESQE KDYKPIAAWY MTKDNEKLLV IHNFGGTAMQ
660 670 680 690
LPLTDKIEKV LFVNGETQQN TDSDSYTLKL GGYASVVFKL GN
Length:692
Mass (Da):77,959
Last modified:June 1, 2003 - v1
Checksum:iEB7EC2281844B0F9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti456 – 4561Y → N in AAB42174. (PubMed:9006015)Curated
Sequence conflicti465 – 4651S → R in AAB42174. (PubMed:9006015)Curated
Sequence conflicti579 – 5791D → H in AAB42174. (PubMed:9006015)Curated
Sequence conflicti607 – 6071G → A in AAB42174. (PubMed:9006015)Curated
Sequence conflicti685 – 6851S → C in AAB42174. (PubMed:9006015)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

InParanoidi Q8A1G3.
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: November 26, 2014
This is version 85 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