Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Alpha-amylase SusG

Gene

susG

Organism
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Status
Reviewed-Annotation score: 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 Ca2+ ion per subunit.1 Publication

Pathwayi: starch degradation

This protein is involved in the pathway starch degradation, which is part of Glycan degradation.
View all proteins of this organism that are known to be involved in the pathway starch degradation and in Glycan degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi73Magnesium1 Publication1
Metal bindingi75Magnesium1 Publication1
Metal bindingi77Magnesium1 Publication1
Metal bindingi79Magnesium; via carbonyl oxygen1 Publication1
Metal bindingi81Magnesium1 Publication1
Metal bindingi153Calcium1 Publication1
Sitei304Starch1 Publication1
Metal bindingi352Calcium1 Publication1
Active sitei388NucleophileBy similarity1
Metal bindingi392Calcium; via carbonyl oxygen1 Publication1
Active sitei431Proton donorBy similarity1
Sitei472 – 473Starch1 Publication2
Sitei498Transition state stabilizer1 Publication1
Sitei545Starch1 Publication1
Sitei549Starch1 Publication1

GO - Molecular functioni

  • alpha-amylase activity Source: UniProtKB
  • calcium ion binding Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • starch binding Source: UniProtKB

GO - Biological processi

  • 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

BRENDAi3.2.1.1. 709.
UniPathwayiUPA00153.

Protein family/group databases

CAZyiCBM58. Carbohydrate-Binding Module Family 58.
GH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylase SusG (EC:3.2.1.11 Publication)
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
Proteomesi
  • UP000001414 Componenti: Chromosome

Subcellular locationi

  • Cell outer membrane 1 Publication; Lipid-anchor PROSITE-ProRule annotation1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi460W → A: Slight reduction in catalytic activity, while it does not affect the catalytic turnover rate; when associated with A-469 and V-473. 1 Publication1
Mutagenesisi469Y → A: Slight reduction in catalytic activity, while it does not affect the catalytic turnover rate; when associated with A-460 and V-473. 1 Publication1
Mutagenesisi473D → V: Slight reduction in catalytic activity, while it does not affect the catalytic turnover rate; when associated with A-460 and A-469. 1 Publication1
Mutagenesisi498D → N: Abolishes alpha-amylase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22PROSITE-ProRule annotationAdd BLAST22
ChainiPRO_000042588723 – 692Alpha-amylase SusGAdd BLAST670

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi23N-palmitoyl cysteinePROSITE-ProRule annotation1
Lipidationi23S-diacylglycerol cysteinePROSITE-ProRule annotation1

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

PaxDbiQ8A1G3.

Expressioni

Inductioni

By maltose.1 Publication

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi226186.BT_3698.

Structurei

Secondary structure

1692
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi63 – 66Combined sources4
Turni68 – 70Combined sources3
Beta strandi74 – 79Combined sources6
Helixi82 – 86Combined sources5
Helixi89 – 93Combined sources5
Turni94 – 96Combined sources3
Beta strandi98 – 102Combined sources5
Beta strandi106 – 110Combined sources5
Beta strandi115 – 117Combined sources3
Turni124 – 126Combined sources3
Helixi129 – 141Combined sources13
Beta strandi145 – 150Combined sources6
Beta strandi153 – 156Combined sources4
Helixi160 – 167Combined sources8
Helixi174 – 176Combined sources3
Beta strandi179 – 181Combined sources3
Helixi183 – 188Combined sources6
Helixi193 – 195Combined sources3
Helixi199 – 202Combined sources4
Helixi205 – 207Combined sources3
Beta strandi208 – 211Combined sources4
Beta strandi218 – 227Combined sources10
Turni229 – 232Combined sources4
Beta strandi235 – 240Combined sources6
Beta strandi258 – 261Combined sources4
Turni262 – 264Combined sources3
Beta strandi265 – 268Combined sources4
Beta strandi270 – 273Combined sources4
Beta strandi276 – 287Combined sources12
Beta strandi289 – 293Combined sources5
Beta strandi296 – 298Combined sources3
Beta strandi304 – 309Combined sources6
Beta strandi325 – 327Combined sources3
Beta strandi331 – 333Combined sources3
Beta strandi340 – 342Combined sources3
Beta strandi350 – 353Combined sources4
Helixi358 – 363Combined sources6
Helixi365 – 378Combined sources14
Turni379 – 381Combined sources3
Beta strandi384 – 387Combined sources4
Helixi390 – 392Combined sources3
Beta strandi393 – 395Combined sources3
Beta strandi397 – 400Combined sources4
Helixi401 – 419Combined sources19
Beta strandi427 – 430Combined sources4
Helixi436 – 439Combined sources4
Helixi440 – 444Combined sources5
Beta strandi447 – 450Combined sources4
Helixi452 – 463Combined sources12
Helixi470 – 482Combined sources13
Beta strandi489 – 491Combined sources3
Helixi502 – 505Combined sources4
Turni506 – 508Combined sources3
Helixi510 – 521Combined sources12
Beta strandi523 – 525Combined sources3
Beta strandi528 – 530Combined sources3
Turni531 – 536Combined sources6
Helixi545 – 548Combined sources4
Helixi570 – 573Combined sources4
Helixi577 – 581Combined sources5
Helixi587 – 600Combined sources14
Helixi602 – 606Combined sources5
Beta strandi608 – 611Combined sources4
Beta strandi613 – 616Combined sources4
Helixi617 – 619Combined sources3
Turni620 – 622Combined sources3
Beta strandi626 – 633Combined sources8
Beta strandi636 – 643Combined sources8
Beta strandi645 – 647Combined sources3
Beta strandi649 – 653Combined sources5
Beta strandi657 – 665Combined sources9
Beta strandi667 – 670Combined sources4
Helixi672 – 674Combined sources3
Beta strandi676 – 680Combined sources5
Beta strandi685 – 690Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3K8KX-ray2.20A/B24-692[»]
3K8LX-ray2.30A/B24-692[»]
3K8MX-ray2.50A/B24-692[»]
ProteinModelPortaliQ8A1G3.
SMRiQ8A1G3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8A1G3.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni154Starch binding1 Publication1
Regioni260 – 263Starch binding1 Publication4
Regioni330 – 333Starch binding1 Publication4
Regioni386 – 392Starch binding1 Publication7
Regioni437Starch binding1 Publication1
Regioni457Starch binding1 Publication1

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG41088V8. Bacteria.
COG0366. LUCA.
InParanoidiQ8A1G3.
OMAiRADISYQ.
OrthoDBiPOG091H07J7.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 3 hits.
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)DescriptionActionsGraphical viewLength
Sequence conflicti456Y → N in AAB42174 (PubMed:9006015).Curated1
Sequence conflicti465S → R in AAB42174 (PubMed:9006015).Curated1
Sequence conflicti579D → H in AAB42174 (PubMed:9006015).Curated1
Sequence conflicti607G → A in AAB42174 (PubMed:9006015).Curated1
Sequence conflicti685S → C in AAB42174 (PubMed:9006015).Curated1

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.
WP_011108937.1. 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.
RefSeqiNP_812609.1. NC_004663.1.
WP_011108937.1. NC_004663.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3K8KX-ray2.20A/B24-692[»]
3K8LX-ray2.30A/B24-692[»]
3K8MX-ray2.50A/B24-692[»]
ProteinModelPortaliQ8A1G3.
SMRiQ8A1G3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226186.BT_3698.

Protein family/group databases

CAZyiCBM58. Carbohydrate-Binding Module Family 58.
GH13. Glycoside Hydrolase Family 13.

Proteomic databases

PaxDbiQ8A1G3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO78803; AAO78803; BT_3698.
GeneIDi1072061.
KEGGibth:BT_3698.
PATRICi21062397. VBIBacThe70966_3758.

Phylogenomic databases

eggNOGiENOG41088V8. Bacteria.
COG0366. LUCA.
InParanoidiQ8A1G3.
OMAiRADISYQ.
OrthoDBiPOG091H07J7.

Enzyme and pathway databases

UniPathwayiUPA00153.
BRENDAi3.2.1.1. 709.

Miscellaneous databases

EvolutionaryTraceiQ8A1G3.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 3 hits.
PfamiPF00128. Alpha-amylase. 2 hits.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 2, 2016
This is version 94 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.