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Protein

Amylosucrase

Gene

ams

Organism
Neisseria polysaccharea
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the synthesis of alpha-glucan from sucrose. Catalyzes, in addition, sucrose hydrolysis, maltose and maltotriose synthesis by successive transfers of the glucosyl moiety of sucrose onto the released glucose, and finally turanose and trehalulose synthesis, these two sucrose isomers being obtained by glucosyl transfer onto fructose.1 Publication

Catalytic activityi

Sucrose + ((1->4)-alpha-D-glucosyl)(n) = D-fructose + ((1->4)-alpha-D-glucosyl)(n+1).2 Publications

Enzyme regulationi

Amylosucrase favors hydrolysis at low sucrose concentrations, and polymerization at high sucrose concentrations. Competitively inhibited by fructose.

Kineticsi

This enzyme does not present a classic Michaelis-Menten behavior for sucrose consumption, that could be related to the presence of a second sucrose binding site. Nevertheless, it is possible to model sucrose consumption rate versus sucrose concentration by two different Michaelis-Menten equations whose apparent kinetic constants are given just above.

  1. KM=1.9 mM for sucrose (in the sucrose consumption assay, when initial sucrose < 20 mM)1 Publication
  2. KM=1.7 mM for sucrose (in the sucrose hydrolysis reaction, when initial sucrose < 20 mM)1 Publication
  3. KM=1.9 mM for sucrose (in the polymerization reaction, when initial sucrose < 20 mM)1 Publication
  4. KM=50.2 mM for sucrose (in the sucrose consumption assay, when initial sucrose > 20 mM)1 Publication
  5. KM=38.7 mM for sucrose (in the sucrose hydrolysis reaction, when initial sucrose > 20 mM)1 Publication
  1. Vmax=470 µmol/min/g enzyme for sucrose consumption (when initial sucrose < 20 mM)1 Publication
  2. Vmax=288 µmol/min/g enzyme for sucrose hydrolysis (when initial sucrose < 20 mM)1 Publication
  3. Vmax=147 µmol/min/g enzyme for polymerization reaction (when initial sucrose < 20 mM)1 Publication
  4. Vmax=1100 µmol/min/g enzyme for sucrose consumption (when initial sucrose > 20 mM)1 Publication
  5. Vmax=472 µmol/min/g enzyme for sucrose hydrolysis (when initial sucrose > 20 mM)1 Publication
  6. Vmax=1620 µmol/min/g enzyme for polymerization reaction (when initial sucrose > 20 mM)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei152Substrate3 Publications1
Binding sitei195Substrate3 Publications1
Binding sitei262Substrate3 Publications1
Binding sitei292Substrate3 Publications1
Active sitei294Nucleophile1 Publication1 Publication1
Active sitei336Proton donor1 Publication1
Binding sitei400Substrate3 Publications1
Binding sitei401Substrate3 Publications1
Sitei452Transition state stabilizerBy similarity1
Binding sitei517Substrate3 Publications1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.1.4. 3596.
SABIO-RKQ9ZEU2.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Amylosucrase (EC:2.4.1.42 Publications)
Gene namesi
Name:ams
OrganismiNeisseria polysaccharea
Taxonomic identifieri489 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi195H → Q: 98% reduction of activity. 1 Publication1
Mutagenesisi294D → E or N: Complete loss of activity. 1 Publication1
Mutagenesisi308E → Q: No effect. 1 Publication1
Mutagenesisi336E → Q: Complete loss of activity. 1 Publication1
Mutagenesisi352E → Q: 30% reduction of activity. 1 Publication1
Mutagenesisi400H → N: 97% reduction of activity. 1 Publication1
Mutagenesisi401D → E: Almost complete loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000451541 – 636AmylosucraseAdd BLAST636

Interactioni

Subunit structurei

Monomer.4 Publications

Protein-protein interaction databases

STRINGi546267.NEIPOLOT_01155.

Structurei

Secondary structure

1636
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 19Combined sources7
Helixi20 – 22Combined sources3
Helixi25 – 33Combined sources9
Helixi35 – 59Combined sources25
Helixi65 – 82Combined sources18
Helixi85 – 95Combined sources11
Helixi98 – 102Combined sources5
Beta strandi108 – 111Combined sources4
Helixi113 – 117Combined sources5
Helixi120 – 125Combined sources6
Helixi127 – 133Combined sources7
Beta strandi136 – 140Combined sources5
Turni152 – 155Combined sources4
Beta strandi160 – 163Combined sources4
Turni165 – 167Combined sources3
Helixi170 – 182Combined sources13
Beta strandi186 – 191Combined sources6
Beta strandi194 – 197Combined sources4
Helixi201 – 207Combined sources7
Helixi211 – 213Combined sources3
Beta strandi219 – 223Combined sources5
Helixi224 – 229Combined sources6
Turni230 – 232Combined sources3
Turni238 – 240Combined sources3
Beta strandi245 – 247Combined sources3
Beta strandi253 – 255Combined sources3
Beta strandi257 – 259Combined sources3
Beta strandi262 – 265Combined sources4
Helixi270 – 284Combined sources15
Turni285 – 287Combined sources3
Beta strandi289 – 293Combined sources5
Helixi296 – 298Combined sources3
Beta strandi307 – 309Combined sources3
Helixi311 – 327Combined sources17
Beta strandi332 – 335Combined sources4
Helixi341 – 344Combined sources4
Helixi345 – 347Combined sources3
Beta strandi352 – 357Combined sources6
Helixi359 – 371Combined sources13
Helixi375 – 383Combined sources9
Beta strandi392 – 397Combined sources6
Helixi409 – 414Combined sources6
Helixi419 – 430Combined sources12
Beta strandi442 – 444Combined sources3
Turni448 – 450Combined sources3
Beta strandi454 – 456Combined sources3
Helixi459 – 463Combined sources5
Helixi465 – 467Combined sources3
Helixi472 – 485Combined sources14
Beta strandi486 – 493Combined sources8
Helixi496 – 498Combined sources3
Helixi506 – 508Combined sources3
Turni510 – 514Combined sources5
Helixi516 – 520Combined sources5
Helixi526 – 529Combined sources4
Turni530 – 533Combined sources4
Helixi538 – 555Combined sources18
Helixi557 – 559Combined sources3
Beta strandi564 – 566Combined sources3
Beta strandi574 – 579Combined sources6
Turni580 – 582Combined sources3
Beta strandi583 – 588Combined sources6
Beta strandi590 – 592Combined sources3
Beta strandi594 – 596Combined sources3
Turni598 – 603Combined sources6
Beta strandi606 – 610Combined sources5
Turni611 – 613Combined sources3
Beta strandi616 – 618Combined sources3
Beta strandi623 – 625Combined sources3
Beta strandi630 – 634Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G5AX-ray1.40A13-636[»]
1JG9X-ray1.66A13-636[»]
1JGIX-ray2.00A13-636[»]
1MVYX-ray2.00A13-636[»]
1MW0X-ray2.01A13-636[»]
1MW1X-ray2.10A13-636[»]
1MW2X-ray2.10A13-636[»]
1MW3X-ray2.00A13-636[»]
1S46X-ray2.20A13-636[»]
1ZS2X-ray2.16A13-636[»]
3UEQX-ray1.85A13-636[»]
4FLOX-ray2.20A13-636[»]
4FLQX-ray2.50A13-636[»]
4FLRX-ray2.40A13-636[»]
4FLSX-ray2.30A13-636[»]
ProteinModelPortaliQ9ZEU2.
SMRiQ9ZEU2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ZEU2.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Phylogenomic databases

eggNOGiENOG4107QW3. Bacteria.
COG0366. LUCA.

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. 2 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9ZEU2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTPTQQVGL ILQYLKTRIL DIYTPEQRAG IEKSEDWRQF SRRMDTHFPK
60 70 80 90 100
LMNELDSVYG NNEALLPMLE MLLAQAWQSY SQRNSSLKDI DIARENNPDW
110 120 130 140 150
ILSNKQVGGV CYVDLFAGDL KGLKDKIPYF QELGLTYLHL MPLFKCPEGK
160 170 180 190 200
SDGGYAVSSY RDVNPALGTI GDLREVIAAL HEAGISAVVD FIFNHTSNEH
210 220 230 240 250
EWAQRCAAGD PLFDNFYYIF PDRRMPDQYD RTLREIFPDQ HPGGFSQLED
260 270 280 290 300
GRWVWTTFNS FQWDLNYSNP WVFRAMAGEM LFLANLGVDI LRMDAVAFIW
310 320 330 340 350
KQMGTSCENL PQAHALIRAF NAVMRIAAPA VFFKSEAIVH PDQVVQYIGQ
360 370 380 390 400
DECQIGYNPL QMALLWNTLA TREVNLLHQA LTYRHNLPEH TAWVNYVRSH
410 420 430 440 450
DDIGWTFADE DAAYLGISGY DHRQFLNRFF VNRFDGSFAR GVPFQYNPST
460 470 480 490 500
GDCRVSGTAA ALVGLAQDDP HAVDRIKLLY SIALSTGGLP LIYLGDEVGT
510 520 530 540 550
LNDDDWSQDS NKSDDSRWAH RPRYNEALYA QRNDPSTAAG QIYQGLRHMI
560 570 580 590 600
AVRQSNPRFD GGRLVTFNTN NKHIIGYIRN NALLAFGNFS EYPQTVTAHT
610 620 630
LQAMPFKAHD LIGGKTVSLN QDLTLQPYQV MWLEIA
Length:636
Mass (Da):72,344
Last modified:May 1, 1999 - v1
Checksum:iB7656C19BF1A2065
GO

Sequence cautioni

The sequence described in PubMed:9150231 differs from that shown. Reason: Frameshift at positions 183, 203, 274, 313, 507, 538 and 579.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14Y → H in AAM51153 (PubMed:12517860).Curated1
Sequence conflicti84 – 85NS → SA in AAM51153 (PubMed:12517860).Curated2
Sequence conflicti89D → N in AAM51153 (PubMed:12517860).Curated1
Sequence conflicti93A → E in AAM51153 (PubMed:12517860).Curated1
Sequence conflicti159S → T AA sequence (PubMed:9150231).Curated1
Sequence conflicti171G → D in AAM51153 (PubMed:12517860).Curated1
Sequence conflicti208Missing AA sequence (PubMed:9150231).Curated1
Sequence conflicti392A → S in AAM51153 (PubMed:12517860).Curated1
Sequence conflicti437S → T AA sequence (PubMed:9150231).Curated1
Sequence conflicti449S → N in AAM51153 (PubMed:12517860).Curated1
Sequence conflicti459A → S in AAM51153 (PubMed:12517860).Curated1
Sequence conflicti463V → A in AAM51153 (PubMed:12517860).Curated1
Sequence conflicti468D → N in AAM51153 (PubMed:12517860).Curated1
Sequence conflicti474D → S in AAM51153 (PubMed:12517860).Curated1
Sequence conflicti501L → P in AAM51153 (PubMed:12517860).Curated1
Sequence conflicti505 – 510DWSQDS → GWAQDG in AAM51153 (PubMed:12517860).Curated6

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ011781 Genomic DNA. Translation: CAA09772.1.
AY099335 Genomic DNA. Translation: AAM51153.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ011781 Genomic DNA. Translation: CAA09772.1.
AY099335 Genomic DNA. Translation: AAM51153.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G5AX-ray1.40A13-636[»]
1JG9X-ray1.66A13-636[»]
1JGIX-ray2.00A13-636[»]
1MVYX-ray2.00A13-636[»]
1MW0X-ray2.01A13-636[»]
1MW1X-ray2.10A13-636[»]
1MW2X-ray2.10A13-636[»]
1MW3X-ray2.00A13-636[»]
1S46X-ray2.20A13-636[»]
1ZS2X-ray2.16A13-636[»]
3UEQX-ray1.85A13-636[»]
4FLOX-ray2.20A13-636[»]
4FLQX-ray2.50A13-636[»]
4FLRX-ray2.40A13-636[»]
4FLSX-ray2.30A13-636[»]
ProteinModelPortaliQ9ZEU2.
SMRiQ9ZEU2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi546267.NEIPOLOT_01155.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107QW3. Bacteria.
COG0366. LUCA.

Enzyme and pathway databases

BRENDAi2.4.1.4. 3596.
SABIO-RKQ9ZEU2.

Miscellaneous databases

EvolutionaryTraceiQ9ZEU2.

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. 2 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAMYS_NEIPO
AccessioniPrimary (citable) accession number: Q9ZEU2
Secondary accession number(s): Q84HD5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: May 1, 1999
Last modified: November 2, 2016
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

Miscellaneous

Like the recombinant protein expressed in E.coli, the amylosucrase may be secreted in N.polysaccharea without cleavage of a signal sequence.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.