ID   AMYS_NEIME              Reviewed;         636 AA.
AC   Q84HD6;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Amylosucrase;
DE            EC=2.4.1.4 {ECO:0000250|UniProtKB:Q9ZEU2};
GN   Name=ams;
OS   Neisseria meningitidis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=487;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=93246;
RX   PubMed=12517860; DOI=10.1128/jcm.41.1.273-278.2003;
RA   Zhu P., Tsang R.S.W., Tsai C.-M.;
RT   "Nonencapsulated Neisseria meningitidis strain produces amylopectin from
RT   sucrose: altering the concept for differentiation between N. meningitidis
RT   and N. polysaccharea.";
RL   J. Clin. Microbiol. 41:273-278(2003).
CC   -!- FUNCTION: Catalyzes the synthesis of alpha-glucan from sucrose.
CC       Catalyzes, in addition, sucrose hydrolysis, maltose and maltotriose
CC       synthesis by successive transfers of the glucosyl moiety of sucrose
CC       onto the released glucose, and finally turanose and trehalulose
CC       synthesis, these two sucrose isomers being obtained by glucosyl
CC       transfer onto fructose (By similarity). {ECO:0000250|UniProtKB:Q9ZEU2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-glucosyl](n) + sucrose = [(1->4)-alpha-D-
CC         glucosyl](n+1) + D-fructose; Xref=Rhea:RHEA:24572, Rhea:RHEA-
CC         COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15444, ChEBI:CHEBI:17992,
CC         ChEBI:CHEBI:37721; EC=2.4.1.4;
CC         Evidence={ECO:0000250|UniProtKB:Q9ZEU2};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9ZEU2}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9ZEU2}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; AY099334; AAM51152.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q84HD6; -.
DR   SMR; Q84HD6; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PRIDE; Q84HD6; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0047669; F:amylosucrase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11324; AmyAc_Amylosucrase; 1.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 3.90.400.10; -; 1.
DR   InterPro; IPR044077; Amylosucrase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR045857; O16G_dom_2.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Secreted; Transferase.
FT   CHAIN           1..636
FT                   /note="Amylosucrase"
FT                   /id="PRO_0000045153"
FT   ACT_SITE        294
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT   ACT_SITE        336
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT   BINDING         195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT   BINDING         262
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT   BINDING         292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT   BINDING         400
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT   BINDING         401
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT   BINDING         517
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT   SITE            452
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   636 AA;  72340 MW;  4EE1D80F1F55B37D CRC64;
     MLTPTQQVGL ILQYLKTRIL DIYTPEQRAG IEKSEDWRQF SRRMDTHFPK LMNELDSVYG
     NNEALLPMLE MLLAQAWQSY SQRSASLKNI DIERENNPDW ILSNKQVGGV CYVDLFAGDL
     KGLKDKIHYF QELGLTYLHL MPLFKCPEGK SDGGYAVSSY RDVNPALGTI GDLREVIAAL
     HEAGISAVVD FIFNHTSNEH EWAQRCAAGD PLFDNFYYIF PDRRMPDQYD RTLREIFPDQ
     HPGGFSQLED GRWVWTTFNS FQWDLNYSNP WVFRAMAGEM MFLANLGVDI LRMDAVAFIW
     KQMGTSCENL PQAHALIRAF NAVMRIAAPA VFFKSEAIVH PDQVVQYIGQ DECQIGYNPL
     QMALLWNTLA TREVNLLHQA LTYRHNLPEH TAWVNYVRSH DDIGWTFADE DAAYLGISGY
     DHRQFLNRFF VNRFDGSFAR GVPFQYNPNT GDCRVSGTSA ALAGLAQNDP HAVSRIKLLY
     SIALSTGGLP LIYLGDEVGT PNDDGWVQDS NKSDDSRWAH RPRYNEALYA QRNDPSTAAG
     QIYQGLRHMI AVRQSNPRFD GGRLVTFNTN NKHIIGYIRN NALLAFGNFS EYPQTVTAHT
     LQAMPFKAHD LIGGKTVSLN QDLTLQPYQV MWLEIA