ID   GLGE2_STRCO             Reviewed;         669 AA.
AC   Q9KY04; O70012;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 2;
DE            Short=GMPMT 2;
DE            EC=2.4.99.16;
DE   AltName: Full=(1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase 2;
GN   Name=glgE2; Synonyms=pep1, pep1B, pep1II; OrderedLocusNames=SCO7335;
GN   ORFNames=SC4G10.14c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3(2) / NRRL B-16638;
RX   PubMed=10821190; DOI=10.1007/s004380051200;
RA   Schneider D., Bruton C.J., Chater K.F.;
RT   "Duplicated gene clusters suggest an interplay of glycogen and trehalose
RT   metabolism during sequential stages of aerial mycelium development in
RT   Streptomyces coelicolor A3(2).";
RL   Mol. Gen. Genet. 263:543-553(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND KINETIC
RP   PARAMETERS.
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=21914799; DOI=10.1074/jbc.m111.279315;
RA   Syson K., Stevenson C.E., Rejzek M., Fairhurst S.A., Nair A., Bruton C.J.,
RA   Field R.A., Chater K.F., Lawson D.M., Bornemann S.;
RT   "Structure of a Streptomyces maltosyltransferase GlgE: a homologue of a
RT   genetically validated anti-tuberculosis target.";
RL   J. Biol. Chem. 286:38298-38310(2011).
CC   -!- FUNCTION: Maltosyltransferase that uses maltose 1-phosphate (M1P) as
CC       the sugar donor to elongate linear or branched alpha-(1->4)-glucans.
CC       Maltooligosaccharides with a degree of polymerization (DP) superior or
CC       equal to 4 are efficient acceptors, with DP6 being optimal in the GlgE-
CC       catalyzed polymerization with M1P. Is probably involved in a branched
CC       alpha-glucan biosynthetic pathway from trehalose, together with TreS,
CC       Mak and GlgB. {ECO:0000269|PubMed:21914799}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-glucosyl](n) + alpha-maltose 1-phosphate =
CC         [(1->4)-alpha-D-glucosyl](n+2) + phosphate; Xref=Rhea:RHEA:42692,
CC         Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:10183, ChEBI:CHEBI:15444,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:63576; EC=2.4.99.16;
CC         Evidence={ECO:0000269|PubMed:21914799};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.3 mM for maltohexaose (in the presence of 5 mM M1P)
CC         {ECO:0000269|PubMed:21914799};
CC         KM=1.2 mM for alpha-maltose 1-phosphate
CC         {ECO:0000269|PubMed:21914799};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgE
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ001206; CAA04606.1; -; Genomic_DNA.
DR   EMBL; AL939131; CAB92881.1; -; Genomic_DNA.
DR   RefSeq; NP_631389.1; NC_003888.3.
DR   RefSeq; WP_011031595.1; NZ_CP042324.1.
DR   AlphaFoldDB; Q9KY04; -.
DR   SMR; Q9KY04; -.
DR   STRING; 100226.SCO7335; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GeneID; 1102773; -.
DR   KEGG; sco:SCO7335; -.
DR   PATRIC; fig|100226.15.peg.7439; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_015798_0_0_11; -.
DR   InParanoid; Q9KY04; -.
DR   OMA; NLRFHHT; -.
DR   PhylomeDB; Q9KY04; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0016758; F:hexosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0030979; P:alpha-glucan biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   HAMAP; MF_02124; GlgE; 1.
DR   InterPro; IPR026585; GlgE.
DR   InterPro; IPR021828; GlgE_dom_N/S.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR10357:SF203; PTHR10357:SF203; 1.
DR   Pfam; PF11896; DUF3416; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..669
FT                   /note="Alpha-1,4-glucan:maltose-1-phosphate
FT                   maltosyltransferase 2"
FT                   /id="PRO_0000054350"
FT   ACT_SITE        385
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        414
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         255
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000250"
FT   BINDING         315
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000250"
FT   BINDING         350
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000250"
FT   BINDING         386
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000250"
FT   BINDING         525..526
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000250"
FT   SITE            471
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        632
FT                   /note="W -> R (in Ref. 1; CAA04606)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   669 AA;  74143 MW;  5463E0134CD66518 CRC64;
     MRMSATVGIG RIPVRDVQPV VEYGRRPAKA VTGETFEVTA TVFREGHDAV AANVVLKDPE
     GRPGPWTPMR ELAPGSDRWG ATVTPGAPGN WTYRVEAWSD PVATWRHAAR IKVPAGIDAG
     LVLEEGSELY RRAAAGVPKD SGRDVLLAAA TALLDDTLPV ATRLAAALTP QVDAVLARHP
     LRDLVTSSDP LPLLVERERA LYGAWYEFFP RSEGTPHTPH GTFRTAARRL PAIAAMGFDV
     VYLPPIHPIG TTHRKGRNNT LSATGDDVGV PWAIGSPEGG HDSIHPALGT LDDFDHFVTE
     AARHGLEIAL DFALQCSPDH PWVHKHPEWF HHRPDGTIAH AENPPKKYQD IYPIAFDADP
     DGLATETVRI LRHWMDHGVR IFRVDNPHTK PVAFWERVIA DINGTDPDVI FLAEAFTRPA
     MMATLAQIGF QQSYTYFTWR NTKQELTEYL EELSGEAAAY MRPNFFANTP DILHAYLQHG
     GRPAFEVRAV LAATLSPTWG IYSGYELCEN TPLREGSEEY LDSEKYQLKP RDWTRAAREG
     TTIAPLVTRL NTIRREHPAL HRLRNLRFHH TDNDALIAYS KRVGSDVVLV VANLDPHRTQ
     EATISLDMPQ LGLDWHDSVP VHDELTGRTY HWGRANYVRL EPGRAPAHVF HVRRPSAAAA
     PQNGGSGAS