GLGE_RHORT
ID GLGE_RHORT Reviewed; 688 AA.
AC Q2RTZ1;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase {ECO:0000255|HAMAP-Rule:MF_02124};
DE Short=GMPMT {ECO:0000255|HAMAP-Rule:MF_02124};
DE EC=2.4.99.16 {ECO:0000255|HAMAP-Rule:MF_02124};
DE AltName: Full=(1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase {ECO:0000255|HAMAP-Rule:MF_02124};
GN Name=glgE {ECO:0000255|HAMAP-Rule:MF_02124}; OrderedLocusNames=Rru_A1604;
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
CC -!- FUNCTION: Maltosyltransferase that uses maltose 1-phosphate (M1P) as
CC the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Is
CC involved in a branched alpha-glucan biosynthetic pathway from
CC trehalose, together with TreS, Mak and GlgB. {ECO:0000255|HAMAP-
CC Rule:MF_02124}.
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:0000255|HAMAP-Rule:MF_02124};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02124}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgE
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_02124}.
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DR EMBL; CP000230; ABC22404.1; -; Genomic_DNA.
DR RefSeq; WP_011389479.1; NC_007643.1.
DR RefSeq; YP_426691.1; NC_007643.1.
DR AlphaFoldDB; Q2RTZ1; -.
DR SMR; Q2RTZ1; -.
DR STRING; 269796.Rru_A1604; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; ABC22404; ABC22404; Rru_A1604.
DR KEGG; rru:Rru_A1604; -.
DR PATRIC; fig|269796.9.peg.1680; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_015798_0_0_5; -.
DR OMA; RPNFWPN; -.
DR OrthoDB; 1573900at2; -.
DR PhylomeDB; Q2RTZ1; -.
DR Proteomes; UP000001929; 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; PF00128; Alpha-amylase; 1.
DR Pfam; PF11896; DUF3416; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycosyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..688
FT /note="Alpha-1,4-glucan:maltose-1-phosphate
FT maltosyltransferase"
FT /id="PRO_0000413901"
FT ACT_SITE 420
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT ACT_SITE 449
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 289
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 349
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 384
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 421
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 560..561
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT SITE 507
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
SQ SEQUENCE 688 AA; 76410 MW; 3DF74E7F2CC962FF CRC64;
MSSALPPFRP SLVSDPLSAR QDPSLPGILP VSAPILIEDI GPRVSDGRYP IKRVLGEGVV
VSAAVFRDGH VPLAAALLWR RSPRPGEPAG GRGAWHEVPL TQIEPGLARW RARFDPPAIG
RFDYLIEAWS DDWAGWRHDT LIKRDAGLDL SLEVLEGMAL IEATIARIDG TDQAADQGLL
SSWLADAQGL ETAGGRATLM LSETLDAVMA RHPDRSGAVR SGPPLSVVVD PPRAGFAAWY
EMAPRSQASE PGRWGTFADC AARLPDIRAM GFDTLYLMPI HPIGRIHRKG PNNSLKAGPD
DPGSPYAIGA AEGGHTAIHP ELGTLDEFRA LVAQAGEMGM DVALDIAIQC APDHPWVSEH
PEWFEFRPDG TIKYAENPPK KYQDIVNLAF WGPHRQELWL ALLEVFTFWA EQGVRVFRVD
NPHTKPVPFW EWLIATVKAR YPDCIFLAEA FTRPPMMKML AKIGFTQSYS YFTWRTTKAE
LTSYMEELVE DDPADYMRVN FFANTPDILP FHLQTGGRPA FMQRLVLAAT LSSVYGIHNG
FELCENAAIP GKEEYADSEK YDFKPRDWNA EGNIKDLIAK VNWIRNENPA LQAFRTLRFF
RADNDQILFY GKMTGDRANI ILVAVNLDPH AGQGGLLWLP LAEMGLSDGQ PFIVEELLSG
TRLEWTGSPH HYWFDPATNP AAIFRITP
