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Database: UniProt
Entry: A4BM96_9GAMM
LinkDB: A4BM96_9GAMM
Original site: A4BM96_9GAMM 
ID   A4BM96_9GAMM            Unreviewed;       666 AA.
AC   A4BM96;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase {ECO:0000256|HAMAP-Rule:MF_02124};
DE            Short=GMPMT {ECO:0000256|HAMAP-Rule:MF_02124};
DE            EC=2.4.99.16 {ECO:0000256|HAMAP-Rule:MF_02124};
DE   AltName: Full=(1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase {ECO:0000256|HAMAP-Rule:MF_02124};
GN   Name=glgE {ECO:0000256|HAMAP-Rule:MF_02124};
GN   ORFNames=NB231_16478 {ECO:0000313|EMBL:EAR23434.1};
OS   Nitrococcus mobilis Nb-231.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Nitrococcus.
OX   NCBI_TaxID=314278 {ECO:0000313|EMBL:EAR23434.1, ECO:0000313|Proteomes:UP000003374};
RN   [1] {ECO:0000313|EMBL:EAR23434.1, ECO:0000313|Proteomes:UP000003374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nb-231 {ECO:0000313|EMBL:EAR23434.1,
RC   ECO:0000313|Proteomes:UP000003374};
RA   Waterbury J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA   Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00000575, ECO:0000256|HAMAP-
CC         Rule:MF_02124};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_02124}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgE
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_02124}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAR23434.1}.
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DR   EMBL; AAOF01000001; EAR23434.1; -; Genomic_DNA.
DR   RefSeq; WP_005004716.1; NZ_CH672427.1.
DR   AlphaFoldDB; A4BM96; -.
DR   STRING; 314278.NB231_16478; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_015798_0_0_6; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000003374; Unassembled WGS sequence.
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   CDD; cd11344; AmyAc_GlgE_like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR   HAMAP; MF_02124; GlgE; 1.
DR   InterPro; IPR026585; GlgE.
DR   InterPro; IPR049171; GLGE_C.
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; PTHR47786:SF2; AAMY DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR47786; ALPHA-1,4-GLUCAN:MALTOSE-1-PHOSPHATE MALTOSYLTRANSFERASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF21702; GLGE_C; 1.
DR   Pfam; PF11896; GlgE_dom_N_S; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_02124};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_02124}; Reference proteome {ECO:0000313|Proteomes:UP000003374};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_02124}.
FT   DOMAIN          201..551
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        384
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT   ACT_SITE        413
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT   BINDING         253
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT   BINDING         313
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT   BINDING         348
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT   BINDING         385
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT   BINDING         526..527
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT   SITE            471
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
SQ   SEQUENCE   666 AA;  76486 MW;  DC3060CA444DCF8F CRC64;
     MAASSQSDGR KRVVIEGVAP AVDAGRFPIK RTLGEKVVVE ADAFVDGHDQ LACVLCYRKA
     ATETWTEVAM RPLGNDRWSG EFAVDELGRY GYTVTAWVDH FRTWCAELKK RTKAEDIASA
     LMIGAELIEA AAARANEPPD AAELHRYAKA LRTAGDPLTR RSQALDPALA QLMAQSPDRM
     FATTYERELM VVVDVAHARF STWYELFPRS CVQEPGTHGS LRSCAERLPY IAAMGFDVLY
     LPPIHPIGTT ARKGRNNTLN ASAEDPGSPW AIGSEAGGHK AVHPQLGTLE DFRHLVRRAR
     EQGLEVALDI AFQCSPDHPY VKQAPQWFRW RPDGTVQYAE NPPKKYQDIY PFNFESEDWQ
     GLWDELEDVF LFWIEQGVRI FRVDNPHTKP FPFWEWLITH VKAQHPEVIF LAEAFTRPKV
     MHRLAKLGFT QSYTYFTWRN NKWELMEYFT ELTQTPSREY FRPNLWPNTP DILNEYLQVG
     GRPAFMTRLV LAATLGANYG IYGPAFELCE ARPREPGSEE YLDSEKYEIR AWELERPDSL
     AHFITRVNQI RRENPALQQD WSLRFHPVDN EALVCYSKHC DALDNVILVV VNVDPHHTQA
     GWVELPLEAL QLLPEHPYQV HDLLSDARYL WQGARNYVEL DPHSAPAHIF RVRRHVRTEH
     DFDYFM
//
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