ID K0DVI4_9BURK Unreviewed; 1150 AA.
AC K0DVI4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
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=BUPH_01489 {ECO:0000313|EMBL:AFT88935.1};
OS Paraburkholderia phenoliruptrix BR3459a.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1229205 {ECO:0000313|EMBL:AFT88935.1, ECO:0000313|Proteomes:UP000010105};
RN [1] {ECO:0000313|EMBL:AFT88935.1, ECO:0000313|Proteomes:UP000010105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR3459a {ECO:0000313|EMBL:AFT88935.1,
RC ECO:0000313|Proteomes:UP000010105};
RX PubMed=23144415; DOI=10.1128/JB.01821-12;
RA de Oliveira Cunha C., Goda Zuleta L.F., Paula de Almeida L.G.,
RA Prioli Ciapina L., Lustrino Borges W., Pitard R.M., Baldani J.I.,
RA Straliotto R., de Faria S.M., Hungria M., Sousa Cavada B., Mercante F.M.,
RA Ribeiro de Vasconcelos A.T.;
RT "Complete Genome Sequence of Burkholderia phenoliruptrix BR3459a (CLA1), a
RT Heat-Tolerant, Nitrogen-Fixing Symbiont of Mimosa flocculosa.";
RL J. Bacteriol. 194:6675-6676(2012).
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}.
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DR EMBL; CP003864; AFT88935.1; -; Genomic_DNA.
DR RefSeq; WP_014972763.1; NC_018672.1.
DR AlphaFoldDB; K0DVI4; -.
DR STRING; 1229205.BUPH_01489; -.
DR GeneID; 27800219; -.
DR KEGG; bpx:BUPH_01489; -.
DR PATRIC; fig|1229205.11.peg.5470; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_007336_1_0_4; -.
DR Proteomes; UP000010105; Chromosome 2.
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; 2.
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; 2.
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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02124}.
FT DOMAIN 666..1011
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1120..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 846
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT ACT_SITE 875
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 714
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 774
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 809
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 847
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 986..987
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT SITE 933
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
SQ SEQUENCE 1150 AA; 127418 MW; 9012DC9AAB4241B6 CRC64;
MEPPNGYAPR IYFFHSLLVG PLDAWPAQFA HAAALGFDHA LIGSLFEPGR ASHGQVVGNH
ARLHPVFEAE QPAGDAIRTL AGEARSHGLT LLADLVIDRV AADGALYAEH ADWFYPLETE
EARLDPRHVH REDNVAYANF SDAGTRAALA DWWTQQLLAL AAAGIGGFRF DSPHRVPVEV
WRQLREAVRA AHPDVRFLAA TPGLARSDLA GLEGAGFDSV FSSVRWWDYR ASWMVEEHAA
LARIGGPIAF PEAPYGTRLA AELSDPHDSG SVERAYRRAL FTASAVGTGW MMPMGFEYGV
SEPMSQTRGD ASQFALACQA KRFDLSQPIS HANELLRNAK ALQVNGELRP LSGPGAPAAV
LLRADQPDLR EAGEAVLIAI NPELGAPVRV DPARFLAGVP GNFTRFVALD APGRASPAAL
TPFTLAPGAV RLFQAMTEKP ICLAPPIDKA NSKRSGRKTV LEAINAPRVA IESVMPSVDN
GRFAAKRSVG ERAEISAAIF AEGHDKIAAA VLWRAADENT WHEVLMAPAQ PAGLDIWKAR
IPLERMGRHE FTVIAWRDDF ASLVEHVEKK LKAGQTVEIE LDEAAHLFAL VLAEVETAEG
ADKAPLEHIV TQFKKADDET KLKLLLDPAT AKAMTTARHR PFLSRDPVTY KIDAERTAAR
FASWYEIFPR SMSDDESRHG TFADVTKKLP RIRDMGFDVL YFPPIHPIGM TNRKGRNNTL
NAQPGDVGSP YAIGAAEGGH TAVHPQLGTL DDFKAMLAAA RAHGLEIALD FAIQCSPDHP
WLKEHPTWFA WRPDGTLRYA ENPPKKYQDI VNPDFYAHDA KPDLWLALRD VILFWIEAGV
HIFRVDNPHT KPLPFWEWMI NDVRSRYPET IFLAEAFTRP RMMNRLGKIG FSQSYTYFTW
RESKRDFIEY LSELTQTGAR DFYRPNFFVN TPDINPRHLQ SQGRTGFLIR AALASTLAGL
WGVYSGFELC EAAALPNSEE YLDSEKYQLR AWDWNRPGNI VAEITALNRI RRANPALQTH
LGLTFLPAHN DNILFFEKAT ESRDNVIVVA INLDPFNEQG ADIELSWETF QKWNLHDHGP
LEVTDQMTGA RFEWHGRWQH VRLGPGQPFS IWRIAPLGGL PAERPDEADS DPTGAPHADA
GNPTPTEGAI
//
