ID B2UHJ2_RALPJ Unreviewed; 1164 AA.
AC B2UHJ2;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=maltose alpha-D-glucosyltransferase {ECO:0000256|ARBA:ARBA00012619};
DE EC=5.4.99.16 {ECO:0000256|ARBA:ARBA00012619};
DE AltName: Full=Maltose alpha-D-glucosyltransferase {ECO:0000256|ARBA:ARBA00031378};
GN OrderedLocusNames=Rpic_3938 {ECO:0000313|EMBL:ACD29043.1};
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29043.1};
RN [1] {ECO:0000313|EMBL:ACD29043.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=12J {ECO:0000313|EMBL:ACD29043.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT "Complete sequence of chromosome2 of Ralstonia pickettii 12J.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-maltose = alpha,alpha-trehalose; Xref=Rhea:RHEA:15145,
CC ChEBI:CHEBI:16551, ChEBI:CHEBI:17306; EC=5.4.99.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001595};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. TreS
CC subfamily. {ECO:0000256|ARBA:ARBA00005496}.
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DR EMBL; CP001069; ACD29043.1; -; Genomic_DNA.
DR AlphaFoldDB; B2UHJ2; -.
DR STRING; 402626.Rpic_3938; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; rpi:Rpic_3938; -.
DR PATRIC; fig|402626.5.peg.177; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG3281; Bacteria.
DR HOGENOM; CLU_007635_0_1_4; -.
DR GO; GO:0047471; F:maltose alpha-D-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11334; AmyAc_TreS; 1.
DR Gene3D; 3.90.1200.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032091; Malt_amylase_C.
DR InterPro; IPR045857; O16G_dom_2.
DR InterPro; IPR012810; TreS/a-amylase_N.
DR InterPro; IPR012811; TreS_maltokin_C_dom.
DR NCBIfam; TIGR02457; TreS_Cterm; 1.
DR NCBIfam; TIGR02456; treS_nterm; 1.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF219; MALTOSE ALPHA-D-GLUCOSYLTRANSFERASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF16657; Malt_amylase_C; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 23..417
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1164 AA; 130417 MW; E953DF84E9272AE0 CRC64;
MTRNPTALLV DDALWYKDAV IYQLHVKSFC DSDNDGVGDF PGLISKLDYI AELGVDVIWL
LPFYPSPRRD DGYDIAEYRG VHPDYGNMAD VRRFIAEAHA RGLRVITELV INHTSDQHPW
FQRARRAKPG SALRDFYVWS DNDKRYAGTR IIFIDTEPSN WTWDPVANAY YWHRFYSHQP
DLNFDNPRVL KAVIGVMKFW LNLGVDGLRL DAVPYLVERE GTSNENLPET HEVLRKIRAA
MDGEFKNRLL LAEANQWPED TQEYFGAGDE CHMAFHFPLM PRMYMAIARE DRFPITDIMR
QTPEVPAGCQ WAIFLRNHDE LTLEMVTDAE RDYLWEVYAS DRRARLNLGI RRRLAPLLER
DRRRVELMNS LLFSMPGTPV MYYGDEIGMG DNIHLGDRDG VRTPMQWSPD RNGGFSRADP
EQLVLPAIMG SLYGYESVNV EAQSRDAHSL LNWTRRLLAT RKRHRVFGRG SIQFLQPSNR
KVLAYIRALE GEAPILCVAN LSRASQAVEL DLSTFAQRVP VELIGGTAFP PIGQLSYLLT
LPPYAFYWLE LRENEPGPTW SQPAAEQLPE FTTLVLRAGL DALADTRQRE AHRQLIEREI
LPTYLPKRRW FAAKDSVLRS AKFAWGAPVP VDAASTNRPL AGATRPEVFL NEVAVTLGSP
DGTERVERYL LPLSIAWESA TLPALPIQLA LARVRRGRHV GYLTDAFTTE TFARALLTNL
VRGTTLEAND GTVHFEPEPN IAELAEPAGA PEAGSTRPAP LPLAPDTPIQ WLAAEQSNSS
LVIGESVIVK LIRRIATGIH PEVEMTRHLT RVGYANTAAL IGEVSHHAAD GERATLAVMQ
SFVPNQGDAW TWALDYLRRT IDELAVQMEG VTTGDGESSP VAVSEARVDT DEALAGYVNF
IGVIGTRLGE LHAALAAPTE DPNFGARIAD ADDATYWIAR VSEQLTRAHD NLTAWQRQNP
DSARQPDVQW LLSQHQALLD AARAHAENGL GATLSRIHGD FHLGQVLVAQ GDAFLIDFEG
EPSRPVEERR RKTSPLRDVA GLMRSLDYVV GAMRQGPDHV AGPAQERRNV LLERFRAAST
ERFLEAYAAA IRGPDLNALD QPVVDFHLLD LFLLEKAAYE VNYEASNRPT WLPIPLEGFT
RVARRLLHAE PPSPAAEDPT GGPP
//
