ID D8G2D1_9CYAN Unreviewed; 1170 AA.
AC D8G2D1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
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 ORFNames=OSCI_3180013 {ECO:0000313|EMBL:CBN56771.1};
OS Kamptonema sp. PCC 6506.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Kamptonema.
OX NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN56771.1, ECO:0000313|Proteomes:UP000004532};
RN [1] {ECO:0000313|EMBL:CBN56771.1, ECO:0000313|Proteomes:UP000004532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6506 {ECO:0000313|EMBL:CBN56771.1,
RC ECO:0000313|Proteomes:UP000004532};
RX PubMed=20675499; DOI=10.1128/JB.00704-10;
RA Mejean A., Mazmouz R., Mann S., Calteau A., Medigue C., Ploux O.;
RT "The genome sequence of the cyanobacterium Oscillatoria sp. PCC 6506
RT reveals several gene clusters responsible for the biosynthesis of toxins
RT and secondary metabolites.";
RL J. Bacteriol. 192:5264-5265(2010).
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}.
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:CBN56771.1}.
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DR EMBL; CACA01000283; CBN56771.1; -; Genomic_DNA.
DR RefSeq; WP_007355980.1; NZ_CACA01000283.1.
DR AlphaFoldDB; D8G2D1; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000004532; Unassembled WGS sequence.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000004532};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 18..412
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1170 AA; 133684 MW; D748946AF65421EE CRC64;
MSILNDDPLW FKDAIIYEVP VRAFADSNAD GIGDFRGLTE KLDYLQDLGV TAIWVLPFFP
SPLRDDGYDT SDYTSVNPIY GNLEDFQNLL DAAHQRGIRV IIELIVNHTS DQHPWFQKAR
RAPKGSKERD FYVWSDTPEK YQDARIIFQD FETSNWAWDA VAKSYYWHRF YSHQPDLNYD
NPAVRQAILD TVDFWLAMGV DGLRMDAVPY LYERDGTNCE NLSETHFFLK QLRKHVDENF
PNRMLLAEAN QWPEDAVQYY AQGDECHMNF HFPLMPRLFM SLQMEDSFPI IDIIQQTPHI
PDNCQWALFL RNHDELTLEM VSDEDRDYMY RVYAQDTQAR INLGIRRRLA PLMGNNRRRI
ELMNALLLSL PGTPVLYYGD EIGMGDNIYL GDRNGVRTPM QWSGDRNAGF SRANPQKLYA
PPILDPEYHY EAINVEAQRS NLNSLWWWMK RLIGIRQHFQ AFGRGTFEFL YPENRKVLAF
MRIYDGEHIL VVANLSRFVQ TVELDLSPFK GSVPIEIFGR SEFPTIGDYP YFLSLTPHSF
YWFTIALKPD VYPQQLPQVK LPTLTISGNW ESIFNPNNKS RVQIATILPK YLRSFRWFGG
KDRTIQAVQI TEVIPISSSG FAGENLGSSS IAAQKQSINT YYLVFLKVDY TEGMAETYVL
PLGYEKISSV GDSGEILADG NVTNYKQNQP SQSLHSAQAI AELKFIGKND EIGVLFDAGG
EKDFLSFPLD AIANSRQYTG TAGKLLATIT KELTPEEDLS HVEPRLIKGE KSNTSVVYGD
RLILKLFRKV EEGINPDLEI GQFLTDKNPL QPYIPVAGAL EYRRPGSESI TIGILHKFIP
EARDAWSYTL DSLSHYFEEV MVVGAKHSND NSSGYGDSYL PTALPLPVQQ PSNSLVSNLS
VEMPELAHEL IGAYLTSAEL LGQRTAELHL TLASDLENPS FAAENFTSFY QRSIYQQMRN
LTGRTLLLLR KGLLKLSPDG QKMAQVILSH PEQLIGKFRS ILNLKITAQR IRCHGDYHLG
QVLYTGKDFI IIDFEGEPAR PLSERRMKRS PLRDVAGMVQ SFNYAATLSL RKEIENGIIR
AETLPTMNQW AKFWYGWVSV AFLKSYLMTA GDANFVPKSM DELQVLLDAY ILEKVVYELA
NELNSHPDWA EITIERILYL IGFPVEQLLG
//
