ID   Q2IYW9_RHOP2            Unreviewed;      1100 AA.
AC   Q2IYW9;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, 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=RPB_1883 {ECO:0000313|EMBL:ABD06591.1};
OS   Rhodopseudomonas palustris (strain HaA2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=316058 {ECO:0000313|EMBL:ABD06591.1, ECO:0000313|Proteomes:UP000008809};
RN   [1] {ECO:0000313|EMBL:ABD06591.1, ECO:0000313|Proteomes:UP000008809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HaA2 {ECO:0000313|EMBL:ABD06591.1,
RC   ECO:0000313|Proteomes:UP000008809};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA   Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL   Submitted (JAN-2006) 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; CP000250; ABD06591.1; -; Genomic_DNA.
DR   RefSeq; WP_011440779.1; NC_007778.1.
DR   AlphaFoldDB; Q2IYW9; -.
DR   STRING; 316058.RPB_1883; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; rpb:RPB_1883; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_1_2_5; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000008809; Chromosome.
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          31..430
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1100 AA;  125023 MW;  93D69A4E13E97A14 CRC64;
     MNVMSPIDST DSRAQADATN ELWYKDAIIY QLHVKAFADS NNDGIGDFAG LTEKLDYLQD
     LGVTALWLLP FYPSPQRDDG YDIADYGSIN PDFGTMKDFR RFIVEAKKRN LRVITELVIN
     HTSDQHDWFK RARRSGKGSS ARDWYVWSDS DQKYQGTRII FTDTEKSNWT WDPEAGQYYW
     HRFFSHQPDL NFDNPHVVGA VVKVMKRWLD TGVDGFRLDA IPYLCERDGT NNENLPETHA
     VIKTLRAELD AYAKGKVLLA EANQWPEDVQ EYFGDSDECH MAYHFPLMPR IYMAIAQEDR
     FPITDIMRQT PEIPANCQWA MFLRNHDELT LEMVTDVERD YLWTTYAADP RARINVGIRR
     RLAPLMDNDR RKIELMNSLL LSFPGTPIIY YGDEIGMGDN IYLGDRNGVR TPMQWSSDRN
     GGFSRADPAR LYAPPIMDPV YGYASVNVEA QARSLSSLLS ATKRLISVRK STLAFGRGTM
     TFIRPVNRSV LSYVRQYEDE VILCVANLSR SAQATELDLS PWKDRVPQEM LGRTKFPAIG
     ELPYMITLAP YGFYWFKLEE RDTSEHVAPA ATVPEFETLV VPLGSTWMTL ARTRGVFERD
     VLPAYLSRTR WFPERSPRAI QPHLTSAIPF SITHDNRPWL TFFEATVRGV NTRYVLPMQI
     DWVRFDRERY NPRAFAAVRQ GAREGTLLDV AADTEFTTLL LDNLRESLVV ENDGDRLEFR
     PGSRLADKPA GPYNHIRAVD TEQSNSTALV DESYVVKLYR RLESGINPEI EMGRFLSEVA
     GYSNTPSLLG SVELVEGDKV SAIAVVHDFV ANQGDGWTVT SGYLDRYVDD QRLLINTEED
     SASDELAPYL RYMQQTGKRV AEMHIALAGH PEVDDFAPVP IADDDARSWT EAVTANAGRV
     LDELARKRDG LRDADRALID DLLAQRNGLS EGLRGLFGSA GGLKIRHHGD FHLGQMLIVK
     DDIFIIDFEG EPRRSQAERR AKAPAARDVA GLIRSIDYST TAALERAQKA LVDESGKIAA
     ALDVWRTRST EAFLAAYRET MADSPVWPVD RAAADQILDF FLIEKALYEI EYELAYRPDW
     LRVPLAGILR ILTRQPEENS
//