ID C6B5F3_RHILS Unreviewed; 1093 AA.
AC C6B5F3;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Maltokinase {ECO:0000256|ARBA:ARBA00013882};
DE EC=2.7.1.175 {ECO:0000256|ARBA:ARBA00011962};
DE EC=5.4.99.16 {ECO:0000256|ARBA:ARBA00012619};
DE AltName: Full=Maltose alpha-D-glucosyltransferase {ECO:0000256|ARBA:ARBA00031378};
DE AltName: Full=Maltose-1-phosphate synthase {ECO:0000256|ARBA:ARBA00031251};
GN OrderedLocusNames=Rleg_5098 {ECO:0000313|EMBL:ACS59311.1};
OS Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OG Plasmid pR132501 {ECO:0000313|EMBL:ACS59311.1,
OG ECO:0000313|Proteomes:UP000002256}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS59311.1, ECO:0000313|Proteomes:UP000002256};
RN [1] {ECO:0000313|EMBL:ACS59311.1, ECO:0000313|Proteomes:UP000002256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM1325 {ECO:0000313|EMBL:ACS59311.1,
RC ECO:0000313|Proteomes:UP000002256};
RC PLASMID=Plasmid pR132501 {ECO:0000313|Proteomes:UP000002256};
RX PubMed=21304718;
RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA Copeland A., Nolan M., Han C., Brettin T., Land M., Ovchinikova G.,
RA Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA Yates R., Howieson J.;
RT "Complete genome sequence of Rhizobium leguminosarum bv. trifolii strain
RT WSM1325, an effective microsymbiont of annual Mediterranean clovers.";
RL Stand. Genomic Sci. 2:347-356(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-maltose = ADP + alpha-maltose 1-phosphate + H(+);
CC Xref=Rhea:RHEA:31915, ChEBI:CHEBI:15378, ChEBI:CHEBI:17306,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:63576, ChEBI:CHEBI:456216;
CC EC=2.7.1.175; Evidence={ECO:0000256|ARBA:ARBA00001537};
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 aminoglycoside phosphotransferase family.
CC {ECO:0000256|ARBA:ARBA00006219}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. TreS
CC subfamily. {ECO:0000256|ARBA:ARBA00005496}.
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DR EMBL; CP001623; ACS59311.1; -; Genomic_DNA.
DR RefSeq; WP_012755457.1; NC_012848.1.
DR AlphaFoldDB; C6B5F3; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; rlg:Rleg_5098; -.
DR HOGENOM; CLU_007635_0_3_5; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000002256; Plasmid pR132501.
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; IPR040999; Mak_N_cap.
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; PF18085; Mak_N_cap; 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};
KW Plasmid {ECO:0000313|EMBL:ACS59311.1}.
FT DOMAIN 22..421
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1093 AA; 123118 MW; 80E2B365F8A0E08D CRC64;
MDTMNADSAS QPLWYKDAII YQLHIKSFYD ANGDGVGDFA GLHQKLDHIA ALGVNAIWLL
PFFPSPRRDD GYDIADYGSV SPDYGTVEDF RAFVDAAHQR NIRVIIELVI NHTSDQHPWF
QRARQSPAGS PERDFYVWSD TDQKFPETRI IFIDTEKSNW TWDAVAGAYY WHRFYSHQPD
LNFDSPLVME ELLRVMRFWL ETGIDGFRLD AIPYLVEREG TINENLPETH AILKRIRAAL
DATHPGVMLL AEANQWPEDT REYFGDGDEC HMAFHFPLMP RMYMAIAKED RFPITDILRQ
TPEIPDNCQW AIFLRNHDEL TLEMVTDAER DYLWETYASD KRARINLGIR RRLAPLMERD
RRRIELMNAL LLSMPGTPVI YYGDEIGMGD NIYLGDRDGV RTPMQWSPDR NGGFSRADPA
RLVLPPVADP LYGFEAVNVE AQSTDAHSLL NWTRRMLALR GRHPAFGRGT LRFLSPENRK
ILAYLREYEG EVLLCVASLS RLPQAVELDL SSFEGRVPIE LTGMSPFPPI GQLTYLLTLP
PYGFFWFQLT ADADPPAWRT APPEQLPDLL TMVIRRSLLD LVDEPGHARI LSGEILPAYL
SRRRWFGAKD QPLQAARLVS ATPIPFADGV VLGELEVVLP NHSESYQLPL TVAWDDAHPS
ALAQQLALGR IRQGRRVGFL TDGFAVEAMA RGILHGLRDR SRTTGRTGTL EFLGTEQLDS
LDISDELPVH WLSAEQSNSS LLVGDVAMIK LIRHIFPGIH PEVEMTRYLT RAGYDHTAPL
LGEVAHTDSS GRRSTLIIVQ GAIRNQGDAW NWMLNNLRRG ADELVLNDPA VQPDDDVFQS
LISFVAMVGL RLGELHVVLA AKTGDEAFSP VVSGDKEVEA MKKAVSGEVA YAMSKLDERE
QNADPAIDLL AAPLLERRSE LAELAGTLAE SCRHTLMTRT HGDFHLGQIL VSEGDAVIID
FEGEPAKNLT ERRAKTNPLR DVAGLLRSLS YLVATAQLDN DAVIEHDNEV RRKAIARFGR
NAEEAFLDAY WQAVSVSKEL DMPPDQRRRV LDAFLLEKAA YEIAYEARNR PKWLPIPLSG
LTEIVSRLAG VTA
//
