ID   B6A1S9_RHILW            Unreviewed;      1093 AA.
AC   B6A1S9;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 97.
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=Rleg2_5383 {ECO:0000313|EMBL:ACI58563.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OG   Plasmid pRLG201 {ECO:0000313|EMBL:ACI58563.1,
OG   ECO:0000313|Proteomes:UP000008330}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395492 {ECO:0000313|EMBL:ACI58563.1, ECO:0000313|Proteomes:UP000008330};
RN   [1] {ECO:0000313|EMBL:ACI58563.1, ECO:0000313|Proteomes:UP000008330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM2304 {ECO:0000313|EMBL:ACI58563.1,
RC   ECO:0000313|Proteomes:UP000008330};
RC   PLASMID=pRLG201 {ECO:0000313|EMBL:ACI58563.1};
RX   PubMed=21304679; DOI=10.4056/sigs.44642;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA   Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
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   WSM2304, an effective microsymbiont of the South American clover Trifolium
RT   polymorphum.";
RL   Stand. Genomic Sci. 2:66-76(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; CP001192; ACI58563.1; -; Genomic_DNA.
DR   RefSeq; WP_012556197.1; NC_011368.1.
DR   AlphaFoldDB; B6A1S9; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; rlt:Rleg2_5383; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_0_3_5; -.
DR   Proteomes; UP000008330; Plasmid pRLG201.
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:ACI58563.1}.
FT   DOMAIN          22..421
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1093 AA;  122826 MW;  A116E7D6662EDB6F CRC64;
     MDTMNPNGIE QPLWYKDAII YQLHIKSFYD ANGDGVGDFA GLHAKLDHIA ALGVNAIWLL
     PFFPSPRRDD GYDIADYGNV SPDYGTLEDF RAFVDAAHQR NIRVIIELVI NHTSDQHPWF
     QRARQAPAGS PERDFYVWSD TDQKFPETRI IFIDTEKSNW TWDAVAGAYY WHRFYSHQPD
     LNFDSPLVME ELLKVMRFWL ETGIDGFRLD AIPYLVEREG TINENLPETH AILKRIRAAL
     DATHPGVMLL AEANQWPEDT REYFGDGDEC HMAFHFPLMP RMYMAIAKED RFPITDILRQ
     TPEIPENCQW AIFLRNHDEL TLEMVTDAER DYLWETYASD KRARINLGIR RRLAPLMERD
     RRRIELMNAL LLSMPGTPVI YYGDEIGMGD NIYLGDRDGV RTPMQWSPDR NGGFSRVDPA
     RLVLPPVADP LYGFEAVNVE AQSTDAHSLL NWTRKMLALR GRHPAFGRGS LRFLAPENRK
     ILAYLREYEG ETLMCVANLS RLPQAVELDL SAFEGRVPIE LTGMSPFPPI GQLTYLLTLP
     PYGFFWFQLE ADADPPAWRT APPEQLPDLV TMVTRRGLLD LVDEPKLARV LSNEILPAYL
     AKRRWFGAKD QPLQAARLIS ATPIPFADGI VLGELEAVLP NHSESYQLPL AVAWDDAQPS
     VLSQQLALGR VRQGRRVGFL TDGFAVEAMA RGILRGLGDR SRTTGRTGTL EFLGTERLDR
     LAVTDDLPVH WLSAEQSNSS LIVGDLAMIK LIRHIFSGIH PEVEMTRYLT RAGYDHTAPL
     LGEVAHTDSS GRRSTLIIVQ GAIRNQGDAW NWMLNNLRRG ADELVLNDPA VQPGDDVFQP
     LISFVAMVGM RLGELHVVLA GETADEAFSP VIAGDSEVEA MKKAVAGEVA YAMSKLAERE
     ENADPAIDLL AAPLLKRRSE LVELAATLTE AARHTLMTRT HGDFHLGQIL VSEGDAVIID
     FEGEPAKNLA ERRAKTNPLR DVAGLLRSLS YLVATAQLDN DAVIEHENEV RREAIARFGR
     QAEEAFLDAY SQAVSASKAL DMPPDQRRRV LDAFLLEKAA YEIAYEARNR PKWLPIPLSG
     LTEIVSRLAG VPA
//