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Database: UniProt/TrEMBL
Entry: B1M6D3_METRJ
LinkDB: B1M6D3_METRJ
Original site: B1M6D3_METRJ 
ID   B1M6D3_METRJ            Unreviewed;      1092 AA.
AC   B1M6D3;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 80.
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=Mrad2831_1598 {ECO:0000313|EMBL:ACB23593.1};
OS   Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS   NBRC 15690 / NCIMB 10815 / 0-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=426355 {ECO:0000313|EMBL:ACB23593.1, ECO:0000313|Proteomes:UP000006589};
RN   [1] {ECO:0000313|EMBL:ACB23593.1, ECO:0000313|Proteomes:UP000006589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 /
RC   0-1 {ECO:0000313|Proteomes:UP000006589};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT   2831.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001001; ACB23593.1; -; Genomic_DNA.
DR   RefSeq; WP_012318581.1; NC_010505.1.
DR   AlphaFoldDB; B1M6D3; -.
DR   STRING; 426355.Mrad2831_1598; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; mrd:Mrad2831_1598; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_1_1_5; -.
DR   OMA; QEDRFPI; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000006589; 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; IPR002575; Aminoglycoside_PTrfase.
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; PF01636; APH; 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   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          17..411
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1092 AA;  122781 MW;  912643A915E6955A CRC64;
     MIDRSDPQWY RDAIIYQIHV KSFFDSNNDG IGDFVGLTQR LDYVRDLGVT AIWLMPFYPS
     PLRDDGYDIA DYRDINPSYG TMEDFKAFVE AAHERGLRVI TELVINHTSD QHPWFQAARE
     APPGSPERNF YVWSDTDEPY KDTRIIFLDT EASNWTWDPV AKQYFWHRFY SHQPDLNFDN
     PAVLEAVIEV MRYWLDMGVD GLRLDAIPYL IERDGTNCEN LAETHEVIKK IRAALDAEYP
     DRMLLAEANQ WPEETAQYFG DGDECHMAFH FPLMPRMYMA IAREDRHPIT DIMRQTPEIP
     EGCQWAIFLR NHDELTLEMV TAEERDYLWS FYAAERRARI NLGIRRRLAP LLENDRRKIE
     LMKSLVLSMP GTPVLYYGDE VGMGDNIYLG DRDGVRTPMQ WSPDRNGGFS RANPQKLFLP
     AIQDPIYGFD AINVEAQTQA QTSLLNWTRR MIAIRNNSVA LGRGTIQFLY PSNRKVLAWI
     REHEDERILC VANLSRAPQA VQLDLSELRT AVPIELTGGT EFPPIGDLPY LLTLPSYGFY
     WFSLSAARSG VVGPQQEPPE LFTLVLTGGI ETLMSGRERV AFERTVVPPF LTSRRWFGAK
     GSRIKATKVV DCAALKDVDG SARFLLPRLQ VQLASGETQE YFVPVGVEEG REDETLMPFA
     VARVRRGPRT GLLYGAAGSN DFAACLIDDM RQAREIPTET GRLVFAVTSA FDPDVTVDVA
     DIRRLSGEQS NTSIAIGSKM MLKLLRRLQP GLHPEIEVGR FLTEQAGFSN TPALLGTLEH
     VAEDGTRTAL AVLQKFVMNQ GDAWTLMLEG LRRDFETVVL TPESEAATPE EAFQAHRPWA
     DLLGRRTAEL HAALAIETDD PAFAAEPFTG DDLAVLARDA RHQAERAFRA LKGLADRGLD
     AGKPACAELG RRRGEVEALI GSLTAAPVRG AHKTRIHGDY HLGQVLVAEN DLIIVDFEGE
     PSRPADERRA KSMPLRDVAG LMRSFAYGAE TVIREITARF ADSEERARDA ATAWRGMIEA
     AFLAGYETAV EGSRAAVTDA DSRARLLRLC LLTKALYEVD YEANNRPDWI EIPARGVLTI
     LDTDGHEPGA SE
//
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