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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//