ID   D7CX34_TRURR            Unreviewed;      1134 AA.
AC   D7CX34;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
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=Trad_1420 {ECO:0000313|EMBL:ADI14542.1};
OS   Truepera radiovictrix (strain DSM 17093 / CIP 108686 / LMG 22925 / RQ-24).
OC   Bacteria; Deinococcota; Deinococci; Trueperales; Trueperaceae; Truepera.
OX   NCBI_TaxID=649638 {ECO:0000313|EMBL:ADI14542.1, ECO:0000313|Proteomes:UP000000379};
RN   [1] {ECO:0000313|Proteomes:UP000000379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17093 / CIP 108686 / LMG 22925 / RQ-24
RC   {ECO:0000313|Proteomes:UP000000379};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ovchinnikova G., Munk A.C., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Tindall B., Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Truepera radiovictris DSM 17093.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADI14542.1, ECO:0000313|Proteomes:UP000000379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17093 / CIP 108686 / LMG 22925 / RQ-24
RC   {ECO:0000313|Proteomes:UP000000379};
RX   PubMed=21475591; DOI=10.4056/sigs.1563919;
RA   Ivanova N., Rohde C., Munk C., Nolan M., Lucas S., Del Rio T.G., Tice H.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Brambilla E., Rohde M.,
RA   Goker M., Tindall B.J., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Truepera radiovictrix type strain (RQ-24).";
RL   Stand. Genomic Sci. 4:91-99(2011).
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; CP002049; ADI14542.1; -; Genomic_DNA.
DR   RefSeq; WP_013177911.1; NC_014221.1.
DR   AlphaFoldDB; D7CX34; -.
DR   STRING; 649638.Trad_1420; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; tra:Trad_1420; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_2_3_0; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000000379; 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; IPR040999; Mak_N_cap.
DR   InterPro; IPR032091; Malt_amylase_C.
DR   InterPro; IPR045857; O16G_dom_2.
DR   InterPro; IPR012810; TreS/a-amylase_N.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000379}.
FT   DOMAIN          49..449
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          925..971
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1134 AA;  127873 MW;  4C80B1821208D67E CRC64;
     MDTTSDTTTD AVSDAARDKP TSEPALGPGT ANDPLVRDPL WYKDAVIYQV HVRSFFDANN
     DGYGDFEGLR QKLPYLEELG VNTLWLLPFY ESPLRDDGYD IADYLKVLPV HGNLDDFKAF
     LDEAHARGMR VITELVLNHT SDQHPWFQEA RQPGSKKRDW YVWSDTAEKY KDVRIIFTDT
     EHSNWTWDPV AGAYYWHRFF SHQPDLNWDN PEVERALHEV LFYWLDMGVD GLRLDAVPYL
     YEREGTSGEN LPETLDAIKR LRAAIEERYG PGRILLAEAN QWPEDTLPYF GDPESGDGVQ
     MAFNFPLMPR MYLALRRESR QPIVEMLRLT DGIPESAQWA LFLRNHDELT LEMVTDEERD
     FMYNEYAADR QFRINLGIRR RLAPLLGGER RRIELMNALM LSLKGSPIIY YGDEIGMGDN
     TFLGDRNGVR TPMQWSADRN GGFSRAPFHQ LFLPPINEGP YSYGFVNVEE AQRSAHSLYG
     FMQRILRLRN QHAKTFGRGS LEVLEVENER VFAFLRHYEG ETILVVANLS RYAQAASLPL
     QRYAGAVPIE LFSQAPFPAI TDGAGGYPLT LSPHGFFWFV LKEPGEETGE AAPEEEPFER
     PLQTLKTSGG LETVLVDTMV QGDAKARLER ALPDFLGAQR WFGSKEKAIA RTKLVDAVRL
     QADPPIYLTL VRVEFEDGSL ERYFLPLTLK TGEAARALLD AHGRAAVAWL SGPSGRALLH
     DATADEGFWL ALYRAAQRSW RGRSLQGLYS AGATPGVRLP EVEHATPAEV EQSNSSASYE
     GKVFGKLYRK LEDERNPELE LLSYLTRAEF PFVPQLQGEV RFRRGELHFT LGVFQSFIPG
     GEDAWRYALE ESARFFGRTA EATPPEGELP TTFADPAPAW LEDAAGESLQ LASLLGVRTA
     ELHAVLARAE GAAMAPEAVT GDDLRALASR VRRNAEETLA QLEAQGTALD RTVLEAKLAA
     LEALAEQEER LTWQQIRIHG DYHLGQVVRA ESELYILDFE GEPIRPLQER RKRDSALRDV
     AGMLRSLEYA GLMAQRTHAQ ETGAAQEATA PWTELLIRWS EAVFLEAYFS TAGEGASFLP
     SDLEARDLLL WAYQLDKVLY EVRYELGSRP DWVWLPLKGL ARLLGASTAE TGAS
//