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
//
