ID E8UY09_TERSS Unreviewed; 1081 AA.
AC E8UY09;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
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=AciPR4_3489 {ECO:0000313|EMBL:ADV84243.1};
OS Terriglobus saanensis (strain ATCC BAA-1853 / DSM 23119 / SP1PR4).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Terriglobus.
OX NCBI_TaxID=401053 {ECO:0000313|EMBL:ADV84243.1, ECO:0000313|Proteomes:UP000006844};
RN [1] {ECO:0000313|EMBL:ADV84243.1, ECO:0000313|Proteomes:UP000006844}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-1853 / DSM 23119 / SP1PR4
RC {ECO:0000313|Proteomes:UP000006844};
RX PubMed=23450133; DOI=10.4056/sigs.3036810;
RA Rawat S.R., Mannisto M.K., Starovoytov V., Goodwin L., Nolan M., Hauser L.,
RA Land M., Davenport K.W., Woyke T., Haggblom M.M.;
RT "Complete genome sequence of Terriglobus saanensis type strain SP1PR4(T),
RT an Acidobacteria from tundra soil.";
RL Stand. Genomic Sci. 7:59-69(2012).
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; CP002467; ADV84243.1; -; Genomic_DNA.
DR RefSeq; WP_013569973.1; NC_014963.1.
DR AlphaFoldDB; E8UY09; -.
DR STRING; 401053.AciPR4_3489; -.
DR KEGG; tsa:AciPR4_3489; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG3281; Bacteria.
DR HOGENOM; CLU_007635_1_1_0; -.
DR OMA; QEDRFPI; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000006844; 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 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 Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006844}.
FT DOMAIN 25..419
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1081 AA; 121179 MW; 5BA3364AE68CCBF0 CRC64;
MSEFATKKQG SATDPLWYKD AVIYELHVKA FADGNGDGIG DFQGLMEKLD YLQALGVTCI
WLLPFFPSPG RDDGYDISDY MSVNPNYGTV EDFQAFLEAA HARDMQVMIE LVINHTSDQH
PWFQQARLAP PGSPERDMYV WSETDKLYSG VRIIFTDTEK SNWTWDETAQ AYYWHRFFSH
QPDLNFDHPR VLEEVLNAMR FWMDMGVDGL RLDAIPYLVE RDGTSCENVP ETHVIIKKIR
AAIDAEYDNR LILAEANMWP ADVRPYFGDG DECQMAFHFP LMPRIYMALR QEDRLPITEI
MAQTPAIPDS CQWGLFLRNH DELTLEMVTD DERDYMYLAY SGDPRMRINV GIRRRLAPLL
DNNRRRIELL NSLLFSFPGT PILYYGDEIG MGDNIYLGDR NGVRTPMQWN SDRNAGFSRA
VPAALYSPVI MDPIWGYQAI NVEAQEQDTS SLLHWTRNMI ALRKLFQVFG RGTQEFLKPE
NRKVLAYVRE YNGERVVCVA NLSRFAQPVT LDLSRWEGMV PVEMLGYVPF PPIDKSAYAI
TLGPYAFLWL ELQDAPKAAE TLPSAPPEVV IPASDIVGVL SGPGLELLQE AILPKYMARQ
RWFGAKTRTI QSTTVADWVL LPVEDAAILL VDVCYVEGPS ERYTLPVAVR FDDTVVDDRF
VLTKVRGGSD AGSVAPSVAG ASLHEGVLVD ALSIQAVRDA VLALIEKNET LTTQHGTLQG
LRGTAVKAAD GLVSRLTSAE QSNTSVLYGD QLILKMFRRI EEGVNPDVEL GRFLTEETGF
AYTAAFAGEI AYTVPGVEDA PEKRYTLGLL QAQVKNVGDG WEWTQAELAR IGTVSQPGIK
EFASYIAAAR VLAERTAEMH RAFAGGASAE IAPEQPTSAK LAADAARLRA QVKRTLSTLK
HKFVDLPEDL EEIAASLLSK RSAMDEVVQR LEKLPATEAG LWTRIHGDYH LGQILRTEKD
FALLDFEGEP AKSLVERRKR QSPLRDVAGM LRSFSYAGAA YAHEHGETSG WVSLWEAEVS
KEFLSAYEAA SGGRLSASRR VMLQAYLLEK AMYELQYELD SRPTWAHIPL RGILRLLGIA
G
//