ID B9L231_THERP Unreviewed; 1123 AA.
AC B9L231;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 74.
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=trd_1931 {ECO:0000313|EMBL:ACM05896.1};
OS Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OC Bacteria; Thermomicrobiota; Thermomicrobia; Thermomicrobiales;
OC Thermomicrobiaceae; Thermomicrobium.
OX NCBI_TaxID=309801 {ECO:0000313|EMBL:ACM05896.1, ECO:0000313|Proteomes:UP000000447};
RN [1] {ECO:0000313|EMBL:ACM05896.1, ECO:0000313|Proteomes:UP000000447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27502 / DSM 5159 / P-2
RC {ECO:0000313|Proteomes:UP000000447};
RX PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A.,
RA Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L.,
RA Eisen J.A.;
RT "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT Thermomicrobium roseum.";
RL PLoS ONE 4:E4207-E4207(2009).
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; CP001275; ACM05896.1; -; Genomic_DNA.
DR RefSeq; WP_015922873.1; NC_011959.1.
DR AlphaFoldDB; B9L231; -.
DR STRING; 309801.trd_1931; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; tro:trd_1931; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG3281; Bacteria.
DR HOGENOM; CLU_007635_1_0_0; -.
DR OMA; QEDRFPI; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000000447; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 31..430
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1123 AA; 129063 MW; 536AF6DAFC143B94 CRC64;
MAVRLTERRR PAPVTQLADD PLWYKDAIIY ELHVRAFFDS NGDGIGDFPG LTQKLDYLED
LGITAVWLLP FYPSPLRDDG YDIADYTDVH PSYGTLRDVK EFIREAHRRG IRVITELVLN
HTSDQHPWFQ RARRAAPGSV WRNFYVWSDT PEKYKEARII FKDFETSNWA WDPVAKAYYW
HRFYAHQPDL NYDNPAVRRA ILRVVDFWMR LGVDGMRLDA VPYLYEREGT NCENLPETHQ
FLKELRRYID ERYPNRMLLA EANQWPEDAV AYFGNGDECH MAFHFPLMPR LFMAIRMEDR
FPIVDILSQT PPIPETAQWA LFLRNHDELT LEMVTDEERD YMYRVYARDP VARINLGIRR
RLAPLLGNNR RRIELMNGLL FSLPGTPVIY YGDEIGMGDN IYLGDRNGVR TPMQWSADRN
AGFSTAPRQR LYLPVIVDAE YHYEAVNVAA QQANPHSLLW WMKRLIGLRK QFKAFGRGSF
EFIPVENRKV LAYVRRYEQE TILVVANLSR FVQWAELDLS AYRGLVPVEL FGRIEFPLIG
DGPYRVMLGP HSFYWFSLER PRAGEEPVEI TTSELPLVPV RESEGTLELG SGQRAFEEIL
PRYLRKRRWF AGKARRIKQV RISEQVPLVT GESPATLVLV TVEYTEGDPE QYVLPLALAR
GERASEIVER TPHAVIARAL VEGSEALLVD ALAEPACVRS LIEQIGRRRR FRGEHGVIAS
QPTAAFRRLV RPDAPLPEPV LSRAEQSNTT VIFPDRVLFK LYRRVEPGPN PELEMERVLS
ERLGFPHVPP LAGSLEYQPA HGEPMTLGIV LGYVPNEGDA WQYTLDELAG FLERALAYSE
DPPSLRLEVE SLLDLAGQTP PTMVYELIDT YVEAVRLLGQ RTGELHRALA SVTDDPAFAP
EPFSMLYQRS LYQAMRSHLL QTLALLRQQL ASLPVSTREQ ADAVLQRERE IVQVYQKLLQ
KLLPAQRTRC HGDYHLGQVL YTGRDFVIID FEGEPARPLS ERRLKRSPLL DVAGMLRSFH
YAASATLLEQ QQRGLLSDLA RAEAWLRFWY GWVSAVFLQG YLEVVGSTAL VPSDSKDLGT
LLEAYLMDKA IYEIRYELGH RPDWLAIPLG GVLELLRARE GSA
//