ID   B9L231_THERP            Unreviewed;      1123 AA.
AC   B9L231;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
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   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   Calcium {ECO:0000256|ARBA:ARBA00022837};
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
//