ID   Q11EX0_CHESB            Unreviewed;      1115 AA.
AC   Q11EX0;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 97.
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=Meso_2678 {ECO:0000313|EMBL:ABG64055.1};
OS   Chelativorans sp. (strain BNC1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Chelativorans.
OX   NCBI_TaxID=266779 {ECO:0000313|EMBL:ABG64055.1};
RN   [1] {ECO:0000313|EMBL:ABG64055.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BNC1 {ECO:0000313|EMBL:ABG64055.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of chromosome of Chelativorans sp. BNC1.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000390; ABG64055.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q11EX0; -.
DR   STRING; 266779.Meso_2678; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; mes:Meso_2678; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_1_1_5; -.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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, ECO:0000313|EMBL:ABG64055.1};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          41..435
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1115 AA;  127836 MW;  DD091B1E12BE6397 CRC64;
     MNTMEKVASE LMSPEEAEAV QVVPPAGPRP PDWYKDAVIY QLHIKAFHDS NGDGMGDFNG
     LMQRLDYVER LGVNTIWLLP FYPSPLRDDG YDIADYRSIN PSYGTMRDFR RFVAEAHRRG
     IRVITELVIN HTSDQHPWFQ RARHAKKGSA ARQFYVWNDD DERYPETRII FLDTEKSNWT
     WDPVAGQFFW HRFYSHQPDL NFDNPRVLDA VIRIMRFWLD MGVDGLRLDA IPYLVERDGT
     NNENLPETHE ILKKIRKALD EKYPDRMLLA EANQWPEDTR PYFGEGDECH MAFHFPLMPR
     IYMALAQEDR HPISDIMRQT PEIPESCQWA IFLRNHDELT LEMVTDRERD YLWRTYAEDV
     RARINLGIRR RLAPLMQNDR RKIELMNALL FSMPGTPIVY YGDELGMGDN IYLGDRDGVR
     TPMQWAPDRN GGFSRANPQM LYLPPIMDPV YGYQTINVEA QEADPSSLLN WVRRVIGVRK
     QHSAFGRGDF TMLYPRNRRI LAYTRSDANE TILCVANLSR SPQAVELDLS KYRNCVPIEL
     VSQSPFPPIG DLPYMLTLTG YGTFWFVLAS EAQAPEWHNN VPEPLPEFIT LTMVDGRIER
     ALEGRERRQL EQDVLPQFMQ RQRWYGAKGE GIRSAGISDI AKLGDEGGLL TIVDVDLSVS
     GRQRYLLPLT VLWGEENVQF GAPKLSVTLA RVRKGSRLGA LIDGAYDDRF ASELMRRMQE
     NQEMQVPGGT LRFYGNEQLT AMHFEETPSP LMGEQSNVSV AFDRQVLLKI FRRLRPGDQP
     EVEVARFLTE VAGFRNTPAF LGMVEYEEQG ARTVLASVSG FVENQGDAWG VFVHALERQI
     EDETLAPPAP AGATPAEGTT AQLLYPLDLL RRLGERTGEM HAALAIETDM EAFRCEPIRR
     ADIASWVKDL KQQAASARAA LERNKDRLPL NIRESVEHLL SLRQRIDRRI SEFGKITPSG
     KKSRIHGDYH LGQVLVSKQD LYIIDFEGEP RRSLEERRGK SSPLRDVAGM LRSFDYAAWT
     AVRQVAARLP DQTRDGSSLA RQWRERMSAE FLEGYRAAAS VAQNQPADGA TWEALLELFL
     LQKGFYEINY ELSNRPDWVG IPVQGVLDLI ERRSG
//