ID   B9M3T6_GEODF            Unreviewed;      1114 AA.
AC   B9M3T6;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 77.
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   Name=treS {ECO:0000313|EMBL:ACM19579.1};
GN   OrderedLocusNames=Geob_1219 {ECO:0000313|EMBL:ACM19579.1};
OS   Geotalea daltonii (strain DSM 22248 / JCM 15807 / FRC-32) (Geobacter
OS   daltonii).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geotalea.
OX   NCBI_TaxID=316067 {ECO:0000313|EMBL:ACM19579.1, ECO:0000313|Proteomes:UP000007721};
RN   [1] {ECO:0000313|EMBL:ACM19579.1, ECO:0000313|Proteomes:UP000007721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22248 / JCM 15807 / FRC-32
RC   {ECO:0000313|Proteomes:UP000007721};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Kostka J., Richardson P.;
RT   "Complete sequence of Geobacter sp. FRC-32.";
RL   Submitted (JAN-2009) 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; CP001390; ACM19579.1; -; Genomic_DNA.
DR   RefSeq; WP_012646308.1; NC_011979.1.
DR   AlphaFoldDB; B9M3T6; -.
DR   STRING; 316067.Geob_1219; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; geo:Geob_1219; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_1_1_7; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000007721; Chromosome.
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: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; 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   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Kinase {ECO:0000313|EMBL:ACM19579.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007721};
KW   Transferase {ECO:0000313|EMBL:ACM19579.1}.
FT   DOMAIN          19..417
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   COILED          904..938
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1114 AA;  129039 MW;  B384BC999D8266D9 CRC64;
     MTGLKDEPLL WYKDAVIYEV HVRSFYDSNG DGIGDFRGLL KKLPFLHDLG VTAVWILPFY
     PSPLKDDGYD IADYYRIHPD YGTLGDFQAV LREAHRLGIR IITELVLNHT SDQHAWFQKS
     RRGGPRSVWR DFYVWSDTPA KYQDARVIFK DFESSNWSWD PVAKAYFWHR FYSHQPDLNY
     DNPRVHEAML QVLDFWLGMG VDGLRLDAVP YLYEREGTNC ENLPETYAFL NKIRQFMDEK
     YPGRMLLAEA NQWPEDAVSY LGSGACHMAF HFPLMPRMFM ALQMEESFPI INILEQTPGI
     SEHSQWALFL RNHDELTLEM VTDEERDYMY RVYASDPRAR INLGIRRRLA PLMGSDRRKI
     ELMNVLLFSL PGTPIIYYGD EIGMGDNYYL GDRNGVRTPM QWSPDRNAGF SAANAQRLFL
     PVIIDPEYHY EAVNVENHTR NPSSLLWWMR RLIDLRKQYK AFSRGSLEFV RLRNPKVIAM
     IRKFEEETIL IFINLSRFSQ VVEIASPEFL GHVPEDIFSR NRFPVIKDSP YVLILGPYNY
     HLLLMSKAQE AEAPAAEYVC PELSVSGSWE NILRRSGLAQ MERRVLPGYL RKTRWFRSKG
     QTISKLIIGD SLPVPADNTS FFLSFIETAY TEGQTETYLL PLHYLPLTEG EEILQEYPEA
     VIARLKVNNE DGILYDAMYS SIFRHVIFGL IAGRKRIEGS EGRVLSGRPG HSFAAIFREK
     KAPLQSRVGK VEQSNTAVHF DESFFFKLYR RVEEGVNPEV EIGRFLTEKD RFAHVAPLVG
     VLEYWQKGTE PITLGIMQGL VENQGDAWGL TMDEVGEYVE RVLASKEDMK VTPRLPANIY
     DADHGALSPK MQELMGGFYL EMVPLLGKRT AQLHLALSAH SKYPAFTPEP FSIFNQRSRF
     QSMRNRVRTV FDLLKRNLKN LKDEIRQEAE HLLLLEQEII KKLGKFTGRR FSAMKTRIHG
     DYHLGQVLYT GQDFIIIDFE GEPARSMRER RIKDSPLRDV AGMINSFQYA AYAVLVQHAH
     IRTEDIPFLE PWAEAWYRYV AGTFLHAYLQ NVKGAQFIPS LEADVQTILD IYILDKAIHD
     LGYEINNRPD WLLIPLRAIQ RLMKNADQAE EMVK
//