ID   B1I2Z5_DESAP            Unreviewed;      1108 AA.
AC   B1I2Z5;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, 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   OrderedLocusNames=Daud_0851 {ECO:0000313|EMBL:ACA59364.1};
OS   Desulforudis audaxviator (strain MP104C).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforudis.
OX   NCBI_TaxID=477974 {ECO:0000313|EMBL:ACA59364.1, ECO:0000313|Proteomes:UP000008544};
RN   [1] {ECO:0000313|Proteomes:UP000008544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP104C {ECO:0000313|Proteomes:UP000008544};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., Land M.L.,
RA   Hauser L., Kyrpides N., Ivanova N.N., Richardson P.;
RT   "Complete sequence of chromosome of Desulforudis audaxviator MP104C.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACA59364.1, ECO:0000313|Proteomes:UP000008544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP104C {ECO:0000313|EMBL:ACA59364.1,
RC   ECO:0000313|Proteomes:UP000008544};
RX   PubMed=18845759; DOI=10.1126/science.1155495;
RA   Chivian D., Brodie E.L., Alm E.J., Culley D.E., Dehal P.S., Desantis T.Z.,
RA   Gihring T.M., Lapidus A., Lin L.H., Lowry S.R., Moser D.P.,
RA   Richardson P.M., Southam G., Wanger G., Pratt L.M., Andersen G.L.,
RA   Hazen T.C., Brockman F.J., Arkin A.P., Onstott T.C.;
RT   "Environmental genomics reveals a single-species ecosystem deep within
RT   Earth.";
RL   Science 322:275-278(2008).
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; CP000860; ACA59364.1; -; Genomic_DNA.
DR   RefSeq; WP_012301950.1; NC_010424.1.
DR   AlphaFoldDB; B1I2Z5; -.
DR   STRING; 477974.Daud_0851; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; dau:Daud_0851; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_1_0_9; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000008544; 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   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008544}.
FT   DOMAIN          16..413
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1108 AA;  127327 MW;  1BC53FB1B0D95D17 CRC64;
     MLDQNPLWYK DAILYELHVR AFFDRNGDGI GDFRGLAEKL DYLQDLGVTA IWLLPFYPSP
     LKDDGYDIAD YTAVHPSYGT LADFKFFVRE AHRRGLRVVT ELVCNHTSDQ HPWFQRARRA
     KAGSVWRNFY VWSDTPEKYR EARIIFKDFE TSNWTWDPAA GAYYWHRFYA HQPDLNYDNP
     MVRKAIFKVL DFWLRIGVDG LRLDAVPYLY ERDGTNCENL PETHAFLKEL RRHVDERFQN
     RMLLAEANQW PEHAAAYLGD ECHMAFHFPL MPRLFMALRM EDRFPVVDIL TQTPPISETS
     QWALFLRNHD ELTLEMVTDE ERDYMYRAYA HDPRMRINLG IRRRLAPLLG NHRRRIELMN
     GLLFSLPGTP VIYYGDEIGM GDNIYLGDRN GVRTPMQWSA DRNAGFSKAD RQRLYLPVIV
     DAEYHYETVN VETLQNNPHS LLSWMKRLIS LRKRYKAFGR GSLEFLHPEN RKVLAYVRRY
     EDESILVIAN LSRFAQCVEL DLNAYRGMIP VEMFGRTEFP PVGDRPYFFT LGPHAFFWFS
     LEPQRLLWER SPGGAPRAGI PTLVLKGSWE AAFWGGDRDA LAEVLPFYLA NCRWFGGKAR
     RLNSTRVTEV IPVPYNGSVA YITLVQADYT EGDPETYILP LALATGEWGR VWEGGRELVQ
     SAVARLQTKD KTGILYDALW DPAFCEVLLD AVPRRRRFKG ESGTMIATPT RQFARLRGPV
     QAPVEPVLIQ AEQSNSTVLF GDRLMLKLFR RAGEGINPDL EISRFLAEQS TFTQVAPLAG
     SLEYFREKDR PVTLAVLQGF VPNKGDAWQY TLGALSRFFG RVRRASGLKV PPLPSKILFA
     QTGEDLSPAT KMIGGYMDKA RLLGRRTAEL HLALAARPDN PDFAPEPFTT FYQRSLYQSM
     RSLTSQVFLT LRRKLAELPE AARAEAQAVL DLEGEVLNRF QTLLTHKIDT VRTRCHGDYH
     LGQLLYTGED FVIIDFDGEP ARPVQESPAK RTPLRDVAGM LRSFHYAAYT ALYNQTGTDG
     PPRGEDRAVL EPWARFWHLK VSAAFLDSYF QTAGRASFLP ETPEQLSVLL DACLLEKAVY
     ELGYELNNRP EWVPIPLKGI LELLQVRA
//