ID   D5H7E6_SALRM            Unreviewed;      1126 AA.
AC   D5H7E6;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 64.
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:CBH23951.1};
GN   OrderedLocusNames=SRM_01030 {ECO:0000313|EMBL:CBH23951.1};
OS   Salinibacter ruber (strain M8).
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC   Salinibacter.
OX   NCBI_TaxID=761659 {ECO:0000313|EMBL:CBH23951.1, ECO:0000313|Proteomes:UP000000933};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=M8;
RA   Pena A., Teeling H., Huerta-Cepas J., Santos F., Yarza P.,
RA   Brito-Echeverria J., Lucio M., Schmitt-Kopplin P., Meseguer I.,
RA   Schenowitz C., Dossat C., Barbe V., Dopazo J., Rossello-Mora R.,
RA   Schuler M., Glockner F.O., Amann R., Gabaldon T., Anton J.;
RT   "Fine-scale evolution: genomic, phenotypic and ecological differentiation
RT   in two coexisting Salinibacter ruber strains.";
RL   ISME J. 4:882-95(2010).
RN   [2] {ECO:0000313|EMBL:CBH23951.1, ECO:0000313|Proteomes:UP000000933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M8 {ECO:0000313|EMBL:CBH23951.1,
RC   ECO:0000313|Proteomes:UP000000933};
RX   PubMed=20164864; DOI=10.1038/ismej.2010.6;
RA   Pena A., Teeling H., Huerta-Cepas J., Santos F., Yarza P.,
RA   Brito-Echeverria J., Lucio M., Schmitt-Kopplin P., Meseguer I.,
RA   Schenowitz C., Dossat C., Barbe V., Dopazo J., Rossello-Mora R.,
RA   Schuler M., Glockner F.O., Amann R., Gabaldon T., Anton J.;
RT   "Fine-scale evolution: genomic, phenotypic and ecological differentiation
RT   in two coexisting Salinibacter ruber strains.";
RL   ISME J. 4:882-895(2010).
RN   [3] {ECO:0000313|Proteomes:UP000000933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M8 {ECO:0000313|Proteomes:UP000000933};
RG   Genoscope;
RT   "Genome sequence of Salinibacter ruber M8.";
RL   Submitted (APR-2010) 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; FP565814; CBH23951.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5H7E6; -.
DR   KEGG; srm:SRM_01030; -.
DR   PATRIC; fig|761659.10.peg.1141; -.
DR   HOGENOM; CLU_007635_1_0_10; -.
DR   Proteomes; UP000000933; 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   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, ECO:0000313|EMBL:CBH23951.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          19..417
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1126 AA;  129538 MW;  069BAA8DBC21D8B9 CRC64;
     MPDDFLDDPL WYKDAVIYEL HVRSFYDSNN DGYGDFQGLR EKLPYLESLG VNTLWLLPFL
     ESPLRDDGYD TADYFKVLPI HGDLDDFRAF LDDAHARGMR VITELVLNHT SDQHPWFQEA
     RDPDSDKHDW YVWSDTDERY DDVRVIFTDT EDSNWAWDPK AEKYYWHRFF SHQPDLNFDN
     PEVREKMKEV MFFWLDMGVD GLRLDAVPYL FEREGTSSEN LPETIAYVKE LRAAVEERYG
     PGKVLLAEAN QWPEDTLPYF GEDAEGESTG VQMAFNFPVM PRLYMALRRE NRRPVVEMLD
     LTSGIPDDAQ WALFLRNHDE LTLEMVTDEE RDYMYHEYGA DDRFRINVGI RRRLTPLLGG
     ERRRIELMNA LLLSLKGSPI IYYGDEIGMG DDPFLGDRNG VRTPMQWSPD KNGGFSRAPH
     HKLFMPPINR GKYSYEFVNV EDAEADPYSL LHFMRRLIAL RQQHKNIFGR GSLELLPVEN
     QSILAFLREY EGERILVVNN LSRFTQSVHI PAREDLQGLA PVELSGQSAF PPIEDDDYHL
     TVGPHHFYWF KLVPKEDVQR DDTRRSGLQP LEDKNGRTRP VLPVAEGLQN VLVPTMAQRR
     GPEQIEALLP EFINEQRWFG GKGEGIEGVE VEDAVRLQSD PVVYLSVLRV DLPEDTSFYT
     LPLMAAPEPE ASDILDEHPN ATLAWLEVED TEERRLVYDA TVNPRFWATL FRWWQRGGTG
     RSLKGLYTAE PSEAMGDAPP DDVRLLTGEQ SNTSAIVNND YFLKLYRRLE EGPNPEKELL
     EHLTDIDFTF SPRLHGTLNF RRRHRQYTLG VLQEALAVDA DAWSYTLSCT TTFLDRVKNS
     PFPHEQAKNT GPSADGPHWT ADRFSDATVP VWLEELAPEL ISFARTLGVR TAEMHHALAQ
     AGGDEMRPVE APTDAGAELG TRIRTEMEET RALLDRQPDR VSGHVPSDPA WSAARDRLAP
     LDDVPGTHDR IRIHGDYHLG QLLRAEGDIY VLDFEGEPTR PLEERRRRKN ALRDVAGMLR
     SLEYAVLASW QDHADVDPDY EPWIDALLYW TETTFLDAYA DTTGDAAFLP AAPARYSFLW
     AFLLDKALYE VRYELNHRPD WAWLPLHGLH RLLAPRDATA SDPLDA
//