ID   Q2S499_SALRD            Unreviewed;      1152 AA.
AC   Q2S499;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 108.
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=SRU_0847 {ECO:0000313|EMBL:ABC44183.1};
OS   Salinibacter ruber (strain DSM 13855 / M31).
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC   Salinibacter.
OX   NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC44183.1, ECO:0000313|Proteomes:UP000008674};
RN   [1] {ECO:0000313|EMBL:ABC44183.1, ECO:0000313|Proteomes:UP000008674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13855 / CECT 5946 / M31
RC   {ECO:0000313|Proteomes:UP000008674};
RX   PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA   Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H.,
RA   Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA   Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA   Legault B., Rodriguez-Valera F.;
RT   "The genome of Salinibacter ruber: convergence and gene exchange among
RT   hyperhalophilic bacteria and archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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; CP000159; ABC44183.1; -; Genomic_DNA.
DR   RefSeq; YP_444982.1; NC_007677.1.
DR   AlphaFoldDB; Q2S499; -.
DR   SMR; Q2S499; -.
DR   STRING; 309807.SRU_0847; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; ABC44183; ABC44183; SRU_0847.
DR   KEGG; sru:SRU_0847; -.
DR   PATRIC; fig|309807.25.peg.873; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_1_0_10; -.
DR   OrthoDB; 9806009at2; -.
DR   Proteomes; UP000008674; 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};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008674}.
FT   DOMAIN          45..443
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1152 AA;  132323 MW;  EED8922FC2BBD8C0 CRC64;
     MAGGPFSRSA VNVPTFNVPT FQRSTRMPDD FLDDPLWYKD AVIYELHVRS FYDSNNDGYG
     DFQGLREKLP YLESLGVNTL WLLPFLESPL RDDGYDTADY FKVLPIHGDL DDFRAFLDDA
     HARGMRVITE LVLNHTSDQH PWFQEARDPD SDKHDWYVWS DTDERYDDVR VIFTDTEDSN
     WAWDPKAEKY YWHRFFSHQP DLNFDNPEVR EKMKEVMFFW LDMGVDGLRL DAVPYLFERE
     GTSSENLPET IAYVKELRAA VEERYGPGKV LLAEANQWPE DTLPYFGEDA EGESTGVQMA
     FNFPVMPRLY MALRRENRRP VVEMLDLTSG IPDDAQWALF LRNHDELTLE MVTDEERDYM
     YHEYGADDRF RINVGIRRRL TPLLGGERRR IELMNALLLS LKGSPIIYYG DEIGMGDDPF
     LGDRNGVRTP MQWSPDKNGG FSRAPHHKLF MPPINRGKYS YEFVNVEDAE ADPYSLLHFM
     RRLIALRQQH KNIFGRGSLE LLPVENQSIL AFLREYEGER ILVVNNLSRF TQSVHIPARE
     DLQGLAPVEL SGQSAFPPIE DDDYHLTVGP HHFYWFKLVP KEDVQRDDTR RSGLQPLEDK
     NGRTRPVLPV AEGLQNVLVP TMAQRRGPEQ IEALLPEFIN EQRWFGGKGE GIEGVEVEDA
     VRLQSDPVVY LSVLRVDLPE DTSFYTLPLM AAPEPEASDI LDEHPNATLA WLEVEDTEER
     RLVYDATVNP RFWATLFRWW QRGGTGRSLK GLYTAEPSEA MGDAPPDDVR LLTGEQSNTS
     AIVNNDYFLK LYRRLEEGPN PEKELLEHLT DIDFTFSPRL HGTLNFRRRH RQYTLGVLQE
     ALAVDADAWS YTLSCTTTFL DRVENSPFPH EQAKNTGPSA DGPQWTADRF SDATVPVWLE
     ELAPELISFA RTLGVRTAEM HHALAQAGGD EMRPVEAPTD AGAELGTRIR TEMEETRALL
     DRQPDRVSGH VPSDPAWSAA RDRLAPLDDV PGTHDRIRIH GDYHLGQLLR AEGDIYVLDF
     EGEPTRPLDE RRRRKNALRD VAGMLRSLEY AVLASWQDHA DVDPDYEPWI DALLYWTETT
     FLDAYADTTG DAAFLPAAPA RYSFLWAFLL DKALYEVRYE LNHRPDWAWL PLHGLHRLLA
     PRDATASDPL DA
//