ID A0A0S8HDW3_9BACT Unreviewed; 1108 AA.
AC A0A0S8HDW3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 ORFNames=AMS25_01350 {ECO:0000313|EMBL:KPK83041.1};
OS Gemmatimonas sp. SM23_52.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=1703359 {ECO:0000313|EMBL:KPK83041.1, ECO:0000313|Proteomes:UP000051975};
RN [1] {ECO:0000313|EMBL:KPK83041.1, ECO:0000313|Proteomes:UP000051975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_52 {ECO:0000313|EMBL:KPK83041.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPK83041.1}.
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DR EMBL; LJUM01000005; KPK83041.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8HDW3; -.
DR PATRIC; fig|1703359.3.peg.3443; -.
DR Proteomes; UP000051975; Unassembled WGS sequence.
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}.
FT DOMAIN 15..409
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1108 AA; 127409 MW; F55E6A6A63241C95 CRC64;
MSGDPLWYKD AIIYQLHVKA FRDSNGDGIG DFQGLTEKLD YLQDLGITAL WLLPFYPSPL
RDDGYDIADY TDVHPTYGTL RDFRTLLREA HRRELRVITE LVVNHTSDQH PWFQRARRAR
PGSRARDFYV WSDTADVYRE ARIIFKDFEH SNWTWDPVAG AYYWHRFYSH QPDLNFDNPA
VRKAILQTLD FWLEMGVDGL RLDAVPYLFE REGSNCENLP ETHAFLKELR RHVDKKYSER
MLLAEANQWP EDAVAYFGDG DECHMAFHFP VMPRLFMGLH MEDRFPVVDI LEQTPAIPEI
SQWAIFLRNH DELTLEMVTD EDRDYMYRVY ASDPRARINL GIRRRLAPLL GHHRRKIELM
KSLLLSLPGT PVLYYGDEIG MGDNIYMGDR DGVRTPMQWS ADRNAGFSRA NPQQLYLPVI
IDPEYHYEAI NVEAQQNNPH SLLWWMKRIL ATRKRFRAFS RGTIEFLQPE NRKVLVFLRH
WENERILVVV NLSRFVQAVE LDLSAFKGMV PVEVFGRTPF PPIGEPPYFL TLGPHTFYWF
TLEPAPAAEE PITVSEAPLR ELVVSGSWEA VLHDKAAAQL ERILPSYLRS RRWFAGKARH
ILSAQIIETI PIGYDGSFAQ LVLIKVSYSD GDPDIYQLPL AFTTGNRAAD LAEHQRHTVI
TRLRVRDNGN EAEGVLYDAT VEEGFCNALL DVIERRRRRS GALGRLRTSR TRQFRAMRGN
LEDKLKPSLL GAEQSNTSVV YGDRLIVKLF RRLDQGVNPD LEIGRFLTER TSFSHMPPLG
GAIEYEHSKG EPLTLAVLQG FVPNQGDAWE YTLDALDEYF ERVLARPADE RQPAVPAGTP
LTHVYAETPP QAKEVIGAYL ELARLLGQRT AELHLALASR SDDAAFAPEP INTMYRRSVY
ESSRTRLDQA FTLLRRRLSA LPEHVRPEAR AVLGQSKQIE QRLRSVVDRK VGGLRIRCHG
DYHLGQVLYT GKDFLIMDFE GEPARPISER QLKRSPLRDV GGMLRSFHYA AVSALIAGRV
RPEDVPILEP RAEVWYLWVA AYFLRAYLDL VADADLVPEG EDELAALLDL CVIDKALYEL
EYELNNRPDW VRIPLRGIAS LIESSTEM
//
