ID C5CVH7_VARPS Unreviewed; 1109 AA.
AC C5CVH7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 65.
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=Vapar_1980 {ECO:0000313|EMBL:ACS18626.1};
OS Variovorax paradoxus (strain S110).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=543728 {ECO:0000313|EMBL:ACS18626.1};
RN [1] {ECO:0000313|EMBL:ACS18626.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S110 {ECO:0000313|EMBL:ACS18626.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Orwin P.,
RA Leadbetter J.R., Spain J.C., Han J.I.;
RT "Complete sequence of chromosome 1 of Variovorax paradoxus S110.";
RL Submitted (JUN-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; CP001635; ACS18626.1; -; Genomic_DNA.
DR AlphaFoldDB; C5CVH7; -.
DR STRING; 543728.Vapar_1980; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; vap:Vapar_1980; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG3281; Bacteria.
DR HOGENOM; CLU_007635_1_1_4; -.
DR OMA; QEDRFPI; -.
DR OrthoDB; 9805159at2; -.
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 Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 31..430
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1109 AA; 125728 MW; ED3CA10E3747DB27 CRC64;
MNAPVSHIAL ETVEIDISDD PLWYRDAVIY QLNVKAFFDS NNDGIGDFKG VTAKLDYVKE
LGVNTIWLMP FYPSPLRDDG YDISAYEDVN PQYGTLDDFR EMLDAAHERG LRVITELVIN
HTSSDHPWFQ AARRAPAGSP ERDFYVWSDT DQIYQGTRII FTDTETSNWA WDPVAKAYYW
HRFFSHQPDL NFDNPAVLEA IFKVMRFWLD MGVDGFRLDA IPYLVERDGT SNENLPETHA
VIKQLRAAID AQYKNRFLLA EANMWPEDVR EYFGDGDECH MAYHFPLMPR MYMAIAQEDR
HPIVEIMQQT PDIPEGCQWA IFLRNHDELT LEMVTSKERD YMYTMYAADL RARINLGIRR
RLAPLMENDI DRVKLMNGML LSMPGSPIIY YGDEIGMGDN VFVGDRNGVR TPMQWSPDRN
AGFSRADPQR LYLQPIMDPM FGYEALNVEA QARDSSSLLN WTKRMLAVRK TSHAFGRGKR
RFLKPGNRKI LAYLSEYDED IILTVFNLSR AAQPVELDLS AFKGRVPIEM LGRAPFPPIG
ELPYLLTLAS YGFYWFRLTS DAEMPSWHQE GVALQEWPTL VLFDGWTSFF RDRVMPWRIG
MSERMRNQFE LETLPRHIEI QRWYASKGTP IERARLADHV IWEAGPLSWM LPLLELDGPP
GGATYFMPLA LAWEERDEER MAGVAQAALA KVRQQAQVGL MGDAFYDEAF CRELVLAIRS
GMELETAQGR LRFRATAAFA EVEADIASLP IGRPSGVSSN TVVTLDETLF LKGYRHLREG
LNPELEMGRF LTEVAKYPHC VPVLGALEYT GNDGRTMTLA MVQSYVSNQG DGWDHTLGYL
ERFLRDFATT NGALPDPMAV HGGFLALMAT LGRRTAELHQ ALALRTGAAA FDPEPLLDSD
IARYAEQARA DATATLALLR ERLAQLPAPA QPDAQALLAM EDALQGSIAA RRPQAQGGIK
SRYHGDLHLG QVLLRDNDFV IIDFEGEPAR SFDERRAKGS PLRDVAGMLR SFNYARWSAL
RRVAQSVEEA AYLGPPAAAW EQSARQAFLD GYMEAGAGEE ATRIDADLLA LFETEKALYE
LRYELNNRID WAQVPLNGVL ALLQVERPG
//