ID Q13S06_PARXL Unreviewed; 1154 AA. AC Q13S06; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 27-MAR-2024, entry version 107. 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=Bxe_B2862 {ECO:0000313|EMBL:ABE33133.1}; OS Paraburkholderia xenovorans (strain LB400). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33133.1, ECO:0000313|Proteomes:UP000001817}; RN [1] {ECO:0000313|EMBL:ABE33133.1, ECO:0000313|Proteomes:UP000001817} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LB400 {ECO:0000313|EMBL:ABE33133.1, RC ECO:0000313|Proteomes:UP000001817}; RX PubMed=17030797; DOI=10.1073/pnas.0606924103; RA Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L., RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V., RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J., RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T., RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.; RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome RT shaped for versatility."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000271; ABE33133.1; -; Genomic_DNA. DR RefSeq; WP_011490513.1; NZ_CP008762.1. DR AlphaFoldDB; Q13S06; -. DR STRING; 266265.Bxe_B2862; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR KEGG; bxb:DR64_5191; -. DR KEGG; bxe:Bxe_B2862; -. DR PATRIC; fig|266265.5.peg.4829; -. DR eggNOG; COG0366; Bacteria. DR eggNOG; COG3281; Bacteria. DR OrthoDB; 9805159at2; -. DR Proteomes; UP000001817; Chromosome 2. 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, ECO:0000313|EMBL:ABE33133.1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}. FT DOMAIN 50..463 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" FT REGION 1..35 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1125..1154 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1154 AA; 129410 MW; F04A010AD9EA815C CRC64; MKRDDPAQTT SQAHSSAATG GVAKARTHRR GKPAALSDDP LWYKDAIIYQ VHIKSFFDAN NDGVGDFPGL IAKLDYIAEL GVNAIWLLPF YPSPRRDDGY DIADYRNVHP DYGNLSDVKR FIQEAHARGI RVITELVINH TSDQHPWFQR ARRAKPGSNH RNYYVWSNTD QKYLETRIIF IDSEPSNWTH DPVAGAYYWH RFYSHQPDLN FDNPAVLREV LQVMRFWLDM GIDGLRLDAV PYLVEREGTN NENLPETHAV LKKIRATIDA EYPNRMLLAE ANQWPEDVKE YFGDEDECHM AFHFPLMPRI YMSIASEDRF PITDIMRQTP DLAETNQWAI FLRNHDELTL EMVTDSERDY LWNTYASDRR ARLNLGIRRR LAPLMERDRR RIELINSLLL SMPGTPVIYY GDELGMGDNI HLGDRDGVRT PMQWSSDRNG GFSRADPEQL VLPPVMGSLY GFDAVNVEAQ SRDPHSLLNW TRRMLATRRA KQTFGRGTIR FLKPENRKIL AYLREMPGEP PILCVANLSR APQAVELDLS EFDGSVPIEM TADSVFPPIG QLTYLLTFPP YGFLWFMLCP GGQRPTWAQA PSEPLPEFVT IVIREGQVGP TPENVRLLES EVLPSWLSRR RWFASKDQKL NAVRLAALTT IPNGGFAFTE IEADVGKHTE RYVVPIAITW GGETTFPLFK QLALARVRRG RNVGHLTDAF ALPIFAHGVM RKLRERAVVP TVQKSEIRFL PTERFAELEG LGERPEIRWL AAEQSNSSLI IADAAVLKLV RRLVSGIHPE AEISRYLTQL GYANTAPLYG EVVRVDPEGV PHTLCILQGY IDNQGDAWNW SLDYLRRSVD ELAIAVDTET QSVPDRSNEA ILVEGYSTLA GIIGRRLGEL HVALASPTDD PAFAPEPASA EQVKAWVDGT QAMLASALDL LAPRIEQMSD TETRALAQSL IDRRAALVAA VDSLVSANAG ALRIRIHGDF HLGQVLVAQG DAYLIDFEGE PARTLEQRRQ KSSPLRDVAG LLRSLSYASA AAQSTTEAAP QQTADRKRAL FDRFRAHAAE KFLNEYRAAA AEAATPLVAP EAEQALLDLF LIEKAAYEIR YEAANRPTWL SLPVRGLAAL TSRLLGDTGA PGHDSSNQAP GAATPPNPAE GDYE //