ID W4S4T9_9XANT Unreviewed; 1101 AA.
AC W4S4T9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=XPU_3058 {ECO:0000313|EMBL:GAE51526.1};
OS Xanthomonas arboricola pv. pruni str. MAFF 311562.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=1414836 {ECO:0000313|EMBL:GAE51526.1, ECO:0000313|Proteomes:UP000019143};
RN [1] {ECO:0000313|EMBL:GAE51526.1, ECO:0000313|Proteomes:UP000019143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 311562 {ECO:0000313|Proteomes:UP000019143};
RA Fujikawa T., Nakazono-Nagaoka E.;
RT "Genome sequence and analysis of Xanthomonas arboricola pv. pruni.";
RL Submitted (JAN-2014) 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}.
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:GAE51526.1}.
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DR EMBL; BAVB01000303; GAE51526.1; -; Genomic_DNA.
DR AlphaFoldDB; W4S4T9; -.
DR Proteomes; UP000019143; 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..415
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1101 AA; 124209 MW; 7C6C7E969C701829 CRC64;
MVADQLWYKD AIIYQVHVKS FFDSNDDGIG DFPGLISKLD YIAELGVDTI WLLPFYPSPR
RDDGYDIAEY MAVHPDYGSI EDFEQLVAQA HARGIRIVTE LVINHTSDLH PWFQRARNAP
AGSPERDFYV WSDTDQEYEG TRIIFCDTEK SNWTWDPVAG QYFWHRFYSH QPDLNFDNPA
VLEAVLEVMR FWLDRGVDGL RLDAVPYLIE RSGTSNENLP ETHAILRKIR ATLDAEYPDR
MLLAEANMWP EDTQQYFGQN ADECHMAFHF PLMPRMYMAI AREDRFPITD IMRQTPEIPE
SCQWAIFLRN HDELTLEMVT DSERDYLWQT YAADRRARIN LGIRRRLAPL LERDRRRIEL
MTSLLLTMPG TPVLYYGDEI GMGDNIHLGD RDGVRTPMQW SIDRNGGFSR ADPAQLVLPP
VMDPLYGFQA VNVEAQIRDQ HSLLTWTRRV LSVRKRYQAF GRGSLRFLYP GNRRMLAYLR
CYQDETVLCV ANLSHTLQAV ELDLSEFEGR VPVDIIGGGS FPPVGRLTYL LTVPPFGFYA
FQLVSEGTLP DWHVPSPVPL PDYRTLVLRS DTDESNALLP HLPTLEAEIL PAWLSARRWF
SAKDQALKHV RISRRTPLPG AEPMSLLELE VELEDGHHES YMLPVGIVWE RDQPSTLAEQ
LALARVRQGR EVGYLTDAFA LKPMVRGVID ALRDNAALEF CDGDDASQQG QVRFEATPAL
ATLEIPQDPE IRWLSAEQSN SSLVVADKAV FKLLRHVANG ANPEIEIGRR LTEMGYANAA
PLLGSVSRID AQGTITTIAL LQGFIRNQGD AWRWTLDHLA RSFDEYATAQ TDESRAEAIA
GYDAFAAVVG KRLAELHEAL SRDTDDADFA PQRIDLPTAN DVVAGVARQV EEMWDTVNAR
LAGSDDATER EALQAVLAER PQLDALLAQA PSVLADSLLT RVHGDFHLGQ ILVAFDDVVL
IDFEGEPAKP LSERRAKASP LRDVAGFLRS LDYASEVSAR GEEGTAARAG VGVDTHLDEF
LVQFRRRSTQ AFLDAYHAVL DASTHPWIAP AAFNAATLLF LVEKACYEVR YEAANRPGWL
MVPIEGLRRI LHRARAGAGD T
//
