ID A0A1Y6HNS9_9XANT Unreviewed; 1116 AA.
AC A0A1Y6HNS9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=PD5205_03866 {ECO:0000313|EMBL:SMR05138.1};
OS Xanthomonas fragariae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=48664 {ECO:0000313|EMBL:SMR05138.1, ECO:0000313|Proteomes:UP000195953};
RN [1] {ECO:0000313|EMBL:SMR05138.1, ECO:0000313|Proteomes:UP000195953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PD5205 {ECO:0000313|EMBL:SMR05138.1};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) 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; LT853885; SMR05138.1; -; Genomic_DNA.
DR RefSeq; WP_002808537.1; NZ_ORZY01000233.1.
DR AlphaFoldDB; A0A1Y6HNS9; -.
DR STRING; 48664.BER92_18810; -.
DR KEGG; xfr:BER92_18810; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG3281; Bacteria.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000195953; Chromosome 1.
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 30..430
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1116 AA; 125726 MW; E4E97653404CE5DA CRC64;
MKAVASLQAD AEQSAVVADQ LWYKDAIIYQ VHVKSFFDSN DDGIGDFPGL ISKLDYIAEL
GVDTIWLLPF YPSPRRDDGY DIAEYMAVHP DYGSIADFEQ LVAQAHARGI RIVTELVINH
TSDQHPWFQR ARNAPAGSPE RDFYVWSDTD QEYEGTRIIF CDTEKSNWTW DPVAGQYFWH
RFYSHQPDLN FDNPAVLEAV LEVMRFWLDR GVDGLRLDAV PYLIERSGTS NENLPETHAI
LRKIRTTLDA EYPDRMLLAE ANMWPEDTQQ YFGKNADECH MAFHFPLMPR MYMAIAREDR
FPITDIMRQT PEIPESCQWA IFLRNHDELT LEMVTDSERD YLWQTYASDR RARINLGIRR
RLAPLLERDR RRIELMTSLL LTMPGTPVLY YGDEIGMGDN IHLGDRDGVR TPMQWSIDRN
GGFSRADPAQ LVLPPVMDPL YGFQAVNVEA QIRDQHSLLT WTRRVLSVRK RYQAFGRGTL
RFLYPGNRRM LAYLRSCHDE TVLCVANLSH TLQAVELDLS EFEGRVPVDI IGGGSFPPIG
RLTYLLTVPP FGFYAFQLVS EGTLPDWHVP TPVPLPDYHT LVLRSDTDES NALLPHLPTL
EAEILPAWLS ARRWFSAKDR VLKNVRISRR TPLPGDEPMS LLELEVELED GHHESYMLPV
GIVWERDQPS TLAEQLALAR VRQGREVGYL TDAFALKTMV RGVIDALREN ATLDFRDGDD
ASQQGQVRFE ATTALAKLDI PQDPDIRWLS AEQSNSSLVV ADKAVFKLLR HVANGANPEI
EIGRRLTEMG YANAAPLLGS VSRIDGQGTV TTIALLQGFI RNQGDAWRWT LDHLARSFDE
YVTAQTDESR AEAIAGYDVF ASVVGKRLAE LHAALSRDTD DADFAPQRID LPTANDVVAG
VARQVEDIWD TVNARLASSD DAIERDALEA VLAERPQLEA LLAKAPSVLA DSLLTRVHGD
FHLGQILVAF DDVILIDFEG EPAKPLAARR AKASPLRDVA GFLRSLDYAS EVSARGEEGT
AARAGVGVDT HLDQFLVEFR RRSTDAFLDA YRAVLDTSVH PWIAPAAFNT ATLLFLVEKA
CYEVRYEAAN RPGWLMVPIE GLRRILQGVR AGAGDT
//
