ID   G0C9Z0_XANCA            Unreviewed;      1116 AA.
AC   G0C9Z0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
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=XCR_4405 {ECO:0000313|EMBL:AEL09261.1};
OS   Xanthomonas campestris pv. raphani 756C.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=990315 {ECO:0000313|EMBL:AEL09261.1, ECO:0000313|Proteomes:UP000001633};
RN   [1] {ECO:0000313|EMBL:AEL09261.1, ECO:0000313|Proteomes:UP000001633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=756C {ECO:0000313|EMBL:AEL09261.1,
RC   ECO:0000313|Proteomes:UP000001633};
RX   PubMed=21784931; DOI=10.1128/JB.05262-11;
RA   Bogdanove A.J., Koebnik R., Lu H., Furutani A., Angiuoli S.V., Patil P.B.,
RA   Van Sluys M.A., Ryan R.P., Meyer D.F., Han S.W., Aparna G., Rajaram M.,
RA   Delcher A.L., Phillippy A.M., Puiu D., Schatz M.C., Shumway M.,
RA   Sommer D.D., Trapnell C., Benahmed F., Dimitrov G., Madupu R., Radune D.,
RA   Sullivan S., Jha G., Ishihara H., Lee S.W., Pandey A., Sharma V.,
RA   Sriariyanun M., Szurek B., Vera-Cruz C.M., Dorman K.S., Ronald P.C.,
RA   Verdier V., Dow J.M., Sonti R.V., Tsuge S., Brendel V.P., Rabinowicz P.D.,
RA   Leach J.E., White F.F., Salzberg S.L.;
RT   "Two new complete genome sequences offer insight into host and tissue
RT   specificity of plant pathogenic Xanthomonas spp.";
RL   J. Bacteriol. 193:5450-5464(2011).
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; CP002789; AEL09261.1; -; Genomic_DNA.
DR   RefSeq; WP_014509514.1; NC_017271.1.
DR   AlphaFoldDB; G0C9Z0; -.
DR   KEGG; xcp:XCR_4405; -.
DR   PATRIC; fig|990315.4.peg.4145; -.
DR   HOGENOM; CLU_007635_1_1_6; -.
DR   Proteomes; UP000001633; Chromosome.
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..425
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1116 AA;  125526 MW;  3499FB98FB28BD5F CRC64;
     MNAVPALQAD AEQSAVVADQ LWYKDAIIYQ VHVKSFFDSN DDGIGDFPGL ISKLDYIAEL
     GVDTIWLLPF YPSPRRDDGY DIAEYMAVHP DYGTIADFEQ LVAQAHARGI RIVTELVINH
     TSDQHPWFQR ARNAPAGSPE RDFYVWSDTD QEYEGTRIIF CDTEKSNWTW DPVAGQYFWH
     RFYSHQPDLN FDNPAVLESV LEVMRFWLDR GVDGLRLDAV PYLIERSGTS NENLPETHAI
     LRKIRATLDA EYPDRMLLAE ANMWPEDTQQ YFGQNADECH MAFHFPLMPR MYMAIAREDR
     FPITDIMRQT PEIPETCQWA IFLRNHDELT LEMVTDSERD YLWQTYASDR RARINLGIRR
     RLAPLLERDR RRIELMTSLL LTMPGTPVLY YGDEIGMGDN IHLGDRDGVR TPMQWSIDRN
     GGFSRADPAA LVLPPVMDPL YGFQAVNVEA QIRDQHSLLT WTRRVLSVRK RYQAFGRGTL
     RFLYPGNRRM LAYLRCYQDE TVLCVANLSH TLQAVELDLS EFEGRVPVDI IGGGSFPPIG
     RLTYLLTVPP FGFYAFQLVS EGTLPDWHVP SPVPLPDYRT LVLRSDTEES AALLPHLATL
     EGEILPAWLS ARRWFSAKDQ ALKSVRISRR TPLPGDEPMS LLELDVELED GHHECYMLPV
     GIVWEREHPS TLAEQLALAR VRQGREVGYL TDAFALKPMV RGVIDALRHD AALDFHDGDD
     ASQQGQVRFE STPALAALEI PDDPEIRWLS AEQSNSSLVV ADKAVFKLLR HVATGANPEI
     EIGRRLTEMG YANAAPLLGS VSRVDAQGTI TTIALLQGFI RNQGDAWRWT LDHLARSFDE
     YATAQTDEAR NEAVAGYDAF AAVVGKRLAE LHEALSRSTD DADFAPQRID LPTANDVVGG
     VARQVEEMWE TVHARLGATD DAAEREALES VLAERPQLDA LLAKAPSVLA ESLLTRVHGD
     FHLGQILVAF DDVVLIDFEG EPAKPLAERR AKASPLRDVA GFLRSLDYAS EVSARGEEGT
     AARAGVGVDA HLDDFLVEFR RRSTQAFLDA YHAVLDASAH PWIAPAAFNA ATLLFLVEKA
     CYEVRYEAAN RPGWLMVPIQ GLRRILQRAR AGAGDT
//