ID   Q8PE49_XANCP            Unreviewed;      1116 AA.
AC   Q8PE49;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 106.
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=XCC0134 {ECO:0000313|EMBL:AAM39453.1};
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485 {ECO:0000313|EMBL:AAM39453.1, ECO:0000313|Proteomes:UP000001010};
RN   [1] {ECO:0000313|EMBL:AAM39453.1, ECO:0000313|Proteomes:UP000001010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25
RC   {ECO:0000313|Proteomes:UP000001010};
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F.Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P.Jr., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A.Jr., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
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; AE008922; AAM39453.1; -; Genomic_DNA.
DR   RefSeq; NP_635529.1; NC_003902.1.
DR   RefSeq; WP_011035392.1; NC_003902.1.
DR   AlphaFoldDB; Q8PE49; -.
DR   STRING; 190485.XCC0134; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; AAM39453; AAM39453; XCC0134.
DR   KEGG; xcc:XCC0134; -.
DR   PATRIC; fig|190485.4.peg.149; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_1_1_6; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000001010; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001010}.
FT   DOMAIN          30..425
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1116 AA;  125542 MW;  6E8F3742FB28A527 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 RRSTQSFLDA YHAVLDASAH PWIAPAAFNA ATLLFLVEKA
     CYEVRYEAAN RPGWLMVPIQ GLRRILQRAR AGAGDT
//