ID   I4CT29_STUST            Unreviewed;      1108 AA.
AC   I4CT29;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
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=A458_09985 {ECO:0000313|EMBL:AFM33236.1};
OS   Stutzerimonas stutzeri CCUG 29243.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Stutzerimonas.
OX   NCBI_TaxID=1196835 {ECO:0000313|EMBL:AFM33236.1, ECO:0000313|Proteomes:UP000006063};
RN   [1] {ECO:0000313|EMBL:AFM33236.1, ECO:0000313|Proteomes:UP000006063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 29243 {ECO:0000313|EMBL:AFM33236.1,
RC   ECO:0000313|Proteomes:UP000006063};
RX   PubMed=23144395; DOI=10.1128/JB.01753-12;
RA   Brunet-Galmes I., Busquets A., Pena A., Gomila M., Nogales B.,
RA   Garcia-Valdes E., Lalucat J., Bennasar A., Bosch R.;
RT   "Complete Genome Sequence of the Naphthalene-Degrading Bacterium
RT   Pseudomonas stutzeri AN10 (CCUG 29243).";
RL   J. Bacteriol. 194:6642-6643(2012).
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; CP003677; AFM33236.1; -; Genomic_DNA.
DR   RefSeq; WP_014820198.1; NC_018028.1.
DR   AlphaFoldDB; I4CT29; -.
DR   KEGG; psc:A458_09985; -.
DR   PATRIC; fig|1196835.3.peg.2006; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_2_0_6; -.
DR   Proteomes; UP000006063; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          24..423
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   COILED          897..942
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1108 AA;  125797 MW;  3750787160FAAE50 CRC64;
     MAKPRKPAAF IKDPLWYKDA VVYQVHLKSF YDSNNDGVGD FPGLIEKLDY IADLGVNTIW
     LLPFYPSPRR DDGYDIADYR GVHPEYGSMA DARRFIAEAH KRGLRVITEL VINHTSDQHP
     WFQRARKAKK GSAARDFYVW SDTDKKYDGT RIIFLDTEKS NWTWDPVAKQ YFWHRFYSHQ
     PDLNFDNPQV MKAVLAVMRY WLDMGIDGLR LDAIPYLVER DGTNNENLPE THAVLKAIRA
     EIDANYPDRM LLAEANQWPE DTQLYFGGED GGPGDECHMA FHFPLMPRMY MAIAQEDRFP
     ITDILRQTPD IPENCQWAIF LRNHDELTLE MVTDKERDYL WNYYASDKRA RINLGIRRRL
     APLLERDRRR IELLNSLLLS MPGTPVIYYG DEIGMGDNIF LGDRDGVRTP MQWSVDRNGG
     FSRADPPNLV LPPVMDPLYG YYTINVEAQQ RDPHSLLNWT RRMLTIRKQF KAFGRGTLKM
     LAPSNRRILA YMREFTGANG ETEIIFCVAN VSRSAQAAEL EMSQYAGMVP VEMVGGSAFP
     PIGQLPYLLT LPHYGFYWFQ LALTNQMPSW HQEPVDTMPD FQTLVLKRLD TLTAANRRIL
     ETEALPAYLP KRRWFAAKDV AIESVRISYC VPFGDPNRPV LLSELCVESA GRSDLYQLPL
     GFLAETEFEV ALPQQLALAR VRRGPQVGLM TDAFALEQFS AAVIQGLRDE LVLPCNDGEI
     RFVPMPQLAD LQLPAHPEVR FISAEQSNSS AIIDNKVMIK LLRRVAPGVH PELEMGGFLT
     ERGFAHISGM LGQVSRINKQ GEPVALMVIQ HFLDSQGDAW VWTLNNLDRA VRDEIAGGVS
     MHENQFSALD ELQAFNRLLG QRLGEMHMAL ATQTEDPAFA YESTSTADTK QWEQSVSAQL
     EQALQRLEEH RSSFDRKEAT ALGQLLARRD KLLEQVQRLA ARTVGGVRTR VHGDLHLGQV
     LVVQGDAYFI DFEGEPARSL DERRAKHSPF KDVSGLLRSF EYAAAMTIRG AQISDSTPEA
     DQARQRIAAS YQSSAQAAFF EAYREATAEL PHDWRDADGA NAALLLFSLE KCAYEIVYEA
     ENRPTWLPVP LQGLLALAQQ LFDGGSND
//