ID   A1TNR8_PARC0            Unreviewed;      1142 AA.
AC   A1TNR8;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 91.
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=Aave_2022 {ECO:0000313|EMBL:ABM32606.1};
OS   Paracidovorax citrulli (strain AAC00-1) (Acidovorax citrulli).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Paracidovorax.
OX   NCBI_TaxID=397945 {ECO:0000313|EMBL:ABM32606.1, ECO:0000313|Proteomes:UP000002596};
RN   [1] {ECO:0000313|EMBL:ABM32606.1, ECO:0000313|Proteomes:UP000002596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAC00-1 {ECO:0000313|EMBL:ABM32606.1,
RC   ECO:0000313|Proteomes:UP000002596};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAC00-1 {ECO:0000313|Proteomes:UP000002596};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL   Submitted (DEC-2006) 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; CP000512; ABM32606.1; -; Genomic_DNA.
DR   RefSeq; WP_011795146.1; NC_008752.1.
DR   AlphaFoldDB; A1TNR8; -.
DR   STRING; 397945.Aave_2022; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; aav:Aave_2022; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_1_1_4; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000002596; 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, ECO:0000313|EMBL:ABM32606.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          50..449
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1142 AA;  128574 MW;  9B877C61D6D9AB31 CRC64;
     MNAPLLRQPL PAADAAAGPL PEPGPVVMPE TPEIDTQGDP QWYRDAVIYQ LNVKAFFDSN
     NDGYGDFKGV TAKLDYVKDL GVNTIWLMPF YPSPLRDDGY DISDYENVHP QYGTLADFKE
     MLDAAHARGL RVITELVINH TSSEHPWFQR ARRAPPGSPE RDFYVWSDTD QIYRGTRIIF
     TDTETSNWAW DPVAKQYYWH RFFSHQPDLN FDNPLVLEAV FKTMRFWLDM GVDGFRLDAI
     PYLVERDGTS NENLPETHAV IKKLRAAIDA EYRNRFLLAE ANMWPEDVRE YFGDGDECHM
     AYHFPLMPRM YMAIAQEDRH PIVEILQQTP DIPEGCQWAI FLRNHDELTL EMVTSKERDY
     MYSMYAADMR ARINLGIRRR LAPLMENDLD RVKLMNGMLL SMPGSPIIYY GDEIGMGDNV
     FVGDRNGVRT PMQWSPDRNG GFSRSDPQRL YLQPIMDAVY GYEALNVEAQ SGDHSSLLHW
     TRRMLAVRKT SRAFGRGRRT FLKPGNRKIL AYVSEHEDDV ILTVFNLSRA AQPVELDLSA
     YRGRTPIEML GRVTFPPIGD LPYLLTLHSY GFYWFRLSNE APMPSWHQEG LDLQERPVLV
     LFDGWTSFFR ERVMPWRIGM AERMRAQFED DTLPRFIELQ RWYADKGATI AGARILDHTV
     WKAGEGCEWM LPLLGVEPAA KPGGAQGAGA TYFVPLALAW EEGSEERMRR ISPAGVARVR
     QQAQVGVMGD AFHDESFCRM VVRAMGEGTE LATDQGGRVR FRRTSAFDAL AAELDTLPVE
     RPGAQSSNTV VALGETLFLK GYRRLREGVN PELEVGRFLT EVARFPHCVP VAGSVEYVAP
     DGATMTLALV QSYVANQGDG WEYTLGYLER FLEDTRLAQA AGPVADMHGG YLALAATLGQ
     RTAQLHQALA RRTGDAAFDP EPVTTQDVAA FGQRARAEAE DTLVLLERRL GELPPAAQTD
     AQAVLARRAL IMERLAAGGA DAPAGTKTRF HGDYHLGQVL VTGNDFVIID FEGEPGRPFE
     ERRAKSSPLR DVAGMLRSFN YARWAALKHM TQSTEEMVRL DEAARHWEHQ VRDAFLAAYA
     AEGLAADPAL ISLFELEKAL YELRYELGNR VDWAQVPLQG ILALIGAAAA PTPTPNLPDT
     PA
//