ID A0A1K1M4G4_9GAMM Unreviewed; 1106 AA.
AC A0A1K1M4G4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN02800691_0115 {ECO:0000313|EMBL:SFW17959.1};
OS Luteibacter sp. UNCMF366Tsu5.1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Luteibacter.
OX NCBI_TaxID=1502758 {ECO:0000313|EMBL:SFW17959.1, ECO:0000313|Proteomes:UP000182005};
RN [1] {ECO:0000313|EMBL:SFW17959.1, ECO:0000313|Proteomes:UP000182005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UNCMF366Tsu5.1 {ECO:0000313|EMBL:SFW17959.1,
RC ECO:0000313|Proteomes:UP000182005};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FPIS01000001; SFW17959.1; -; Genomic_DNA.
DR RefSeq; WP_072320614.1; NZ_FPIS01000001.1.
DR AlphaFoldDB; A0A1K1M4G4; -.
DR STRING; 1502758.SAMN02800691_0115; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000182005; Unassembled WGS sequence.
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:0016740; F:transferase activity; 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:UP000182005};
KW Transferase {ECO:0000313|EMBL:SFW17959.1}.
FT DOMAIN 30..443
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1106 AA; 124725 MW; A0C34B05A61AA6A7 CRC64;
MATRVKGKKQ AATRDFSSDP LWYKDAIIYQ VHVKSFFDAN DDGVGDFQGL IDKLDYIAEL
GVNTLWLLPF YPSPRRDDGY DIAEYKAVHP DYGKLADAKR FIAEAHARGL RVITELVINH
TSDQHPWFQR ARHAKKGSAA RDFYVWSDTD QAYDGTRIIF LDTEKSNWTW DPVAGQYFWH
RFFSHQPDLN FDNPAVLKAV LDVMRFWLDL GVDGLRLDAV PYLIEREGTN NENLPETHQI
LKLMRAEIDQ HYPDRMLLAE ANQWPEDTQD YFGQGDECHM AFHFPLMPRM YMAIAREDRF
PITDIMRQTP AIPDNCQWAI FLRNHDELTL EMVTDSERDY LWQTYAADRR ARINLGIRRR
LAPLLERDRR RIELMNALLL SMPGTPVLYY GDEIGMGDNI HLGDRDGVRT PMQWSVDRNG
GFSRADPASL VLPPIMDPLY GFQAINVEAQ SRDPHSLLNW TRRMLAVRKR YKAFGRGTLK
FLYPGNRKVL AYLREFEGEQ VLCVANMSRS LQAVELDLGG FDGQVPIEIM GGSSFPPIGQ
LPYLLTLPPY GFYAFQICPN AQMPSWHEVP AEPMPDYETL VLRGALVEGP VMAHHRGVIE
KQVLPNYLSV RRWFAAKDRG IEGVRILYAV PWPDRGDDLI FTEVEATLSD GGTERYSLPA
GIVWEDENPT SRAQQLALAR VRRGRRIGLL TDGFALEAFA SGLLIGLRQN AELPIHSGGA
VRFETTAAFA TVTFDLAIEN RWLSAEQSNS SMILHDAGVV KLFRRTSAGI NPEVEMSRYL
TENGYANTAP LLGEVVRVDE HGERTTLAVL QGFLRNQGDA WGWTLDYLRR SYDEYSHSDD
EERCAEIEGG YDAFATAVGT RLGELHALLA RPSELPAFAP ETAGNDTMAA WREDVRTQLG
RAMHSVESAK DLPEALASEA KALREQAESL GRRLDDLAAA GQGALATRTH GDFHLGQVLV
VQDDAYIIDF EGEPARSLEE RRGKRSPLRD VAGFLRSLDY AAAMARRGED GLAPIEDAGF
GPYLERFHAR SAKVFLDAYR AVLAAAPVRW VDAEAFDALL ELFVIEKAAY EIVYEANNRP
AWLDVPLRGL LALAQGGSGH AREKNV
//
