ID A0A089YQS1_9PSED Unreviewed; 1107 AA.
AC A0A089YQS1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=LT40_11305 {ECO:0000313|EMBL:AIS17939.1};
OS Pseudomonas rhizosphaerae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216142 {ECO:0000313|EMBL:AIS17939.1, ECO:0000313|Proteomes:UP000029499};
RN [1] {ECO:0000313|EMBL:AIS17939.1, ECO:0000313|Proteomes:UP000029499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16299 {ECO:0000313|EMBL:AIS17939.1};
RX PubMed=25483321; DOI=10.1016/j.jbiotec.2014.11.031;
RA Kwak Y., Jung B.K., Shin J.H.;
RT "Complete genome sequence of Pseudomonas rhizosphaerae IH5T (=DSM 16299T),
RT a phosphate-solubilizing rhizobacterium for bacterial biofertilizer.";
RL J. Biotechnol. 193:137-138(2015).
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; CP009533; AIS17939.1; -; Genomic_DNA.
DR RefSeq; WP_043189966.1; NZ_CP009533.1.
DR AlphaFoldDB; A0A089YQS1; -.
DR STRING; 216142.LT40_11305; -.
DR KEGG; prh:LT40_11305; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG3281; Bacteria.
DR HOGENOM; CLU_007635_1_1_6; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000029499; 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:UP000029499}.
FT DOMAIN 24..423
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1107 AA; 124813 MW; 533879A013689271 CRC64;
MAKKPRSQAF IDDPLWYKDA VIYQVHVKSF FDSDNDGIGD FPGLIAKLDY IADLGVNTIW
LLPFYPSPRR DDGYDIAEYK AVHPDYGTLA DARRFINEAH KRGLRVITEL VINHTSDQHP
WFQRARKAKK GSKARDFYVW SDTDEKYDGT RIIFLDTEKS NWTWDPVAGQ YFWHRFYSHQ
PDLNFDNPQV MKAVIDVMRY WLDMGIDGLR LDAIPYLIER DGTNNENLTE THQVLKQIRA
EIDANYPDRM LLAEANQWPE DTQLYFGDAK GDNGDECHMA FHFPLMPRMY MALAQEDRFP
VTDILRQTPA IPANCQWAIF LRNHDELTLE MVTDRERDYL WNYYAADSRA RINLGIRRRL
APLLERDRRR VELLNSLLLS MPGTPTLYYG DEIGMGDNIY LGDRDGVRTP MQWSIDRNGG
FSRADPASLV LPPIMDPLYG YQSVNVETQA NDPHSLLNWT RRMLAVRRQQ KAFGRGSLTM
LTPTNRRILA YVREYTGSDG KTEIVLCVAN VSRAAQAAEL DLSPYAGMVP VEMLGGSAFP
PIGQLNFLLT LPPYGFYWFL LASETQMPSW HVEPAQSMPD FQTLVLKQRM EELLDEPSRS
TLEHTSLMQY LPKRRWFGGK DVAIDNLRIA YGVRFGTKTN PVLLSELEVT AGGQTSRYQF
PFGFIPEEHS GSPLPLQLAL SRVRRGREVG LITDAFVLES FIHSVIDGLQ ADQTLATGEG
EIHFKATDHL AGLNLNETSV IRYLSAEQSN SSVVIGGSLV LKMIRRVSGG IHPELEMGAY
LTAAGYANIS PLMGSVSRVD ASGTPHLLMI AQGYLNNQGD AWEWTQNNLE RAIRDEMAFA
HSEQGQRYDA LGELADFAGM LGQRLGEMHV ALAAPGAQAD FLARVSTEKD AQAWTDSICS
QVERALGLLE QRRADFAEQD QALVAELLSE RDTLLAHVEQ LSKQAVGGLI MRVHGDLHLG
QMLVVQGDAY LIDFEGEPAR PLEERRAKYS PYKDVGGVLR SFDYAAAMAV RNVQSTDASE
EATAARQRVA KRYLAQARQA FITAYDLATQ AVPHQWQAAD GARAALDLFS LEKAAYEIAY
EAENRPSWLA VPLHGLFGLL STRENKQ
//
