ID A0A085VLZ4_PSESX Unreviewed; 1107 AA.
AC A0A085VLZ4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=IV01_09055 {ECO:0000313|EMBL:KFE56457.1};
OS Pseudomonas syringae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=317 {ECO:0000313|EMBL:KFE56457.1, ECO:0000313|Proteomes:UP000028631};
RN [1] {ECO:0000313|EMBL:KFE56457.1, ECO:0000313|Proteomes:UP000028631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAW0119 {ECO:0000313|EMBL:KFE56457.1,
RC ECO:0000313|Proteomes:UP000028631};
RA Baltrus D.A., Berge O., Morris C.;
RT "Draft Genome Sequences of Environmental Pseudomonas syringae strains.";
RL Submitted (JUL-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFE56457.1}.
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DR EMBL; JPQU01000027; KFE56457.1; -; Genomic_DNA.
DR RefSeq; WP_032627706.1; NZ_JPQU01000027.1.
DR AlphaFoldDB; A0A085VLZ4; -.
DR PATRIC; fig|317.175.peg.1877; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000028631; 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: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}.
FT DOMAIN 24..423
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1107 AA; 124968 MW; AA949CFD30E28C30 CRC64;
MAKKPKSAAF IKDPLWYKDA VIYQVHVKSF FDSNNDGIGD FPGLISKLDY IAELGVNTIW
LLPFYPSPRR DDGYDIADYR GVHSDYGTMA DAKKFIAEAH KRGLRVITEL VINHTSDQHP
WFQKARAAKK GSKARDFYVW SDTDHKYDGT RIIFLDTEKS NWTWDPVAEQ YFWHRFYSHQ
PDLNFDNPQV MEAVLEVMRY WLDMGIDGLR LDAIPYLIER DGTNNENLPE THAVLKKIRA
EIDANYPDRM LLAEANQWPE DTQLYFGDTK GKDGDECHMA FHFPLMPRMY MALAQEDRFP
ITDILRQTPE IPENCQWAIF LRNHDELTLE MVTDRERDYL WNYYAADRRA RINLGIRRRL
APLVERDRRR VELLNSMLLS MPGTPTLYYG DEIGMGDNIY LGDRDGVRTP MQWSIDRNGG
FSRADPASLV LPPIMDPLYG FQSVNVETQN NDPHSLLNWN RRMLAVRKQQ KAFGRGILKM
LSPSNRRILA YTREYTGADG HTEIILCVAN VSSASQAAEL ELSNYAGTVP VEMLGGSAFP
PIGQLNYLLT LPPYGFYWFL LASENQMPSW HVEPAQSMPD FPTMVLKKRL EELLDEPLRS
TMEQNSLAVY LPKRRWFASK DQAIDKVHIA YAVRFGDAAH PVLLSEIEVT TGDQSARYQL
PFGLLAEDDI SSALPQQLAL ARVRRGRQVG LITDAFTLET FIRAVIHGMQ VQTVLPSSEG
ELRFEHTALL EPLALSNESE VRYLSAEQSN SSVVVGGSLV LKMLRRVSPG IHPELEMGAF
LTDAGYQHIS PLLGSVVRVG NDGEHNLLMI AQGYLSNQGD AWEWTQNNLE RAVRDEMSHG
VSGQEQHYNA LLELADFAAN LGKRLGEMHQ VLAASTDNPD FAVEVTSAKD SLASGKSVAE
QMEYALQLLE QNKASLEPVD QKLVNDLLAN RKKVLAHVQA LAKRSVGGLR IRVHGDLHLG
QVLVVKGDAY LIDFEGEPAR SVQERRAKYS PFKDVSGVLR SFDYAAAMAV RSAQSVDSSP
EASAARRLVA DTYLSQAREA FIESYRSVTV EIPHAWKDAK GESAALELFT LEKTAYEVVY
EARNRPSWLA VPLQGLRGLL NLSDGES
//
