ID B8IPJ0_METNO Unreviewed; 1088 AA.
AC B8IPJ0;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 74.
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=Mnod_7546 {ECO:0000313|EMBL:ACL62282.1};
OS Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL62282.1, ECO:0000313|Proteomes:UP000008207};
RN [1] {ECO:0000313|EMBL:ACL62282.1, ECO:0000313|Proteomes:UP000008207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC {ECO:0000313|Proteomes:UP000008207};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Marx C.J.,
RA Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium nodulans ORS 2060.";
RL Submitted (JAN-2009) 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; CP001349; ACL62282.1; -; Genomic_DNA.
DR RefSeq; WP_015933836.1; NC_011894.1.
DR AlphaFoldDB; B8IPJ0; -.
DR STRING; 460265.Mnod_7546; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; mno:Mnod_7546; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG3281; Bacteria.
DR HOGENOM; CLU_007635_1_1_5; -.
DR OMA; QEDRFPI; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000008207; 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 Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008207}.
FT DOMAIN 17..416
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1088 AA; 123245 MW; 0E8FC9CDAB692A97 CRC64;
MIDRSDPQWY RDAIIYQVHV KSFFDANNDG IGDFDGLTAK LDYIRDLGVT AIWLMPFYPS
PLRDDGYDIA DYKGINPSYG TMRDFRRFVR EAHDRGLRVV TELVINHTSD QHPWFQRARN
APKGSKWRDF YVWSDTDDRY RDTRIIFLDT EASNWTWDPV AKAYYWHRFY SHQPDLNFDN
PRVLEAVIDV MRYWLDMGVD GLRLDAIPYL IEREHTNCEN LPETHDVIKK IRAALDAGYP
DRMLLAEANQ WPEETAQYFG NGDECHMAFH FPLMPRMYMA IAQEDRHPIT DIMRQTPEIP
EGCQWAIFLR NHDELTLEMV TDKERDYLWS FYAADRRARI NLGIRRRLAP LLENDRRKIE
LMKFLLLSMP GTPVLYYGDE IGMGDNIYLG DRDGVRTPMQ WSPDRNGGFS RADPARLFLP
TIQDPIYGFD AVNVEAHSRA QTSLLNWTRR MIAIRNNQRA LGRGALRFLY PSNRKVLAWL
RELDTEKVLC VANLSRAPQA VQLDLSELRN AVPVELTGGT SFPPIGDLPY LLTLPAYGFY
WFQLAQGQAE TAPRVEPPEL FTLVLTGGVE TLMKGRERLA FERTVAPLFI GSRRWFGAKG
SRIRSVQVTD SATLPDRTGK GSFLLPRLAV SLANGERQAY FTPLAVDEGR EDEALLDHAV
ARVRRGPRMG LLYGASSSTE FALSMVDGIR RGLDLSSEEG VLQFRATTLF DPELDLDPAD
IRRLSTEQSN TSIAFGSRLM LKILRRLQPG VHPEVEVGRF LSEAAGFRNT PALLGSVEHV
APDGTRTALA LLQAFVRNQG DAWTLMREYL RRDLDTIVLV PESEAPTPEE VFATHLRWAS
LLGQRTAEMH RAFAMETDDP AFAAEPFTAD DLATLVADTR RQAEKAMRGV AGIGPAAAES
AREAAAEILA SRNELDALIT RLGQHEPLGA CKIRIHGDYH LGQVLASQDD LIIVDFEGEP
SRPVDERRAK STPLRDVAGV LRSFAYGGET VTREIVSRFA EASDRTVTTV AAWRAMITAA
FLETYGLAVR GSRAAVSDDA THDRLLRLCL LNKALYEIDY EANNRPDWIE IPARGVLSLL
DEMRKVPE
//