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Database: UniProt/TrEMBL
Entry: B8IPJ0_METNO
LinkDB: B8IPJ0_METNO
Original site: B8IPJ0_METNO 
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
//
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