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Database: UniProt/TrEMBL
Entry: M4ZNL1_9BRAD
LinkDB: M4ZNL1_9BRAD
Original site: M4ZNL1_9BRAD 
ID   M4ZNL1_9BRAD            Unreviewed;      1101 AA.
AC   M4ZNL1;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=maltose alpha-D-glucosyltransferase {ECO:0000256|ARBA:ARBA00012619};
DE            EC=5.4.99.16 {ECO:0000256|ARBA:ARBA00012619};
DE   AltName: Full=Maltose alpha-D-glucosyltransferase {ECO:0000256|ARBA:ARBA00031378};
GN   ORFNames=S58_18030 {ECO:0000313|EMBL:BAM87810.1};
OS   Bradyrhizobium oligotrophicum S58.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1245469 {ECO:0000313|EMBL:BAM87810.1, ECO:0000313|Proteomes:UP000011841};
RN   [1] {ECO:0000313|EMBL:BAM87810.1, ECO:0000313|Proteomes:UP000011841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S58 {ECO:0000313|EMBL:BAM87810.1,
RC   ECO:0000313|Proteomes:UP000011841};
RX   PubMed=23396330; DOI=10.1128/AEM.00009-13;
RA   Okubo T., Fukushima S., Itakura M., Oshima K., Longtonglang A.,
RA   Teaumroong N., Mitsui H., Hattori M., Hattori R., Hattori T.,
RA   Minamisawa K.;
RT   "Genome analysis suggests that the soil oligotrophic bacterium Agromonas
RT   oligotrophica (Bradyrhizobium oligotrophicum) is a nitrogen-fixing symbiont
RT   of Aeschynomene indica.";
RL   Appl. Environ. Microbiol. 79:2542-2551(2013).
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 glycosyl hydrolase 13 family. TreS
CC       subfamily. {ECO:0000256|ARBA:ARBA00005496}.
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DR   EMBL; AP012603; BAM87810.1; -; Genomic_DNA.
DR   RefSeq; WP_015664938.1; NC_020453.1.
DR   AlphaFoldDB; M4ZNL1; -.
DR   STRING; 1245469.S58_18030; -.
DR   KEGG; aol:S58_18030; -.
DR   PATRIC; fig|1245469.3.peg.1838; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_1_2_5; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000011841; 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; 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; 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}.
FT   DOMAIN          30..429
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1101 AA;  125719 MW;  7BE0A7EE7A400263 CRC64;
     MNVMSSLDAT DLVTTTDGDG LWYKDAIIYQ LHVKAFADSN NDGVGDFAGL TDKLDYLQDL
     GVTTLWLLPF YPSPGRDDGY DIADYGSINP DFGTMKDFKR FIQEAKRRGL RVITELVVNH
     TSDQHHWFKR ARRSPPGSSA RNWYVWSDTD QKYQGTRIIF TDTEKSNWTW DPEAGQFYWH
     RFFSHQPDLN FDNPRVVNAI IQVMKRWLDA GVDGFRLDAI PYLCERDGTN NENLPETHAI
     IKRLRVELDN YAKDKLLLAE ANQWPEDVQE YFGQGDECHM AYHFPLMPRI YMAIAQEDRF
     PITDILRQTP DIPATCQWAL FLRNHDELTL EMVTDVERDY LWSTYANDPR ARINVGIRRR
     LAPLMDNDRR KIELMNSLLL SFPGTPIIYY GDEIGMGDNI YLGDRNGVRT PMQWTPDRNG
     GFSRADPARL YAPMIMDPVY GYEAVNVEAQ SRSLSSLLNA TKKLISVRKS TLAFGRGTMA
     FIRPANRSVL AYVRQYKDEV ILCVANLSRS AQATELDLSA FKDRIPVEML GRSRFPAIGT
     LPYMITLAPY GFYWFQLKER EKSEPVVQRA VPEFETLVVP LGSTWVSLAR TRSLFERDVL
     PDHLARTRWY PERSAEAIHP TLTAAIPFCD IGDNRPWLIF FKAAERQDAL RYLLPMQIDW
     VRFDRERYNP QAFAAVRQGA REGTLLDAAT TPIFLALLLR NLGQSLIVEE NGLRLEFLPT
     SRFPDKPIRE SEQVRIIETD RCSSKAVVNN EFFIKIYREL EAGSHPEVDV GRFLTEIVGF
     ANVPPLLGSV EVMQDGGRWT IGSVHGFVEN QGDGWTVSAA YLDRYIDDQR VFAASGDERQ
     SEELLPYLRY MAQAGRRVGE LHAALASRDD MAEFAPEPTT ADALDHWIDR LRAQAGRIFA
     VLSERRDHFK DHERALVDQV LAKRSDLSER LSNLIPHHVG GFDIRVHGDF HLGQMLIVKD
     DVFIIDFDGD EEQPLAERQR KAPPARDIAG FLRSIDCSVG VALDRALRAG PDDHGRIAAA
     LLDWRDRAIA AFLAGYRENR TQQRLWPDDP HTAEALLNFF MLEKALGALE YDLAHRPDWL
     RVALGNLLRV LFVPAPASES S
//
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