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
//