ID Q3SJM9_THIDA Unreviewed; 1095 AA.
AC Q3SJM9;
DT 11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 94.
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 OrderedLocusNames=Tbd_1172 {ECO:0000313|EMBL:AAZ97125.1};
OS Thiobacillus denitrificans (strain ATCC 25259).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=292415 {ECO:0000313|EMBL:AAZ97125.1, ECO:0000313|Proteomes:UP000008291};
RN [1] {ECO:0000313|EMBL:AAZ97125.1, ECO:0000313|Proteomes:UP000008291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25259 {ECO:0000313|EMBL:AAZ97125.1,
RC ECO:0000313|Proteomes:UP000008291};
RX PubMed=16452431; DOI=10.1128/JB.188.4.1473-1488.2006;
RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT anaerobic bacterium Thiobacillus denitrificans.";
RL J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ97125.1; -; Genomic_DNA.
DR RefSeq; WP_011311684.1; NC_007404.1.
DR AlphaFoldDB; Q3SJM9; -.
DR STRING; 292415.Tbd_1172; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; tbd:Tbd_1172; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG3281; Bacteria.
DR HOGENOM; CLU_007635_1_1_4; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000008291; 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 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008291}.
FT DOMAIN 16..415
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1095 AA; 124584 MW; E8207596865E104A CRC64;
MEENDPLWYK DAIVYELHVK AFFDANGDGA GDFRGLISKL DYLQELGVNA LWLLPFYPSP
GRDDGYDISD YHNLHPSFGD MADFRRFIRE AHQRGLRVIT ELVVNHTSDQ HPWFQAARRA
PPGSVKRNYY VWSDTDTRFS ETRIIFSDTE KSNWAWDEVA QAYYWHRFFS HQPDLNFNNP
HVFKAIMRTM RFWFDAGVDG MRLDAVPYLC ERDGTSNENL PETHAVIRRM RAELDARYSN
RMFLAEANQW PEDVREYFGN GDECHMAYHF PLMPRMYMAI AQEDRHPIVE IMEQTPDIPD
LCQWAVFLRN HDELTLEMVT DRERDYLYQA YASDPQARLN LGIRRRLAPL LDNDRHRIEL
MNLLLMTMPG SPIVYYGDEI GMGDNLLLGD RNGVRTPMQW DGGPNGGFSS APTERLFLPP
ITDPVYGYGA VNVEAQQRNP SSLLNWTRRL IAMRKAHRAL GRGTLRFLRP GNRKVLAYLR
EYEGETILCV ANVARAPQAV ELDLSPFKGH VPVELMGRSS FPPIGELPYL LTLGGYGCFV
FRLATDVEAP AWHEERPVPP DLPVLVLVDA GWRTLFARTD EGVNQLMVRR AREQLERQII
PRYFRTQPWF VYSEAALEKF EFGTLREWGT DSGTWLLATV TVTLLDGSIY HYALPLGLAW
EDEDEGRVAA LLHVTLAKVR RLARVGILFD AFWDDGFCCA IVSAMERGET LAYGDGHLTF
RTASAYPGFF CPLVTSSITR TVSEHGRLRV NLNDQLVLKS YPRQMQGTHP ELEMSRFLTE
TAKFAHIPQL GGTVEYVASS GRHSTLAILE RYAPNQGDAW AYTLNYLERF LDLSRTTGEQ
APDGRHGRYM GLMKTLGERT AEFHRALATP DRSGDFGSEP IAPPDILEWV NKVRHEMGVM
YELLERALPA LPEPVAVAAQ QLFLVRPKLY RRVIRASRVR VDASKTRCHG NYHLGQVWLV
QNDFLIANYG GIPGRSWEER RAKHAPLRDV ASMLLSLSQA GAAALARVAG DSVDVMAALQ
PHVDAWELAA RKAFYRGYRK GMDGHAAYPT DATAAEALLT LFLAEKAIAE LTEALERRAV
GSAAAMRRLV QVTRR
//
