ID Q08TR7_STIAD Unreviewed; 551 AA.
AC Q08TR7;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 83.
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 Name=treS {ECO:0000313|EMBL:EAU63877.1};
GN OrderedLocusNames=STAUR_4170 {ECO:0000313|EMBL:ADO71952.1};
GN ORFNames=STIAU_6363 {ECO:0000313|EMBL:EAU63877.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU63877.1, ECO:0000313|Proteomes:UP000032702};
RN [1] {ECO:0000313|EMBL:EAU63877.1, ECO:0000313|Proteomes:UP000032702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU63877.1,
RC ECO:0000313|Proteomes:UP000032702};
RA Nierman W.C.;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADO71952.1, ECO:0000313|Proteomes:UP000001351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO71952.1,
RC ECO:0000313|Proteomes:UP000001351};
RX PubMed=21037205; DOI=10.1093/molbev/msq292;
RA Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA Sogaard-Andersen L.;
RT "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL Mol. Biol. Evol. 28:1083-1097(2011).
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; CP002271; ADO71952.1; -; Genomic_DNA.
DR EMBL; AAMD01000141; EAU63877.1; -; Genomic_DNA.
DR RefSeq; WP_002617220.1; NZ_AAMD01000141.1.
DR STRING; 378806.STAUR_4170; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; sur:STAUR_4170; -.
DR PATRIC; fig|378806.16.peg.2778; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_006462_2_1_7; -.
DR OMA; WNQPEVH; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000001351; Chromosome.
DR Proteomes; UP000032702; Unassembled WGS sequence.
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; 3.20.20.80; 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; 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.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:EAU63877.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 15..413
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 551 AA; 64923 MW; 96D3618637CAF4CD CRC64;
MEQDPLWYKK ALIYELHIRA FHDSNGDGHG DIPGLIEKLP YLQDLGVDCL WLLPHYPSPL
RDDGYDIADF YGIHPDYGTL ADFQRLVEAA HQRGLRIITE LVVNHTSDQH PWFQESRRDP
KSPKRDWYVW SDTEEKYKGT RIIFLDTERS NWTWDPVAKQ YFWHRFFSHQ PDLNYDNPEV
QEAMLDVMRF WLNMGVDGFR CDAVPYLFER EGTNCENLPE THAFLKRLRK TIDAEYPSKM
LLAEANQWPA DVRVYFGDGD EFNMGFHFPV MPRLFMAVRR EDRNPIVEIL QQTPDIPETC
QWAIFLRNHD ELTLEMVTDE DRDYMYREYA MDPRMRLNLG IRRRLAPLMD NGRRRIELMH
SLLFSLPGTP VMYYGDEIGM GDNIYLGDRN GVRTPMQWTG DRNAGFSRTD SARLYAPVIA
DPVYGYQGIN VEAQERVKAS LLHWVKRLIK VRQRYPAFAM GKLRFVNPDN RRVLAFTREH
EGQTILIICN LSRFAQPAVL DLREWEGYVP IELMGETEFP RISSLPYQLS MGPYMFLWFR
LEKPLPGRTL A
//