ID   L7UBW4_MYXSD            Unreviewed;       551 AA.
AC   L7UBW4;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 55.
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=MYSTI_04255 {ECO:0000313|EMBL:AGC45553.1};
OS   Myxococcus stipitatus (strain DSM 14675 / JCM 12634 / Mx s8).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=1278073 {ECO:0000313|EMBL:AGC45553.1, ECO:0000313|Proteomes:UP000011131};
RN   [1] {ECO:0000313|EMBL:AGC45553.1, ECO:0000313|Proteomes:UP000011131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14675 / JCM 12634 / Mx s8
RC   {ECO:0000313|Proteomes:UP000011131};
RX   PubMed=23516218; DOI=10.1128/genomeA.00100-13;
RA   Huntley S., Kneip S., Treuner-Lange A., Sogaard-Andersen L.;
RT   "Complete genome sequence of Myxococcus stipitatus strain DSM 14675, a
RT   fruiting myxobacterium.";
RL   Genome Announc. 1:E0010013-E0010013(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; CP004025; AGC45553.1; -; Genomic_DNA.
DR   RefSeq; WP_015349813.1; NC_020126.1.
DR   AlphaFoldDB; L7UBW4; -.
DR   STRING; 1278073.MYSTI_04255; -.
DR   KEGG; msd:MYSTI_04255; -.
DR   PATRIC; fig|1278073.3.peg.4326; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_006462_2_1_7; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000011131; 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; 3.20.20.80; 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   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
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;  64605 MW;  8F90A5D411A6D14B CRC64;
     MELDPLWYKK ALIYELHLRA FHDSNGDGHG DIPGLIEKLP YLQDLGIDCL WILPHYPSPL
     RDDGYDIADF YGVHPDYGTL ADFQRLIDEA HKRGLRIITE LVVNHTSDQH PWFQEARSDP
     KSPKRDWYVW SDTDDRYKGA RIIFTDTERS NWTWDPVAKQ YFWHRFFSHQ PDLNYDNPQV
     QEAMLDVMRF WLNMGVDGFR CDAVPYLFER EGTNCENLPE THAFLKRLRK TIDAEYPGKM
     LLAEANQWPA DVRVYFGDGD EFNMGFHFPV MPRLFMGIRR EDRTPIVEIM QQTPDIPESC
     QWALFLRNHD ELTLEMVTDE DRDYMYREYA TDPRMRLNLG IRRRLAPLMD NGRRRIELMH
     SLLFTLPGTP VLYYGDEIGM GDNIYLGDRN GVRTPMQWTG DRNAGFSRAD YARLYAPVIA
     DPVYGYQSIN VEAQDRVKSS LLHWVKRMIR IRQRYPVFAL GTLRFLPAEN RKVLAFVREW
     EGQTVLVVCS LSRFAQPAVL DLRDWAGMVP VEMIGDTPFP RITDAPYQFS MGPYMFLWFR
     LDRPLPGGGR A
//