ID   Q2IDW4_ANADE            Unreviewed;       572 AA.
AC   Q2IDW4;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 87.
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=Adeh_3002 {ECO:0000313|EMBL:ABC82772.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC82772.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA   Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA   Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000251; ABC82772.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2IDW4; -.
DR   STRING; 290397.Adeh_3002; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; ade:Adeh_3002; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_006462_2_1_7; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000001935; 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, ECO:0000313|EMBL:ABC82772.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935}.
FT   DOMAIN          41..440
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   572 AA;  66206 MW;  23BEA754A9DE0AC1 CRC64;
     MYLTDSCHGL AGPRGPGRHM AISQRRRAVD PLWFKDAVIY ETHVKSFYDS NGDGVGDLRG
     LVEKLDYLQD LGITCLWLLP FFPSPLRDDG YDIADYKGIH PDYGTVDDFR QLVAAAHARG
     IRVVVELVVN HTSDQHPWFQ RARRAPAGSP ERAYYVWSDT DERYRDARII FTDTEKSNWT
     WDPEAKQYYW HRFFSHQPDL NFENAVVLGE VLDALRFWAE MGVDGFRLDA VPYLIEQDGT
     SCENLPGTHE VIRKIRAYVD QHFPGRMLLA EANQWPADVR PYFGEGDECH MAFHFPLMPR
     IFMALRLEDV EPIVEIMRRT PAIPDTCQWA LFLRNHDELT LEMVTADERD YMYLAYSQDP
     RMKLNVGIRR RLAPLVDNSR RRMELLNSLL FSFPGTPIVY YGDELGMGDN IYLHDRNGVR
     TPMQWSPDRN AGFSRADPGR LYSAPISDAV YGYQAVNVEA QLRDPSSLLH WMRNTIALRK
     LFRAFGRGTM EFLPVQNRKV LAYVRRHDED VILCVANVSR FAQPAQLDLS HLEGYVPVEM
     VGYTEFPRIG RQPYALTLAP YGYFWFELRK PA
//