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Database: UniProt
Entry: C6WGB6_ACTMD
LinkDB: C6WGB6_ACTMD
Original site: C6WGB6_ACTMD 
ID   C6WGB6_ACTMD            Unreviewed;       604 AA.
AC   C6WGB6;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 74.
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=Amir_6073 {ECO:0000313|EMBL:ACU39880.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064
OS   / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU39880.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU39880.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 /
RC   NRRL B-12336 / IMRU 3971 / 101 {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L.,
RA   Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., Mavromatis K.,
RA   Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA   Detter J.C., Han C., Chain P., Tindall B.J., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
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; CP001630; ACU39880.1; -; Genomic_DNA.
DR   RefSeq; WP_015804765.1; NC_013093.1.
DR   AlphaFoldDB; C6WGB6; -.
DR   STRING; 446462.Amir_6073; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; ami:Amir_6073; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_006462_2_1_11; -.
DR   OrthoDB; 9043248at2; -.
DR   Proteomes; UP000002213; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213}.
FT   DOMAIN          58..460
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   604 AA;  69055 MW;  1899B66EE7EB406B CRC64;
     MHDEEPRPDA ALGLDGIPHT GEAIGADGLL VEPQAEDFKS AREVPRDQAW YKGAVFYEVL
     VRAFSDSNGD GTGDLRGLAS RLDYLEWLGV DCLWLPPFYA SPLRDGGYDI SDFRAVLPEF
     GTVDDFVYLL DEAHRRGIRV ITDLVLNHTS DAHPWFQQSR AEPDGPYGEY YVWSDDDSRY
     ADARVIFVDT ESSNWTYDPV RGQFFWHRFF SHQPDLNFEN PDVQEAMLDI LRFWLDLGID
     GFRLDAVPYL FEQEGTNCEN LPRTHDFLKR CRKVVDDEYP GRVLLAEANQ WPADVVEYFG
     DPEVGGDECH MAFHFPLMPR IFMAVRRESR FPISEILAQT PSIPDGSQWG IFLRNHDELT
     LEMVTDEERD YMYAEYAKDP RMKANIGIRR RLAPLLENDR NQQELFTAML LSLPGSPVLY
     YGDEIGMGDN IWLGDRDGVR TPMQWTPDRN AGFSGCDPGR LYLPVIMDPV YGYQALNVEA
     QLNNQSSLLN WTRRMIEIRK QHHAFAEGDF DDLGGSNPSV LAYRRRWARP DGQEDIVLCV
     NNLSRFPQPV ELDLGEHRGL RPVELTGGVR FPQIGELSYL LTLPGHGFYW FQLVAAGDDG
     ESSR
//
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