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
//