ID A0A0K1FD30_9MICO Unreviewed; 580 AA.
AC A0A0K1FD30;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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 ORFNames=ADJ73_15560 {ECO:0000313|EMBL:AKT52341.1};
OS Arsenicicoccus sp. oral taxon 190.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Arsenicicoccus.
OX NCBI_TaxID=1658671 {ECO:0000313|EMBL:AKT52341.1, ECO:0000313|Proteomes:UP000065578};
RN [1] {ECO:0000313|Proteomes:UP000065578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0371 {ECO:0000313|Proteomes:UP000065578};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (JUL-2015) 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}.
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DR EMBL; CP012070; AKT52341.1; -; Genomic_DNA.
DR RefSeq; WP_050349013.1; NZ_CP012070.1.
DR AlphaFoldDB; A0A0K1FD30; -.
DR STRING; 1658671.ADJ73_15560; -.
DR KEGG; ars:ADJ73_15560; -.
DR PATRIC; fig|1658671.3.peg.3168; -.
DR OrthoDB; 9043248at2; -.
DR Proteomes; UP000065578; 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 25..425
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 580 AA; 65721 MW; 1A2AD539EF16AEF5 CRC64;
MQGLNLNQPG LKHDPSWFRK AVFYEVLVRA FADSNGSGAG DFTGLLGKLD YLQWLGVDCL
WLPPFYASPL RDGGYDIADY RAVLPEFGTL PEFKELVSQA HARGIRIITD FVMNHTSDQH
PWFQASRSEP EGPYGDYYVW SDDDTKYSEA RIIFVDTEVS NWTFDPVRRQ FFWHRFFSHQ
PDLNFENPKV QDEMFDIVRY WMDMGIDGFR LDAVPYLFEE EGHNGENHPR THEFLARLRE
MVDEEYPGRI LLAEANQMPH EVVDYFGSEE APECQMCFHF PVMPRLYYAL REGKATPIVK
VLEETPAIPT GTQWGTFLRN HDELTLEMVD AEERAAMYGW YAPDPRMKAN VGIRRRLAPL
LDNSRAEIEL INALVLSLPG SPCLYYGDEI GMGDNIWLTD RDAVRTPMQW TPDRNAGFST
ADPGKLYLPV IQSLVYHHNN VNVEAAMASS SSLLHWMRGM LQVRKHHPVM GMGTFEVMPT
DNDAILAFVR DLSPQDATED APAESVLCVN NLSPRPQGTR VQLPASYAGA QAVDLFGGSG
FGSVDADGRF TVTMGSRDFF WLQLIRRTPA EETGAAGGEV
//