ID K6VIV0_9MICO Unreviewed; 571 AA.
AC K6VIV0;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
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 Name=treS {ECO:0000313|EMBL:GAB76659.1};
GN ORFNames=AUCHE_02_00180 {ECO:0000313|EMBL:GAB76659.1};
OS Austwickia chelonae NBRC 105200.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Austwickia.
OX NCBI_TaxID=1184607 {ECO:0000313|EMBL:GAB76659.1, ECO:0000313|Proteomes:UP000008495};
RN [1] {ECO:0000313|EMBL:GAB76659.1, ECO:0000313|Proteomes:UP000008495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105200 {ECO:0000313|EMBL:GAB76659.1,
RC ECO:0000313|Proteomes:UP000008495};
RA Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Austwickia chelonae NBRC 105200.";
RL Submitted (AUG-2012) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAB76659.1}.
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DR EMBL; BAGZ01000002; GAB76659.1; -; Genomic_DNA.
DR RefSeq; WP_006501410.1; NZ_BAGZ01000002.1.
DR AlphaFoldDB; K6VIV0; -.
DR STRING; 100225.SAMN05421595_1792; -.
DR eggNOG; COG0366; Bacteria.
DR OrthoDB; 9043248at2; -.
DR Proteomes; UP000008495; Unassembled WGS sequence.
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:UP000008495}.
FT DOMAIN 25..425
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 571 AA; 64866 MW; FAE894CF065CE8FC CRC64;
MHGLNLTQPG LRHDPDWYKT AVFYEVLVRA FADSKGSGSG DFTGLIGKLD YLQWLGVDCL
WLPPFYASPL RDGGYDISDY TAVLPEFGTL PEFTELVSQA HARGIRIITD LVMNHTSDQH
PWFQASRSDP DGPYGDFYVW SDDDTKYAEA RIIFVDTEVS NWTFDPVRRQ FFWHRFFSHQ
PDLNFENPAV QDAMFDTVRF WMDLGIDGFR LDAVPYLFEE EGHNGENHPK THEFLARLRT
MVDTEYPGRI LLAEANQMPS EVVDYFGTDE EPECQMCFHF PVMPRLYYAL RAEKAAPIID
VLNDTPAVPG GGQWGTFLRN HDELTLEMVS PEERTAMYGW YAPDPRMRAN VGIRRRLSPL
LDNSRAEVEL IHALLLSLPG SPCLYYGDEI GMGDNIWLDD RDAVRTPMQW TPDRNAGFSS
ADPGKLYLPV IQSLVYHHNN VNVEAQVASS SSLLHWLRAM LQIRSQHPVF GLGIFSLRDC
DNEAVLAFTR TLEADPSQGR EENVHVLCLH NLSSRPQAGT VHLPERLAGA KARDLFGGSG
FPGVTEDATY RFTVGSRDFF WLSLQEREHD G
//
