ID A0A077M3U4_9MICO Unreviewed; 574 AA.
AC A0A077M3U4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:CCH78815.1};
GN ORFNames=BN12_350021 {ECO:0000313|EMBL:CCH78815.1};
OS Tetrasphaera japonica T1-X7.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Tetrasphaera.
OX NCBI_TaxID=1194083 {ECO:0000313|EMBL:CCH78815.1, ECO:0000313|Proteomes:UP000035721};
RN [1] {ECO:0000313|EMBL:CCH78815.1, ECO:0000313|Proteomes:UP000035721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T1-X7 {ECO:0000313|EMBL:CCH78815.1,
RC ECO:0000313|Proteomes:UP000035721};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(2013).
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:CCH78815.1}.
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DR EMBL; CAJB01000279; CCH78815.1; -; Genomic_DNA.
DR RefSeq; WP_048550976.1; NZ_HF570958.1.
DR AlphaFoldDB; A0A077M3U4; -.
DR STRING; 1194083.BN12_350021; -.
DR OrthoDB; 9043248at2; -.
DR Proteomes; UP000035721; 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, ECO:0000313|EMBL:CCH78815.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000035721}.
FT DOMAIN 28..428
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 574 AA; 65007 MW; D7518490E9A110FE CRC64;
MTAVQGLALS QPGLQHDPEW FRKAVFYEVL VRAFADSNGS GAGDFNGLLA RLDYLQWLGI
DCIWLPPFYA SPLRDGGYDI ADYTSVLPEF GTLPDFRQLI TEAHARGIRI VTDFVMNHTS
DQHPWFQASR SDPEGPFGDF YVWSDTDDKY TDARVIFIDT EVSNWTFDPV RRQFFWHRFF
SHQPDLNFEN EAVHEAMFEV VRFWMDMGID GFRLDAVPYL YEEEGHNGEN HPKTHAFLVK
LRAMIDEEYP GRILLAEANQ PPADVVDYFG TEGAPECQMC FHFPIMPMLY YALREQKAAP
IVDILADTPP IPSGTQWGTF LRNHDELTLE MVTPEQRAAM YGWYAPDPRM RANVGIRRRL
APLLDNSRPE IELIHALLLS LPGSPCLYYG DEIGMGDNIW LNDRDAVRTP MQWTPDRNAG
FSTADPGRLY LPVISSLVYH YNTANVEAQM ATGSSFLHWL KAMLAVRGQH PVFGLGDFTV
AAADNDSILA FVRVVESDDA DHPTEVVLCV NNLAARPAAG HITVPERFAG WSTVDLFGGH
GFPDLDDAGR IHMTLGSRDF FWLRLYPPTE TRRG
//
