ID K5BA99_MYCHD Unreviewed; 595 AA.
AC K5BA99;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
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:EKF21870.1};
GN ORFNames=C731_4185 {ECO:0000313|EMBL:EKF21870.1};
OS Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 /
OS 3849) (Mycobacterium hassiacum).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1122247 {ECO:0000313|EMBL:EKF21870.1, ECO:0000313|Proteomes:UP000006265};
RN [1] {ECO:0000313|EMBL:EKF21870.1, ECO:0000313|Proteomes:UP000006265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44199 / CIP 105218 / JCM 12690 / 3849
RC {ECO:0000313|Proteomes:UP000006265};
RX PubMed=23209251; DOI=10.1128/JB.01880-12;
RA Tiago I., Maranha A., Mendes V., Alarico S., Moynihan P.J., Clarke A.J.,
RA Macedo-Ribeiro S., Pereira P.J., Empadinhas N.;
RT "Genome sequence of Mycobacterium hassiacum DSM 44199, a rare source of
RT heat-stable mycobacterial proteins.";
RL J. Bacteriol. 194:7010-7011(2012).
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:EKF21870.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMRA01000112; EKF21870.1; -; Genomic_DNA.
DR RefSeq; WP_005631173.1; NZ_LR026975.1.
DR AlphaFoldDB; K5BA99; -.
DR STRING; 1122247.GCA_000379865_01265; -.
DR PATRIC; fig|1122247.3.peg.4015; -.
DR eggNOG; COG0366; Bacteria.
DR OrthoDB; 9043248at2; -.
DR Proteomes; UP000006265; 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:EKF21870.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006265}.
FT DOMAIN 54..456
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 595 AA; 68325 MW; D69445BB0593C039 CRC64;
MSPSPASEPT AEHDPAAGSH VEYGVVEHPT ADDFGQARVL PADRTWFKRA VFYEVLVRAF
YDSNADGIGD LPGLTEQLDY IKWLGVDCIW LPPFYDSPLR DGGYDIRDFY RVLPEFGTVD
DFVNLLDAAH RRGIRVITDL VMNHTSDQHP WFQESRRDPD GPYGDFYVWS DTAEKYSQAR
IIFVDTEESN WTFDPVRRQF YWHRFFSHQP DLNYDNPAVQ QAMLDVLRFW LDLGIDGFRL
DAVPYLFERE GTNCENLPET HAFLKHCRKV IDDEYPGRVL LAEANQWPAD VVAYFGDPDT
GGDECHMAFH FPLMPRIFMA VRRESRFPIS EILAQTPDIP EMAQWGIFLR NHDELTLEMV
TDEERDYMYA EYAKDPRMKA NVGIRRRLAP LLENDRNQME LFTALLLSLP GSPVLYYGDE
IGMGDIIWLG DRDAVRTPMQ WTPDRNTGFS KANPGRLYLP PNQDPVYGYQ AVNVEAQRDN
SSSLLNWTRT MLAVRRRHDA FAVGGFRELG GSNPSVLAFV REYTGDGQRD IVLCVNNLSR
FPQPIELNLQ HWSGYTPVEM TGHVEFPPIG QLPYLLTLPG HGFYWFALRA EPGAP
//
