ID A0A2U1CLC1_9BURK Unreviewed; 1141 AA.
AC A0A2U1CLC1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=C7440_2539 {ECO:0000313|EMBL:PVY61806.1};
OS Pusillimonas noertemannii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pusillimonas.
OX NCBI_TaxID=305977 {ECO:0000313|EMBL:PVY61806.1, ECO:0000313|Proteomes:UP000246145};
RN [1] {ECO:0000313|EMBL:PVY61806.1, ECO:0000313|Proteomes:UP000246145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10065 {ECO:0000313|EMBL:PVY61806.1,
RC ECO:0000313|Proteomes:UP000246145};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (APR-2018) 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:PVY61806.1}.
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DR EMBL; QEKO01000003; PVY61806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1CLC1; -.
DR STRING; 1231391.GCA_000308195_00350; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000246145; 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; 3.90.1200.10; -; 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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032091; Malt_amylase_C.
DR InterPro; IPR045857; O16G_dom_2.
DR InterPro; IPR012810; TreS/a-amylase_N.
DR InterPro; IPR012811; TreS_maltokin_C_dom.
DR NCBIfam; TIGR02457; TreS_Cterm; 1.
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.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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:UP000246145}.
FT DOMAIN 34..433
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1141 AA; 127633 MW; 95139DC25D9EDC17 CRC64;
MTKRSDAGST SAKRGSVPVS RNEPGWYKDA VIYQLHVKSF HDADGDGVGD FQGLISRLDY
IAELGVDTVW LLPFYPSPRL DDGYDIADYR NVHPDYGSLA DVRRFIRAAH ARGLHVITEL
VVNHTSDQHP WFQRARHARP GSAARDYYVW SDNDQAYAGT RIIFCDTEKS NWSWDPVAGA
YFWHRFYSHQ PDLNYDNPRV LKEIIGVMRF WLDMGVDGLR LDAVPYLVER EGTNNENLPE
THDVLRRIRA VMDEHYPDRL LLAEANQWPE DAQEYFGKGD ECHMSFHFPL MPRMYMAIAR
ADRFPITDIM RQTPPIPESC QWAIFLRNHD ELTLEMVTSS ERDYLWDFYA ADRRARINLG
IRRRLAPLLQ RDRRRIELMN SLLLSMPGTP VLYYGDELGM GDNIHLGDRD GVRTPMQWTP
DRNGGFSRAD PEHLILPLLM GPLYGYEAVN VEAQQRDAHS LLNWTRRMLA KRQQTRAFGR
GGLRFIFPGN RKVLAYLREY QDEVLLCVAN LSDASQPVEL DLGQMAGRVP VELLGGTPFP
SIGEAPYMLT LPPYGFYWFE LSTSASSPSW HTAVPDQAPD YVTLVLRRAA SGPRLLDESR
KALCQEVLPP YLARQRWFPQ DGPVGRVALG YAVPLAGDPD LVLCELDVGQ GQGGQAYFLP
MAMLWGEAAT PLQQQHGLAR VRRTAETGLL VDAVSLPRFA LAMLDCFRAG VSLPLPGEEA
GRLEFHAEEG LTGLADIEPD DIGWFRGEQS NSSLLLGETA VLKLLRHVVA GEHPEAEMTR
YLTRAGYANN AALLGELRRV GDDGTPRTLA LLHARIPNQG DAWSWTNDYL RRSLESAALT
GESRSDYRED LAGYTAVAET IGVRLAQMHA MLADAGEDPA FAPERATAAD ARRWAKDIRA
MVQAAIASAW RHRERLPAAG LAQAEALRKQ QASLLKRVDA AAARLSGHWR LRIHGDLHLG
QVLIAQNDVY FIDFEGEPDR PLEARRSKAS PWRDVAGLLR SIDYAAHGFT EPEPAAEPAA
GPQAASEKTG DNVDGSSLAL PAAQTTRERH ARLLEQFRES ARDAFLDGYR KAALDSRPEL
LDESTDGILL DLALLEKAAY EVCYEAAHRP DWLPIPLQGL TRIAEGLLSP ASSDATEGDH
G
//
