ID A0A2S6N699_RHOGL Unreviewed; 1099 AA.
AC A0A2S6N699;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=CCS01_19765 {ECO:0000313|EMBL:PPQ30139.1};
OS Rhodopila globiformis (Rhodopseudomonas globiformis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Rhodopila.
OX NCBI_TaxID=1071 {ECO:0000313|EMBL:PPQ30139.1, ECO:0000313|Proteomes:UP000239724};
RN [1] {ECO:0000313|EMBL:PPQ30139.1, ECO:0000313|Proteomes:UP000239724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 161 {ECO:0000313|EMBL:PPQ30139.1,
RC ECO:0000313|Proteomes:UP000239724};
RX PubMed=29423563;
RA Imhoff J.F., Rahn T., Kunzel S., Neulinger S.C.;
RT "New insights into the metabolic potential of the phototrophic purple
RT bacterium Rhodopila globiformis DSM 161(T) from its draft genome sequence
RT and evidence for a vanadium-dependent nitrogenase.";
RL Arch. Microbiol. 0:0-0(2018).
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:PPQ30139.1}.
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; NHRY01000216; PPQ30139.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6N699; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000239724; 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:0016740; F:transferase activity; 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:UP000239724};
KW Transferase {ECO:0000313|EMBL:PPQ30139.1}.
FT DOMAIN 29..429
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1099 AA; 123791 MW; BCE5193C6DDBDF6A CRC64;
MNVAHPRPQV AAAAADLDPL WYKDAIIYQL HVKSFSDANN DGIGDFPGLI SKLDYIAELG
VNVIWLLPFY PSPRLDDGYD IADYRGVHPD YGSLQDVKRF IAAAHERGIR VITELVVNHT
SDQHPWFQRA RTSKPGSTYR DFYVWSNDDR KYAGTRIIFV DSERSNWTWD DTAKAYYWHR
FYHHQPDLNF DNPRVMREVL SVLRYWAELG VDGLRLDAVP YLVEREGTNN ENLPETHAVL
KRIRRELQGH YPDKMLLAEA NQWPEDTKDY FGDGDECHMA FHFPLMPRMY MAIAREDRFP
ITDILRQTPD IPGNCQWAIF LRNHDELTLE MVTESERDFL WATYAADRRA RLNLGIRRRL
APLLERDRRR IELMHYLLFS MPGTPVIYYG DEIGMGDNIH LGDRNGVRTP MQWSSDRNGG
FSRVADPSRL VLPMVMDPLY DFQSVNVEAQ SADPHSLLMW MRRTIAIRRQ YKVFGRGGYR
LLYPKNRKIL AYLREGEDTT ILCVANLSRT PQAVELDLSE FQGRIPIELD GHSVFPPIGQ
LTYLLTLPPY GFYWFLLSEA DDWPSTHTPA PEPMPEYQTI VMRRDLADAV LAMRSVIERE
ILPPYLAKRR WYAQKDQKLK SVRIALLTRI MSEEALLVEI ETETTAGKAR WLLPLGIVWG
DGATPPLPTQ LALARIRRGP KVGLLTDAFA LAGFPTGVLS GLAQRDVIAT EHGVVRFEPT
SRIKDIVVPD GVELQWISAE QSNSSVIVGD IAIIKMFRRV TSGPHPEAEM GRYLTEQGFA
NTPALLGEVV RIDPKGVRHA MVIAQAFVRN QGDAWSWTLD LLVRGLSDIT SGDGATAADA
ANHADYAGFG ELLGTRLGEM HAILARPSRD EAFAPVTAGA DDGRAVAERV RDQLDAAYAA
IEATTQWEPA AEPDRQTVLG VRDALFARLP ALANAIQGST LTRIHGDLHL GQVLVVNGDV
SIIDFEGEPA RPVEARRAKD HPLRDVAGMI RSFAYAAAVV KRRSQASHAH VPDEQVNAFL
DSFVTRATEC FLAGYRKAFA STDAGSPVSL QQDLLDLFLI EKAAYEVVYE SANRPTWIDV
PLHGLAVRTR HLLGVEAVA
//
