ID   I0HRC1_RUBGI            Unreviewed;      1121 AA.
AC   I0HRC1;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
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:BAL95558.1};
GN   OrderedLocusNames=RGE_22170 {ECO:0000313|EMBL:BAL95558.1};
OS   Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Rubrivivax.
OX   NCBI_TaxID=983917 {ECO:0000313|EMBL:BAL95558.1, ECO:0000313|Proteomes:UP000007883};
RN   [1] {ECO:0000313|EMBL:BAL95558.1, ECO:0000313|Proteomes:UP000007883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100245 / IL144 {ECO:0000313|Proteomes:UP000007883};
RX   PubMed=22689232; DOI=10.1128/JB.00511-12;
RA   Nagashima S., Kamimura A., Shimizu T., Nakamura-isaki S., Aono E.,
RA   Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S., Fujita N.,
RA   Shimada K., Hanada S., Nagashima K.V.P.;
RT   "Complete genome sequence of phototrophic betaproteobacterium Rubrivivax
RT   gelatinosus IL144.";
RL   J. Bacteriol. 194:3541-3542(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}.
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DR   EMBL; AP012320; BAL95558.1; -; Genomic_DNA.
DR   RefSeq; WP_014428420.1; NC_017075.1.
DR   AlphaFoldDB; I0HRC1; -.
DR   STRING; 983917.RGE_22170; -.
DR   KEGG; rge:RGE_22170; -.
DR   PATRIC; fig|983917.3.peg.2145; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_0_1_4; -.
DR   Proteomes; UP000007883; Chromosome.
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; 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:UP000007883}.
FT   DOMAIN          37..436
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1121 AA;  124307 MW;  F1DF8FEB0BB1188E CRC64;
     MKGEDLSAIT ATQTQPPADA AAPALDPLWF KDAVIYELHI KSFADSNGDG IGDLAGLISK
     LDYVRDLGVN TIWLLPFYPS PLRDDGYDVA DFMAVNPAYG TAADVARLVA EAHARGLRVI
     TELVVNHTSD QHPWFQRARR APRGSPERDF YVWSDDPTRY AGTRIIFTDT EKSNWTWDEV
     AGQYFWHRFF SHQPDLNFDN PAVREAVFGI MEFWLEQGVD GFRLDAIPYL VEREGTSNEN
     LRETHEVIKE IRRRLDAKYP GKLLLAEANM WPEDVREYFG EDDECHMAYH FPLMPRMYMA
     IAQEDRHPVV EILQQTPDIS PQCQWAIFLR NHDELTLEMV TSRERDYMYS MYAADPRARL
     NLGIRRRLAP LLENDAERIK LMNSLLLSMP GSPVLYYGDE IGMGDNIFLG DRDGVRTPMQ
     WTSDRNGGFS RADPQRLVLP AIQDPIYGFE AVNVEAQSRD ASSLLNWTRR MLAIRRSTQV
     FGRGRIRMLH PGNRKVLAYL RELGDEVVLC VANLGRAPQP VELDLSRYKG RVPVEMGAHT
     AFPPIGELPY LLTLAGHGFF WFRLATDAAP PDWHADRRPV EHLPVLVMFD GWNSFFRDRV
     VPWRIAMAGK TLAQLEDELL PPHLARQRWF DAGEPPAQAR IGTHATLAQD GREWLLALVD
     TRGGPHEDAR WFSPLAVAWE DDEADQGRLG QLGPAALAKA RMQARIGLLG DAGGDEAFCR
     ALVAAVAAGR SLPAAGGGQI RFVALRGFDA GIAAELDTLA VRAVPQGRNT TLQLGDRLFV
     KLLRRLRPGV NVEVEMGRHL REVAHFEHAV VPVGHVEHVA ADGTVSTLAV LQPWVVHQGN
     AWDFALMQLT RHLERAAPAP AESVGAAEGG LMARVRALAE RLAALHEALA LRRGDAAFDP
     EPLQPEDLRR AAAATAQLAH TTLALLAEAT PRLPAAQQPL ARRLAAGERT LRDRLAACAA
     HGAGGPKLRI HGALRLQEVL LVHEDFVLAD FEGDPSLPPA ERRARQSPLR DVAGLLHSLD
     LVRAAALQRG AHTEAENRRR EALADAWAGE LRRAFVDSYA ERALALGLVA GADAFEGPAS
     TLALFEIDAA LRELHDELRR RPAGATAPLA ALATLAQRLG P
//